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Ligand source activities (1 row/activity)

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Ligands					Receptor			Assay information							Chemical information
Sel. page	Common name	GPCRdb ID	#Vendors	Reference ligand	Fold selectivity (Potency)	# tested GPCRs (Potency)	Species	p-value (-log)	Type	Activity Relation	Activity Value	Assay Type	Assay Description	Source	Mol weight	Rot Bonds	H don	H acc	LogP	Smiles	DOI
	10353365	82820	1	None	13	3	Human	10.1	pEC50	=	10.1	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	82820	1	None	13	3	Human	10.1	pEC50	=	10.1	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	117972056	141589	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	5	0	4	5.2	Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3883435	141589	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	5	0	4	5.2	Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1	10.1016/j.bmc.2016.11.018
	117971665	141682	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	415	5	0	4	5.8	FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884532	141682	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	415	5	0	4	5.8	FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117971685	141669	0	None	-	1	Human	9.3	pEC50	=	9.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	387	5	0	4	5.0	FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884187	141669	0	None	-	1	Human	9.3	pEC50	=	9.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	387	5	0	4	5.0	FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	1395	2482	9	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	2482	9	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	2482	9	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	1395	2482	9	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	9837317	2482	9	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL121053	2482	9	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	71131322	122877	0	None	43	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	122877	0	None	43	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	90098428	122876	0	None	60	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	122876	0	None	60	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	68109941	155569	0	None	-	1	Human	9.0	pEC50	=	9.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	155569	0	None	-	1	Human	9.0	pEC50	=	9.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	1395	2482	9	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	2482	9	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	2482	9	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	123289788	141693	0	None	-	1	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884636	141693	0	None	-	1	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117972250	141768	3	None	32	2	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	141768	3	None	32	2	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	134130172	141615	0	None	-	1	Human	8.8	pEC50	=	8.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3883634	141615	0	None	-	1	Human	8.8	pEC50	=	8.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1	10.1016/j.bmc.2016.11.018
	117968349	141656	0	None	-	1	Human	8.7	pEC50	=	8.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	429	6	0	4	6.0	FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884094	141656	0	None	-	1	Human	8.7	pEC50	=	8.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	429	6	0	4	6.0	FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	1393	1504	58	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1396	1504	58	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	213056	1504	58	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	CHEMBL8759	1504	58	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	117968551	141679	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	393	6	0	4	5.0	CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884343	141679	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	393	6	0	4	5.0	CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	146036859	173965	4	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	293	2	0	3	3.8	Brc1cccc2c1nnn2CC1CCCCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4556144	173965	4	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	293	2	0	3	3.8	Brc1cccc2c1nnn2CC1CCCCC1	10.1021/acs.jmedchem.8b00161
	68108471	82222	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	436	4	0	4	5.4	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/jm3010724
	CHEMBL2179326	82222	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	436	4	0	4	5.4	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/jm3010724
	156020355	177444	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	177444	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	67060140	166832	0	None	26	2	Rat	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4295230	166832	0	None	26	2	Rat	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	71135411	122868	0	None	5	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	122868	0	None	5	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	57459497	83473	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	442	4	0	5	5.0	COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206439	83473	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	442	4	0	5	5.0	COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1	10.1021/jm300912k
	44361501	118786	0	None	-	1	Rat	7.0	pEC50	=	7	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O	10.1021/jm030967o
	CHEMBL343994	118786	0	None	-	1	Rat	7.0	pEC50	=	7	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O	10.1021/jm030967o
	70683631	74224	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	384	6	0	4	5.4	CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029795	74224	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	384	6	0	4	5.4	CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	70689929	74244	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	387	6	0	5	5.2	Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL2029813	74244	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	387	6	0	5	5.2	Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	70689930	74248	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029817	74248	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	66785101	157489	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	157489	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	71136186	151525	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	CHEMBL3967432	151525	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	151031	157736	7	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	59951973	157736	7	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	CHEMBL408899	157736	7	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	168298834	192082	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219313	192082	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	11951272	66879	0	None	-	1	Human	6.0	pEC50	=	6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	12	1	6	6.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL187939	66879	0	None	-	1	Human	6.0	pEC50	=	6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	12	1	6	6.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	59234239	114048	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337502	114048	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459640	82211	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	366	4	0	4	4.7	Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179314	82211	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	366	4	0	4	4.7	Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	11545979	165232	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL424795	165232	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	44595851	3730	1	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	3730	1	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	3730	1	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	11950926	66908	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.4	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188080	66908	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.4	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	155514221	169261	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	191	2	0	3	2.0	Fc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4439927	169261	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	191	2	0	3	2.0	Fc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	118714735	114046	0	None	-	1	Human	5.0	pEC50	=	5.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	309	6	0	4	3.4	CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337500	114046	0	None	-	1	Human	5.0	pEC50	=	5.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	309	6	0	4	3.4	CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	70681520	74242	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029811	74242	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1	10.1021/jm2016864
	59599475	148614	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	7	2	8	3.7	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3943547	148614	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	7	2	8	3.7	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O	10.1016/j.bmcl.2016.11.049
	46225569	199667	0	None	12	2	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL604467	199667	0	None	12	2	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1021/jm101414h
	59599577	144340	0	None	-1	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3909995	144340	0	None	-1	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	11646457	65967	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL184917	65967	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46226934	198352	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	373	5	0	7	2.7	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL595587	198352	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	373	5	0	7	2.7	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12	10.1016/j.bmcl.2009.11.008
	69093509	83482	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	448	5	0	5	5.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	CHEMBL2206448	83482	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	448	5	0	5	5.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	117972256	141654	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl	10.1016/j.bmc.2016.11.018
	CHEMBL3884075	141654	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl	10.1016/j.bmc.2016.11.018
	117972015	141678	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	407	6	0	4	5.2	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884332	141678	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	407	6	0	4	5.2	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	68107863	191764	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5207431	191764	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	1393	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1396	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	213056	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL8759	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1393	1504	58	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1396	1504	58	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	213056	1504	58	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL8759	1504	58	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1393	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1396	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	213056	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL8759	1504	58	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	71136653	122874	0	None	51	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	122874	0	None	51	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	156013901	176654	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	176654	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	71137034	122870	0	None	7	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	122870	0	None	7	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71454787	80382	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	428	4	0	4	6.0	N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152118	80382	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	428	4	0	4	6.0	N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	70685763	74223	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	370	7	0	4	4.9	CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029794	74223	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	370	7	0	4	4.9	CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	51357934	61631	0	None	-	1	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	CHEMBL1774227	61631	0	None	-	1	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	9815617	113988	7	None	-1	2	Rat	6.0	pEC50	=	6.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	113988	7	None	-1	2	Rat	6.0	pEC50	=	6.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	57459485	82209	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	6	3.6	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12	10.1021/jm3010724
	CHEMBL2179312	82209	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	6	3.6	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12	10.1021/jm3010724
	11951989	67670	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	11	1	6	5.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL191391	67670	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	11	1	6	5.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C	10.1016/j.bmcl.2005.06.017
	70685761	74217	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029787	74217	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	49822037	82213	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	412	3	0	4	5.0	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179316	82213	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	412	3	0	4	5.0	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	57459500	82216	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	374	3	0	4	4.7	CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179320	82216	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	374	3	0	4	4.7	CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	71117470	145137	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	498	5	1	6	4.7	Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1	nan
	CHEMBL3916091	145137	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	498	5	1	6	4.7	Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1	nan
	25173448	183670	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL483754	183670	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	71681826	89616	0	None	-1	3	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	89616	0	None	-1	3	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	44155423	8596	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095750	8596	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	24809653	74219	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	314	5	0	4	3.6	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F	10.1021/jm2016864
	CHEMBL2029790	74219	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	314	5	0	4	3.6	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F	10.1021/jm2016864
	11950744	126274	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	6	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL365440	126274	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	6	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71117232	153345	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	398	7	1	7	2.3	Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	nan
	CHEMBL3983091	153345	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	398	7	1	7	2.3	Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	nan
	155523303	170258	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4453680	170258	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	46887460	8743	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097044	8743	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	90643858	111361	0	None	25	2	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	111361	0	None	25	2	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	156013901	176654	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	176654	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	68109335	156557	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	156557	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71136640	122873	0	None	60	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	122873	0	None	60	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	46215878	80381	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	388	2	0	4	5.1	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21	10.1021/jm201561r
	CHEMBL2152117	80381	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	388	2	0	4	5.1	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21	10.1021/jm201561r
	156012835	176850	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	176850	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156016100	177103	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	177103	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	46887271	8587	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	275	8	0	2	4.8	CCCCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095701	8587	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	275	8	0	2	4.8	CCCCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	156016100	177103	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	177103	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	162669954	182077	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	353	6	0	4	4.0	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4789052	182077	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	353	6	0	4	4.0	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	44155986	8448	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094462	8448	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	71117222	145540	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3919237	145540	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	57459655	82207	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	359	2	0	5	4.3	CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179310	82207	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	359	2	0	5	4.3	CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	68107697	82221	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	4	4.7	FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179325	82221	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	4	4.7	FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	156012835	176850	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	176850	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	58103861	82228	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	4.7	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm3010724
	CHEMBL2179332	82228	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	4.7	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm3010724
	90668093	109037	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221832	109037	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O	10.1039/C0MD00200C
	53322147	57404	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669380	57404	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325451	57423	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	404	6	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669398	57423	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	404	6	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46190878	1834	3	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	6253	1834	3	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	CHEMBL595759	1834	3	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	155548817	173258	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	90668101	109048	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	384	7	1	4	5.8	CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221842	109048	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	384	7	1	4	5.8	CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O	10.1039/C0MD00200C
	1310	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	1369	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	33032	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	44272391	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	88747398	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	CHEMBL575060	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	DB00142	2276	108	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	70694131	74237	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.7	Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029806	74237	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.7	Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	71137012	122871	0	None	11	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	122871	0	None	11	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	117971683	141762	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885312	141762	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	134131394	141770	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885396	141770	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155536450	171603	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	406	3	0	4	5.4	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4473537	171603	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	406	3	0	4	5.4	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	25008958	61620	0	None	-	1	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	404	4	0	5	4.4	COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1	10.1021/jm101414h
	CHEMBL1774112	61620	0	None	-	1	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	404	4	0	5	4.4	COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1	10.1021/jm101414h
	50992248	165978	0	None	1	2	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4279401	165978	0	None	1	2	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	71137010	122869	0	None	5	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	122869	0	None	5	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162651557	179595	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	319	6	0	3	4.3	c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4749289	179595	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	319	6	0	3	4.3	c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	24815439	200241	0	None	-18	2	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.ejmech.2019.111881
	CHEMBL607689	200241	0	None	-18	2	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.ejmech.2019.111881
	46887273	8589	5	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	219	4	0	2	3.2	CCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095703	8589	5	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	219	4	0	2	3.2	CCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	6604704	100917	32	None	2	3	Human	4.9	pEC50	=	4.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970207b
	CHEMBL29726	100917	32	None	2	3	Human	4.9	pEC50	=	4.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970207b
	1310	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	2276	108	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44397878	123869	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	389	6	1	5	5.6	CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL363945	123869	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	389	6	1	5	5.6	CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71116730	148518	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	CHEMBL3942904	148518	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	44155989	8447	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094461	8447	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	25073615	165900	0	None	-4	2	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	CHEMBL4278070	165900	0	None	-4	2	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	11951270	66974	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.3	CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188455	66974	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.3	CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	156817945	189880	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5179002	189880	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	162676513	182921	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	4	0	3	3.5	c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799794	182921	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	4	0	3	3.5	c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	70689928	74243	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	5.0	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029812	74243	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	5.0	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	46887493	8483	1	None	-	1	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094762	8483	1	None	-	1	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	162674797	182876	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799164	182876	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	155562956	174595	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	365	2	0	3	4.0	Brc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4570470	174595	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	365	2	0	3	4.0	Brc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	67060162	166399	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4287326	166399	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	71116701	144314	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	CHEMBL3909811	144314	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	146036860	172697	5	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	2	0	3	2.9	CC(C)Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4525401	172697	5	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	2	0	3	2.9	CC(C)Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	155552571	173574	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	319	2	0	3	3.6	FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4546739	173574	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	319	2	0	3	3.6	FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	118714748	114059	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337514	114059	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	155519836	169791	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4447702	169791	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1	10.1021/acs.jmedchem.8b00161
	46227787	198001	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	390	4	1	4	5.2	N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL593168	198001	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	390	4	1	4	5.2	N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	25173776	183710	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	267	3	0	2	3.7	C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484128	183710	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	267	3	0	2	3.7	C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	59599515	147603	0	None	-10	2	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3935529	147603	0	None	-10	2	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	24815882	61613	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774104	61613	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21	10.1021/jm101414h
	71137008	122875	0	None	7	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	122875	0	None	7	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	25195461	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	8946	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337527	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	DB12059	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	68109272	158060	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	158060	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	70689926	74235	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	1	5	4.6	CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029804	74235	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	1	5	4.6	CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	70977933	170728	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	241	2	0	3	2.9	FC(F)(F)c1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4460927	170728	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	241	2	0	3	2.9	FC(F)(F)c1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	57459517	82219	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	372	3	0	4	4.3	FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179323	82219	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	372	3	0	4	4.3	FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	25173286	172115	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL450207	172115	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	155534303	171368	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4470447	171368	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	155567633	175417	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	175417	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66785780	158186	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	158186	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	58103890	80384	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	457	4	2	4	6.1	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1	10.1021/jm201561r
	CHEMBL2152120	80384	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	457	4	2	4	6.1	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1	10.1021/jm201561r
	11531870	63967	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	420	10	1	4	5.6	CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181089	63967	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	420	10	1	4	5.6	CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	59234231	2103	1	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	6330	2103	1	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	6331	2103	1	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337510	2103	1	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	118714757	114068	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337523	114068	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	66785393	156340	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	156340	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	9815616	114289	6	None	-2	4	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	CHEMBL334014	114289	6	None	-2	4	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	11530877	64532	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182166	64532	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	9815616	114289	6	None	-2	4	Rat	6.8	pEC50	=	6.8	Functional	Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	CHEMBL334014	114289	6	None	-2	4	Rat	6.8	pEC50	=	6.8	Functional	Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	156014194	176626	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	176626	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	177330	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	177330	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	7504549	170935	1	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	3	0	3	4.1	c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4464043	170935	1	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	3	0	3	4.1	c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1	10.1021/acs.jmedchem.8b00161
	71462632	82226	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	344	4	0	4	4.5	CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179330	82226	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	344	4	0	4	4.5	CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	168299101	192138	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220917	192138	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O	10.1021/acs.jmedchem.2c00969
	44591744	188070	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL503697	188070	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	156020355	177444	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	177444	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	53321493	57422	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669397	57422	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46227786	198153	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	407	5	0	4	5.6	N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL594334	198153	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	407	5	0	4	5.6	N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	155533313	171276	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	171276	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	155548817	173258	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	90668097	109043	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	7	1	3	4.5	CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221838	109043	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	7	1	3	4.5	CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	68109333	157075	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	157075	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	53323491	57407	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	287	3	1	3	3.5	CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669383	57407	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	287	3	1	3	3.5	CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24815355	61612	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774103	61612	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	51030965	166586	0	None	1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL4290744	166586	0	None	1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	60096246	155394	0	None	-6	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	CHEMBL4061162	155394	0	None	-6	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	117972153	141758	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3885265	141758	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1	10.1016/j.bmc.2016.11.018
	49822115	2106	17	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	8947	2106	17	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	CHEMBL3947764	2106	17	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	71136746	148056	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	148056	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	71136655	122872	0	None	12	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	122872	0	None	12	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	9815617	113988	7	None	-1	2	Rat	7.8	pEC50	=	7.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	113988	7	None	-1	2	Rat	7.8	pEC50	=	7.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	46215704	80383	0	None	33	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	447	3	1	4	6.2	O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1	10.1021/jm201561r
	CHEMBL2152119	80383	0	None	33	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	447	3	1	4	6.2	O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1	10.1021/jm201561r
	156020355	177444	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	177444	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	156014194	176626	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	176626	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	177330	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	177330	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	10976811	109212	0	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	214	2	3	5	-1.0	N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1	10.1021/jm0308085
	CHEMBL322887	109212	0	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	214	2	3	5	-1.0	N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1	10.1021/jm0308085
	1310	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	1369	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	33032	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	44272391	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	88747398	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	CHEMBL575060	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	DB00142	2276	108	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	11310142	2379	16	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	2379	16	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	2379	16	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	51357397	61614	0	None	-	1	Rat	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	330	3	0	4	3.8	Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774105	61614	0	None	-	1	Rat	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	330	3	0	4	3.8	Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21	10.1021/jm101414h
	70696263	74246	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029815	74246	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	49822116	146447	7	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3926416	146447	7	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	168299087	192130	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	320	4	1	4	3.8	CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220552	192130	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	320	4	1	4	3.8	CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	46216056	80375	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	358	2	1	5	3.8	N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152110	80375	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	358	2	1	5	3.8	N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25008437	61617	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21	10.1021/jm101414h
	CHEMBL1774109	61617	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21	10.1021/jm101414h
	117972044	141739	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1	10.1016/j.bmc.2016.11.018
	CHEMBL3885097	141739	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1	10.1016/j.bmc.2016.11.018
	155566740	175302	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	2	0	3	3.9	Clc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4586335	175302	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	2	0	3	3.9	Clc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	49765871	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	60096236	157864	0	None	-3	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4090293	157864	0	None	-3	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	66784246	155811	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	155811	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785300	155919	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	155919	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	59599580	152172	0	None	8	2	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3973048	152172	0	None	8	2	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	71116952	146769	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3929070	146769	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	59497100	114069	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	342	4	0	3	4.3	O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	CHEMBL3337524	114069	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	342	4	0	3	4.3	O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	162659390	180600	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.1	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4761080	180600	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.1	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	1402	122	36	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	9825084	122	36	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	CHEMBL108939	122	36	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	10608207	118246	5	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	203	2	3	3	-0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	CHEMBL341888	118246	5	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	203	2	3	3	-0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	11537726	66345	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185490	66345	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	25004010	74233	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	399	6	1	5	4.7	CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029802	74233	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	399	6	1	5	4.7	CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	168298053	192135	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	356	3	1	3	4.8	FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	CHEMBL5220838	192135	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	356	3	1	3	4.8	FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	44155644	8747	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccccc2C#N)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097054	8747	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccccc2C#N)C(=O)O1	10.1016/j.bmcl.2010.03.089
	1310	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	2276	108	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	71117549	146299	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	437	4	0	6	1.8	CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3925103	146299	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	437	4	0	6	1.8	CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	155548817	173258	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	118714745	114056	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	5	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337511	114056	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	5	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O	10.1021/jm500496m
	57459504	82214	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	434	4	0	4	5.4	FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm3010724
	CHEMBL2179317	82214	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	434	4	0	4	5.4	FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm3010724
	134131242	141735	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	353	4	0	4	4.3	Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885072	141735	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	353	4	0	4	4.3	Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155519900	169821	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl	10.1021/acs.jmedchem.8b00161
	CHEMBL4448031	169821	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl	10.1021/acs.jmedchem.8b00161
	155565817	175038	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1cccc(Cn2nnc3c(Br)cccc32)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580527	175038	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1cccc(Cn2nnc3c(Br)cccc32)c1	10.1021/acs.jmedchem.8b00161
	60096190	157955	0	None	-9	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091203	157955	0	None	-9	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10353365	82820	1	None	13	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	82820	1	None	13	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	49822115	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	1393	1504	58	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	1396	1504	58	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	213056	1504	58	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	CHEMBL8759	1504	58	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	66787355	155672	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	155672	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66784572	156354	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	156354	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	134130477	141780	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	313	5	0	4	3.9	Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885492	141780	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	313	5	0	4	3.9	Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	162644700	178833	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	4	3.8	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4740255	178833	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	4	3.8	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155527610	170672	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4460043	170672	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)nc1	10.1021/acs.jmedchem.8b00161
	44591797	184051	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484958	184051	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	104766	34	36	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	1365	34	36	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	CHEMBL34453	34	36	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	1310	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	1369	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	33032	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	44272391	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	88747398	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	CHEMBL575060	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	DB00142	2276	108	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	1310	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	2276	108	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44591771	183648	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	351	4	0	3	4.6	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483561	183648	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	351	4	0	3	4.6	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	162649571	179531	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	311	3	0	3	3.7	Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4748614	179531	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	311	3	0	3	3.7	Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	51356833	61629	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	400	3	0	4	4.9	Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774225	61629	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	400	3	0	4	4.9	Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21	10.1021/jm101414h
	46227797	199940	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL605921	199940	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25004352	74225	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	400	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029796	74225	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	400	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	46227797	199940	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL605921	199940	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	11655609	165337	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL424998	165337	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71476419	122880	0	None	51	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	122880	0	None	51	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096204	155571	0	None	-2	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4063336	155571	0	None	-2	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11220424	158403	0	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095995	158403	0	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71456562	80377	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	394	4	0	4	5.3	N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152113	80377	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	394	4	0	4	5.3	N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	155519573	172687	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4525207	172687	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	44155748	8404	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2cccc(O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094124	8404	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2cccc(O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	118263352	114071	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	4	0	3	4.5	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O	10.1021/jm500496m
	CHEMBL3337526	114071	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	4	0	3	4.5	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O	10.1021/jm500496m
	25009651	61618	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21	10.1021/jm101414h
	CHEMBL1774110	61618	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21	10.1021/jm101414h
	11559813	64662	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	374	10	1	4	5.3	Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182316	64662	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	374	10	1	4	5.3	Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	90668095	109040	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	6	1	3	4.4	CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221835	109040	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	6	1	3	4.4	CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668102	109049	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	376	6	1	4	4.9	CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221843	109049	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	376	6	1	4	4.9	CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O	10.1039/C0MD00200C
	46917716	109050	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	1	3	4.7	CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221844	109050	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	1	3	4.7	CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O	10.1039/C0MD00200C
	53326710	57421	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	389	5	0	3	6.5	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669396	57421	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	389	5	0	3	6.5	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46190877	1833	3	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	6252	1833	3	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	CHEMBL605836	1833	3	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	24815976	198067	0	None	-5	2	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593745	198067	0	None	-5	2	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225336	198355	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595609	198355	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	90668098	109044	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	292	5	1	3	4.0	CCCn1ccc2c(NCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221839	109044	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	292	5	1	3	4.0	CCCn1ccc2c(NCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	10197984	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1394	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL275079	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	10197984	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	10197984	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	1394	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL275079	2378	37	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	66786902	158902	0	None	-	1	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	158902	0	None	-	1	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71457756	83474	0	None	66	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206440	83474	0	None	66	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	134130276	141760	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885277	141760	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155536501	171618	1	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	265	2	0	3	3.0	Brc1cccc2c1nnn2CC1CCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4473685	171618	1	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	265	2	0	3	3.0	Brc1cccc2c1nnn2CC1CCC1	10.1021/acs.jmedchem.8b00161
	68108457	148012	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3938796	148012	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5074658	212542	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1	10.1021/acs.jmedchem.1c00563
	71137011	122878	0	None	58	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	122878	0	None	58	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	53240406	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	50992248	165978	0	None	-1	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4279401	165978	0	None	-1	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	1392	73	42	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	5310984	73	42	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL40086	73	42	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	104766	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	1365	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	CHEMBL34453	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	11596869	143093	0	None	-8	2	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	417	7	2	8	3.9	CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3899832	143093	0	None	-8	2	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	417	7	2	8	3.9	CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	25173287	169795	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	6	0	3	4.4	CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL444778	169795	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	6	0	3	4.4	CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	24809687	74234	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	351	5	0	5	3.3	CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029803	74234	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	351	5	0	5	3.3	CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	156817927	191000	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	433	5	0	5	4.2	Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5195400	191000	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	433	5	0	5	4.2	Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	44363330	36228	0	None	-	1	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL144747	36228	0	None	-	1	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	53240406	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11275666	89612	1	None	1	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381647	89612	1	None	1	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	156018305	177250	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	177250	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	155539343	172250	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4514174	172250	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	104766	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	1365	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL34453	34	36	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	24815434	198004	0	None	5	2	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL593196	198004	0	None	5	2	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1021/jm101414h
	156018305	177250	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	177250	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	42610167	80374	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	420	3	0	5	4.5	N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152109	80374	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	420	3	0	5	4.5	N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	71117258	146004	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	467	6	1	8	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21	nan
	CHEMBL3922773	146004	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	467	6	1	8	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21	nan
	46887416	8443	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094416	8443	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	51357936	61633	0	None	3	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	CHEMBL1774231	61633	0	None	3	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	24815439	200241	0	None	18	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL607689	200241	0	None	18	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1021/jm101414h
	53240406	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	25173773	184331	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL485336	184331	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	71117730	143387	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	CHEMBL3902193	143387	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	66784890	155497	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	155497	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	68109425	157733	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	157733	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	155560108	174327	1	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	225	1	0	3	2.2	CCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4564533	174327	1	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	225	1	0	3	2.2	CCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	11950745	123114	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	497	9	1	6	5.9	CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL361934	123114	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	497	9	1	6	5.9	CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	59599555	153002	0	None	1	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3980125	153002	0	None	1	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	11951806	66456	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	487	12	1	6	6.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1	10.1016/j.bmcl.2005.06.017
	CHEMBL186018	66456	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	487	12	1	6	6.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1	10.1016/j.bmcl.2005.06.017
	162654261	180062	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	6	0	4	3.9	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4755053	180062	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	6	0	4	3.9	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	9979770	65991	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185054	65991	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46227789	198025	1	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	361	3	0	7	2.5	CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL593399	198025	1	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	361	3	0	7	2.5	CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	155531064	171062	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4465783	171062	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	9834591	137062	65	None	2	3	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL375611	137062	65	None	2	3	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	46215709	80376	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	354	2	0	4	4.5	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21	10.1021/jm201561r
	CHEMBL2152112	80376	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	354	2	0	4	4.5	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21	10.1021/jm201561r
	156013901	176654	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	176654	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	70685768	74249	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	5	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	CHEMBL2029818	74249	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	5	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	134130478	141781	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	364	5	0	5	4.5	Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885493	141781	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	364	5	0	5	4.5	Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	44300122	13003	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	CHEMBL1190517	13003	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	CHEMBL541050	13003	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	156013901	176654	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	176654	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	42610166	199974	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	5.0	N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL606153	199974	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	5.0	N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	1310	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	68107863	191764	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5207431	191764	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	25173617	188061	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	4	0	3	3.7	CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL503572	188061	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	4	0	3	3.7	CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	57459501	82217	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	402	5	0	4	5.5	CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179321	82217	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	402	5	0	4	5.5	CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	46887372	8701	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096713	8701	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	162669368	182176	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	330	5	0	4	3.7	N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4790241	182176	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	330	5	0	4	3.7	N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44300605	13229	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1192345	13229	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL543568	13229	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	71136654	122879	0	None	3	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	122879	0	None	3	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162659966	180659	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	3	0	3	3.4	Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4761771	180659	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	3	0	3	3.4	Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	156014680	176666	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	176666	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	51357400	61627	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	408	4	0	5	4.4	Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774222	61627	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	408	4	0	5	4.4	Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	51357399	61626	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	392	3	0	4	4.5	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774221	61626	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	392	3	0	4	4.5	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	68108857	156784	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	156784	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	71458417	80386	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	437	4	0	3	6.8	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12	10.1021/jm201561r
	CHEMBL2152122	80386	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	437	4	0	3	6.8	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12	10.1021/jm201561r
	44155645	8593	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095745	8593	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	51030965	166586	0	None	-1	2	Rat	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL4290744	166586	0	None	-1	2	Rat	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL5083384	213075	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1	10.1021/acs.jmedchem.1c00563
	CHEMBL5090853	213498	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1F	10.1021/acs.jmedchem.1c00563
	156014680	176666	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	176666	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	59497075	114070	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	376	4	0	3	4.7	O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	CHEMBL3337525	114070	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	376	4	0	3	4.7	O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	46917791	57425	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	472	6	0	4	6.7	CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669400	57425	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	472	6	0	4	6.7	CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668094	109038	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221833	109038	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	69344751	109039	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221834	109039	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	58966955	109042	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	337	7	0	4	4.0	CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221837	109042	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	337	7	0	4	4.0	CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668103	109051	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	340	6	0	3	4.6	CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221845	109051	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	340	6	0	3	4.6	CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	49801371	158183	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	158183	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	53326074	57408	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	5	0	4	4.0	CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669384	57408	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	5	0	4	4.0	CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225334	198353	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595607	198353	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225583	198480	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596527	198480	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24815883	199767	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604993	199767	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	53325603	57402	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669377	57402	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	21393580	8590	0	None	-	1	Human	4.6	pEC50	=	4.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	253	3	0	2	3.3	O=C1OC(Cc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095704	8590	0	None	-	1	Human	4.6	pEC50	=	4.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	253	3	0	2	3.3	O=C1OC(Cc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	60096211	89614	0	None	-1	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381649	89614	0	None	-1	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	1310	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	2276	108	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	69093106	83478	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F	10.1021/jm300912k
	CHEMBL2206444	83478	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F	10.1021/jm300912k
	44591748	184448	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485528	184448	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	60096183	158725	0	None	-3	2	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL4099470	158725	0	None	-3	2	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	24809650	74221	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	326	6	0	5	3.5	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC	10.1021/jm2016864
	CHEMBL2029792	74221	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	326	6	0	5	3.5	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC	10.1021/jm2016864
	162665716	181777	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	5	0	4	4.0	c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4784990	181777	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	5	0	4	4.0	c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	1310	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	1369	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	33032	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	44272391	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	88747398	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	CHEMBL575060	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	DB00142	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	1310	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	1369	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	33032	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	44272391	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	88747398	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	CHEMBL575060	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	DB00142	2276	108	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	25173365	184212	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	5	0	3	3.6	CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL485175	184212	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	5	0	3	3.6	CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	70685767	74245	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.6	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL2029814	74245	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.6	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL5073573	212519	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc([N+](=O)[O-])c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	9815616	114289	6	None	-2	4	Rat	5.6	pEC50	=	5.6	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	114289	6	None	-2	4	Rat	5.6	pEC50	=	5.6	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	71136188	145210	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	CHEMBL3916627	145210	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	155515810	169436	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4442487	169436	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	3954	657	53	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	9868580	657	53	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	CHEMBL593013	657	53	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	49765871	2105	40	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	2105	40	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	2105	40	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	162677102	182934	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	401	5	0	4	4.8	Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799882	182934	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	401	5	0	4	4.8	Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	155511507	169016	1	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	239	2	0	3	2.6	CCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4436220	169016	1	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	239	2	0	3	2.6	CCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	44156621	8633	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	7	0	4	3.4	CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096080	8633	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	7	0	4	3.4	CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	134131309	141630	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	359	2	0	3	6.1	Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1	10.1016/j.bmc.2016.11.018
	CHEMBL3883923	141630	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	359	2	0	3	6.1	Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1	10.1016/j.bmc.2016.11.018
	67060140	166832	0	None	-26	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4295230	166832	0	None	-26	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	162661604	180911	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	307	4	0	4	3.1	COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4764905	180911	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	307	4	0	4	3.1	COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44591746	184322	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1	10.1016/j.bmcl.2009.03.032
	CHEMBL485330	184322	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1	10.1016/j.bmcl.2009.03.032
	70685766	74241	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029810	74241	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	60096231	157101	11	None	-48	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	157101	11	None	-48	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	44591715	190869	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL519341	190869	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	117967312	141766	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885353	141766	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117967312	141766	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885353	141766	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155551721	174846	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4576215	174846	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	51357935	61632	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	372	3	0	4	4.4	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F	10.1021/jm101414h
	CHEMBL1774229	61632	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	372	3	0	4	4.4	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F	10.1021/jm101414h
	168299593	192120	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	385	7	0	5	4.7	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220316	192120	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	385	7	0	5	4.7	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	71116726	144731	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	CHEMBL3912982	144731	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	137652500	156635	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	156635	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	71128768	144035	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3907644	144035	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	44591714	183709	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484127	183709	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL5069547	212438	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(F)cc1	10.1021/acs.jmedchem.1c00563
	118714743	114055	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	4	0	4	3.8	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337509	114055	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	4	0	4	3.8	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	25010196	61619	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21	10.1021/jm101414h
	CHEMBL1774111	61619	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21	10.1021/jm101414h
	134131502	141608	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	363	5	0	4	5.1	Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883585	141608	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	363	5	0	4	5.1	Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155525998	170458	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	371	3	0	3	5.3	Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4456816	170458	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	371	3	0	3	5.3	Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	9815616	114289	6	None	-2	4	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	114289	6	None	-2	4	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	66785010	155310	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	155310	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	66787433	155910	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	155910	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	49801369	158191	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	158191	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	25073303	166469	0	None	11	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4288731	166469	0	None	11	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	156018381	177338	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	177338	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	70689923	74222	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	336	7	0	4	4.2	CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029793	74222	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	336	7	0	4	4.2	CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	155524603	170349	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	322	2	0	4	3.3	Clc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4455228	170349	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	322	2	0	4	3.3	Clc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL5091768	213541	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccc(Cl)cc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	11690196	142222	0	None	4	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	416	7	2	7	4.5	CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3892611	142222	0	None	4	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	416	7	2	7	4.5	CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	156018381	177338	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	177338	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	118714734	114045	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	296	6	0	4	3.3	CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337499	114045	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	296	6	0	4	3.3	CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	57459483	82227	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.9	CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179331	82227	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.9	CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	51357937	61635	0	None	2	2	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774233	61635	0	None	2	2	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	60096201	158010	0	None	-5	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091735	158010	0	None	-5	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10198133	204772	10	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL8839	204772	10	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	10198133	204772	10	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	204772	10	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	42629118	183667	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	319	3	0	2	4.5	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483750	183667	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	319	3	0	2	4.5	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	70696264	74250	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	407	6	0	5	5.6	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029819	74250	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	407	6	0	5	5.6	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	162662455	181430	2	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4780781	181430	2	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	146036862	175055	5	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	279	2	0	3	3.4	Brc1cccc2c1nnn2CC1CCCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580916	175055	5	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	279	2	0	3	3.4	Brc1cccc2c1nnn2CC1CCCC1	10.1021/acs.jmedchem.8b00161
	162662455	181430	2	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL4780781	181430	2	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL5085978	213223	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1	10.1021/acs.jmedchem.1c00563
	66785087	157583	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	157583	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	11362035	43	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	6328	43	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	6329	43	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	CHEMBL105296	43	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	156010124	176447	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	176447	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	1377	1308	19	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	5310979	1308	19	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	CHEMBL284193	1308	19	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	1368	2248	31	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	5310956	2248	31	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	CHEMBL280563	2248	31	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	44361316	34733	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL143267	34733	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O	10.1021/jm030967o
	1392	73	42	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	5310984	73	42	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL40086	73	42	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	521212	66982	50	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	209	2	0	3	2.5	c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL1884989	66982	50	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	209	2	0	3	2.5	c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	156010124	176447	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	176447	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	44591812	191944	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL521175	191944	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	59599459	148885	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3945882	148885	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	118714740	114052	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	5	0	6	2.5	CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337506	114052	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	5	0	6	2.5	CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459482	83472	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	433	4	0	6	4.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1	10.1021/jm300912k
	CHEMBL2206438	83472	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	433	4	0	6	4.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1	10.1021/jm300912k
	118714756	114067	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337522	114067	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	44178197	61637	0	None	1	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774235	61637	0	None	1	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL5078863	212809	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	25073615	165900	0	None	4	2	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	CHEMBL4278070	165900	0	None	4	2	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	25002940	1083	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	6320	1083	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	CHEMBL2029821	1083	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	53326709	57419	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	405	6	0	5	5.1	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669394	57419	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	405	6	0	5	5.1	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53324151	57420	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	4	0	3	4.7	CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669395	57420	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	4	0	3	4.7	CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668099	109046	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221840	109046	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	156017237	177177	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	177177	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	53317704	57409	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	5	1	4	4.1	CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669385	57409	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	5	1	4	4.1	CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225582	199920	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL605831	199920	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	118714738	114050	0	None	-	1	Human	4.5	pEC50	=	4.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	273	4	0	4	2.8	CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337504	114050	0	None	-	1	Human	4.5	pEC50	=	4.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	273	4	0	4	2.8	CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O	10.1021/jm500496m
	70683629	74218	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1	10.1021/jm2016864
	CHEMBL2029788	74218	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1	10.1021/jm2016864
	11951099	67124	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	479	8	1	5	7.1	CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189264	67124	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	479	8	1	5	7.1	CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	59599568	145505	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3918914	145505	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44591772	190861	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	4	0	3	4.7	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL519332	190861	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	4	0	3	4.7	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	117972047	141627	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	327	6	0	4	4.0	Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883827	141627	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	327	6	0	4	4.0	Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	46215876	80380	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	374	2	1	3	5.1	N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152116	80380	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	374	2	1	3	5.1	N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	162670769	182376	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	4	4.2	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4793069	182376	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	4	4.2	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	156016100	177103	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	177103	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156017237	177177	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	177177	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71136746	148056	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	148056	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	156015654	176937	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	176937	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156016100	177103	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	177103	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	11631795	64453	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181953	64453	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	155531978	171156	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	363	3	0	5	4.2	N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4467158	171156	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	363	3	0	5	4.2	N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	51357934	61631	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	CHEMBL1774227	61631	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	66784529	156539	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	156539	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	71451227	80379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	438	3	1	5	5.4	N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152115	80379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	438	3	1	5	5.4	N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25073303	166469	0	None	-11	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4288731	166469	0	None	-11	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	156015654	176937	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	176937	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	44155754	8412	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2cccc(N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094146	8412	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2cccc(N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44300258	13525	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1194540	13525	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL552836	13525	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	51357396	61611	0	None	-	1	Rat	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774102	61611	0	None	-	1	Rat	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21	10.1021/jm101414h
	118714737	114049	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337503	114049	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O	10.1021/jm500496m
	71117091	148805	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	412	4	1	6	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21	nan
	CHEMBL3945222	148805	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	412	4	1	6	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21	nan
	127030385	138620	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	217	5	4	4	-1.0	N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL3787264	138620	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	217	5	4	4	-1.0	N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	137635882	155341	0	None	1	2	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	155341	0	None	1	2	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	9815617	113988	7	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	113988	7	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	1393	1504	58	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	1504	58	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	1504	58	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	1504	58	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	11187949	65257	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183319	65257	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	162649047	179201	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	3	4.2	Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4744761	179201	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	3	4.2	Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	44591796	184050	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484957	184050	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	24905705	183430	1	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	183430	1	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	46887319	8890	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098388	8890	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	25003298	74240	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029809	74240	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	10047169	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	1403	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	CHEMBL182371	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	10047169	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	1403	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	CHEMBL182371	3161	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	44591713	183708	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484126	183708	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	118714753	114064	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1	10.1021/jm500496m
	CHEMBL3337519	114064	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1	10.1021/jm500496m
	44178197	61637	0	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774235	61637	0	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	51354020	61638	0	None	23	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/acs.jmedchem.1c00563
	CHEMBL1774236	61638	0	None	23	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/acs.jmedchem.1c00563
	1393	1504	58	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	1396	1504	58	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	213056	1504	58	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL8759	1504	58	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	71457756	83474	0	None	66	2	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	83474	0	None	66	2	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	46887371	8700	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096712	8700	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	162661233	180920	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4765006	180920	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL5076606	212671	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	136950	8591	24	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	269	4	0	3	3.1	O=C1OC(COc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095705	8591	24	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	269	4	0	3	3.1	O=C1OC(COc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	59066632	204834	84	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	92136	204834	84	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	CHEMBL88804	204834	84	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	44300135	13158	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL1191723	13158	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL542862	13158	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	11951271	67156	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	10	1	6	5.7	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189516	67156	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	10	1	6	5.7	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	118714746	114057	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	389	5	0	4	4.4	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O	10.1021/jm500496m
	CHEMBL3337512	114057	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	389	5	0	4	4.4	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O	10.1021/jm500496m
	71117198	149753	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	358	3	1	4	1.7	CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3952803	149753	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	358	3	1	4	1.7	CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	11950746	66743	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	419	9	1	6	5.1	CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL187342	66743	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	419	9	1	6	5.1	CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	627502	8481	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094733	8481	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	46887370	8699	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096711	8699	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	46887322	8893	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098391	8893	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	59391336	114044	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	294	6	0	3	3.6	CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337498	114044	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	294	6	0	3	3.6	CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	10176836	35630	0	None	-	1	Rat	4.4	pEC50	=	4.4	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	221	2	3	3	-0.2	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F	10.1021/jm000346k
	CHEMBL144201	35630	0	None	-	1	Rat	4.4	pEC50	=	4.4	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	221	2	3	3	-0.2	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F	10.1021/jm000346k
	70685762	74220	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	330	5	0	4	4.1	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	CHEMBL2029791	74220	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	330	5	0	4	4.1	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	69093439	83477	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206443	83477	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	71457756	83474	0	None	66	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	83474	0	None	66	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	155560423	174493	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	387	3	0	3	5.8	FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4568356	174493	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	387	3	0	3	5.8	FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	44300820	13252	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1192558	13252	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL543811	13252	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	68108457	148012	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3938796	148012	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	25002941	74253	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	6	0	5	5.1	CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029823	74253	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	6	0	5	5.1	CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O	10.1021/jm2016864
	66786069	155908	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	155908	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	44591794	184048	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	370	4	0	4	4.1	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484956	184048	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	370	4	0	4	4.1	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	44155534	8581	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095638	8581	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44591647	184214	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	4.1	O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485176	184214	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	4.1	O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	11531272	64856	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	392	10	1	4	5.4	Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182511	64856	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	392	10	1	4	5.4	Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	11710164	65989	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185046	65989	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	57459481	82212	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	340	3	0	4	4.3	CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179315	82212	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	340	3	0	4	4.3	CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	23770349	8807	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccccc2Cl)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097656	8807	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccccc2Cl)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	57459635	82218	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	418	4	0	4	5.2	FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179322	82218	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	418	4	0	4	5.2	FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	59599552	147759	0	None	12	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3936830	147759	0	None	12	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	71135411	122868	0	None	5	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	122868	0	None	5	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	25002939	74252	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029822	74252	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL5083201	213069	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Cl)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	71136199	142143	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	3	0	7	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3892060	142143	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	3	0	7	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	11310142	2379	16	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	2379	16	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	2379	16	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	25002587	74238	2	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029807	74238	2	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O	10.1021/jm2016864
	53320818	57416	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	346	4	0	4	4.3	CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669391	57416	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	346	4	0	4	4.3	CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325452	57424	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	438	6	0	4	6.4	CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669399	57424	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	438	6	0	4	6.4	CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668096	109041	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	350	7	0	4	4.1	CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221836	109041	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	350	7	0	4	4.1	CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	53324803	57406	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	299	3	0	4	3.5	CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669382	57406	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	299	3	0	4	3.5	CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24815439	200241	0	None	-18	2	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607689	200241	0	None	-18	2	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225581	200293	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL608103	200293	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44361401	31111	0	None	1	5	Rat	8.4	pEC50	=	8.4	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	31111	0	None	1	5	Rat	8.4	pEC50	=	8.4	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	117972155	141711	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884833	141711	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71457757	83483	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	466	5	0	5	5.4	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	CHEMBL2206449	83483	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	466	5	0	5	5.4	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	71137012	122871	0	None	11	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	122871	0	None	11	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162654912	180060	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	387	6	0	4	4.1	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4755035	180060	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	387	6	0	4	4.1	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	162674461	182739	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	403	6	0	4	4.4	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4797417	182739	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	403	6	0	4	4.4	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL5083122	213060	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1Cc1ccc(Cl)cc1	10.1021/acs.jmedchem.1c00563
	66785551	156599	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	156599	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66784675	156620	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	156620	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	162642952	181145	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	3	5.2	Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4777206	181145	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	3	5.2	Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155554782	174016	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	203	3	0	4	1.9	COc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4557213	174016	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	203	3	0	4	1.9	COc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	57459524	82220	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	358	3	0	4	4.2	FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179324	82220	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	358	3	0	4	4.2	FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	10474978	13333	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1193146	13333	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	CHEMBL544508	13333	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	59599576	141995	0	None	-5	2	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3890848	141995	0	None	-5	2	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44591745	191736	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL520677	191736	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	68109677	156639	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	156639	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786493	156706	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	156706	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	46887415	8442	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094415	8442	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	70685764	74226	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	0	4	5.2	CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029797	74226	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	0	4	5.2	CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	137659992	158677	0	None	-8	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4098939	158677	0	None	-8	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	162645511	179008	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	305	5	0	3	3.9	c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4742196	179008	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	305	5	0	3	3.9	c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44392708	65734	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	423	11	1	7	4.7	Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183807	65734	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	423	11	1	7	4.7	Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	25008615	61616	0	None	1	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774108	61616	0	None	1	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	71116772	147124	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	CHEMBL3931730	147124	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	44591793	183760	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	269	3	0	4	2.5	C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484403	183760	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	269	3	0	4	2.5	C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	71137008	122875	0	None	7	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	122875	0	None	7	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	156019582	177427	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	177427	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	3954	657	53	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	9868580	657	53	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	CHEMBL593013	657	53	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	44155643	8746	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097053	8746	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	156019582	177427	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	177427	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	46227795	198270	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	357	2	0	3	5.3	CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1	10.1016/j.bmcl.2009.11.008
	CHEMBL595043	198270	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	357	2	0	3	5.3	CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1	10.1016/j.bmcl.2009.11.008
	46227792	198399	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	415	3	0	7	3.0	Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1	10.1016/j.bmcl.2009.11.008
	CHEMBL595967	198399	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	415	3	0	7	3.0	Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1	10.1016/j.bmcl.2009.11.008
	70689927	74236	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029805	74236	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	10822010	36141	1	None	-	1	Rat	5.4	pEC50	=	5.4	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	CHEMBL144678	36141	1	None	-	1	Rat	5.4	pEC50	=	5.4	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	1377	1308	19	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	5310979	1308	19	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL284193	1308	19	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	11344646	126242	1	None	2	3	Human	7.4	pEC50	=	7.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	CHEMBL365368	126242	1	None	2	3	Human	7.4	pEC50	=	7.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	46887493	8483	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094762	8483	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	11951449	66374	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL185659	66374	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	51356571	61628	0	None	-	1	Rat	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.8	C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C	10.1021/jm101414h
	CHEMBL1774224	61628	0	None	-	1	Rat	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.8	C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C	10.1021/jm101414h
	11494153	65735	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	356	10	1	4	5.2	Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183808	65735	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	356	10	1	4	5.2	Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	118714752	114063	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	401	4	0	4	4.5	N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337518	114063	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	401	4	0	4	4.5	N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	71136640	122873	0	None	60	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	122873	0	None	60	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	53240406	122867	13	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	70689925	74232	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	295	5	1	4	3.5	CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029801	74232	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	295	5	1	4	3.5	CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	118714741	114053	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	364	6	0	5	3.1	CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337507	114053	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	364	6	0	5	3.1	CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459480	82208	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	347	4	0	6	3.1	COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179311	82208	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	347	4	0	6	3.1	COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	60096231	157101	11	None	-48	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	157101	11	None	-48	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	59599565	144770	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3913281	144770	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44300587	12908	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189911	12908	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539761	12908	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	162647052	179039	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4742843	179039	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1	10.1016/j.ejmech.2019.111881
	156014680	176666	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	176666	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	70692086	74228	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029799	74228	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	44591774	191485	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL520300	191485	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	54583299	61609	0	None	-	1	Rat	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	390	4	0	6	3.7	Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1	10.1021/jm101414h
	CHEMBL1774100	61609	0	None	-	1	Rat	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	390	4	0	6	3.7	Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1	10.1021/jm101414h
	118714751	114062	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337517	114062	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	25008615	61616	0	None	-1	2	Rat	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774108	61616	0	None	-1	2	Rat	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	53240406	122867	13	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71119170	148228	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3940610	148228	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	1392	73	42	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	5310984	73	42	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL40086	73	42	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	156014680	176666	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	176666	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	10330132	100899	1	None	10	2	Rat	5.3	pEC50	=	5.3	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL297150	100899	1	None	10	2	Rat	5.3	pEC50	=	5.3	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(99)00266-8
	1374	2042	31	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	5311455	2042	31	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	CHEMBL39372	2042	31	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	168299034	192070	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219080	192070	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	118714750	114061	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337516	114061	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	168295099	192438	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219090	192438	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5223017	192438	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	46830123	1052	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	6321	1052	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	CHEMBL1094763	1052	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	46197780	5492	0	None	-25	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	273	7	4	4	-0.2	N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1076865	5492	0	None	-25	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	273	7	4	4	-0.2	N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O	10.1021/jm901523t
	44591684	183744	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL484340	183744	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	44361401	31111	0	None	1	5	Rat	8.3	pEC50	=	8.3	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	31111	0	None	1	5	Rat	8.3	pEC50	=	8.3	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	1393	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	1396	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	213056	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	CHEMBL8759	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	1393	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	1396	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	213056	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	CHEMBL8759	1504	58	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	71476419	122880	0	None	51	2	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	122880	0	None	51	2	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71457756	83474	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	83474	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	71457756	83474	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	83474	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	117968589	141724	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	423	6	0	4	5.7	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884936	141724	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	423	6	0	4	5.7	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1	10.1016/j.bmc.2016.11.018
	53240406	122867	13	None	107	4	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	107	4	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	68109580	157967	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	157967	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	162650622	179460	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	431	6	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br	10.1016/j.ejmech.2019.111881
	CHEMBL4747716	179460	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	431	6	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br	10.1016/j.ejmech.2019.111881
	162662472	181461	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	371	6	0	4	3.6	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4781224	181461	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	371	6	0	4	3.6	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F	10.1016/j.ejmech.2019.111881
	155513095	169126	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	329	2	0	3	3.4	Brc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4437986	169126	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	329	2	0	3	3.4	Brc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	155540333	171919	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4483344	171919	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL5074997	212570	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1CC1CCC1	10.1021/acs.jmedchem.1c00563
	CHEMBL5091657	213535	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1F	10.1021/acs.jmedchem.1c00563
	10807972	35574	1	None	-3	4	Rat	7.3	pEC50	=	7.3	Functional	Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	CHEMBL144151	35574	1	None	-3	4	Rat	7.3	pEC50	=	7.3	Functional	Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	104766	34	36	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	1365	34	36	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL34453	34	36	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	46215708	80378	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	424	3	0	5	5.3	N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152114	80378	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	424	3	0	5	5.3	N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	71450118	82224	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	330	3	0	4	4.2	CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179328	82224	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	330	3	0	4	4.2	CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	53320175	57417	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669392	57417	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668092	109036	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221831	109036	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	90668100	109047	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221841	109047	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668105	109053	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	356	6	0	4	4.6	CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221847	109053	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	356	6	0	4	4.6	CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	53325603	57402	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669377	57402	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53316861	57403	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	320	3	1	4	3.0	CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669378	57403	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	320	3	1	4	3.0	CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53323493	57412	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	341	4	0	4	4.2	CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669388	57412	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	341	4	0	4	4.2	CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24849462	198066	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593744	198066	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	90668104	109052	0	None	-	1	Human	4.3	pEC50	=	4.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	0	3	4.6	CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221846	109052	0	None	-	1	Human	4.3	pEC50	=	4.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	0	3	4.6	CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	60096194	156035	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068679	156035	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	156014194	176626	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	176626	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	177330	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	177330	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71117065	148731	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	539	3	1	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21	nan
	CHEMBL3944557	148731	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	539	3	1	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21	nan
	156014194	176626	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	176626	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	177330	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	177330	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	57459542	82223	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	401	4	0	5	4.5	FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179327	82223	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	401	4	0	5	4.5	FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	28407322	182245	7	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	277	3	0	3	3.1	c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4791292	182245	7	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	277	3	0	3	3.1	c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	3756397	8215	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	4041087	8215	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1092727	8215	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	44591747	184323	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485331	184323	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	71137034	122870	0	None	7	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	122870	0	None	7	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	156012835	176850	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	176850	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156012835	176850	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	176850	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71137010	122869	0	None	5	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	122869	0	None	5	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162646719	179019	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	3	4.7	Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4742364	179019	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	3	4.7	Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	162662970	181340	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	343	5	0	4	3.6	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4779768	181340	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	343	5	0	4	3.6	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL5090065	213456	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)nc1	10.1021/acs.jmedchem.1c00563
	156015654	176937	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	176937	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	118714744	114041	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	4	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O	10.1021/jm500496m
	CHEMBL3337456	114041	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	4	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O	10.1021/jm500496m
	66788653	82210	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	394	3	0	4	4.9	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179313	82210	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	394	3	0	4	4.9	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	156015654	176937	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	176937	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	70681519	74231	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029800	74231	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	162669063	182144	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	4	4.7	Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4789937	182144	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	4	4.7	Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44392629	64422	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	456	10	1	4	5.9	CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181921	64422	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	456	10	1	4	5.9	CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	11271167	66452	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	11	1	6	6.1	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL185994	66452	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	11	1	6	6.1	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	11950927	122900	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	11	1	6	6.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL361724	122900	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	11	1	6	6.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	57459477	82229	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm3010724
	CHEMBL2179333	82229	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm3010724
	71117141	146904	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	CHEMBL3930164	146904	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	57459477	82229	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm300912k
	CHEMBL2179333	82229	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm300912k
	49801368	159099	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	159099	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	59599616	145719	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3920609	145719	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	25125217	549	17	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	549	17	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	549	17	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	549	17	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	44428730	144161	1	None	-	1	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL390863	144161	1	None	-	1	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	137652320	156720	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	156720	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	24779944	7771	0	None	-36	3	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	225	6	4	4	-0.9	N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1089852	7771	0	None	-36	3	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	225	6	4	4	-0.9	N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O	10.1021/jm901523t
	44428730	144161	1	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL390863	144161	1	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	11546303	64888	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	10	1	5	5.0	CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182668	64888	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	10	1	5	5.0	CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	44392671	64923	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	7	1	5	6.4	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182822	64923	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	7	1	5	6.4	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46887369	8772	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097380	8772	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL5081320	212960	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccc(F)cc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	44155863	8446	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094460	8446	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	25173209	188426	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	5	0	3	3.6	O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL509096	188426	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	5	0	3	3.6	O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	44155315	8552	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095385	8552	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155642	8745	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097052	8745	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	46887367	8770	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097378	8770	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	71117030	145308	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	5	1	7	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21	nan
	CHEMBL3917329	145308	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	5	1	7	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21	nan
	44591795	191832	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	320	3	0	3	3.9	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL520837	191832	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	320	3	0	3	3.9	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	11952168	66991	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	14	1	6	6.2	CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL188538	66991	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	14	1	6	6.2	CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	57459494	83476	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206442	83476	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	155566352	175351	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	416	3	0	4	5.1	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4587631	175351	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	416	3	0	4	5.1	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	11626955	151267	0	None	18	2	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3965244	151267	0	None	18	2	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	117971699	141741	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	397	6	0	4	4.9	FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885115	141741	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	397	6	0	4	4.9	FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71131322	122877	0	None	43	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	122877	0	None	43	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096228	156234	0	None	-2	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4070866	156234	0	None	-2	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71137011	122878	0	None	58	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	122878	0	None	58	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	134130002	141623	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883801	141623	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	69093928	83481	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206447	83481	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	60096250	158363	0	None	-1	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095567	158363	0	None	-1	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	117972041	141665	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884170	141665	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1	10.1016/j.bmc.2016.11.018
	155559961	174313	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	2	0	3	3.3	Clc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4564190	174313	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	2	0	3	3.3	Clc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	155567522	175388	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	3	0	3	3.0	CCCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4588508	175388	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	3	0	3	3.0	CCCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL5086642	213258	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CCC1	10.1021/acs.jmedchem.1c00563
	CHEMBL5088821	213395	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1F	10.1021/acs.jmedchem.1c00563
	CHEMBL5093895	213667	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC2CCC1C2	10.1021/acs.jmedchem.1c00563
	155522079	170124	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	304	3	0	4	3.7	Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4451873	170124	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	304	3	0	4	3.7	Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	57459487	83471	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	402	4	0	4	5.0	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1	10.1021/jm300912k
	CHEMBL2206437	83471	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	402	4	0	4	5.0	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1	10.1021/jm300912k
	1310	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	1369	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	33032	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	44272391	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	88747398	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	CHEMBL575060	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	DB00142	2276	108	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	10376615	80142	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL214917	80142	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL544505	80142	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL5074682	212545	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4cccc(F)c4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	10473248	14056	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1198741	14056	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL540015	14056	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	42610165	80372	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	435	4	0	5	5.2	N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152107	80372	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	435	4	0	5	5.2	N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL5079928	212872	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3ccccc3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	155559438	174277	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	198	2	0	4	1.7	N#Cc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4563304	174277	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	198	2	0	4	1.7	N#Cc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	66785027	157781	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	157781	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL5076356	212650	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccccc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	53316862	57405	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669381	57405	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53323492	57411	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	356	7	0	4	4.5	CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669387	57411	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	356	7	0	4	4.5	CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325450	57418	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	418	7	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669393	57418	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	418	7	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225584	197983	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593056	197983	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46226929	200917	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	366	5	0	7	2.3	CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O	10.1016/j.bmcl.2009.11.008
	CHEMBL612133	200917	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	366	5	0	7	2.3	CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O	10.1016/j.bmcl.2009.11.008
	68109379	156671	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	156671	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	24815434	198004	0	None	-5	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593196	198004	0	None	-5	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225337	198284	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595151	198284	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225335	198354	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595608	198354	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24849789	198440	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596270	198440	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225569	199667	0	None	-12	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604467	199667	0	None	-12	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44591813	184066	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484972	184066	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	11950742	66756	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL187398	66756	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	70685769	74251	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	405	5	0	5	5.3	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1	10.1021/jm2016864
	CHEMBL2029820	74251	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	405	5	0	5	5.3	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1	10.1021/jm2016864
	155552204	173560	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4546388	173560	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	71136691	143077	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	CHEMBL3899706	143077	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	68109605	157833	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	157833	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	9815616	114289	6	None	-2	4	Rat	7.2	pEC50	=	7.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	114289	6	None	-2	4	Rat	7.2	pEC50	=	7.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	44155538	8408	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2cccc(F)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094134	8408	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2cccc(F)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155316	8595	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095749	8595	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155420	8656	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2cccc(C)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096423	8656	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2cccc(C)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	46227790	198398	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	375	4	0	7	2.9	CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL595966	198398	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	375	4	0	7	2.9	CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	70689924	74227	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029798	74227	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O	10.1021/jm2016864
	162665242	181516	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	4	5.3	Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4781971	181516	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	4	5.3	Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl	10.1016/j.ejmech.2019.111881
	11951987	67875	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC	10.1016/j.bmcl.2005.06.017
	CHEMBL191579	67875	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC	10.1016/j.bmcl.2005.06.017
	46887320	8891	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098389	8891	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	118714739	114051	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	350	5	0	5	3.1	CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337505	114051	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	350	5	0	5	3.1	CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	46197778	8119	0	None	-6	5	Rat	5.2	pEC50	=	5.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	237	6	4	4	-0.3	N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1092243	8119	0	None	-6	5	Rat	5.2	pEC50	=	5.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	237	6	4	4	-0.3	N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O	10.1021/jm901523t
	11626305	66306	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	437	10	1	5	5.7	CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185290	66306	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	437	10	1	5	5.7	CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	44428731	142603	0	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL389585	142603	0	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	11575058	65255	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183304	65255	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	118714755	114066	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337521	114066	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	155550797	174538	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4569581	174538	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	59599538	144500	0	None	-1	2	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3911282	144500	0	None	-1	2	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	71136653	122874	0	None	51	2	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	122874	0	None	51	2	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	57459475	82225	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	331	3	0	5	3.5	CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179329	82225	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	331	3	0	5	3.5	CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	1393	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1396	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	213056	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	CHEMBL8759	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1393	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	1504	58	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	156817932	191466	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5202739	191466	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	60096224	155992	0	None	-43	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068189	155992	0	None	-43	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71461395	83479	1	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206445	83479	1	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	23725156	61615	0	None	-	1	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	357	3	0	3	4.7	Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774107	61615	0	None	-	1	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	357	3	0	3	4.7	Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1021/jm101414h
	49801370	156481	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	156481	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	90098428	122876	0	None	60	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	122876	0	None	60	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	25173616	183902	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484731	183902	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	156010124	176447	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	176447	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	156010124	176447	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	176447	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	44591773	183668	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	3	0	2	4.0	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483751	183668	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	3	0	2	4.0	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	162662443	181419	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	369	6	0	4	4.0	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4780663	181419	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	369	6	0	4	4.0	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1	10.1016/j.ejmech.2019.111881
	162675793	182823	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	375	5	0	4	4.6	Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4798495	182823	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	375	5	0	4	4.6	Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	155546950	173077	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	320	3	0	4	4.2	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4534604	173077	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	320	3	0	4	4.2	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1	10.1021/acs.jmedchem.8b00161
	155565811	175037	1	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	269	2	0	3	2.7	Fc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580525	175037	1	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	269	2	0	3	2.7	Fc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	146036861	175465	5	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	251	2	0	3	2.6	Brc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4590535	175465	5	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	251	2	0	3	2.6	Brc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	155549028	173215	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	3	0	3	4.4	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4538026	173215	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	3	0	3	4.4	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1	10.1021/acs.jmedchem.8b00161
	71460259	80373	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	434	4	1	5	5.2	N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152108	80373	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	434	4	1	5	5.2	N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	44155535	8407	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccccc2F)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094133	8407	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccccc2F)C(=O)O1	10.1016/j.bmcl.2010.03.089
	134130007	141647	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	391	6	0	6	4.4	Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884042	141647	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	391	6	0	6	4.4	Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	44428731	142603	0	None	-	1	Rat	4.1	pEC50	=	4.1	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL389585	142603	0	None	-	1	Rat	4.1	pEC50	=	4.1	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	68107827	191876	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5208947	191876	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	155535327	171439	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	281	3	0	4	2.6	COc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4471540	171439	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	281	3	0	4	2.6	COc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	71136654	122879	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	122879	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	57459636	82206	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	357	4	0	5	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179309	82206	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	357	4	0	5	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	66786816	157799	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	157799	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	162675603	182704	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	6	0	4	4.8	FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4796990	182704	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	6	0	4	4.8	FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	54580322	61630	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	402	3	0	4	5.0	Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774226	61630	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	402	3	0	4	5.0	Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21	10.1021/jm101414h
	25173691	188411	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL508821	188411	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	162643509	181077	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4776355	181077	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	11951986	123787	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	445	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1	10.1016/j.bmcl.2005.06.017
	CHEMBL363531	123787	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	445	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1	10.1016/j.bmcl.2005.06.017
	44591792	192757	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL525075	192757	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	168298153	192127	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	421	6	0	4	5.8	FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	CHEMBL5220484	192127	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	421	6	0	4	5.8	FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	25173778	184320	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL485329	184320	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	51357936	61633	0	None	-3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	CHEMBL1774231	61633	0	None	-3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	44155747	8594	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095746	8594	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	11951991	133386	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	12	1	6	5.7	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL371578	133386	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	12	1	6	5.7	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C	10.1016/j.bmcl.2005.06.017
	66786131	156612	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	156612	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11510036	65881	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL184531	65881	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	11952169	67175	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	459	10	1	6	5.8	CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189623	67175	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	459	10	1	6	5.8	CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	24815976	198067	0	None	5	2	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL593745	198067	0	None	5	2	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	46887418	8896	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098406	8896	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	22368592	8649	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096318	8649	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	51354014	61634	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C	10.1021/jm101414h
	CHEMBL1774232	61634	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C	10.1021/jm101414h
	11952347	67080	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	7	5.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12	10.1016/j.bmcl.2005.06.017
	CHEMBL188977	67080	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	7	5.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12	10.1016/j.bmcl.2005.06.017
	155518831	169780	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	353	3	0	3	5.5	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4447550	169780	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	353	3	0	3	5.5	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL5093066	213620	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		Cn1c(CN2CCN(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ncccc21	10.1021/acs.jmedchem.1c00563
	156019582	177427	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	177427	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	59234231	2103	1	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	2103	1	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	2103	1	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	2103	1	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	156019582	177427	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	177427	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	67060124	166213	0	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	388	4	0	5	3.8	O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4283963	166213	0	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	388	4	0	5	3.8	O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2	10.1016/j.bmcl.2018.08.022
	46887272	8588	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	233	5	0	2	3.6	CCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095702	8588	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	233	5	0	2	3.6	CCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155540	8624	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095970	8624	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	53322148	57410	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	342	6	0	4	4.1	CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669386	57410	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	342	6	0	4	4.1	CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53326075	57413	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	383	4	0	5	4.0	CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669389	57413	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	383	4	0	5	4.0	CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53322149	57415	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	4	0	4	4.1	CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669390	57415	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	4	0	4	4.1	CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53324152	57426	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	264	3	0	3	3.5	CCCn1ccc2cc(-c3cccnc3)ccc2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669402	57426	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	264	3	0	3	3.5	CCCn1ccc2cc(-c3cccnc3)ccc2c1=O	10.1016/j.bmcl.2010.12.048
	10176324	114316	1	None	4	4	Rat	8.1	pEC50	=	8.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	173	3	3	3	-0.6	C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O	10.1021/jm030967o
	CHEMBL334160	114316	1	None	4	4	Rat	8.1	pEC50	=	8.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	173	3	3	3	-0.6	C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O	10.1021/jm030967o
	57459488	83475	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206441	83475	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	68107827	191876	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5208947	191876	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	60096178	156327	0	None	-10	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4071962	156327	0	None	-10	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	156018381	177338	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	177338	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	70209638	157055	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	157055	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	156018381	177338	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	177338	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	146036869	175154	5	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	287	2	0	3	3.2	Brc1cccc2c1nnn2Cc1ccccc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4583006	175154	5	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	287	2	0	3	3.2	Brc1cccc2c1nnn2Cc1ccccc1	10.1021/acs.jmedchem.8b00161
	162657401	180514	2	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4760211	180514	2	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	162657401	180514	2	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL4760211	180514	2	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1021/acs.jmedchem.1c00563
	118714747	114058	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337513	114058	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	51354020	61638	0	None	-23	2	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774236	61638	0	None	-23	2	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	11495483	66319	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185392	66319	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	49822116	146447	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3926416	146447	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	46830123	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	6321	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	CHEMBL1094763	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	44450470	95627	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	CHEMBL260122	95627	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	70685765	74239	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029808	74239	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	156817932	191466	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5202739	191466	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	25173697	172107	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL450076	172107	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	46887417	8841	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097984	8841	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	44450470	95627	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	CHEMBL260122	95627	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	58081135	80385	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	383	2	1	2	5.9	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12	10.1021/jm201561r
	CHEMBL2152121	80385	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	383	2	1	2	5.9	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12	10.1021/jm201561r
	1310	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	1369	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	33032	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	44272391	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	88747398	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	CHEMBL575060	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	DB00142	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	46226952	198159	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	387	3	0	7	2.4	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL594386	198159	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	387	3	0	7	2.4	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	66612837	74216	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029786	74216	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm2016864
	66612837	74216	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL2029786	74216	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	155553087	173522	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4545027	173522	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1	10.1021/acs.jmedchem.8b00161
	51356569	61610	2	None	10	3	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1021/jm101414h
	CHEMBL1774101	61610	2	None	10	3	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1021/jm101414h
	168299005	192142	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5221091	192142	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O	10.1021/acs.jmedchem.2c00969
	66785182	156624	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	156624	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	59599545	146614	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3927834	146614	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	71136655	122872	0	None	12	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	122872	0	None	12	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	51356569	61610	2	None	-10	3	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1016/j.ejmech.2019.111881
	CHEMBL1774101	61610	2	None	-10	3	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1016/j.ejmech.2019.111881
	118714736	114047	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	321	4	0	4	3.3	CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337501	114047	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	321	4	0	4	3.3	CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O	10.1021/jm500496m
	11951447	67129	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189290	67129	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	44591712	183720	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	318	5	0	4	3.8	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL484178	183720	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	318	5	0	4	3.8	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	118714749	114060	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337515	114060	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	44392645	64898	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182715	64898	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	54584258	61608	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	456	5	0	6	3.3	COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1	10.1021/jm101414h
	CHEMBL1774099	61608	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	456	5	0	6	3.3	COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1	10.1021/jm101414h
	137634033	156088	0	None	-1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	156088	0	None	-1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	51357937	61635	0	None	-2	2	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774233	61635	0	None	-2	2	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	156018305	177250	0	None	89	2	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	177250	0	None	89	2	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	156018305	177250	0	None	89	2	Human	8.0	pEC50	=	8.0	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	177250	0	None	89	2	Human	8.0	pEC50	=	8.0	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	69093344	83480	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206446	83480	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	66786493	159120	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	159120	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	156020355	177444	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	177444	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	6604805	200991	2	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	195	3	3	3	-0.6	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F	10.1021/jm030967o
	CHEMBL61605	200991	2	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	195	3	3	3	-0.6	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F	10.1021/jm030967o
	162659759	180719	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4762556	180719	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	162662067	180817	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	349	6	0	4	3.7	Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O	10.1016/j.ejmech.2019.111881
	CHEMBL4763686	180817	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	349	6	0	4	3.7	Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O	10.1016/j.ejmech.2019.111881
	162662384	181460	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	5	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4781222	181460	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	5	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155518472	169726	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	207	2	0	3	2.5	Clc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4446625	169726	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	207	2	0	3	2.5	Clc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	156017237	177177	0	None	1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	177177	0	None	1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156017237	177177	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	177177	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156817945	189880	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5179002	189880	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	3954	657	53	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	657	53	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	657	53	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	66784262	157674	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	157674	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	70694132	74247	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029816	74247	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O	10.1021/jm2016864
	11655609	165337	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL424998	165337	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	1395	2482	9	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	2482	9	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	2482	9	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	57459512	82215	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	367	4	0	5	3.7	Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179318	82215	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	367	4	0	5	3.7	Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	118714742	114054	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	5	0	4	3.9	CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337508	114054	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	5	0	4	3.9	CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	71117214	150563	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	446	4	0	8	2.1	Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1	nan
	CHEMBL3959189	150563	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	446	4	0	8	2.1	Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1	nan
	44591770	191710	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL520639	191710	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	68109333	158833	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	158833	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	162649465	179475	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	3	5.0	Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4747874	179475	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	3	5.0	Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	46226930	200223	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.5	CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL607518	200223	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.5	CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	118714754	114065	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1	10.1021/jm500496m
	CHEMBL3337520	114065	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1	10.1021/jm500496m
	11950553	66943	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188286	66943	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71117402	149886	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	532	5	1	6	5.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21	nan
	CHEMBL3953950	149886	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	532	5	1	6	5.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21	nan
	51354017	61636	0	None	-	1	Rat	6.0	pEC50	=	6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774234	61636	0	None	-	1	Rat	6.0	pEC50	=	6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	131636309	159486	0	None	-	1	Human	9.0	pIC50	=	9.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	445	4	0	5	5.6	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4108184	159486	0	None	-	1	Human	9.0	pIC50	=	9.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	445	4	0	5	5.6	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636462	159610	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	4.8	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	CHEMBL4109246	159610	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	4.8	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	131636310	159987	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	4	0	5	5.3	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4112479	159987	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	4	0	5	5.3	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636389	159547	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108743	159547	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636463	159751	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4110543	159751	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	78319942	159621	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4109319	159621	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636453	160011	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112624	160011	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	11484819	55998	0	None	-2	2	Human	8.0	pIC50	=	8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	55998	0	None	-2	2	Human	8.0	pIC50	=	8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	44450479	95803	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261050	95803	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	9909080	154731	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402886	154731	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317744	55979	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629844	55979	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	22317767	55982	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629847	55982	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11235624	55997	0	None	-1	3	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	55997	0	None	-1	3	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317431	56104	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631864	56104	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	78324632	159694	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4110016	159694	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	78320556	160098	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	CHEMBL4113304	160098	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	131636370	159319	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106787	159319	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636447	160184	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113943	160184	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636434	150829	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC	nan
	CHEMBL3961419	150829	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC	nan
	131636342	142349	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3893630	142349	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1	nan
	76318479	105610	0	None	-	1	Human	7.0	pIC50	=	7	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	446	6	1	5	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1	10.1039/C3MD00110E
	CHEMBL3133886	105610	0	None	-	1	Human	7.0	pIC50	=	7	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	446	6	1	5	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1	10.1039/C3MD00110E
	131636402	159865	0	None	-	1	Human	7.0	pIC50	=	7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4111387	159865	0	None	-	1	Human	7.0	pIC50	=	7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	10778385	78314	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	269	6	3	4	1.2	NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112581	78314	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	269	6	3	4	1.2	NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10826383	78317	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	277	7	3	3	1.5	NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112584	78317	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	277	7	3	3	1.5	NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	44348769	16587	0	None	-3	2	Human	6.0	pIC50	=	6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	279	6	4	4	0.8	N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL124483	16587	0	None	-3	2	Human	6.0	pIC50	=	6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	279	6	4	4	0.8	N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	49858118	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	6224	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	CHEMBL1630807	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	11269030	55996	0	None	-1	3	Rat	7.0	pIC50	=	7	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	55996	0	None	-1	3	Rat	7.0	pIC50	=	7	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	155550334	173715	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550009	173715	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155550334	173715	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550009	173715	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	131636325	160129	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113523	160129	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	155559601	174273	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563183	174273	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155566989	175294	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4586203	175294	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155559601	174273	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563183	174273	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155566989	175294	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4586203	175294	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	131636415	159326	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	463	7	1	7	3.9	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4106864	159326	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	463	7	1	7	3.9	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	9845873	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL411440	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22224657	95712	0	None	2	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	95712	0	None	2	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	95848	0	None	1	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	95848	0	None	1	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	11474913	56098	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631858	56098	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9845873	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	160240	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	90354590	145136	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3916087	145136	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	90354676	159840	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4111258	159840	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	131636304	160052	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1	nan
	CHEMBL4112952	160052	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1	nan
	131636458	159952	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112214	159952	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	10515174	78306	0	None	1	2	Human	6.0	pIC50	=	6.0	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	255	5	3	3	1.5	NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112574	78306	0	None	1	2	Human	6.0	pIC50	=	6.0	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	255	5	3	3	1.5	NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	44272296	65846	1	None	-	1	Rat	5.0	pIC50	=	5.0	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	245	4	4	3	0.4	C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O	10.1016/S0960-894X(97)00177-7
	CHEMBL18439	65846	1	None	-	1	Rat	5.0	pIC50	=	5.0	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	245	4	4	3	0.4	C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O	10.1016/S0960-894X(97)00177-7
	90643971	111496	0	None	-1	2	Rat	6.0	pIC50	=	6.0	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288667	111496	0	None	-1	2	Rat	6.0	pIC50	=	6.0	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	134138062	146955	0	None	-1	2	Human	6.0	pIC50	=	6.0	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	374	5	4	5	0.9	N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3930511	146955	0	None	-1	2	Human	6.0	pIC50	=	6.0	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	374	5	4	5	0.9	N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	162658781	183099	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4759209	183099	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803105	183099	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	18548766	95406	0	None	-	1	Rat	6.9	pIC50	=	6.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259053	95406	0	None	-	1	Rat	6.9	pIC50	=	6.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636289	160170	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	CHEMBL4113819	160170	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	22224854	94927	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256812	94927	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	131636351	149952	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F	nan
	CHEMBL3954434	149952	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F	nan
	90354488	160377	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4115442	160377	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	131636294	159464	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108019	159464	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	67705089	151711	0	None	1	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3969063	151711	0	None	1	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	90367533	159524	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4108547	159524	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636379	160185	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113948	160185	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	137635882	155341	0	None	1	2	Human	4.9	pIC50	=	4.9	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	155341	0	None	1	2	Human	4.9	pIC50	=	4.9	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	162644419	183030	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4778355	183030	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802356	183030	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	22448689	97093	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270616	97093	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	11281280	56099	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	56099	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	90354550	159383	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107291	159383	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636419	147563	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1	nan
	CHEMBL3935209	147563	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1	nan
	131636316	159333	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4106929	159333	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78324633	160022	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4112706	160022	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636296	160295	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114910	160295	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354846	159449	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4107888	159449	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	131636366	159681	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4109916	159681	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636405	159570	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108937	159570	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354352	144180	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3908808	144180	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	76318478	105607	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1	10.1039/C3MD00110E
	CHEMBL3133883	105607	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1	10.1039/C3MD00110E
	44328753	206010	0	None	-45	6	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	8	3	4	4.2	CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL95868	206010	0	None	-45	6	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	8	3	4	4.2	CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	76336598	105608	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1	10.1039/C3MD00110E
	CHEMBL3133884	105608	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1	10.1039/C3MD00110E
	44329033	206231	0	None	-34	5	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	7	3	4	4.1	CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL97200	206231	0	None	-34	5	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	7	3	4	4.1	CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	90643959	111488	0	None	-1	2	Rat	5.9	pIC50	=	5.9	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	460	4	1	7	3.2	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288646	111488	0	None	-1	2	Rat	5.9	pIC50	=	5.9	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	460	4	1	7	3.2	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	11158623	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	10115228	95713	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260642	95713	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	53324715	56110	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631870	56110	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636423	159475	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	471	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	CHEMBL4108112	159475	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	471	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	122580887	159947	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112158	159947	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636280	159307	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106725	159307	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636375	160357	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4115306	160357	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	10710505	78313	0	None	-1	2	Human	5.9	pIC50	=	5.9	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	316	6	3	4	1.6	Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21	10.1021/jm970497w
	CHEMBL2112580	78313	0	None	-1	2	Human	5.9	pIC50	=	5.9	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	316	6	3	4	1.6	Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21	10.1021/jm970497w
	155526616	170559	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	CHEMBL4458387	170559	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	155530126	170892	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4463498	170892	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155526616	170559	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	CHEMBL4458387	170559	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	155530126	170892	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4463498	170892	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	162654849	183078	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4755204	183078	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802906	183078	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	155550549	174526	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4569114	174526	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155550549	174526	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4569114	174526	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	134139744	145414	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3918170	145414	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11442010	56001	0	None	-5	3	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	56001	0	None	-5	3	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	18548908	95804	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261051	95804	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	9891158	155034	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL404463	155034	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317918	55992	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629858	55992	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	131636418	160028	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	4	5.7	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4112763	160028	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	4	5.7	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636410	160269	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	CHEMBL4114609	160269	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	131636388	159800	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4110884	159800	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636353	160367	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115388	160367	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636385	160233	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	6	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4114364	160233	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	6	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	49858117	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	6223	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	CHEMBL1630806	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	155566841	175277	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4585786	175277	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	155566841	175277	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4585786	175277	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	71681826	89616	0	None	-1	3	Human	4.8	pIC50	=	4.8	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	89616	0	None	-1	3	Human	4.8	pIC50	=	4.8	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	90643958	111487	0	None	-6	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288644	111487	0	None	-6	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12	10.1016/j.bmcl.2014.04.051
	22224970	154942	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404080	154942	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	22317715	55989	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629854	55989	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	53326017	56112	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631872	56112	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636403	159336	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106954	159336	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636317	160016	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4112663	160016	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	69669747	183061	7	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	183061	7	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	183061	7	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	90354858	159305	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	CHEMBL4106716	159305	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	67705326	152702	0	None	2	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	457	7	4	6	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3977508	152702	0	None	2	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	457	7	4	6	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	131636349	144687	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3912677	144687	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636444	159318	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.6	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4106785	159318	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.6	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636315	159970	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112341	159970	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	22317185	55983	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629848	55983	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44345358	112838	0	None	1	2	Human	5.8	pIC50	=	5.8	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	215	5	3	3	0.5	CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL331753	112838	0	None	1	2	Human	5.8	pIC50	=	5.8	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	215	5	3	3	0.5	CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970497w
	10456810	107380	0	None	-13	5	Rat	5.8	pIC50	=	5.8	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	457	8	3	4	4.7	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL319279	107380	0	None	-13	5	Rat	5.8	pIC50	=	5.8	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	457	8	3	4	4.7	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O	10.1016/s0960-894x(98)00510-1
	134132133	144244	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3909237	144244	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44450391	168258	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437835	168258	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9820321	154457	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	154457	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	135544097	155112	0	None	269	2	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404886	155112	0	None	269	2	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	9820321	154457	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	154457	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	67633340	183129	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4780402	183129	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803381	183129	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636443	159287	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	6	0	5	5.5	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	CHEMBL4106566	159287	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	6	0	5	5.5	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	131636400	159442	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4107829	159442	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	131636337	152131	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3972702	152131	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636401	159836	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4111225	159836	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	11503055	2358	2	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	9694	2358	2	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	CHEMBL2204436	2358	2	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	155538435	171791	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4476138	171791	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155539352	172256	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4514334	172256	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155562175	175241	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4584801	175241	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155539352	172256	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4514334	172256	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155562175	175241	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4584801	175241	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155538435	171791	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4476138	171791	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	11298568	69018	1	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	CHEMBL192977	69018	1	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	90643974	111498	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288675	111498	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	90643963	111490	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	366	2	0	5	4.2	Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288653	111490	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	366	2	0	5	4.2	Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	22224670	95807	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261081	95807	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	53316736	55976	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629715	55976	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	22317847	56101	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631861	56101	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11212447	56108	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631868	56108	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636450	160079	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113175	160079	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636373	159299	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106692	159299	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636397	159424	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4107640	159424	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F	nan
	131636360	149703	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3952383	149703	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636427	160122	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4113474	160122	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	67707808	148098	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	432	6	4	6	1.3	COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3939492	148098	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	432	6	4	6	1.3	COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	131636372	159651	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4109618	159651	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636299	159711	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4110209	159711	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	10492773	16591	0	None	-2	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	277	6	3	3	1.4	Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL124501	16591	0	None	-2	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	277	6	3	3	1.4	Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	44348993	114074	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	297	6	3	3	1.8	N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL333771	114074	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	297	6	3	3	1.8	N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	44348706	116369	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	281	6	3	3	1.3	N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL338282	116369	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	281	6	3	3	1.3	N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	10828532	78340	0	None	-22	2	Human	5.8	pIC50	=	5.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	307	7	4	4	0.8	NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL2112634	78340	0	None	-22	2	Human	5.8	pIC50	=	5.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	307	7	4	4	0.8	NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	10359073	154423	1	None	-1	2	Human	4.8	pIC50	=	4.8	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	CHEMBL40123	154423	1	None	-1	2	Human	4.8	pIC50	=	4.8	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	18613455	95591	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259924	95591	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	44329031	107775	0	None	-15	7	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	437	10	3	4	5.0	CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL319732	107775	0	None	-15	7	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	437	10	3	4	5.0	CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	18548739	159806	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL411095	159806	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548739	159806	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL411095	159806	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636333	153642	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3985799	153642	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636339	159577	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4108997	159577	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636378	159929	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4111987	159929	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	131636395	159943	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4112129	159943	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636373	159299	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106692	159299	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636407	159544	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	3	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108700	159544	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	3	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636408	160201	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114047	160201	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636329	144092	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C	nan
	CHEMBL3908089	144092	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C	nan
	131636284	159945	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112146	159945	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354963	160087	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	4	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	CHEMBL4113235	160087	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	4	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	131636406	159817	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111067	159817	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90355009	159690	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4109993	159690	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	86695984	149221	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	472	7	3	8	1.9	Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1016/j.bmcl.2016.10.067
	CHEMBL3948272	149221	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	472	7	3	8	1.9	Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1016/j.bmcl.2016.10.067
	53316798	56096	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631856	56096	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	44348846	116498	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL2111822	116498	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL338911	116498	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	90643954	111485	0	None	-2	2	Rat	5.7	pIC50	=	5.7	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	430	3	1	6	3.2	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288636	111485	0	None	-2	2	Rat	5.7	pIC50	=	5.7	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	430	3	1	6	3.2	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	155523578	170331	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4454867	170331	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155523578	170331	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4454867	170331	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	11304010	55999	0	None	2	3	Rat	8.7	pIC50	=	8.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	55999	0	None	2	3	Rat	8.7	pIC50	=	8.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	122580902	159446	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4107872	159446	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636451	159451	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107913	159451	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636422	159483	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	5	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4108163	159483	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	5	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636461	159565	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108918	159565	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320558	159888	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111659	159888	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354985	160120	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	425	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113466	160120	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	425	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78319944	160172	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4113834	160172	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	78320252	159966	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4112321	159966	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	90354835	160005	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112598	160005	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636455	159845	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111276	159845	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636460	159920	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4111924	159920	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	1397	2483	11	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	9886034	2483	11	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL186453	2483	11	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	22317728	55981	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629846	55981	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566598	142146	10	None	1	3	Human	7.7	pIC50	=	7.7	Functional	Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	142146	10	None	1	3	Human	7.7	pIC50	=	7.7	Functional	Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	67637138	183026	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4776989	183026	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802329	183026	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636365	159436	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107737	159436	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636282	160020	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112692	160020	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636409	159902	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	6	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1	nan
	CHEMBL4111753	159902	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	6	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1	nan
	131636331	144355	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3910129	144355	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636297	159423	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4107635	159423	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	122580890	159917	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111874	159917	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	10807972	35574	1	None	-12	4	Human	6.7	pIC50	=	6.7	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL144151	35574	1	None	-12	4	Human	6.7	pIC50	=	6.7	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	1378	2374	48	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	1399	2374	48	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	9819927	2374	48	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	CHEMBL432038	2374	48	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	10358265	101643	0	None	-2	2	Human	4.7	pIC50	=	4.7	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL302411	101643	0	None	-2	2	Human	4.7	pIC50	=	4.7	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1	10.1016/s0960-894x(98)00352-7
	162663798	183127	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4779554	183127	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4803378	183127	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	1378	2374	48	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	1399	2374	48	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	9819927	2374	48	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	CHEMBL432038	2374	48	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	131636435	147846	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	5	0	5	4.5	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC	nan
	CHEMBL3937514	147846	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	5	0	5	4.5	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC	nan
	131636361	160115	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113439	160115	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636283	160225	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4114284	160225	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636454	159406	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107497	159406	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636290	159940	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112105	159940	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	122580905	159507	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108383	159507	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636285	160388	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.2	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4115529	160388	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.2	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	134154496	151966	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3971347	151966	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	134141510	146523	0	None	-2	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	339	5	4	5	0.1	Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1016/j.bmcl.2016.10.067
	CHEMBL3927108	146523	0	None	-2	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	339	5	4	5	0.1	Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1016/j.bmcl.2016.10.067
	44329029	162957	0	None	2	6	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	479	13	3	4	6.2	CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL420262	162957	0	None	2	6	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	479	13	3	4	6.2	CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	9952648	95848	0	None	1	2	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	95848	0	None	1	2	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	118906265	145403	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	CHEMBL3918111	145403	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	131636314	159482	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4108162	159482	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636448	159981	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112439	159981	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636346	151956	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	CHEMBL3971278	151956	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	131636369	160258	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114534	160258	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636276	145362	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3917816	145362	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	90367528	143537	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3903357	143537	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	44348911	16374	0	None	1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	331	6	3	3	2.1	N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL123847	16374	0	None	1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	331	6	3	3	2.1	N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	10688450	16412	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL124078	16412	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	155547618	173004	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4533083	173004	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155547618	173004	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4533083	173004	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	134129940	141902	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	359	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3890112	141902	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	359	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	162652146	179623	0	None	1	2	Human	5.6	pIC50	=	5.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4749728	179623	0	None	1	2	Human	5.6	pIC50	=	5.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	1378	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	1399	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	9819927	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	CHEMBL432038	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	22224852	95407	0	None	-2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	95407	0	None	-2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	160240	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	160240	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	160240	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	160240	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	131636382	159848	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	CHEMBL4111287	159848	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	131636396	159682	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	3	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4109918	159682	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	3	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636301	159877	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111566	159877	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	10852666	78316	0	None	1	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	313	6	3	3	2.3	NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112583	78316	0	None	1	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	313	6	3	3	2.3	NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10567792	78319	0	None	3	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	321	6	3	3	2.5	NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112586	78319	0	None	3	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	321	6	3	3	2.5	NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	90355016	160143	0	None	-	1	Human	6.6	pIC50	=	6.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	1	6	3.7	COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4113592	160143	0	None	-	1	Human	6.6	pIC50	=	6.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	1	6	3.7	COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	86298614	111499	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288676	111499	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	86298614	111499	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288676	111499	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	11211597	56000	0	None	-1	3	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	56000	0	None	-1	3	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636336	148120	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	378	2	0	5	4.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3939714	148120	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	378	2	0	5	4.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	131636311	152104	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	4	0	5	4.3	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3972441	152104	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	4	0	5	4.3	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl	nan
	131636326	160000	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112588	160000	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636323	147517	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3934756	147517	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1	nan
	131636298	159569	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4108936	159569	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1	nan
	122580894	160134	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113546	160134	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	155538978	172203	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4513332	172203	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538978	172203	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4513332	172203	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155514808	169320	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4440771	169320	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155514808	169320	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4440771	169320	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	11269030	55996	0	None	-1	3	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	55996	0	None	-1	3	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	131636328	148201	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3940380	148201	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636354	159791	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	392	2	0	5	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110789	159791	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	392	2	0	5	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	67705376	144794	0	None	-1	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	416	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3913414	144794	0	None	-1	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	416	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	69669820	183048	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4746125	183048	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802570	183048	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	131636374	159541	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108665	159541	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354688	159980	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112422	159980	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	1378	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	2374	48	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	131636393	159513	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	4.9	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108446	159513	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	4.9	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636442	160392	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	6	0	5	5.2	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	CHEMBL4115553	160392	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	6	0	5	5.2	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	18613373	95714	0	None	-	1	Rat	6.6	pIC50	=	6.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260643	95714	0	None	-	1	Rat	6.6	pIC50	=	6.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	22224657	95712	0	None	2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	95712	0	None	2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	95848	0	None	1	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	95848	0	None	1	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	131636338	147437	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3934173	147437	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	131636432	149745	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3952745	149745	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1	nan
	69669646	183087	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4757159	183087	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4802990	183087	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	131636367	146092	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	459	5	0	6	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3923457	146092	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	459	5	0	6	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636357	160146	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113614	160146	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354626	159304	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.7	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4106714	159304	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.7	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636286	159337	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	6	4.6	COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106958	159337	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	6	4.6	COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636319	153516	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3984622	153516	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	134144441	149849	0	None	-1	2	Human	6.6	pIC50	=	6.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3953570	149849	0	None	-1	2	Human	6.6	pIC50	=	6.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44329042	168506	0	None	-38	5	Rat	5.5	pIC50	=	5.5	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	381	6	3	4	3.5	CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL439775	168506	0	None	-38	5	Rat	5.5	pIC50	=	5.5	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	381	6	3	4	3.5	CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	155555318	173736	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550517	173736	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155555318	173736	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550517	173736	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	131636300	159574	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	4	0	5	4.1	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4108984	159574	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	4	0	5	4.1	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	131636399	160157	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4113737	160157	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	131636312	159745	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.9	C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1	nan
	CHEMBL4110503	159745	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.9	C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1	nan
	22224852	95407	0	None	-2	2	Rat	6.5	pIC50	=	6.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	95407	0	None	-2	2	Rat	6.5	pIC50	=	6.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	11158623	3287	7	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	3287	7	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	3287	7	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	11484819	55998	0	None	2	2	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	55998	0	None	2	2	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	11406781	56116	0	None	-	1	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631876	56116	0	None	-	1	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636376	160097	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4113300	160097	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	78319946	160373	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115420	160373	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636324	159553	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108816	159553	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320250	159903	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4111755	159903	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	78320247	159899	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4111744	159899	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78324635	159907	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111773	159907	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636416	160336	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4115199	160336	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636417	159458	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	446	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4107975	159458	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	446	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636305	159526	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1	nan
	CHEMBL4108564	159526	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1	nan
	78319945	159783	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4110721	159783	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	78319941	160383	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4115490	160383	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636446	159983	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4112442	159983	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	22317318	56115	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631875	56115	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636456	159309	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	1	6	4.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106741	159309	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	1	6	4.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636412	159626	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	6	1	6	3.9	Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	CHEMBL4109387	159626	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	6	1	6	3.9	Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	131636306	150718	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl	nan
	CHEMBL3960280	150718	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl	nan
	15392101	99960	0	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL290509	99960	0	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/j.bmcl.2007.10.026
	4694355	98272	31	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1016/S0960-894X(97)00177-7
	CHEMBL277961	98272	31	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1016/S0960-894X(97)00177-7
	134144056	150092	0	None	-1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	307	5	4	5	-0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3955458	150092	0	None	-1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	307	5	4	5	-0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	131636303	160246	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114464	160246	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636293	159580	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4109021	159580	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636343	144326	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.5	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3909878	144326	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.5	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	90354563	149138	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	3	0	5	4.6	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br	nan
	CHEMBL3947609	149138	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	3	0	5	4.6	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br	nan
	44348859	16372	0	None	-15	2	Human	5.5	pIC50	=	5.5	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	278	6	4	4	0.7	Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL123842	16372	0	None	-15	2	Human	5.5	pIC50	=	5.5	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	278	6	4	4	0.7	Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	21309795	150278	0	None	-3	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3956934	150278	0	None	-3	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	90643961	111489	0	None	-2	2	Rat	5.5	pIC50	=	5.5	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	3	0	6	3.9	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288649	111489	0	None	-2	2	Rat	5.5	pIC50	=	5.5	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	3	0	6	3.9	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	155538001	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538001	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	171769	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	131636355	160307	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4114983	160307	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636341	147406	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3933840	147406	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	131636359	160213	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	CHEMBL4114183	160213	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	162665071	183136	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4781638	183136	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803454	183136	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	18548862	157384	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408455	157384	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	134137754	147403	0	None	1	2	Human	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	400	6	3	5	2.3	[N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3933829	147403	0	None	1	2	Human	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	400	6	3	5	2.3	[N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	131636320	150155	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3956003	150155	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1	nan
	155550453	173687	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4549344	173687	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155550453	173687	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4549344	173687	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	22448579	155225	0	None	4	2	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL405895	155225	0	None	4	2	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636302	159462	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	3	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4108010	159462	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	3	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	22224825	158436	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL409638	158436	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	11211597	56000	0	None	-1	3	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	56000	0	None	-1	3	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636347	142467	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	CHEMBL3894707	142467	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	131636457	159990	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112521	159990	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636386	160403	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	6	0	6	4.4	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4115662	160403	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	6	0	6	4.4	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	131636358	148462	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3942377	148462	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	44302608	100366	0	None	-2	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	340	5	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL293434	100366	0	None	-2	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	340	5	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	155531624	171097	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4466304	171097	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155531624	171097	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4466304	171097	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	9952648	95848	0	None	1	2	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	95848	0	None	1	2	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636291	159727	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110331	159727	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	44302856	102245	0	None	1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	354	6	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL304919	102245	0	None	1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	354	6	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	11235624	55997	0	None	-6	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	55997	0	None	-6	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636394	160019	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	4.6	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4112680	160019	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	4.6	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636398	159685	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4109944	159685	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	134152341	152917	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3979475	152917	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	155542028	172511	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4520084	172511	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155542028	172511	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4520084	172511	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	18548824	157182	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408229	157182	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548824	157182	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL408229	157182	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	90643966	111493	0	None	-1	2	Rat	5.4	pIC50	=	5.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	448	3	1	6	3.3	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288660	111493	0	None	-1	2	Rat	5.4	pIC50	=	5.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	448	3	1	6	3.3	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	11351088	55990	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629856	55990	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317928	55991	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629857	55991	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	11281280	56099	0	None	1	3	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	56099	0	None	1	3	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636425	159926	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4111952	159926	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636383	160183	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4113929	160183	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	69669747	183061	7	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	183061	7	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	183061	7	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	78320560	159361	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4107140	159361	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	78320248	160187	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4113962	160187	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636390	159523	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	442	3	0	6	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108541	159523	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	442	3	0	6	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	77461009	159738	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4110444	159738	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	90354889	160144	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.8	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	CHEMBL4113601	160144	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.8	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	131636421	159411	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4107565	159411	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636313	160042	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112898	160042	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636356	160210	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114150	160210	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636348	159303	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106709	159303	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636391	159549	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108785	159549	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636431	159728	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4110332	159728	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	131636429	160041	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112889	160041	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78320559	160344	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4115237	160344	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636295	160369	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115390	160369	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320249	159705	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4110153	159705	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	131636424	159342	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4106969	159342	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636279	143181	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3900589	143181	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636345	143570	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F	nan
	CHEMBL3903640	143570	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F	nan
	21309795	150278	0	None	-3	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.6b01119
	CHEMBL3956934	150278	0	None	-3	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.6b01119
	11281280	56099	0	None	-5	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	56099	0	None	-5	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636287	159951	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112202	159951	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636411	159944	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.5	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4112136	159944	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.5	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	44302686	199222	0	None	-1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	332	4	3	4	1.4	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL60164	199222	0	None	-1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	332	4	3	4	1.4	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	155540306	172320	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4516001	172320	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	90643968	111494	0	None	-6	2	Rat	6.4	pIC50	=	6.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288662	111494	0	None	-6	2	Rat	6.4	pIC50	=	6.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	155540306	172320	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4516001	172320	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	131636392	159759	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	469	5	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	CHEMBL4110601	159759	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	469	5	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	44348939	117977	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	293	7	3	4	1.1	COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL341457	117977	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	293	7	3	4	1.1	COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	1373	2430	46	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	139055582	2430	46	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	446355	2430	46	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	CHEMBL257626	2430	46	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	DB04256	2430	46	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	11777615	98392	0	None	2	2	Rat	4.4	pIC50	=	4.4	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	265	2	3	4	1.2	CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1	10.1016/S0960-894X(97)00177-7
	CHEMBL278949	98392	0	None	2	2	Rat	4.4	pIC50	=	4.4	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	265	2	3	4	1.2	CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1	10.1016/S0960-894X(97)00177-7
	10783272	85681	0	None	-15	2	Human	5.4	pIC50	=	5.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2311086	85681	0	None	-15	2	Human	5.4	pIC50	=	5.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	131636380	160159	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4113748	160159	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	155538001	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538001	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	171769	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	131636274	144093	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3908096	144093	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1	nan
	69669702	183083	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4756556	183083	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4802948	183083	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636368	159528	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108571	159528	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	10732318	78318	0	None	6	2	Human	6.4	pIC50	=	6.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	291	8	3	3	1.9	NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112585	78318	0	None	6	2	Human	6.4	pIC50	=	6.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	291	8	3	3	1.9	NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10385210	12907	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189910	12907	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539760	12907	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	10250423	12888	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189797	12888	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539516	12888	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	57338826	149083	0	None	1	5	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3947221	149083	0	None	1	5	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	131636459	160296	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	CHEMBL4114912	160296	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	44302931	162707	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	270	4	3	4	0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL418650	162707	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	270	4	3	4	0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1	10.1016/s0960-894x(98)00352-7
	90643973	111497	0	None	-1	2	Rat	5.3	pIC50	=	5.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	4	1	6	3.4	O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO	10.1016/j.bmcl.2014.04.051
	CHEMBL3288674	111497	0	None	-1	2	Rat	5.3	pIC50	=	5.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	4	1	6	3.4	O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO	10.1016/j.bmcl.2014.04.051
	22224570	95456	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259269	95456	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	131636344	147770	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	4	0	5	4.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3936936	147770	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	4	0	5	4.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1	nan
	131636362	159453	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107924	159453	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	22317491	55988	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629853	55988	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636437	143462	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl	nan
	CHEMBL3902842	143462	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl	nan
	1297	169674	33	None	-1	2	Human	4.3	pIC50	=	4.3	Functional	Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm00019a002
	CHEMBL444589	169674	33	None	-1	2	Human	4.3	pIC50	=	4.3	Functional	Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm00019a002
	162658340	183094	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4760856	183094	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803084	183094	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636321	148821	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3945334	148821	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1	nan
	70051296	89613	0	None	-1	3	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381648	89613	0	None	-1	3	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	22317724	55980	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629845	55980	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	53317987	55993	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629859	55993	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	11362246	56100	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631860	56100	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	53325611	56107	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631867	56107	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636413	159531	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	6	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4108588	159531	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	6	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636381	160010	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112623	160010	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636384	160242	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114409	160242	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	78320251	160385	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4115497	160385	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	131636430	160161	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	7	0	6	4.9	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4113756	160161	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	7	0	6	4.9	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	90354553	159355	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4107066	159355	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	131636464	159746	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	CHEMBL4110505	159746	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	131636420	159797	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4110839	159797	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636426	159378	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4107266	159378	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78320557	159756	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4110578	159756	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	1393	1504	58	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	1396	1504	58	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	213056	1504	58	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	CHEMBL8759	1504	58	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	78324634	159743	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110486	159743	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636363	159481	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108148	159481	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354342	159661	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4109709	159661	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636441	159578	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	5	0	5	5.2	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	CHEMBL4109004	159578	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	5	0	5	5.2	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	53320632	55987	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629852	55987	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636445	159404	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107450	159404	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	1222	101254	56	None	3	2	Human	4.3	pIC50	=	4.3	Functional	Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm960059+
	CHEMBL299683	101254	56	None	3	2	Human	4.3	pIC50	=	4.3	Functional	Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm960059+
	6324634	147399	7	None	6	2	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00352-7
	CHEMBL39338	147399	7	None	6	2	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00352-7
	44302609	200937	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL61281	200937	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1	10.1016/s0960-894x(98)00352-7
	6324634	147399	7	None	6	2	Human	4.3	pIC50	=	4.3	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	CHEMBL39338	147399	7	None	6	2	Human	4.3	pIC50	=	4.3	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	131636364	160302	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	CHEMBL4114951	160302	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	10091203	12827	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189303	12827	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL538489	12827	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	11269030	55996	0	None	-1	3	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	55996	0	None	-1	3	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	10201802	96186	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL263649	96186	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	10428048	3297	26	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	3955	3297	26	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	CHEMBL305406	3297	26	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	71566598	142146	10	None	-1	3	Rat	7.3	pIC50	=	7.3	Functional	Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	142146	10	None	-1	3	Rat	7.3	pIC50	=	7.3	Functional	Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	131636332	150747	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3960577	150747	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	155545491	172799	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4527834	172799	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	155545491	172799	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4527834	172799	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	137634033	156088	0	None	-1	2	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	156088	0	None	-1	2	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	90643964	111491	0	None	-1	2	Rat	6.3	pIC50	=	6.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288656	111491	0	None	-1	2	Rat	6.3	pIC50	=	6.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12	10.1016/j.bmcl.2014.04.051
	131636436	153016	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3980239	153016	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	155554668	174021	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4557272	174021	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155554668	174021	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4557272	174021	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	131636322	144848	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	5	0	5	4.7	CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F	nan
	CHEMBL3913916	144848	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	5	0	5	4.7	CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F	nan
	22317741	56103	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631863	56103	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317620	56109	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631869	56109	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL5076351	212649	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	90355554	159371	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	CHEMBL4107197	159371	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	131636428	160346	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	6	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	CHEMBL4115246	160346	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	6	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	131636307	159374	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4107211	159374	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	67637415	183095	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4759992	183095	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803099	183095	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636377	159334	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4106932	159334	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	117821319	118300	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	431	2	0	5	4.7	C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21	10.1021/ml5005365
	CHEMBL3421840	118300	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	431	2	0	5	4.7	C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21	10.1021/ml5005365
	131636438	150680	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3960039	150680	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	44309100	102145	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/j.bmcl.2007.10.026
	CHEMBL304285	102145	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/j.bmcl.2007.10.026
	131636340	144219	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	3	0	5	4.5	Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	CHEMBL3909077	144219	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	3	0	5	4.5	Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	44302930	100234	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	278	5	3	4	0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL292553	100234	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	278	5	3	4	0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	52944782	16751	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level	ChEMBL	241	4	3	3	0.9	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1	10.1016/j.bmc.2010.06.051
	CHEMBL1253502	16751	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level	ChEMBL	241	4	3	3	0.9	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1	10.1016/j.bmc.2010.06.051
	19702198	160763	14	None	1	2	Rat	4.2	pIC50	=	4.2	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL412445	160763	14	None	1	2	Rat	4.2	pIC50	=	4.2	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	10.1016/s0960-894x(01)00329-8
	131636335	152723	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3977681	152723	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	131636278	146922	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C	nan
	CHEMBL3930304	146922	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C	nan
	10607617	78311	0	None	-2	2	Human	5.2	pIC50	=	5.2	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	187	4	3	3	-0.1	CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112579	78311	0	None	-2	2	Human	5.2	pIC50	=	5.2	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	187	4	3	3	-0.1	CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	134155683	150817	0	None	1	2	Human	7.2	pIC50	=	7.2	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	377	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3961306	150817	0	None	1	2	Human	7.2	pIC50	=	7.2	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	377	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	155553540	173597	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4547431	173597	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155553540	173597	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4547431	173597	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155551226	173400	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4541942	173400	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155559283	174276	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563286	174276	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155551226	173400	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4541942	173400	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155559283	174276	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563286	174276	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	11304010	55999	0	None	-2	3	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	55999	0	None	-2	3	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	22317892	55995	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629860	55995	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317279	56105	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631865	56105	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636308	160243	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4114419	160243	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	90354432	160260	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	1	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4114578	160260	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	1	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	78319943	159352	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107040	159352	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636404	159780	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110709	159780	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354881	159532	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108597	159532	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636327	160083	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.5	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	CHEMBL4113208	160083	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.5	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	1378	2374	48	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	2374	48	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	2374	48	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	2374	48	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	131636281	160125	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113495	160125	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354538	159803	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	485	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4110899	159803	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	485	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636440	160355	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	CHEMBL4115297	160355	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	10979251	89615	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381650	89615	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	10979251	89615	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381650	89615	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	22317408	55985	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629850	55985	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636433	144032	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3907628	144032	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	10297067	95844	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261263	95844	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	131636277	151110	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3963950	151110	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	18548910	95475	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259340	95475	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	155565564	174987	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4579281	174987	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	155565564	174987	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4579281	174987	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	18548737	56094	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631854	56094	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44302819	162673	0	None	-	1	Human	4.1	pIC50	=	4.1	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	298	4	3	4	0.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL418462	162673	0	None	-	1	Human	4.1	pIC50	=	4.1	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	298	4	3	4	0.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	155564600	174969	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	CHEMBL4578758	174969	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	155564600	174969	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	CHEMBL4578758	174969	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	162666357	183139	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4784701	183139	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803523	183139	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	137656301	158124	0	None	-	1	Human	5.1	pIC50	=	5.1	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4093017	158124	0	None	-	1	Human	5.1	pIC50	=	5.1	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	44300389	13533	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1194613	13533	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL552984	13533	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	131636292	159967	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	353	2	0	4	4.5	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112325	159967	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	353	2	0	4	4.5	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636439	153282	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3982561	153282	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	117821004	118299	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	3	0	4	4.9	CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21	10.1021/ml5005365
	CHEMBL3421839	118299	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	3	0	4	4.9	CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21	10.1021/ml5005365
	155511336	168961	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4435396	168961	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155511336	168961	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4435396	168961	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	11235624	55997	0	None	-1	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	55997	0	None	-1	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11442010	56001	0	None	-2	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	56001	0	None	-2	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	25210562	213183	20	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay	ChEMBL		None	None	None		N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1	10.1021/acs.jmedchem.1c02004
	CHEMBL5085417	213183	20	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay	ChEMBL		None	None	None		N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1	10.1021/acs.jmedchem.1c02004
	131636350	143278	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3901364	143278	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1	nan
	117824335	118298	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	2	0	4	4.5	Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1	10.1021/ml5005365
	CHEMBL3421838	118298	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	2	0	4	4.5	Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1	10.1021/ml5005365
	49836087	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	6222	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	CHEMBL1630805	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	3335	2954	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	5311344	2954	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	CHEMBL39573	2954	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	131636449	159859	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	461	5	0	6	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4111376	159859	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	461	5	0	6	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90643970	111495	0	None	1	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	464	3	1	6	3.8	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288664	111495	0	None	1	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	464	3	1	6	3.8	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	10587622	78315	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112582	78315	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10587622	78315	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL2112582	78315	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	90643956	111486	0	None	-5	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288639	111486	0	None	-5	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	155564325	174835	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4575990	174835	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155564325	174835	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4575990	174835	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155521127	169973	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4450016	169973	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155521127	169973	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4450016	169973	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	76332991	105606	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	428	2	1	4	3.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1	10.1039/C3MD00110E
	CHEMBL3133882	105606	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	428	2	1	4	3.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1	10.1039/C3MD00110E
	76322144	105611	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	534	4	1	5	5.6	COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	CHEMBL3133887	105611	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	534	4	1	5	5.6	COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	155515940	169430	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4442453	169430	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155515940	169430	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4442453	169430	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	9888376	94758	1	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256011	94758	1	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	18548795	56092	0	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631757	56092	0	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	131636414	159695	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	483	7	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4110033	159695	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	483	7	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	131636334	149610	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3951588	149610	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636352	159876	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	CHEMBL4111531	159876	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	131636387	160361	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4115328	160361	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636371	159581	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4109036	159581	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636452	160111	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113408	160111	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	67633284	183055	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4748699	183055	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802655	183055	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636275	142317	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	5	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1	nan
	CHEMBL3893337	142317	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	5	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1	nan
	76322143	105609	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	400	3	1	5	4.4	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	CHEMBL3133885	105609	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	400	3	1	5	4.4	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	131636330	147924	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.6	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3938055	147924	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.6	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL5089623	213433	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	CHEMBL5089623	213433	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	131636318	143050	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3899445	143050	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636288	160265	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	CHEMBL4114600	160265	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	90354465	147701	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3936284	147701	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	44322537	204917	0	None	-	0	Human	6.0	pKi	=	6	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	517	7	0	7	6.2	CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1021/jm000007r
	CHEMBL89293	204917	0	None	-	0	Human	6.0	pKi	=	6	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	517	7	0	7	6.2	CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1021/jm000007r
	1393	1504	58	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	1396	1504	58	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	213056	1504	58	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	CHEMBL8759	1504	58	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	10428048	3297	26	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	3955	3297	26	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	CHEMBL305406	3297	26	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	44322840	112066	0	None	-	0	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	201	2	4	4	-1.5	N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O	10.1021/jm000007r
	CHEMBL330097	112066	0	None	-	0	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	201	2	4	4	-1.5	N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O	10.1021/jm000007r
	1415	2566	36	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	3972752	2566	36	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	CHEMBL86508	2566	36	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	1310	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	1369	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	33032	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	44272391	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	88747398	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	CHEMBL575060	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	DB00142	2276	108	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	10359073	154423	1	None	-1	2	Human	4.8	pKi	=	4.8	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL40123	154423	1	None	-1	2	Human	4.8	pKi	=	4.8	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	10197984	2378	37	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	1394	2378	37	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	CHEMBL275079	2378	37	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	3246152	160733	27	None	-	0	Human	5.7	pKi	=	5.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	4	3	3	-0.5	C[C@@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL41221	160733	27	None	-	0	Human	5.7	pKi	=	5.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	4	3	3	-0.5	C[C@@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	1297	169674	33	None	-1	2	Human	4.7	pKi	=	4.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm000007r
	CHEMBL444589	169674	33	None	-1	2	Human	4.7	pKi	=	4.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm000007r
	1378	2374	48	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	1399	2374	48	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	9819927	2374	48	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	CHEMBL432038	2374	48	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	439282	141040	6	None	-	0	Human	6.6	pKi	=	6.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	159	4	3	3	-0.6	C=C(C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL38499	141040	6	None	-	0	Human	6.6	pKi	=	6.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	159	4	3	3	-0.6	C=C(C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	11820180	17863	1	None	-	0	Human	4.6	pKi	=	4.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	4	3	6	-2.1	N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O	10.1021/jm000007r
	CHEMBL126608	17863	1	None	-	0	Human	4.6	pKi	=	4.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	4	3	6	-2.1	N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O	10.1021/jm000007r
	10058694	204867	0	None	-	0	Human	8.4	pKi	=	8.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O	10.1021/jm000007r
	CHEMBL88999	204867	0	None	-	0	Human	8.4	pKi	=	8.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O	10.1021/jm000007r
	4694355	98272	31	None	-	1	Human	4.5	pKi	=	4.5	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1021/jm000007r
	CHEMBL277961	98272	31	None	-	1	Human	4.5	pKi	=	4.5	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1021/jm000007r
	16739377	91730	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	CHEMBL242344	91730	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	16739377	91730	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	CHEMBL242344	91730	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	44322921	205100	1	None	-	0	Human	6.5	pKi	=	6.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O	10.1021/jm000007r
	CHEMBL90501	205100	1	None	-	0	Human	6.5	pKi	=	6.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O	10.1021/jm000007r
	59066632	204834	84	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	92136	204834	84	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL88804	204834	84	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	44322745	105673	0	None	-	0	Human	4.4	pKi	=	4.4	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	203	3	3	6	-2.1	C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O	10.1021/jm000007r
	CHEMBL313713	105673	0	None	-	0	Human	4.4	pKi	=	4.4	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	203	3	3	6	-2.1	C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O	10.1021/jm000007r
	1392	73	42	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	5310984	73	42	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	CHEMBL40086	73	42	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	10330132	100899	1	None	-	2	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1021/jm000007r
	CHEMBL297150	100899	1	None	-	2	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1021/jm000007r
	1368	2248	31	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	5310956	2248	31	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL280563	2248	31	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	104766	34	36	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	1365	34	36	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	CHEMBL34453	34	36	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	6324634	147399	7	None	6	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL39338	147399	7	None	6	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	1222	101254	56	None	3	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm000007r
	CHEMBL299683	101254	56	None	3	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm000007r
	10198359	73595	7	None	-10	4	Human	4.3	pKi	=	4.3	Functional	Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1021/jm000007r
	CHEMBL2021372	73595	7	None	-10	4	Human	4.3	pKi	=	4.3	Functional	Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1021/jm000007r
	44428738	168174	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	CHEMBL437169	168174	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	44428738	168174	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	CHEMBL437169	168174	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	44322529	205129	1	None	-	0	Human	7.1	pKi	=	7.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1021/jm000007r
	CHEMBL90675	205129	1	None	-	0	Human	7.1	pKi	=	7.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1021/jm000007r
	1439	2424	13	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	5311457	2424	13	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	CHEMBL41013	2424	13	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	1310	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1310	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	25195461	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	8946	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	CHEMBL3337527	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	DB12059	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	1310	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	1369	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	33032	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	44272391	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	88747398	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	CHEMBL575060	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	DB00142	2276	108	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	11281345	113	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	411	8	1	5	3.3	CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1	15717213
	6258	113	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	411	8	1	5	3.3	CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1	15717213
	25002940	1083	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	6320	1083	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	CHEMBL2029821	1083	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	25125217	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	7678	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	CHEMBL3937907	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	DB16073	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	46182736	972	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	6323	972	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	CHEMBL1651219	972	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	46190878	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	6253	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	CHEMBL595759	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	3954	657	53	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	9868580	657	53	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	CHEMBL593013	657	53	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	3372	798	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	9864510	798	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	CHEMBL4303163	798	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	46830123	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	6321	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	CHEMBL1094763	1052	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	46190877	1833	3	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	6252	1833	3	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	CHEMBL605836	1833	3	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	6256	992	0	None	-	1	Rat	7.2	pEC50	=	7.2	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2	18812259
	73755202	992	0	None	-	1	Rat	7.2	pEC50	=	7.2	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2	18812259
	59234231	2103	1	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	2103	1	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	2103	1	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	2103	1	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	59234231	2103	1	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	2103	1	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	2103	1	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	2103	1	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6255	970	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	6	0	5	3.9	Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2	18812259
	73755201	970	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	6	0	5	3.9	Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2	18812259
	6254	968	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2	18812259
	73755200	968	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2	18812259
	44335556	1268	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	6257	1268	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	CHEMBL321968	1268	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	44595851	3730	1	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	6259	3730	1	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	CHEMBL4092105	3730	1	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	49765871	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	6317	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	11362035	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	6328	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	6329	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	CHEMBL105296	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	44595851	3730	1	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	6259	3730	1	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	CHEMBL4092105	3730	1	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	3335	2954	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	5311344	2954	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	CHEMBL39573	2954	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	1402	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	1402	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	1402	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	1402	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	9825084	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	9825084	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	9825084	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	9825084	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	CHEMBL108939	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	CHEMBL108939	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	CHEMBL108939	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	CHEMBL108939	122	36	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	49858117	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	6223	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	CHEMBL1630806	1068	3	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	49858118	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	6224	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	CHEMBL1630807	1087	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	49836087	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	6222	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	CHEMBL1630805	1041	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	10428048	3297	26	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	3955	3297	26	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	CHEMBL305406	3297	26	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	6219	2538	0	None	-1	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	73755191	2538	0	None	-1	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	6221	2540	0	None	-2	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	73755193	2540	0	None	-2	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	11158623	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	11158623	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6226	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	CHEMBL1629855	3287	7	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6219	2538	0	None	1	3	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	73755191	2538	0	None	1	3	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	6220	2539	0	None	-1	3	Rat	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	73755192	2539	0	None	-1	3	Rat	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	6220	2539	0	None	1	3	Human	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	73755192	2539	0	None	1	3	Human	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	11158623	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6226	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	CHEMBL1629855	3287	7	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6221	2540	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	73755193	2540	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	6324	3289	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	73755205	3289	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	10047169	3161	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	1403	3161	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	CHEMBL182371	3161	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	10275802	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	10275802	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	10275802	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	1401	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	1401	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	1401	107	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213

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Ligands					Receptor			Assay information							Chemical information
Sel. page	Common name	GPCRdb ID	#Vendors	Reference ligand	Fold selectivity (Affinity)	# tested GPCRs (Affinity)	Species	p-value (-log)	Type	Activity Relation	Activity Value	Assay Type	Assay Description	Source	Mol weight	Rot Bonds	H don	H acc	LogP	Smiles	DOI
	9794208	89605	4	None	-	0	Human	9.8	pEC50	=	9.8	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	4	-1.3	N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381640	89605	4	None	-	0	Human	9.8	pEC50	=	9.8	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	4	-1.3	N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	139119037	89617	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	15479143	89617	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381652	89617	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	70051926	89606	2	None	-	0	Human	8.9	pEC50	=	8.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	197	2	3	3	-0.3	C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381641	89606	2	None	-	0	Human	8.9	pEC50	=	8.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	197	2	3	3	-0.3	C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	44335501	109156	0	None	-	0	Human	7.0	pEC50	=	7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL322465	109156	0	None	-	0	Human	7.0	pEC50	=	7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	50993966	57018	0	None	-	0	Rat	7.0	pEC50	=	7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	449	7	1	3	5.9	CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651212	57018	0	None	-	0	Rat	7.0	pEC50	=	7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	449	7	1	3	5.9	CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	24815976	198067	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593745	198067	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24815883	199767	0	None	-	2	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604993	199767	0	None	-	2	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225581	200293	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL608103	200293	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	11768848	114740	11	None	-	1	Human	5.0	pEC50	=	5	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347671	114740	11	None	-	1	Human	5.0	pEC50	=	5	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	10198359	73595	7	None	-	1	Human	5.0	pEC50	=	5	Binding	Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1016/s0960-894x(98)00265-0
	CHEMBL2021372	73595	7	None	-	1	Human	5.0	pEC50	=	5	Binding	Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1016/s0960-894x(98)00265-0
	90643871	111359	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287693	111359	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	164617451	184359	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1	10.1016/j.bmcl.2021.128342
	CHEMBL4853794	184359	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1	10.1016/j.bmcl.2021.128342
	90643884	111385	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287719	111385	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	89735528	137457	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	10.1016/j.bmcl.2016.01.021
	CHEMBL3764544	137457	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	10.1016/j.bmcl.2016.01.021
	90643857	111388	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287722	111388	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	10050046	65727	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	463	12	2	7	3.5	CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL183756	65727	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	463	12	2	7	3.5	CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	11656255	122782	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	498	8	1	5	6.9	CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361570	122782	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	498	8	1	5	6.9	CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643896	111370	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	CHEMBL3287704	111370	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	68109941	155569	0	None	-	1	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	155569	0	None	-	1	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	53390518	82268	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1	10.1021/jm3005306
	CHEMBL2179635	82268	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1	10.1021/jm3005306
	53390519	82269	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	441	6	1	3	5.8	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179636	82269	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	441	6	1	3	5.8	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	23521689	4759	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104248	4759	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	89735510	137358	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763263	137358	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21	10.1016/j.bmcl.2016.01.021
	164610619	184161	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4850952	184161	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	164627219	185789	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4875653	185789	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	44578904	180977	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	409	6	0	4	5.0	Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476791	180977	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	409	6	0	4	5.0	Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	90643904	111379	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287713	111379	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	90643900	111374	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287708	111374	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O	10.1021/jm5000563
	71117141	146904	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	CHEMBL3930164	146904	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	69929497	139745	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	434	3	0	7	2.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805900	139745	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	434	3	0	7	2.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21	10.1021/acsmedchemlett.5b00459
	90643881	111380	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287714	111380	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	11648184	62699	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	454	5	1	4	5.9	CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL178823	62699	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	454	5	1	4	5.9	CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71681826	89616	0	None	-4	2	Human	5.9	pEC50	=	5.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381651	89616	0	None	-4	2	Human	5.9	pEC50	=	5.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	162649186	183052	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4748285	183052	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802609	183052	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	1310	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	2276	108	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	71681825	89610	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381645	89610	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	104766	34	36	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	34	36	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	34	36	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	11583075	63145	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	442	5	1	5	5.3	O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	CHEMBL179939	63145	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	442	5	1	5	5.3	O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	162647509	183045	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4744407	183045	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802513	183045	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	56929215	111342	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287671	111342	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643902	111377	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	390	10	2	5	4.4	CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287711	111377	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	390	10	2	5	4.4	CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	67056056	139658	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	429	2	0	7	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804910	139658	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	429	2	0	7	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21	10.1021/acsmedchemlett.5b00459
	46190878	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	6253	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	CHEMBL595759	1834	3	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	46225407	198045	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593532	198045	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21	10.1016/j.bmcl.2009.11.032
	46225359	198137	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	418	5	0	6	3.9	Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	CHEMBL594236	198137	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	418	5	0	6	3.9	Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	46225334	198353	0	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595607	198353	0	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225358	200167	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	485	5	0	5	5.5	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1	10.1016/j.bmcl.2009.11.032
	CHEMBL607195	200167	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	485	5	0	5	5.5	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1	10.1016/j.bmcl.2009.11.032
	24815439	200241	0	None	-	3	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607689	200241	0	None	-	3	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225384	198205	5	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	328	3	1	5	2.3	Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	CHEMBL594673	198205	5	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	328	3	1	5	2.3	Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	46225383	198404	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	395	3	1	4	4.0	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1	10.1016/j.bmcl.2009.11.032
	CHEMBL595991	198404	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	395	3	1	4	4.0	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1	10.1016/j.bmcl.2009.11.032
	69929646	139776	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	329	2	1	6	1.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806226	139776	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	329	2	1	6	1.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21	10.1021/acsmedchemlett.5b00459
	127038185	137403	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	248	2	0	4	2.4	COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3763995	137403	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	248	2	0	4	2.4	COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	90643868	111356	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287690	111356	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	164608826	183875	0	None	-	0	Rat	7.9	pEC50	=	7.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4846872	183875	0	None	-	0	Rat	7.9	pEC50	=	7.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	68108429	149135	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	448	5	0	4	5.7	FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3947590	149135	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	448	5	0	4	5.7	FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	53390677	82262	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	451	6	1	5	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179629	82262	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	451	6	1	5	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	53390520	82270	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	445	6	1	3	5.7	O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	CHEMBL2179637	82270	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	445	6	1	3	5.7	O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	6604704	100917	32	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970719q
	CHEMBL29726	100917	32	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970719q
	49822195	145637	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3919978	145637	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	162657776	183091	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4759458	183091	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803052	183091	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	25195461	2104	42	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	86765132	111391	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	428	10	2	5	5.6	Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287725	111391	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	428	10	2	5	5.6	Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	164613604	184591	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4857426	184591	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	11362035	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	6328	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	6329	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	CHEMBL105296	43	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	23521659	4762	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	6	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104260	4762	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	6	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	23521713	109268	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL323138	109268	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	49822116	146447	7	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	44395191	65953	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.6	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL184838	65953	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.6	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	164621278	184940	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862801	184940	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	49765871	2105	40	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	6317	2105	40	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	CHEMBL2179319	2105	40	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	90643858	111361	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	111361	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	90643905	111381	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287715	111381	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	67056141	139666	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	4	0	8	2.9	Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1	10.1021/acsmedchemlett.5b00459
	CHEMBL3805017	139666	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	4	0	8	2.9	Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1	10.1021/acsmedchemlett.5b00459
	68107810	145609	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3919807	145609	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	68108457	148012	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3938796	148012	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	127039577	137425	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	462	6	1	5	5.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764173	137425	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	462	6	1	5	5.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21	10.1016/j.bmcl.2016.01.021
	9885608	4767	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1021/jm034015u
	CHEMBL104296	4767	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1021/jm034015u
	9885608	4767	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104296	4767	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	90643863	111351	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287683	111351	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643865	111353	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287687	111353	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643878	111367	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287701	111367	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	90668092	109036	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221831	109036	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	46225371	198131	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	453	6	0	6	4.1	COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594204	198131	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	453	6	0	6	4.1	COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225372	199670	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	356	4	0	6	2.8	CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604472	199670	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	356	4	0	6	2.8	CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225582	199920	0	None	-	2	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL605831	199920	0	None	-	2	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	3461070	116830	1	None	-	0	Human	4.8	pEC50	=	4.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	307	3	0	5	2.3	Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL339714	116830	1	None	-	0	Human	4.8	pEC50	=	4.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	307	3	0	5	2.3	Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44335554	108723	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL321746	108723	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	71479388	139680	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805139	139680	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	23521708	4742	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104191	4742	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	23521727	4818	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104541	4818	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	44335514	4867	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.3	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104785	4867	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.3	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	44404948	70195	0	None	-	1	Rat	4.8	pEC50	=	4.8	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	CHEMBL194787	70195	0	None	-	1	Rat	4.8	pEC50	=	4.8	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	1310	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	2276	108	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	90643895	111369	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	CHEMBL3287703	111369	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	90643880	111375	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287709	111375	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	24905705	183430	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	183430	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	25195461	2104	42	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	164616255	184355	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	445	10	2	5	5.1	CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F	10.1016/j.bmcl.2021.128342
	CHEMBL4853748	184355	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	445	10	2	5	5.1	CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F	10.1016/j.bmcl.2021.128342
	11663312	63124	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	497	7	0	4	7.8	O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	CHEMBL179839	63124	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	497	7	0	4	7.8	O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	24905705	183430	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	183430	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	44335555	4952	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.4	CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105193	4952	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.4	CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	49765871	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	134156113	150326	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	483	5	0	5	5.3	FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3957311	150326	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	483	5	0	5	5.3	FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	71117730	143387	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	CHEMBL3902193	143387	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	46182736	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	6323	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	CHEMBL1651219	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	53390521	82271	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O	10.1021/jm3005306
	CHEMBL2179638	82271	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O	10.1021/jm3005306
	46182736	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	6323	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	CHEMBL1651219	972	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	1402	122	36	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	9825084	122	36	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	CHEMBL108939	122	36	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	90643882	111382	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	10	2	5	4.6	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O	10.1021/jm5000563
	CHEMBL3287716	111382	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	10	2	5	4.6	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O	10.1021/jm5000563
	90643876	111365	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287699	111365	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	44335578	109173	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.2	CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL322588	109173	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.2	CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	66787355	155672	0	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	155672	0	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	23521698	108046	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	384	7	0	3	4.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL320151	108046	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	384	7	0	3	4.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11648824	57013	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	488	6	1	3	7.4	Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1021/jm1012165
	CHEMBL1651207	57013	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	488	6	1	3	7.4	Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1021/jm1012165
	1310	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1369	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	33032	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	44272391	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	88747398	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	CHEMBL575060	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	DB00142	2276	108	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1310	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	2276	108	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	89497771	137454	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764530	137454	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21	10.1016/j.bmcl.2016.01.021
	1310	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	2276	108	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	10407808	66327	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	386	11	2	5	4.5	CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185419	66327	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	386	11	2	5	4.5	CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643887	111389	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287723	111389	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	89735344	137503	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	0	5	3.5	COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765257	137503	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	0	5	3.5	COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	11213605	64119	2	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	8	0	4	7.4	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL181364	64119	2	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	8	0	4	7.4	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	127042771	137512	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765337	137512	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21	10.1016/j.bmcl.2016.01.021
	90643869	111357	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287691	111357	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	89497792	137495	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765103	137495	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21	10.1016/j.bmcl.2016.01.021
	164611067	184023	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4849142	184023	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	11633075	65044	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	5	1	5	4.8	CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL182946	65044	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	5	1	5	4.8	CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	25125217	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	7678	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3937907	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	DB16073	549	17	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	24815434	198004	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593196	198004	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225335	198354	0	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595608	198354	0	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225583	198480	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596527	198480	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225408	200179	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607313	200179	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21	10.1016/j.bmcl.2009.11.032
	46225387	198071	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	477	3	0	5	5.0	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593756	198071	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	477	3	0	5	5.0	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21	10.1016/j.bmcl.2009.11.032
	56968082	143367	0	None	-	0	Human	8.6	pEC50	=	8.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	428	5	0	4	5.3	CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1	10.1021/acs.jmedchem.6b00913
	CHEMBL3901998	143367	0	None	-	0	Human	8.6	pEC50	=	8.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	428	5	0	4	5.3	CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1	10.1021/acs.jmedchem.6b00913
	25051025	181875	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL478646	181875	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	53390433	82265	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	443	6	2	4	5.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O	10.1021/jm3005306
	CHEMBL2179632	82265	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	443	6	2	4	5.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O	10.1021/jm3005306
	66799514	82277	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	431	4	1	2	6.3	O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179646	82277	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	431	4	1	2	6.3	O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	23521677	106955	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL318309	106955	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1	10.1016/j.bmcl.2004.04.017
	53390754	82274	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	490	7	1	7	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1	10.1021/jm3005306
	CHEMBL2179643	82274	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	490	7	1	7	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1	10.1021/jm3005306
	90643897	111371	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287705	111371	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	104766	34	36	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	1365	34	36	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	CHEMBL34453	34	36	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	25195461	2104	42	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	10002415	165462	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	423	11	2	7	4.0	CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL425540	165462	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	423	11	2	7	4.0	CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643889	111392	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1021/jm5000563
	CHEMBL3287726	111392	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1021/jm5000563
	49822115	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	8947	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL3947764	2106	17	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11275666	89612	1	None	-15	2	Human	7.7	pEC50	=	7.7	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381647	89612	1	None	-15	2	Human	7.7	pEC50	=	7.7	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	164627946	185792	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4875695	185792	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	44335500	5038	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.0	COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105671	5038	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.0	COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	23521734	109259	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL323080	109259	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	25051018	183757	0	None	-	0	Rat	5.7	pEC50	=	5.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	334	5	0	5	2.7	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21	10.1016/j.bmcl.2008.09.026
	CHEMBL484398	183757	0	None	-	0	Rat	5.7	pEC50	=	5.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	334	5	0	5	2.7	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21	10.1016/j.bmcl.2008.09.026
	54761054	137540	0	None	-	2	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	137540	0	None	-	2	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	71136691	143077	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	CHEMBL3899706	143077	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	134157889	153670	0	None	-	0	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	465	5	0	5	4.7	Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3985987	153670	0	None	-	0	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	465	5	0	5	4.7	Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	50993967	57019	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	433	6	1	3	5.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651213	57019	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	433	6	1	3	5.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	51037131	139741	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	356	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805883	139741	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	356	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21	10.1021/acsmedchemlett.5b00459
	90643860	111344	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287675	111344	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	164611059	183986	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4848600	183986	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	11496256	63440	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180186	63440	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	11656483	123073	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	514	9	1	6	6.3	CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361837	123073	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	514	9	1	6	6.3	CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643873	111362	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	13	2	6	5.4	Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287696	111362	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	13	2	6	5.4	Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	9979770	65991	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185054	65991	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	49765871	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	44335614	5200	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	446	9	0	6	3.3	CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL106561	5200	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	446	9	0	6	3.3	CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	45082292	114739	2	None	-3	3	Human	4.6	pEC50	=	4.6	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347670	114739	2	None	-3	3	Human	4.6	pEC50	=	4.6	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	90643906	111383	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287717	111383	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	49822116	146447	7	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	90643875	111364	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287698	111364	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578992	181030	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	333	5	0	4	3.3	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477376	181030	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	333	5	0	4	3.3	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	44335556	1268	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	6257	1268	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	CHEMBL321968	1268	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	53390753	82275	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F	10.1021/jm3005306
	CHEMBL2179644	82275	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F	10.1021/jm3005306
	44395327	66576	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	438	11	2	7	4.7	CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL186584	66576	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	438	11	2	7	4.7	CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643862	111350	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	458	11	1	4	6.7	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	CHEMBL3287682	111350	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	458	11	1	4	6.7	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	44401995	69718	1	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	13	3	6	4.9	Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL193982	69718	1	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	13	3	6	4.9	Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	71117222	145540	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3919237	145540	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	53390676	82259	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	7	1	5	6.1	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179626	82259	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	7	1	5	6.1	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	54761054	137540	0	None	-	2	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	137540	0	None	-	2	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	44335650	4719	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	7	1	4	3.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104129	4719	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	7	1	4	3.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	25050850	191182	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL519817	191182	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	46225385	199668	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	439	4	0	6	4.0	COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C	10.1016/j.bmcl.2009.11.032
	CHEMBL604469	199668	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	439	4	0	6	4.0	COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C	10.1016/j.bmcl.2009.11.032
	46225375	200178	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	437	5	0	5	4.8	CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607311	200178	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	437	5	0	5	4.8	CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	60096211	89614	0	None	-5	2	Human	6.6	pEC50	=	6.6	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381649	89614	0	None	-5	2	Human	6.6	pEC50	=	6.6	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	164619969	184937	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862778	184937	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	2104	42	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	90643891	111347	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	424	11	1	4	6.0	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	CHEMBL3287678	111347	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	424	11	1	4	6.0	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	90643898	111372	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	376	9	2	5	4.0	CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287706	111372	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	376	9	2	5	4.0	CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	44578946	181010	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	375	6	0	4	4.5	CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL477169	181010	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	375	6	0	4	4.5	CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	44578947	181011	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	367	5	0	4	4.0	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477170	181011	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	367	5	0	4	4.0	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	25110722	188936	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL514218	188936	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	68108294	146742	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	444	6	0	5	4.8	COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3928875	146742	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	444	6	0	5	4.8	COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	68108567	153207	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3981882	153207	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	89735130	137410	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764057	137410	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	71128768	144035	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3907644	144035	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	50993968	57020	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	469	6	1	3	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651214	57020	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	469	6	1	3	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	164619502	185608	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4872955	185608	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	2104	42	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	44335577	5790	3	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.0	CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL107948	5790	3	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.0	CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	49765871	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11677757	65755	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	500	8	1	6	6.0	CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183911	65755	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	500	8	1	6	6.0	CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	1402	122	36	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	9825084	122	36	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	CHEMBL108939	122	36	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	50994049	57021	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.6	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651215	57021	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.6	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	11598292	129640	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	486	7	1	6	5.6	CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL367823	129640	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	486	7	1	6	5.6	CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	164611777	184332	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4853369	184332	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	164621310	184973	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	429	10	2	6	5.0	Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4863303	184973	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	429	10	2	6	5.0	Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	11344646	126242	1	None	-1	2	Human	7.5	pEC50	=	7.5	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL365368	126242	1	None	-1	2	Human	7.5	pEC50	=	7.5	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	162650303	183056	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4748549	183056	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802664	183056	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	11625861	65514	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	6	1	5	4.9	CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183541	65514	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	6	1	5	4.9	CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71136188	145210	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	CHEMBL3916627	145210	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	44335626	5307	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	4.7	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL107114	5307	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	4.7	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1	10.1016/j.bmcl.2004.04.017
	51036108	139684	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805203	139684	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	127052897	139765	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	139765	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	1310	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	1369	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	33032	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	44272391	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	88747398	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	CHEMBL575060	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	DB00142	2276	108	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	11697718	63836	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	431	8	0	4	6.7	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180871	63836	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	431	8	0	4	6.7	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O	10.1016/j.bmcl.2005.01.077
	164624801	185619	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4873125	185619	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71136186	151525	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	CHEMBL3967432	151525	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	25110723	189037	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL515034	189037	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	1377	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	5310979	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL284193	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	50994823	57025	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651221	57025	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	44578996	180993	0	None	-	0	Rat	5.5	pEC50	=	5.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	6	0	4	4.1	c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476965	180993	0	None	-	0	Rat	5.5	pEC50	=	5.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	6	0	4	4.1	c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	10251009	66433	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.1	CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185911	66433	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.1	CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	164611874	184521	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4856242	184521	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	56651050	137418	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	294	2	0	3	4.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764108	137418	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	294	2	0	3	4.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21	10.1016/j.bmcl.2016.01.021
	44335670	4879	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104818	4879	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	50994757	57024	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651220	57024	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl	10.1021/jm1012165
	89735684	137486	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1	10.1016/j.bmcl.2016.01.021
	CHEMBL3764850	137486	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1	10.1016/j.bmcl.2016.01.021
	46225336	198355	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595609	198355	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225320	199488	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL603443	199488	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225569	199667	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604467	199667	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44335573	4741	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	388	7	0	4	3.8	CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104190	4741	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	388	7	0	4	3.8	CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	10846649	100748	4	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O	10.1021/jm970719q
	CHEMBL296054	100748	4	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O	10.1021/jm970719q
	11743092	64244	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	12	2	7	4.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL181648	64244	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	12	2	7	4.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	51036916	139770	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	350	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806176	139770	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	350	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21	10.1021/acsmedchemlett.5b00459
	90643893	111349	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287680	111349	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	9999945	66787	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	382	9	2	7	3.3	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187537	66787	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	382	9	2	7	3.3	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	90643883	111384	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O	10.1021/jm5000563
	CHEMBL3287718	111384	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O	10.1021/jm5000563
	10047169	3161	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	1403	3161	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	CHEMBL182371	3161	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	1377	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	5310979	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL284193	1308	19	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	53321382	57022	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	551	7	1	3	7.5	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651216	57022	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	551	7	1	3	7.5	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	59066632	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	92136	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	CHEMBL88804	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	6603885	101718	17	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	6971208	101718	17	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	CHEMBL30285	101718	17	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	59066632	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	92136	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	CHEMBL88804	204834	84	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	23521697	4943	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	400	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105151	4943	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	400	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1	10.1016/j.bmcl.2004.04.017
	69930179	139729	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	433	3	0	6	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805718	139729	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	433	3	0	6	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21	10.1021/acsmedchemlett.5b00459
	23521709	163902	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL421406	163902	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	44404948	70195	0	None	-	1	Rat	4.4	pEC50	=	4.4	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	CHEMBL194787	70195	0	None	-	1	Rat	4.4	pEC50	=	4.4	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	69929785	139652	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	407	3	0	8	2.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804845	139652	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	407	3	0	8	2.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21	10.1021/acsmedchemlett.5b00459
	9837114	114753	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	CHEMBL334842	114753	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	9837114	114753	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	CHEMBL334842	114753	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	11691077	64348	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL181869	64348	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	164624284	185437	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4870631	185437	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	54761055	137348	1	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763172	137348	1	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21	10.1016/j.bmcl.2016.01.021
	69092138	142251	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3892865	142251	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	1368	2248	31	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	5310956	2248	31	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL280563	2248	31	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	10318576	66365	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.7	CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185602	66365	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.7	CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	3954	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	9868580	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	CHEMBL593013	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	3954	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	9868580	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	CHEMBL593013	657	53	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	10560963	163954	1	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	CHEMBL42148	163954	1	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	164610692	184309	0	None	-	0	Rat	5.4	pEC50	=	5.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	459	10	1	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4853089	184309	0	None	-	0	Rat	5.4	pEC50	=	5.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	459	10	1	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	49765871	2105	40	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	46225584	197983	0	None	-	3	Human	7.4	pEC50	=	7.4	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593056	197983	0	None	-	3	Human	7.4	pEC50	=	7.4	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	49765871	2105	40	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	90643858	111361	0	None	-	0	Rat	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	111361	0	None	-	0	Rat	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	71116701	144314	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	CHEMBL3909811	144314	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	1310	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	1369	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	33032	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	44272391	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	88747398	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	CHEMBL575060	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	DB00142	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	1310	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	2276	108	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	139054390	203205	101	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	23327	203205	101	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	CHEMBL76232	203205	101	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	10465478	21570	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	CHEMBL131922	21570	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	10465478	21570	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	CHEMBL131922	21570	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	90643892	111348	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287679	111348	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	25050849	183650	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21	10.1016/j.bmcl.2008.09.026
	CHEMBL483569	183650	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21	10.1016/j.bmcl.2008.09.026
	23521725	5609	0	None	-	0	Human	5.4	pEC50	=	5.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL107806	5609	0	None	-	0	Human	5.4	pEC50	=	5.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	10026879	66679	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	13	2	7	5.0	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187077	66679	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	13	2	7	5.0	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	90643879	111368	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	12	2	6	5.4	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287702	111368	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	12	2	6	5.4	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	51036701	139656	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	302	2	0	5	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804903	139656	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	302	2	0	5	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21	10.1021/acsmedchemlett.5b00459
	71116772	147124	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	CHEMBL3931730	147124	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	23521693	5268	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL106909	5268	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11496550	63545	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	473	5	1	4	5.8	CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1	10.1016/j.bmcl.2005.01.077
	CHEMBL180455	63545	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	473	5	1	4	5.8	CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1	10.1016/j.bmcl.2005.01.077
	164615875	184852	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4861618	184852	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	49822116	146447	7	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	90643861	111345	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287676	111345	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	90643867	111355	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287689	111355	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	49765871	2105	40	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	127038550	137522	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765412	137522	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21	10.1016/j.bmcl.2016.01.021
	90643888	111390	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287724	111390	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	71681824	89611	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381646	89611	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	53390605	82261	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	467	7	1	5	6.3	CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179628	82261	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	467	7	1	5	6.3	CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	1310	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	2276	108	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	164623088	184893	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862244	184893	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71574840	85830	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL2312685	85830	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	89497505	137388	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	378	3	1	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763754	137388	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	378	3	1	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	164610947	184659	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	415	10	2	6	4.7	Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4858387	184659	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	415	10	2	6	4.7	Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71574840	85830	0	None	-	0	Rat	4.3	pEC50	=	4.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL2312685	85830	0	None	-	0	Rat	4.3	pEC50	=	4.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	44395282	122628	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL361248	122628	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	46182745	57014	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL1651208	57014	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	46182745	57014	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651208	57014	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	90643899	111373	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287707	111373	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	164620553	185177	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4866466	185177	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	46225386	198070	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	434	3	0	6	3.8	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593755	198070	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	434	3	0	6	3.8	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21	10.1016/j.bmcl.2009.11.032
	11690041	64522	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	408	6	1	5	4.5	CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL182138	64522	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	408	6	1	5	4.5	CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	104766	34	36	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	34	36	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	34	36	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	46225373	198132	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	386	6	0	7	2.4	COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594205	198132	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	386	6	0	7	2.4	COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225337	198284	0	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595151	198284	0	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	851990	198013	5	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	306	3	0	4	2.9	Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593300	198013	5	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	306	3	0	4	2.9	Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	164618046	184870	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	471	10	1	6	5.1	COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4861837	184870	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	471	10	1	6	5.1	COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	71116730	148518	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	CHEMBL3942904	148518	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	90643864	111352	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287684	111352	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578997	180994	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476966	180994	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	164625596	185150	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4866163	185150	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	11699129	131430	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	509	6	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL369526	131430	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	509	6	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643885	111386	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287720	111386	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	117972250	141768	3	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	141768	3	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71128783	139665	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	397	3	0	7	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805005	139665	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	397	3	0	7	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21	10.1021/acsmedchemlett.5b00459
	162677305	183201	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4800093	183201	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4804159	183201	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	71116952	146769	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3929070	146769	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	10775369	177780	1	None	-	0	Human	4.3	pEC50	=	4.3	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	CHEMBL46527	177780	1	None	-	0	Human	4.3	pEC50	=	4.3	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	11684927	63131	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	511	7	0	4	8.2	CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL179876	63131	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	511	7	0	4	8.2	CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643877	111366	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287700	111366	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	68108604	146859	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	480	7	0	5	5.2	Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3929786	146859	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	480	7	0	5	5.2	Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	68107740	150999	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	466	6	0	5	5.0	Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3963034	150999	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	466	6	0	5	5.0	Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	89735006	137405	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3764005	137405	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	88593167	150214	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	482	5	0	4	5.8	FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3956434	150214	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	482	5	0	4	5.8	FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	53390675	82260	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	6	1	5	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179627	82260	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	6	1	5	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	11676185	65244	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	422	7	1	5	4.8	CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183234	65244	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	422	7	1	5	4.8	CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	44390403	121809	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	457	7	0	4	7.1	Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2005.01.077
	CHEMBL359909	121809	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	457	7	0	4	7.1	Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2005.01.077
	50994051	57023	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	8	1	3	6.3	CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651217	57023	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	8	1	3	6.3	CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	11663353	122709	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	499	6	2	6	5.1	CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361358	122709	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	499	6	2	6	5.1	CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	54761054	137540	0	None	-	2	Human	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	137540	0	None	-	2	Human	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	90643870	111358	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287692	111358	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	54761054	137540	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	137540	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	11691314	181308	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	470	6	2	4	6.5	Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	CHEMBL4779278	181308	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	470	6	2	4	6.5	Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	162660656	183114	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4762369	183114	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803219	183114	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	90643901	111376	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287710	111376	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	23521692	108073	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	436	8	0	4	4.6	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL320292	108073	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	436	8	0	4	4.6	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11691221	122798	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	464	5	1	5	5.4	CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361633	122798	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	464	5	1	5	5.4	CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	54761054	137540	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1021/acsmedchemlett.5b00459
	CHEMBL3765778	137540	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1021/acsmedchemlett.5b00459
	164616933	184472	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4855540	184472	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	46225357	198105	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	423	4	0	5	4.4	CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594011	198105	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	423	4	0	5	4.4	CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	11310142	2379	16	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	11614	2379	16	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	CHEMBL192051	2379	16	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	51036108	139684	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805203	139684	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	90643872	111360	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287694	111360	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	25050844	183651	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL483570	183651	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	44335613	168563	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	432	9	0	6	2.9	CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL440328	168563	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	432	9	0	6	2.9	CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	53390678	82258	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	425	5	1	5	5.2	Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179625	82258	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	425	5	1	5	5.2	Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	69093542	146882	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3929950	146882	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	25195461	2104	42	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	53390604	82263	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	481	8	1	5	6.7	CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179630	82263	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	481	8	1	5	6.7	CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	49822116	146447	7	None	-	1	Human	5.2	pEC50	=	5.2	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	5.2	pEC50	=	5.2	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	127052897	139765	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	139765	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	11568710	179829	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	CHEMBL4752318	179829	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	71116726	144731	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	CHEMBL3912982	144731	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	90643866	111354	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287688	111354	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578905	180996	0	None	-	0	Rat	8.2	pEC50	=	8.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	5	0	4	3.6	Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476998	180996	0	None	-	0	Rat	8.2	pEC50	=	8.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	5	0	4	3.6	Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	11084869	89608	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381643	89608	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	70052526	89607	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381642	89607	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	50993963	57015	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	435	6	1	3	5.6	CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651209	57015	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	435	6	1	3	5.6	CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	89735186	137363	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	295	2	0	4	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763395	137363	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	295	2	0	4	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21	10.1016/j.bmcl.2016.01.021
	10249222	4927	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105065	4927	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	90643886	111387	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	11	2	5	4.8	CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287721	111387	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	11	2	5	4.8	CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	53390680	82273	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	459	6	1	5	6.4	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1	10.1021/jm3005306
	CHEMBL2179642	82273	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	459	6	1	5	6.4	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1	10.1021/jm3005306
	1310	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	1369	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	33032	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	44272391	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	88747398	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	CHEMBL575060	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	DB00142	2276	108	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	127052897	139765	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	139765	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	164614107	184537	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4856556	184537	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	1368	2248	31	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	5310956	2248	31	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL280563	2248	31	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	44395381	65793	0	None	-	0	Human	5.1	pEC50	=	5.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	10	2	8	3.5	CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL184098	65793	0	None	-	0	Human	5.1	pEC50	=	5.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	10	2	8	3.5	CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	11539379	65252	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	436	8	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183286	65252	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	436	8	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	25195461	2104	42	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	104766	34	36	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	34	36	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	34	36	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	49822116	146447	7	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	168278157	189755	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	435	4	0	3	6.4	Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1016/j.bmc.2022.116614
	CHEMBL5177038	189755	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	435	4	0	3	6.4	Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1016/j.bmc.2022.116614
	164616491	184799	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4860693	184799	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	23521714	4723	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104140	4723	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1	10.1016/j.bmcl.2004.04.017
	11516962	63551	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	402	4	1	5	4.5	CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180488	63551	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	402	4	1	5	4.5	CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	46190877	1833	3	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	6252	1833	3	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	CHEMBL605836	1833	3	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	24849462	198066	0	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593744	198066	0	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225374	198162	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	370	5	0	6	3.2	CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594428	198162	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	370	5	0	6	3.2	CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24849789	198440	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596270	198440	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	798232	198441	9	None	-	1	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	340	3	0	4	3.5	Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596271	198441	9	None	-	1	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	340	3	0	4	3.5	Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44578948	181029	0	None	-	0	Rat	8.1	pEC50	=	8.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	385	5	0	4	4.1	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477375	181029	0	None	-	0	Rat	8.1	pEC50	=	8.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	385	5	0	4	4.1	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	71681823	89609	0	None	-	0	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381644	89609	0	None	-	0	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	66799669	82264	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179631	82264	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	53390432	82266	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	487	8	1	5	5.5	COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179633	82266	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	487	8	1	5	5.5	COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	50993964	57016	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	7	1	3	5.7	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651210	57016	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	7	1	3	5.7	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	89735530	137483	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764820	137483	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21	10.1016/j.bmcl.2016.01.021
	164620998	185281	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4868114	185281	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	89735654	137408	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	313	2	0	4	3.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764024	137408	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	313	2	0	4	3.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21	10.1016/j.bmcl.2016.01.021
	90643903	111378	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287712	111378	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	90643859	111343	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287672	111343	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	69092138	148191	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3940264	148191	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	164612248	184297	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4852903	184297	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	11648510	62923	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	7	0	4	7.3	CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL179171	62923	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	7	0	4	7.3	CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	11712790	180664	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	484	7	1	4	6.8	COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O	10.1016/j.bmcl.2020.127212
	CHEMBL4761801	180664	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	484	7	1	4	6.8	COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O	10.1016/j.bmcl.2020.127212
	44578949	180951	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	401	5	0	4	4.3	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476551	180951	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	401	5	0	4	4.3	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	25050845	183796	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL484578	183796	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	86691853	137533	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	339	3	1	5	3.2	Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765537	137533	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	339	3	1	5	3.2	Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	164609025	183849	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	10	2	5	5.9	Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4846460	183849	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	10	2	5	5.9	Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	10343566	66352	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	446	9	2	7	3.8	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185529	66352	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	446	9	2	7	3.8	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	44335615	109564	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	460	9	0	6	3.7	CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL323541	109564	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	460	9	0	6	3.7	CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	71119170	148228	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3940610	148228	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	66786069	155908	0	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	155908	0	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11654949	47192	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	432	5	1	3	6.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL154542	47192	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	432	5	1	3	6.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71136746	148056	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	148056	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	68107813	144446	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3910866	144446	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	53390517	82267	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	CHEMBL2179634	82267	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	50993965	57017	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	6	1	3	5.8	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651211	57017	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	6	1	3	5.8	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	44395299	66700	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187151	66700	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	162644103	183027	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4777845	183027	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802343	183027	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	10413231	124504	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	488	11	2	7	4.8	CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL364324	124504	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	488	11	2	7	4.8	CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	10070087	66886	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	409	11	3	7	4.0	CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187959	66886	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	409	11	3	7	4.0	CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	162646759	183040	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4740929	183040	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802473	183040	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	90643874	111363	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287697	111363	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	44578903	180976	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	3.7	c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476790	180976	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	3.7	c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	44578995	180974	0	None	-	0	Rat	5.0	pEC50	=	5.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	330	5	0	3	4.0	c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476756	180974	0	None	-	0	Rat	5.0	pEC50	=	5.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	330	5	0	3	4.0	c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	90643890	111346	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	398	11	1	4	5.5	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C	10.1021/jm5000563
	CHEMBL3287677	111346	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	398	11	1	4	5.5	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C	10.1021/jm5000563
	49822116	146447	7	None	-	1	Human	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	162666879	183141	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4786847	183141	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803552	183141	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	53390837	82276	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	506	6	0	5	6.8	CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179645	82276	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	506	6	0	5	6.8	CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	89554832	142257	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	484	7	2	6	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3892899	142257	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	484	7	2	6	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71565964	143706	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	CHEMBL3904730	143706	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	124201729	146017	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	CHEMBL3922857	146017	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	89554927	146337	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	1	5	3.7	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1	nan
	CHEMBL3925389	146337	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	1	5	3.7	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1	nan
	71566125	146505	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	CHEMBL3926942	146505	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	89554857	147554	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3935153	147554	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	71565965	147740	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	CHEMBL3936681	147740	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	71566127	148093	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	CHEMBL3939455	148093	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	89554768	148907	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	CHEMBL3946016	148907	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	71566207	149809	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3953157	149809	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554874	152925	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1	nan
	CHEMBL3979547	152925	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1	nan
	89554726	160152	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL4113710	160152	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	156012009	176773	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4637618	176773	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317767	55982	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629847	55982	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11269030	55996	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	55996	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	22317741	56103	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631863	56103	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317279	56105	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631865	56105	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566440	143098	0	None	-	0	Human	7.0	pIC50	=	7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1	nan
	CHEMBL3899883	143098	0	None	-	0	Human	7.0	pIC50	=	7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1	nan
	22224818	146133	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	4	3.9	CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL392381	146133	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	4	3.9	CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1	10.1016/j.bmcl.2007.10.026
	71565597	153410	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	4	1	4	2.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1	nan
	CHEMBL3983624	153410	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	4	1	4	2.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1	nan
	9905849	202346	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69970	202346	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71565672	150720	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	3	3.0	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3960294	150720	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	3	3.0	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554824	151993	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	6	4.3	CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3971590	151993	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	6	4.3	CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	89554770	143547	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903459	143547	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554787	149365	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	455	5	1	6	3.4	NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3949371	149365	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	455	5	1	6	3.4	NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554900	150612	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	CHEMBL3959588	150612	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	89554749	151461	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	151461	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	89554828	159658	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1	nan
	CHEMBL4109697	159658	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1	nan
	89545222	159819	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4111091	159819	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	10115228	95713	0	None	-	0	Rat	8.0	pIC50	=	8.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260642	95713	0	None	-	0	Rat	8.0	pIC50	=	8.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	57459488	83475	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206441	83475	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	57459494	83476	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206442	83476	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	10428048	3297	26	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	3955	3297	26	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL305406	3297	26	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	71566276	143879	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	381	5	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1	nan
	CHEMBL3906311	143879	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	381	5	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1	nan
	117642007	145186	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3916486	145186	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554827	152782	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1	nan
	CHEMBL3978247	152782	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1	nan
	89554725	160266	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL4114602	160266	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	44309100	102145	0	None	-	0	Rat	4.9	pIC50	=	4.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL304285	102145	0	None	-	0	Rat	4.9	pIC50	=	4.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/s0960-894x(99)00346-7
	89554830	151326	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3965612	151326	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554917	142592	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	3.6	CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3895775	142592	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	3.6	CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	89554812	144031	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	3	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1	nan
	CHEMBL3907626	144031	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	3	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1	nan
	89554781	159434	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1	nan
	CHEMBL4107730	159434	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1	nan
	53320741	56106	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	471	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631866	56106	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	471	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566277	142221	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	5	1	5	4.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3892604	142221	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	5	1	5	4.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1	nan
	71566125	146505	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	CHEMBL3926942	146505	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	89554755	151324	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3965606	151324	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554749	151461	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	151461	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	89554734	159602	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL4109210	159602	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1	nan
	22224657	95712	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	95712	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	18548739	159806	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL411095	159806	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	156016312	177149	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642428	177149	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317847	56101	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631861	56101	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9952648	95848	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	95848	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	18548739	159806	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL411095	159806	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	89554801	142320	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3893351	142320	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	18548785	56097	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	415	3	2	6	3.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631857	56097	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	415	3	2	6	3.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2	10.1016/j.bmcl.2010.09.125
	44309123	202163	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	365	4	0	4	5.7	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL68739	202163	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	365	4	0	4	5.7	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71565668	149874	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1	nan
	CHEMBL3953821	149874	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1	nan
	71566518	151744	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	CHEMBL3969392	151744	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	71566202	151825	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	3	1	3	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1	nan
	CHEMBL3970177	151825	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	3	1	3	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1	nan
	53323293	55986	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629851	55986	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71565594	142483	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	2	4	4.2	CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3894815	142483	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	2	4	4.2	CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	123632099	142858	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	4	4.9	[C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3897968	142858	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	4	4.9	[C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1	nan
	89554871	143032	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	5	3.6	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3899261	143032	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	5	3.6	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	71565883	147022	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1	nan
	CHEMBL3930893	147022	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1	nan
	89554967	148135	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	0	5	3.6	COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1	nan
	CHEMBL3939827	148135	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	0	5	3.6	COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1	nan
	89554841	148352	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	382	4	1	4	4.0	N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3941663	148352	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	382	4	1	4	4.0	N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554833	160236	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1	nan
	CHEMBL4114374	160236	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1	nan
	89554925	160252	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	5	1	6	3.7	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4114497	160252	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	5	1	6	3.7	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	9909080	154731	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402886	154731	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	156015264	176958	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4640203	176958	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317724	55980	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629845	55980	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	11212447	56108	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631868	56108	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317620	56109	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631869	56109	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	53326017	56112	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631872	56112	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	44450454	95661	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	381	2	1	5	3.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260343	95661	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	381	2	1	5	3.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	11347391	66503	0	None	2	2	Rat	6.9	pIC50	=	6.9	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186214	66503	0	None	2	2	Rat	6.9	pIC50	=	6.9	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71566520	144003	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1	nan
	CHEMBL3907349	144003	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1	nan
	89554899	146975	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	364	4	2	4	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1	nan
	CHEMBL3930631	146975	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	364	4	2	4	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1	nan
	89554784	142207	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	3.3	COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3892501	142207	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	3.3	COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	156010547	176580	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	280	1	1	4	2.4	O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12	10.1016/j.bmcl.2020.127066
	CHEMBL4634351	176580	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	280	1	1	4	2.4	O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12	10.1016/j.bmcl.2020.127066
	117642134	146515	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	4	3.4	CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3927029	146515	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	4	3.4	CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	44309303	202356	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.0	FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1	10.1016/s0960-894x(99)00346-7
	CHEMBL70026	202356	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.0	FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1	10.1016/s0960-894x(99)00346-7
	117644742	147089	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	3	1	3	3.1	COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	CHEMBL3931394	147089	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	3	1	3	3.1	COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	89554852	147594	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3935453	147594	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1	nan
	89554870	147695	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	1	6	3.2	COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	CHEMBL3936247	147695	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	1	6	3.2	COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	71566126	148238	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3940665	148238	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	89554745	149046	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3946940	149046	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	71566207	149809	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3953157	149809	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554909	159775	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	468	5	1	6	4.1	C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4110690	159775	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	468	5	1	6	4.1	C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	89554960	160156	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1	nan
	CHEMBL4113735	160156	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1	nan
	22317185	55983	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629848	55983	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317918	55992	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629858	55992	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	22448874	94841	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	493	5	2	6	4.3	CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL256424	94841	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	493	5	2	6	4.3	CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	89554836	160065	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	4	2	7	3.2	C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4113073	160065	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	4	2	7	3.2	C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	156017916	177221	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4643527	177221	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554840	149969	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	3	0	5	4.5	Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3954534	149969	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	3	0	5	4.5	Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	89554892	150056	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL3955188	150056	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	71566275	151096	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1	nan
	CHEMBL3963813	151096	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1	nan
	117642068	153729	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1	nan
	CHEMBL3986471	153729	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1	nan
	71566522	148799	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3945170	148799	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	10.1016/j.bmcl.2020.127066
	49765871	2105	40	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	2105	40	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	89554911	142450	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	142450	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	89554889	144259	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	368	4	1	6	2.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1	nan
	CHEMBL3909377	144259	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	368	4	1	6	2.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1	nan
	89554788	145838	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL3921588	145838	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1	nan
	89554753	146229	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3924490	146229	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	117642146	147943	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3938177	147943	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71566048	150179	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	CHEMBL3956202	150179	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	89554977	150597	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1	nan
	CHEMBL3959505	150597	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1	nan
	117641924	151863	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3970507	151863	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	71565961	152949	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	3.0	CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3979694	152949	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	3.0	CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	124201730	159843	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	CHEMBL4111267	159843	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	44434257	150883	0	None	-	0	Rat	5.8	pIC50	=	5.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	318	1	1	2	4.5	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL396181	150883	0	None	-	0	Rat	5.8	pIC50	=	5.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	318	1	1	2	4.5	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2	10.1016/j.bmcl.2007.10.026
	22224695	88262	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	1	1	2	5.2	O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL236035	88262	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	1	1	2	5.2	O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	89543901	150029	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3955040	150029	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565963	152168	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	487	5	1	6	3.5	NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3973004	152168	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	487	5	1	6	3.5	NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554753	146229	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3924490	146229	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	89554752	146838	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3929631	146838	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71565525	149372	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	4	1	4	2.9	NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3949476	149372	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	4	1	4	2.9	NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	71566048	150179	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	CHEMBL3956202	150179	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	89554891	160101	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	CHEMBL4113348	160101	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	9952648	95848	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	95848	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	95848	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	95848	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	89554732	159611	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4109248	159611	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156017027	177143	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642338	177143	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	53325611	56107	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631867	56107	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22448864	88738	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	494	2	1	6	3.7	N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236669	88738	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	494	2	1	6	3.7	N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554793	145796	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	2	4	4.0	CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3921230	145796	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	2	4	4.0	CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	89554846	142605	0	None	-	0	Human	5.8	pIC50	=	5.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	6	3.1	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1	nan
	CHEMBL3895854	142605	0	None	-	0	Human	5.8	pIC50	=	5.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	6	3.1	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1	nan
	89545189	152350	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	nan
	CHEMBL3974648	152350	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	nan
	71565885	152888	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	6	1	7	1.6	COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3979211	152888	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	6	1	7	1.6	COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554890	160306	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL4114982	160306	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	71566522	148799	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	nan
	CHEMBL3945170	148799	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	nan
	89554932	149375	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	2.8	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1	nan
	CHEMBL3949512	149375	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	2.8	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1	nan
	71566349	153622	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1	nan
	CHEMBL3985577	153622	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1	nan
	89554829	142407	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL3894162	142407	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	71565596	144247	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.3	CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	CHEMBL3909273	144247	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.3	CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	89554881	147704	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	CHEMBL3936318	147704	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	89554933	150879	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	490	6	2	5	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3961788	150879	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	490	6	2	5	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	22224852	95407	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	95407	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	18548908	95804	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261051	95804	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	22224670	95807	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261081	95807	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554950	147674	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	443	5	1	5	4.5	Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1	nan
	CHEMBL3936050	147674	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	443	5	1	5	4.5	Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1	nan
	117642183	152829	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	354	4	0	4	4.5	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	CHEMBL3978639	152829	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	354	4	0	4	4.5	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	22224972	97233	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	430	2	1	4	5.4	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1	10.1016/j.bmcl.2007.12.005
	CHEMBL271319	97233	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	430	2	1	4	5.4	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1	10.1016/j.bmcl.2007.12.005
	11503055	2358	2	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	9694	2358	2	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	CHEMBL2204436	2358	2	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	71566435	152110	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	318	2	1	2	3.9	NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1	nan
	CHEMBL3972482	152110	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	318	2	1	2	3.9	NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1	nan
	89554799	160237	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1	nan
	CHEMBL4114381	160237	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1	nan
	89554919	143246	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	6	3.2	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3901084	143246	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	6	3.2	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1	nan
	71566204	148148	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1	nan
	CHEMBL3939934	148148	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1	nan
	22448830	88993	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	416	3	1	5	4.3	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL237091	88993	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	416	3	1	5	4.3	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	22448689	97093	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270616	97093	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317408	55985	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629850	55985	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11211597	56000	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	56000	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	89554780	144838	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	3	4.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1	nan
	CHEMBL3913806	144838	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	3	4.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1	nan
	89554777	144752	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	2.9	CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3913090	144752	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	2.9	CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	89554839	152846	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	5	1	6	3.3	NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3978791	152846	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	5	1	6	3.3	NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554772	144246	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1	nan
	CHEMBL3909260	144246	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1	nan
	89554745	149046	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3946940	149046	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554794	151855	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3970463	151855	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554732	159611	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL4109248	159611	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	10297067	95844	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261263	95844	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	156016312	177149	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642428	177149	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156018942	177286	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	507	6	2	6	4.6	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4644424	177286	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	507	6	2	6	4.6	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554861	149280	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3948794	149280	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1	nan
	71565804	143371	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	444	6	2	5	4.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1	nan
	CHEMBL3902047	143371	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	444	6	2	5	4.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1	nan
	89554886	159323	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4106809	159323	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	11158623	3287	7	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	3287	7	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	3287	7	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	11351088	55990	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629856	55990	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317928	55991	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629857	55991	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	11406781	56116	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631876	56116	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	1378	2374	48	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	1399	2374	48	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	9819927	2374	48	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	CHEMBL432038	2374	48	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	89554746	143211	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3900813	143211	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554931	147011	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	5	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1	nan
	CHEMBL3930820	147011	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	5	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1	nan
	1397	2483	11	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	9886034	2483	11	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186453	2483	11	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22224970	154942	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404080	154942	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	135544097	155112	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404886	155112	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317715	55989	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629854	55989	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9885546	110036	0	None	-	1	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL325140	110036	0	None	-	1	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	1378	2374	48	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	1399	2374	48	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	9819927	2374	48	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	CHEMBL432038	2374	48	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	44309302	202355	0	None	-	0	Rat	5.7	pIC50	=	5.7	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	345	5	0	4	4.8	Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1	10.1016/s0960-894x(99)00346-7
	CHEMBL70025	202355	0	None	-	0	Rat	5.7	pIC50	=	5.7	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	345	5	0	4	4.8	Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1	10.1016/s0960-894x(99)00346-7
	89554729	145850	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	514	8	2	7	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3921665	145850	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	514	8	2	7	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	121447916	169370	1	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	409	4	1	5	2.8	C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4441595	169370	1	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	409	4	1	5	2.8	C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	66791078	142130	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	489	6	2	6	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3891986	142130	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	489	6	2	6	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554746	143211	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3900813	143211	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71566596	143602	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	4	1	4	2.5	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3903901	143602	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	4	1	4	2.5	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554855	145997	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F	nan
	CHEMBL3922719	145997	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F	nan
	89554970	146669	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1	nan
	CHEMBL3928272	146669	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1	nan
	71566599	146761	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.8	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1	nan
	CHEMBL3929001	146761	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.8	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1	nan
	89554806	148673	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F	nan
	CHEMBL3944124	148673	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F	nan
	89554883	149656	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3951983	149656	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1	nan
	71566130	151337	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	384	5	1	6	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3965748	151337	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	384	5	1	6	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	89554794	151855	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3970463	151855	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554759	159487	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL4108213	159487	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	71566672	152285	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3973949	152285	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	22224962	95843	0	None	-	0	Rat	6.7	pIC50	=	6.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	342	3	1	4	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261251	95843	0	None	-	0	Rat	6.7	pIC50	=	6.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	342	3	1	4	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1	10.1016/j.bmcl.2008.02.076
	11559750	95496	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL259435	95496	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	89554860	144826	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1	nan
	CHEMBL3913733	144826	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1	nan
	71566519	153297	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	292	3	1	3	3.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	CHEMBL3982696	153297	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	292	3	1	3	3.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	89554797	142571	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	1	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1	nan
	CHEMBL3895570	142571	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	1	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1	nan
	22448579	155225	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL405895	155225	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	11084869	89608	2	None	-	1	Human	7.7	pIC50	=	7.7	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL2381643	89608	2	None	-	1	Human	7.7	pIC50	=	7.7	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11405687	66109	0	None	2	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185210	66109	0	None	2	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	117646988	148937	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	5	2.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1	nan
	CHEMBL3946311	148937	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	5	2.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1	nan
	10192719	65768	0	None	2	2	Rat	6.6	pIC50	=	6.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL183956	65768	0	None	2	2	Rat	6.6	pIC50	=	6.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	89554911	142450	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	142450	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	71565881	142481	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	380	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1	nan
	CHEMBL3894799	142481	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	380	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1	nan
	71566672	152285	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	nan
	CHEMBL3973949	152285	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	nan
	89554767	152869	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3978978	152869	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	9891158	155034	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL404463	155034	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317491	55988	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629853	55988	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	1378	2374	48	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	1399	2374	48	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	9819927	2374	48	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	CHEMBL432038	2374	48	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	89554965	143978	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1	nan
	CHEMBL3907125	143978	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1	nan
	89554894	149560	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1	nan
	CHEMBL3951081	149560	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1	nan
	89554916	153383	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1	nan
	CHEMBL3983396	153383	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1	nan
	156014599	176589	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	1	6	5.0	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4634754	176589	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	1	6	5.0	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554911	142450	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	142450	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	71565884	142881	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	4	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3898121	142881	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	4	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	71565736	152029	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	nan
	CHEMBL3971819	152029	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	nan
	89554728	152329	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3974406	152329	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554776	152607	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	478	5	1	4	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1	nan
	CHEMBL3976706	152607	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	478	5	1	4	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1	nan
	11257636	167797	0	None	1	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434536	167797	0	None	1	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22448659	154053	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	434	4	2	5	3.3	N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL399186	154053	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	434	4	2	5	3.3	N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89555004	143087	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	7	1	4	3.2	COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3899807	143087	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	7	1	4	3.2	COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554821	146805	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1	nan
	CHEMBL3929361	146805	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1	nan
	89554837	147294	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1	nan
	CHEMBL3933004	147294	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1	nan
	117641885	142472	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3894759	142472	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1	nan
	89554923	145901	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	5	3.3	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1	nan
	CHEMBL3922052	145901	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	5	3.3	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1	nan
	89554968	149043	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	4	1	5	3.4	CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3946909	149043	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	4	1	5	3.4	CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554820	149330	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3949126	149330	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	89554792	149852	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	CHEMBL3953648	149852	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	89554765	150919	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3962095	150919	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	22224729	95670	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260415	95670	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1	10.1016/j.bmcl.2008.02.076
	156020940	177523	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	489	6	2	6	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4647980	177523	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	489	6	2	6	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554884	142664	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3896344	142664	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554835	148978	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	4	2.9	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1	nan
	CHEMBL3946509	148978	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	4	2.9	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1	nan
	44309103	102387	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	323	4	0	4	4.5	Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL305799	102387	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	323	4	0	4	4.5	Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	9845873	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	44434259	88212	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	336	1	1	2	4.5	O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL235806	88212	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	336	1	1	2	4.5	O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	22448890	88875	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	490	4	2	5	4.7	CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236883	88875	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	490	4	2	5	4.7	CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	9845873	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL411440	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	9845873	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	22317318	56115	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631875	56115	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9845873	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	160240	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	89554791	159285	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	2	5	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4106552	159285	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	2	5	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	22224765	88317	0	None	-	0	Rat	4.6	pIC50	=	4.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	343	1	2	4	3.1	CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236258	88317	0	None	-	0	Rat	4.6	pIC50	=	4.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	343	1	2	4	3.1	CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	71565962	149096	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	462	5	1	6	4.1	NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3947299	149096	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	462	5	1	6	4.1	NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	22224583	154054	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	1	1	2	5.6	O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL399187	154054	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	1	1	2	5.6	O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	44309086	202227	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	346	5	0	5	4.2	Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69204	202227	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	346	5	0	5	4.2	Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71566597	149328	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	1	4	3.4	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3949122	149328	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	1	4	3.4	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554867	149540	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	1	5	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C	nan
	CHEMBL3950864	149540	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	1	5	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C	nan
	71565671	149964	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	5	1	5	2.7	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	CHEMBL3954513	149964	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	5	1	5	2.7	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	89554775	153289	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	476	5	2	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1	nan
	CHEMBL3982636	153289	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	476	5	2	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1	nan
	18548766	95406	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259053	95406	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	156019727	177408	0	None	-	0	Human	5.6	pIC50	=	5.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	497	7	2	6	4.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4646222	177408	0	None	-	0	Human	5.6	pIC50	=	5.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	497	7	2	6	4.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554914	160055	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C	nan
	CHEMBL4112966	160055	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C	nan
	89554778	142809	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	408	5	3	5	1.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1	nan
	CHEMBL3897537	142809	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	408	5	3	5	1.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1	nan
	53320742	56111	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	452	4	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631871	56111	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	452	4	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9868835	148408	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	459	2	1	5	4.2	CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL394201	148408	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	459	2	1	5	4.2	CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	89554888	142065	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1	nan
	CHEMBL3891468	142065	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1	nan
	89554859	149483	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	4	1	5	3.9	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1	nan
	CHEMBL3950438	149483	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	4	1	5	3.9	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1	nan
	71565521	149939	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1	nan
	CHEMBL3954371	149939	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1	nan
	22448614	88873	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	5	1	5	4.4	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236881	88873	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	5	1	5	4.4	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	44434256	88163	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	284	1	1	2	4.1	Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL235599	88163	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	284	1	1	2	4.1	Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2	10.1016/j.bmcl.2007.10.026
	71565526	150902	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3961948	150902	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	18548910	95475	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259340	95475	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	22317258	56114	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	480	3	1	5	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631874	56114	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	480	3	1	5	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11279365	67204	0	None	1	2	Rat	7.5	pIC50	=	7.5	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189814	67204	0	None	1	2	Rat	7.5	pIC50	=	7.5	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	44434258	88164	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	275	1	1	3	3.3	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL235600	88164	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	275	1	1	3	3.3	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	11158623	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	6226	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	CHEMBL1629855	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	11158623	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	6226	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	CHEMBL1629855	3287	7	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	89543886	148230	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	3	1	3	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1	nan
	CHEMBL3940628	148230	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	3	1	3	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1	nan
	44452714	158709	0	None	-	0	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL409928	158709	0	None	-	0	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	71566669	144939	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	5	1	4	3.8	CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3914560	144939	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	5	1	4	3.8	CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554938	146130	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3923798	146130	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1	nan
	89554823	148488	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1	nan
	CHEMBL3942629	148488	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1	nan
	22224615	89619	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL238167	89619	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	22224975	88315	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	368	1	1	5	3.9	N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236256	88315	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	368	1	1	5	3.9	N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	10359073	154423	1	None	-2	2	Human	5.5	pIC50	=	5.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	CHEMBL40123	154423	1	None	-2	2	Human	5.5	pIC50	=	5.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	89554903	152106	0	None	-	0	Human	5.5	pIC50	=	5.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	345	3	0	3	4.0	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	nan
	CHEMBL3972456	152106	0	None	-	0	Human	5.5	pIC50	=	5.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	345	3	0	3	4.0	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	nan
	71566274	146347	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	3	4.4	Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3925507	146347	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	3	4.4	Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565738	149719	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	6	1	5	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1	nan
	CHEMBL3952509	149719	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	6	1	5	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1	nan
	71565805	151774	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3969686	151774	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	71566206	153101	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3981039	153101	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	89554764	153409	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	4	4.5	CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3983614	153409	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	4	4.5	CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	22224825	158436	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL409638	158436	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	44309101	201861	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	278	6	0	5	3.1	CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1	10.1016/s0960-894x(99)00346-7
	CHEMBL66701	201861	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	278	6	0	5	3.1	CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1	10.1016/s0960-894x(99)00346-7
	22224682	89165	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	367	1	1	4	4.5	N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL237523	89165	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	367	1	1	4	4.5	N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554733	141996	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	5	1	7	3.2	COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3890866	141996	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	5	1	7	3.2	COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	71566126	148238	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3940665	148238	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	89554774	153330	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	1	4	3.3	CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3982968	153330	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	1	4	3.3	CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	89543925	151881	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	284	2	1	2	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1	nan
	CHEMBL3970688	151881	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	284	2	1	2	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1	nan
	89554911	142450	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	142450	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	89554971	146739	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	6	2.8	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1	nan
	CHEMBL3928860	146739	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	6	2.8	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1	nan
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2008.02.076
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2008.02.076
	22224841	89618	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL238166	89618	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	44285839	99676	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	353	4	3	4	2.9	CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21	10.1021/jm980571q
	CHEMBL287831	99676	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	353	4	3	4	2.9	CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21	10.1021/jm980571q
	9820321	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	154457	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	117642059	143165	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	4	1	4	4.5	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3900371	143165	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	4	1	4	4.5	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1	nan
	53318106	56095	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	4	5.1	Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631855	56095	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	4	5.1	Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1	10.1016/j.bmcl.2010.09.125
	22224908	88309	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	2	2	3	3.6	NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236244	88309	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	2	2	3	3.6	NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	117642047	141990	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	6	2	6	3.9	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3890814	141990	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	6	2	6	3.9	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554868	148798	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	402	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3945166	148798	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	402	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	10204007	97055	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	446	3	1	6	4.2	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270402	97055	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	446	3	1	6	4.2	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2007.12.005
	89554759	159487	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4108213	159487	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156015207	176989	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4640529	176989	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22224803	89471	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	449	2	1	4	4.0	O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL237938	89471	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	449	2	1	4	4.0	O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	156013741	176682	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	282	1	1	4	2.3	O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12	10.1016/j.bmcl.2020.127066
	CHEMBL4636186	176682	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	282	1	1	4	2.3	O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12	10.1016/j.bmcl.2020.127066
	71566438	152316	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12	nan
	CHEMBL3974279	152316	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12	nan
	89554845	145864	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1	nan
	CHEMBL3921799	145864	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1	nan
	22448617	88607	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	446	2	1	5	4.3	N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236467	88607	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	446	2	1	5	4.3	N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	136152920	94756	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	467	3	3	7	3.5	O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256008	94756	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	467	3	3	7	3.5	O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71566600	145652	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1	nan
	CHEMBL3920092	145652	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1	nan
	89554814	152338	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	4	1	5	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1	nan
	CHEMBL3974523	152338	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	4	1	5	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1	nan
	18613455	95591	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259924	95591	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	89554808	144679	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1	nan
	CHEMBL3912631	144679	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1	nan
	89554869	144121	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	4	1	5	3.5	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	CHEMBL3908309	144121	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	4	1	5	3.5	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	89554849	150410	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1	nan
	CHEMBL3958094	150410	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1	nan
	22224570	95456	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259269	95456	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	53316798	56096	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631856	56096	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	89554811	147317	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1	nan
	CHEMBL3933190	147317	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1	nan
	71566521	142783	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1	nan
	CHEMBL3897268	142783	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1	nan
	89554885	143759	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3905282	143759	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554951	153727	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	361	3	0	5	3.4	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1	nan
	CHEMBL3986465	153727	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	361	3	0	5	3.4	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1	nan
	89554872	148854	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	CHEMBL3945590	148854	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	44450479	95803	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261050	95803	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	11235624	55997	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	55997	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11304010	55999	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	55999	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	11474913	56098	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631858	56098	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11281280	56099	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	56099	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	22317431	56104	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631864	56104	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11559750	95496	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL259435	95496	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	71565740	144024	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	418	6	1	6	3.6	CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3907527	144024	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	418	6	1	6	3.6	CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	22448643	88608	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	5	5.0	N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236468	88608	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	5	5.0	N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	53324715	56110	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631870	56110	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11382367	66588	0	None	1	2	Rat	7.4	pIC50	=	7.4	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186630	66588	0	None	1	2	Rat	7.4	pIC50	=	7.4	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22224567	166846	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	325	1	1	3	3.9	C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL429629	166846	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	325	1	1	3	3.9	C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	6324634	147399	7	None	-1	2	Human	6.4	pIC50	=	6.4	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	CHEMBL39338	147399	7	None	-1	2	Human	6.4	pIC50	=	6.4	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	156009702	176587	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	277	1	1	1	3.9	O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21	10.1016/j.bmcl.2020.127066
	CHEMBL4634600	176587	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	277	1	1	1	3.9	O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21	10.1016/j.bmcl.2020.127066
	71566442	144702	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	276	2	1	2	3.6	Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	CHEMBL3912824	144702	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	276	2	1	2	3.6	Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	156017399	177130	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	5	1	6	4.7	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642255	177130	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	5	1	6	4.7	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	117642070	150505	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	5	1	7	2.1	COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3958736	150505	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	5	1	7	2.1	COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	71566668	143681	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	359	3	0	4	3.6	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3904529	143681	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	359	3	0	4	3.6	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554730	142470	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1	nan
	CHEMBL3894724	142470	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1	nan
	89554897	144870	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1	nan
	CHEMBL3914040	144870	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1	nan
	89554771	149116	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1	nan
	CHEMBL3947441	149116	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1	nan
	89554802	152108	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3972468	152108	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1	nan
	18613373	95714	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260643	95714	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	71565807	142287	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	424	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1	nan
	CHEMBL3893078	142287	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	424	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1	nan
	44450484	96219	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	370	2	1	4	4.4	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL263906	96219	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	370	2	1	4	4.4	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554879	153174	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1	nan
	CHEMBL3981623	153174	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1	nan
	22448569	88737	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	478	2	1	5	4.0	N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236668	88737	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	478	2	1	5	4.0	N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	71565669	142418	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL3894283	142418	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4515671	142418	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	71565522	142406	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	495	4	1	6	5.8	CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C	nan
	CHEMBL3894156	142406	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	495	4	1	6	5.8	CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C	nan
	89554819	147771	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	1	4	4.8	Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3936939	147771	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	1	4	4.8	Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554826	149940	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1	nan
	CHEMBL3954377	149940	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1	nan
	71566278	151698	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	4	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1	nan
	CHEMBL3968939	151698	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	4	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1	nan
	89554896	159403	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4107449	159403	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	22448868	154746	0	None	-	0	Rat	7.3	pIC50	=	7.3	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	480	5	2	6	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402963	154746	0	None	-	0	Rat	7.3	pIC50	=	7.3	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	480	5	2	6	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	44450455	166996	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	345	3	1	5	3.9	CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL430053	166996	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	345	3	1	5	3.9	CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	89554847	144376	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	357	4	1	3	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1	nan
	CHEMBL3910265	144376	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	357	4	1	3	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1	nan
	89554756	149172	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.7	CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	CHEMBL3947898	149172	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.7	CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	71565803	152760	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	6	1	6	4.6	CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F	nan
	CHEMBL3978058	152760	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	6	1	6	4.6	CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F	nan
	44309314	202270	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69461	202270	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	89554962	152552	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	3	0	4	4.6	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1	nan
	CHEMBL3976206	152552	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	3	0	4	4.6	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1	nan
	10130658	66405	0	None	2	2	Rat	6.3	pIC50	=	6.3	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185822	66405	0	None	2	2	Rat	6.3	pIC50	=	6.3	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	89554743	150406	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	4	1	4	3.6	N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3958048	150406	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	4	1	4	3.6	N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554738	150415	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	150415	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	89554921	153251	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	5	1	6	2.7	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3982294	153251	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	5	1	6	2.7	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	22224756	147407	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	397	1	1	3	4.7	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL393385	147407	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	397	1	1	3	4.7	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554738	150415	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	150415	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	89554866	146050	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3923126	146050	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554768	148907	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	CHEMBL3946016	148907	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	89554800	151200	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1	nan
	CHEMBL3964644	151200	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1	nan
	71552551	151971	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	4	1	4	3.0	Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	CHEMBL3971388	151971	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	4	1	4	3.0	Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	22317744	55979	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629844	55979	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	18548795	56092	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631757	56092	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	69093928	83481	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206447	83481	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	89554792	149852	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	CHEMBL3953648	149852	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	10428048	3297	26	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	3955	3297	26	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL305406	3297	26	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	71566525	148138	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	3	1	4	3.2	NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1	nan
	CHEMBL3939839	148138	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	3	1	4	3.2	NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1	nan
	89554842	159328	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL4106872	159328	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	89554876	147614	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	5	4.5	COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1	nan
	CHEMBL3935571	147614	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	5	4.5	COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1	nan
	89554795	152897	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	2.9	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3979288	152897	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	2.9	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1	nan
	89554817	143567	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1	nan
	CHEMBL3903609	143567	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1	nan
	89554934	159609	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	5	1	6	4.5	C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4109232	159609	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	5	1	6	4.5	C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	71565808	150719	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	360	4	1	4	3.7	Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3960284	150719	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	360	4	1	4	3.7	Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554773	143146	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1	nan
	CHEMBL3900236	143146	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1	nan
	89554798	144659	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	6	2.3	CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3912490	144659	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	6	2.3	CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	117644752	145906	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	4	3.7	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1	nan
	CHEMBL3922089	145906	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	4	3.7	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1	nan
	89544007	146501	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	358	4	1	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1	nan
	CHEMBL3926904	146501	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	358	4	1	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1	nan
	71566128	147025	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	1	4	4.8	COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl	nan
	CHEMBL3930919	147025	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	1	4	4.8	COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl	nan
	89554803	151705	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1	nan
	CHEMBL3968972	151705	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1	nan
	89554805	148170	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3940116	148170	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71566439	143532	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1	nan
	CHEMBL3903327	143532	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1	nan
	71565735	149840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3953417	149840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	44309315	101777	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1	10.1016/s0960-894x(99)00346-7
	CHEMBL303193	101777	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1	10.1016/s0960-894x(99)00346-7
	71565523	152780	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	3	0	4	3.3	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O	nan
	CHEMBL3978239	152780	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	3	0	4	3.3	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O	nan
	71566671	149824	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	4	2	4	3.0	CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3953282	149824	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	4	2	4	3.0	CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	71565735	149840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	nan
	CHEMBL3953417	149840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	nan
	89554738	150415	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	150415	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	53324292	56113	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	460	3	1	4	6.3	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631873	56113	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	460	3	1	4	6.3	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	89554993	148384	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	427	6	1	6	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1	nan
	CHEMBL3941863	148384	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	427	6	1	6	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1	nan
	89554892	150056	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3955188	150056	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554749	151461	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	151461	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	71565966	152256	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3973721	152256	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554893	153435	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3983863	153435	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	22224854	94927	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256812	94927	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317728	55981	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629846	55981	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	53320632	55987	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629852	55987	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11442010	56001	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	56001	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44450453	155345	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	337	2	1	5	3.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL406061	155345	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	337	2	1	5	3.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2008.02.076
	18613404	88606	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	2	1	4	4.5	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236466	88606	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	2	1	4	4.5	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	22448865	88874	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	4	2	5	3.9	N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236882	88874	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	4	2	5	3.9	N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	44450444	95674	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	353	3	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260455	95674	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	353	3	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554779	145548	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	nan
	CHEMBL3919306	145548	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	nan
	89554779	145548	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3919306	145548	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	10.1016/j.bmcl.2020.127066
	71565737	143428	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1	nan
	CHEMBL3902679	143428	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1	nan
	89554831	146959	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	1	4	3.8	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	CHEMBL3930529	146959	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	1	4	3.8	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	71566670	146363	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	4	3.3	CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	CHEMBL3925652	146363	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	4	3.3	CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	89554761	150022	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	346	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1	nan
	CHEMBL3954993	150022	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	346	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1	nan
	22224809	153441	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	375	1	1	3	4.7	Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL398392	153441	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	375	1	1	3	4.7	Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	9847181	94595	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	462	5	2	6	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL255151	94595	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	462	5	2	6	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	10089411	7431	0	None	-	1	Human	5.2	pIC50	=	5.2	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL108735	7431	0	None	-	1	Human	5.2	pIC50	=	5.2	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	353213	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2007.12.005
	353213	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL394287	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL394287	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2008.02.076
	353213	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL394287	148514	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2010.09.125
	71566437	146931	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	268	2	1	3	3.4	Cc1cscc1-c1cc(C(N)=O)nc2ccccc12	nan
	CHEMBL3930346	146931	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	268	2	1	3	3.4	Cc1cscc1-c1cc(C(N)=O)nc2ccccc12	nan
	44434255	88162	0	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	280	2	1	3	3.5	COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL235598	88162	0	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	280	2	1	3	3.5	COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554731	151567	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	438	5	1	4	5.7	CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3967755	151567	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	438	5	1	4	5.7	CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554972	153639	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	460	5	1	4	4.2	CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	CHEMBL3985765	153639	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	460	5	1	4	4.2	CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	22317369	56102	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	2	1	3	6.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631862	56102	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	2	1	3	6.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566346	148943	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	4	1	3	3.6	NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1	nan
	CHEMBL3946344	148943	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	4	1	3	3.6	NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1	nan
	71566348	150394	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	328	3	1	4	3.5	Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1	nan
	CHEMBL3957842	150394	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	328	3	1	4	3.5	Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1	nan
	89554750	141984	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	498	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3890746	141984	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	498	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71566347	148153	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	252	2	1	4	1.7	Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1	nan
	CHEMBL3939979	148153	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	252	2	1	4	1.7	Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1	nan
	25195461	2104	42	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	8946	2104	42	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337527	2104	42	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	DB12059	2104	42	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	22224822	89472	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL237944	89472	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	89545189	152350	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3974648	152350	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	10.1016/j.bmcl.2020.127066
	156011740	176840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	6	2	6	3.8	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4638570	176840	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	6	2	6	3.8	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554955	144636	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1	nan
	CHEMBL3912345	144636	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1	nan
	89554762	151969	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1	nan
	CHEMBL3971379	151969	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1	nan
	1393	1504	58	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	1396	1504	58	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	213056	1504	58	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL8759	1504	58	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	89554982	146307	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	6	2	6	3.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1	nan
	CHEMBL3925177	146307	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	6	2	6	3.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1	nan
	89554981	147914	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	409	6	1	6	3.5	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1	nan
	CHEMBL3937970	147914	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	409	6	1	6	3.5	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1	nan
	89554880	149500	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	372	5	1	4	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	CHEMBL3950572	149500	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	372	5	1	4	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	71565593	150417	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	3.2	CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	CHEMBL3958138	150417	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	3.2	CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	89554910	150850	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	4	1	5	4.4	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3961599	150850	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	4	1	5	4.4	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1	nan
	71565966	152256	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3973721	152256	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	18548862	157384	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408455	157384	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	44450391	168258	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437835	168258	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	22317892	55995	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629860	55995	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	69093344	83480	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206446	83480	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	44450434	167125	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	4	1	6	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL430231	167125	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	4	1	6	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	71566601	149679	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	467	5	1	4	4.4	CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3952222	149679	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	467	5	1	4	4.4	CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	44450483	168230	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	380	2	1	4	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437646	168230	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	380	2	1	4	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	9845127	167204	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	422	2	1	6	3.7	O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL430408	167204	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	422	2	1	6	3.7	O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71565886	143504	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903111	143504	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554822	144097	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	5	1	4	5.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1	nan
	CHEMBL3908110	144097	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	5	1	4	5.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1	nan
	44453878	95220	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	416	2	1	4	5.0	Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL258113	95220	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	416	2	1	4	5.0	Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	89554929	149792	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3953060	149792	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1	nan
	89554907	160043	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL4112899	160043	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	44309080	202334	0	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	265	4	0	4	2.9	CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F	10.1016/s0960-894x(99)00346-7
	CHEMBL69869	202334	0	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	265	4	0	4	2.9	CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F	10.1016/s0960-894x(99)00346-7
	89554959	142795	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	362	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1	nan
	CHEMBL3897362	142795	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	362	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1	nan
	71566205	151752	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	386	5	1	3	4.7	COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1	nan
	CHEMBL3969476	151752	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	386	5	1	3	4.7	COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1	nan
	89554739	159347	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL4107013	159347	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1	nan
	22224639	161209	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	395	1	1	3	5.1	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL413979	161209	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	395	1	1	3	5.1	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	1439	2424	13	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	5311457	2424	13	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	CHEMBL41013	2424	13	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	89554782	149490	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	2	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1	nan
	CHEMBL3950507	149490	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	2	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1	nan
	122539788	161983	11	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	326	5	1	5	2.3	Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4168094	161983	11	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	326	5	1	5	2.3	Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1	10.1021/acs.jmedchem.8b01266
	71565669	142418	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	CHEMBL3894283	142418	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	CHEMBL4515671	142418	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	71565964	143706	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	CHEMBL3904730	143706	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	89554964	144678	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3912615	144678	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554887	147787	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1	nan
	CHEMBL3937038	147787	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1	nan
	71566127	148093	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	CHEMBL3939455	148093	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	89554858	150555	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3959134	150555	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	89554984	151977	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	423	6	1	6	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1	nan
	CHEMBL3971450	151977	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	423	6	1	6	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1	nan
	89554790	159308	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1	nan
	CHEMBL4106729	159308	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1	nan
	89554915	159542	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	CHEMBL4108673	159542	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	89554961	159725	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4110317	159725	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	53317987	55993	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629859	55993	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	11484819	55998	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	55998	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	18548737	56094	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631854	56094	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11362246	56100	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631860	56100	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	70052526	89607	2	None	-	1	Human	8.1	pIC50	=	8.1	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL2381642	89607	2	None	-	1	Human	8.1	pIC50	=	8.1	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	71566598	142146	10	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	142146	10	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	89554908	141922	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	5	2	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1	nan
	CHEMBL3890277	141922	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	5	2	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1	nan
	9864190	88213	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	370	1	1	2	5.2	O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL235807	88213	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	370	1	1	2	5.2	O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	89554895	149689	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	4	5.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1	nan
	CHEMBL3952287	149689	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	4	5.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1	nan
	89554978	150160	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	5	1	6	3.5	CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3956019	150160	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	5	1	6	3.5	CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	89555003	144680	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	339	5	1	4	3.1	CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3912634	144680	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	339	5	1	4	3.1	CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554744	147794	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1	nan
	CHEMBL3937068	147794	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1	nan
	22448756	154052	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	474	3	1	5	5.0	COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL399185	154052	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	474	3	1	5	5.0	COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	89554949	147637	0	None	-	0	Human	6.1	pIC50	=	6.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	238	2	1	2	2.9	NC(=O)c1cc(C2=CCCC2)c2ccccc2n1	nan
	CHEMBL3935751	147637	0	None	-	0	Human	6.1	pIC50	=	6.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	238	2	1	2	2.9	NC(=O)c1cc(C2=CCCC2)c2ccccc2n1	nan
	89554741	146662	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	366	6	2	4	2.1	CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3928211	146662	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	366	6	2	4	2.1	CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554957	149832	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	2	6	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1	nan
	CHEMBL3953345	149832	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	2	6	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1	nan
	117642124	146796	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	6	2	6	4.1	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3929304	146796	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	6	2	6	4.1	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554862	143440	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1	nan
	CHEMBL3902752	143440	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1	nan
	89554838	160376	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	461	4	1	6	3.5	Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	CHEMBL4115433	160376	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	461	4	1	6	3.5	Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	22318000	55984	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	438	3	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629849	55984	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	438	3	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22224608	88316	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	362	1	1	4	3.8	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236257	88316	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	362	1	1	4	3.8	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554735	146083	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1	nan
	CHEMBL3923360	146083	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1	nan
	1408	263	28	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	6604820	263	28	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	CHEMBL285043	263	28	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	CHEMBL288635	263	28	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	89554810	150771	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	4	6.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1	nan
	CHEMBL3960845	150771	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	4	6.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1	nan
	71566598	142146	10	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3892073	142146	10	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554770	143547	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903459	143547	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565965	147740	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	CHEMBL3936681	147740	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	89554985	149894	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3954035	149894	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1	nan
	89554980	153431	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	2	5	3.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1	nan
	CHEMBL3983820	153431	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	2	5	3.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1	nan
	89554809	153652	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	4	1	6	3.5	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3985872	153652	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	4	1	6	3.5	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	89554789	159643	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL4109555	159643	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	10201802	96186	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL263649	96186	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548824	157182	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408229	157182	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	9888376	94758	1	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256011	94758	1	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71566598	142146	10	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	142146	10	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	53316736	55976	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629715	55976	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	18548824	157182	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL408229	157182	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71461395	83479	1	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206445	83479	1	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	89554912	145429	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	2	4	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1	nan
	CHEMBL3918313	145429	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	2	4	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1	nan
	89554815	144601	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	6	3.8	CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3912111	144601	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	6	3.8	CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	71565670	176636	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	363	4	1	3	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL4635528	176636	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	363	4	1	3	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	44450445	95816	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	371	2	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261128	95816	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	371	2	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	9886745	88739	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236670	88739	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	117641966	145999	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1	nan
	CHEMBL3922743	145999	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1	nan
	89554924	142164	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1	nan
	CHEMBL3892213	142164	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1	nan
	117642073	148431	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	7	1	6	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC	nan
	CHEMBL3942209	148431	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	7	1	6	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC	nan
	22224730	154194	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	366	2	1	3	4.6	COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL400018	154194	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	366	2	1	3	4.6	COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554920	145018	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	439	5	1	7	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1	nan
	CHEMBL3915181	145018	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	439	5	1	7	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1	nan
	9931956	94631	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL255356	94631	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22224761	166051	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	434	2	1	4	5.2	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2007.12.005
	CHEMBL428066	166051	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	434	2	1	4	5.2	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2007.12.005
	71566203	148091	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	3	1	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1	nan
	CHEMBL3939409	148091	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	3	1	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1	nan
	3335	2954	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	5311344	2954	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	CHEMBL39573	2954	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	68109335	156557	0	None	-	1	Human	9.0	pKd	=	9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	156557	0	None	-	1	Human	9.0	pKd	=	9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785087	157583	0	None	-	1	Human	9.0	pKd	=	9.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	157583	0	None	-	1	Human	9.0	pKd	=	9.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	49801370	156481	0	None	-	1	Human	8.9	pKd	=	8.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	156481	0	None	-	1	Human	8.9	pKd	=	8.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	68109941	155569	0	None	-	1	Human	8.8	pKd	=	8.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	155569	0	None	-	1	Human	8.8	pKd	=	8.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786131	156612	0	None	-	1	Human	8.0	pKd	=	8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	156612	0	None	-	1	Human	8.0	pKd	=	8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66786493	156706	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	156706	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	137652500	156635	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	156635	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109677	156639	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	156639	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	44595851	3730	1	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	3730	1	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	3730	1	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	68109605	157833	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	157833	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	66786069	155908	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	155908	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66784529	156539	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	156539	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66785027	157781	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	157781	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	66785551	156599	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	156599	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785393	156340	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	156340	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	66784675	156620	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	156620	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	68109333	157075	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	157075	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66784246	155811	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	155811	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109272	158060	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	158060	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	3954	657	53	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	657	53	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	657	53	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	66785780	158186	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	158186	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	66787433	155910	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	155910	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	66784262	157674	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	157674	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	70209638	157055	0	None	-	1	Human	8.6	pKd	=	8.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	157055	0	None	-	1	Human	8.6	pKd	=	8.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109580	157967	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	157967	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	66784890	155497	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	155497	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	66785101	157489	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	157489	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	66786816	157799	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	157799	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	68109425	157733	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	157733	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	68108857	156784	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	156784	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786493	159120	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	159120	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	49801369	158191	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	158191	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785300	155919	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	155919	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	66787355	155672	0	None	-	1	Human	8.4	pKd	=	8.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	155672	0	None	-	1	Human	8.4	pKd	=	8.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	49801371	158183	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	158183	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	66785182	156624	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	156624	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	59234231	2103	1	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	2103	1	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	2103	1	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	2103	1	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	68109379	156671	0	None	-	1	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	156671	0	None	-	1	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66785010	155310	0	None	-	1	Human	8.2	pKd	=	8.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	155310	0	None	-	1	Human	8.2	pKd	=	8.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	25125217	549	17	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	549	17	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	549	17	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	549	17	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	66786902	158902	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	158902	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109333	158833	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	158833	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66784572	156354	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	156354	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	137652320	156720	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	156720	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	49801368	159099	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	159099	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	68109941	155569	0	None	-	1	Human	9.1	pKi	=	9.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	155569	0	None	-	1	Human	9.1	pKi	=	9.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	117972250	141768	3	None	-	1	Human	9.0	pKi	=	9	Binding	Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	141768	3	None	-	1	Human	9.0	pKi	=	9	Binding	Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	11325656	126235	0	None	-	1	Rat	9.0	pKi	=	9.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	6	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365305	126235	0	None	-	1	Rat	9.0	pKi	=	9.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	6	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11211507	65101	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL182972	65101	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11339150	126619	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL365680	126619	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	66786902	158902	0	None	-	1	Human	8.8	pKi	=	8.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	158902	0	None	-	1	Human	8.8	pKi	=	8.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	11177216	65976	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL184983	65976	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11383191	96143	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	CHEMBL263312	96143	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	68108857	156784	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	156784	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66785551	156599	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	156599	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109605	157833	0	None	-	1	Human	8.0	pKi	=	8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	157833	0	None	-	1	Human	8.0	pKi	=	8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	66785027	157781	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	157781	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	67637138	183026	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4776989	183026	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802329	183026	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	49836087	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	6222	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	CHEMBL1630805	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	15461589	99950	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL290416	99950	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	11756841	160759	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41242	160759	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	11768848	114740	11	None	-	1	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347671	114740	11	None	-	1	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	11195342	123503	0	None	-	1	Rat	7.0	pKi	=	7.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363034	123503	0	None	-	1	Rat	7.0	pKi	=	7.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	68109333	157075	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	157075	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66787433	155910	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	155910	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	66784675	156620	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	156620	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	11188098	122568	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL361024	122568	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1377	1308	19	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	5310979	1308	19	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	CHEMBL284193	1308	19	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	1310	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	1369	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	33032	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	44272391	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	88747398	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	CHEMBL575060	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	DB00142	2276	108	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	71476419	122880	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	122880	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	155533313	171276	0	None	-	1	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	171276	0	None	-	1	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	60096194	156035	0	None	-10	2	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068679	156035	0	None	-10	2	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11462089	66990	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188532	66990	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1310	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	1369	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	33032	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	44272391	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	88747398	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	CHEMBL575060	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	DB00142	2276	108	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	162652146	179623	0	None	-1	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4749728	179623	0	None	-1	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	71135411	122868	0	None	-1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	122868	0	None	-1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	71681826	89616	0	None	-4	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	89616	0	None	-4	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	1393	1504	58	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	1396	1504	58	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	213056	1504	58	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	CHEMBL8759	1504	58	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	71131322	122877	0	None	4	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	122877	0	None	4	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096250	158363	0	None	-60	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095567	158363	0	None	-60	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10197984	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	10197984	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	1394	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL275079	2378	37	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	69669646	183087	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4757159	183087	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4802990	183087	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	11348518	125760	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365018	125760	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66784246	155811	0	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	155811	0	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71136640	122873	0	None	1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	122873	0	None	1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	53240406	122867	13	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	122867	13	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	9834591	137062	65	None	-1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL375611	137062	65	None	-1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	49765871	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11393152	66645	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	324	5	4	5	0.4	Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL186891	66645	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	324	5	4	5	0.4	Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	49822116	146447	7	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	146447	7	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	9914583	141421	0	None	-	1	Rat	5.8	pKi	=	5.8	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL38729	141421	0	None	-	1	Rat	5.8	pKi	=	5.8	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	60096183	158725	0	None	-6	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL4099470	158725	0	None	-6	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	137635882	155341	0	None	-1	2	Human	5.8	pKi	=	5.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	155341	0	None	-1	2	Human	5.8	pKi	=	5.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11310142	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	155533313	171276	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	171276	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	70052526	89607	2	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL2381642	89607	2	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11164815	121824	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359973	121824	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71137008	122875	0	None	-2	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	122875	0	None	-2	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	155548817	173258	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66785101	157489	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	157489	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	25195461	2104	42	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	2104	42	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	2104	42	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	2104	42	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	1310	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1369	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	33032	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	44272391	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	88747398	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	CHEMBL575060	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	DB00142	2276	108	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	60096246	155394	0	None	-40	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	CHEMBL4061162	155394	0	None	-40	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	11172339	66009	0	None	-	1	Rat	6.7	pKi	=	6.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185135	66009	0	None	-	1	Rat	6.7	pKi	=	6.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	11326253	64970	0	None	-	1	Rat	8.7	pKi	=	8.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	CHEMBL182899	64970	0	None	-	1	Rat	8.7	pKi	=	8.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	68109580	157967	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	157967	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	66786493	159120	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	159120	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	1397	2483	11	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	9886034	2483	11	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL186453	2483	11	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	49801370	156481	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	156481	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11382367	66588	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186630	66588	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1397	2483	11	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	9886034	2483	11	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186453	2483	11	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11405687	66109	0	None	2	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185210	66109	0	None	2	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	70209638	157055	0	None	-	1	Human	8.6	pKi	=	8.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	157055	0	None	-	1	Human	8.6	pKi	=	8.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11257636	167797	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434536	167797	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11375886	123824	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	521	6	3	4	5.0	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363724	123824	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	521	6	3	4	5.0	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11198402	126551	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	334	5	3	5	0.7	N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL365647	126551	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	334	5	3	5	0.7	N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	57338826	149083	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3947221	149083	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11259548	66339	0	None	-	1	Rat	7.7	pKi	=	7.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185456	66339	0	None	-	1	Rat	7.7	pKi	=	7.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	162658340	183094	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4760856	183094	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803084	183094	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	10197984	2378	37	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	2378	37	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	2378	37	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	15518713	99791	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1	10.1016/s0960-894x(99)00227-9
	CHEMBL288902	99791	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1	10.1016/s0960-894x(99)00227-9
	15461591	161336	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	521	6	0	6	6.5	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41513	161336	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	521	6	0	6	6.5	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	15461594	162609	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.6	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41808	162609	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.6	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	162658781	183099	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4759209	183099	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803105	183099	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	66786131	156612	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	156612	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	60096190	157955	0	None	-102	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091203	157955	0	None	-102	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096236	157864	0	None	-38	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4090293	157864	0	None	-38	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	9815617	113988	7	None	1	2	Rat	7.7	pKi	=	7.7	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	113988	7	None	1	2	Rat	7.7	pKi	=	7.7	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	68109425	157733	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	157733	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	45082292	114739	2	None	-3	3	Human	4.7	pKi	=	4.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347670	114739	2	None	-3	3	Human	4.7	pKi	=	4.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	44361401	31111	0	None	-7	2	Human	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	31111	0	None	-7	2	Human	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	1393	1504	58	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	1396	1504	58	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	213056	1504	58	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	CHEMBL8759	1504	58	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	11084869	89608	2	None	-	1	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL2381643	89608	2	None	-	1	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	155548817	173258	0	None	-	1	Human	6.6	pKi	=	6.6	Binding	Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	6.6	pKi	=	6.6	Binding	Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	69669702	183083	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4756556	183083	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4802948	183083	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	15518714	99847	0	None	-	1	Rat	5.6	pKi	=	5.6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL289394	99847	0	None	-	1	Rat	5.6	pKi	=	5.6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	137652500	156635	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	156635	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11361140	123786	0	None	-	1	Rat	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363526	123786	0	None	-	1	Rat	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	59234231	2103	1	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	2103	1	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	2103	1	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	2103	1	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	71136655	122872	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	122872	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162644419	183030	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4778355	183030	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802356	183030	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	71137011	122878	0	None	2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	122878	0	None	2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10089411	7431	0	None	-	1	Human	5.6	pKi	=	5.6	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL108735	7431	0	None	-	1	Human	5.6	pKi	=	5.6	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	162663798	183127	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4779554	183127	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4803378	183127	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	11220424	158403	0	None	-43	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095995	158403	0	None	-43	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	66784529	156539	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	156539	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	11200955	64261	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL181710	64261	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11177217	66328	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL185423	66328	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	1378	2374	48	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	1399	2374	48	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	9819927	2374	48	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	CHEMBL432038	2374	48	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	66785780	158186	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	158186	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	11279365	67204	0	None	1	2	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189814	67204	0	None	1	2	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11221617	67039	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188787	67039	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1395	2482	9	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	2482	9	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	2482	9	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	11314439	121499	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359491	121499	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66784572	156354	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	156354	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	66785087	157583	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	157583	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	11418500	121808	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	411	5	3	4	2.8	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359905	121808	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	411	5	3	4	2.8	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10807972	35574	1	None	1	2	Rat	8.4	pKi	=	8.4	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	CHEMBL144151	35574	1	None	1	2	Rat	8.4	pKi	=	8.4	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	11248009	126017	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365244	126017	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11153780	123300	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	399	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362459	123300	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	399	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11212336	123820	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	421	6	3	4	2.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363696	123820	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	421	6	3	4	2.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11485742	168896	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL442967	168896	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785300	155919	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	155919	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	162665071	183136	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4781638	183136	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803454	183136	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	15518719	167904	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL435174	167904	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	60096201	158010	0	None	-13	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091735	158010	0	None	-13	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	68109333	158833	0	None	-	1	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	158833	0	None	-	1	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	10130658	66405	0	None	2	2	Rat	7.5	pKi	=	7.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185822	66405	0	None	2	2	Rat	7.5	pKi	=	7.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	15518717	162809	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	505	6	0	6	6.0	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41932	162809	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	505	6	0	6	6.0	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	60096204	155571	0	None	-75	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4063336	155571	0	None	-75	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71136654	122879	0	None	-4	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	122879	0	None	-4	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10197984	2378	37	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	2378	37	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	2378	37	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	25125217	549	17	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	549	17	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	549	17	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	549	17	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	68109272	158060	0	None	-	1	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	158060	0	None	-	1	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	10192719	65768	0	None	2	2	Rat	7.4	pKi	=	7.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL183956	65768	0	None	2	2	Rat	7.4	pKi	=	7.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	137659992	158677	0	None	-14	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4098939	158677	0	None	-14	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11360426	123273	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362325	123273	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11749464	124503	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL364320	124503	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	155567633	175417	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	175417	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	11484738	165713	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL426983	165713	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11268934	66776	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL187482	66776	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1378	2374	48	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	2374	48	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	2374	48	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	2374	48	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	11188099	66478	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186107	66478	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10353365	82820	1	None	-5	2	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	82820	1	None	-5	2	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	11255753	121748	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	323	5	3	4	1.1	Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL359805	121748	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	323	5	3	4	1.1	Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	11290903	66986	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188511	66986	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11188380	67111	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	387	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189186	67111	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	387	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11163717	123140	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362092	123140	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10198133	204772	10	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	204772	10	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	10198133	204772	10	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL8839	204772	10	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	15518715	99844	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.5	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL289388	99844	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.5	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	15518712	100015	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	483	7	0	7	5.2	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL291017	100015	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	483	7	0	7	5.2	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21	10.1016/s0960-894x(99)00227-9
	15392100	168518	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	474	5	0	6	6.3	CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC	10.1016/s0960-894x(99)00227-9
	CHEMBL439925	168518	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	474	5	0	6	6.3	CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC	10.1016/s0960-894x(99)00227-9
	11310142	2379	16	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	2379	16	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	2379	16	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	60096231	157101	11	None	-446	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	157101	11	None	-446	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	10979251	89615	0	None	-3	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381650	89615	0	None	-3	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162666357	183139	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4784701	183139	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803523	183139	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11275666	89612	1	None	-15	2	Human	5.4	pKi	=	5.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381647	89612	1	None	-15	2	Human	5.4	pKi	=	5.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	9815616	114289	6	None	1	2	Rat	7.3	pKi	=	7.3	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	114289	6	None	1	2	Rat	7.3	pKi	=	7.3	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	66787355	155672	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	155672	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11196276	167766	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	261	5	3	4	0.0	CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434338	167766	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	261	5	3	4	0.0	CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	67637415	183095	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4759992	183095	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803099	183095	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	66786069	155908	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	155908	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	69669747	183061	7	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	183061	7	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	183061	7	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11268363	124206	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL364201	124206	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11450243	67104	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	327	5	3	4	0.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189139	67104	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	327	5	3	4	0.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11451742	123913	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363980	123913	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11349412	67189	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	1.8	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189710	67189	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	1.8	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	155567633	175417	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	175417	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	11338331	65188	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL183073	65188	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11313770	123344	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	339	6	3	5	0.8	COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL362708	123344	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	339	6	3	5	0.8	COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	10353365	82820	1	None	-5	2	Human	6.3	pKi	=	6.3	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	82820	1	None	-5	2	Human	6.3	pKi	=	6.3	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	66785182	156624	0	None	-	1	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	156624	0	None	-	1	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	60096228	156234	0	None	-5	2	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4070866	156234	0	None	-5	2	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096224	155992	0	None	-32	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068189	155992	0	None	-32	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL5076351	212649	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	CHEMBL5076351	212649	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	137634033	156088	0	None	-2	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	156088	0	None	-2	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	68109335	156557	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	156557	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109677	156639	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	156639	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	155548817	173258	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66786816	157799	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	157799	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	44396480	66488	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	275	5	3	4	0.4	CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186145	66488	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	275	5	3	4	0.4	CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785010	155310	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	155310	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	3954	657	53	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	657	53	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	657	53	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	71136653	122874	0	None	2	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	122874	0	None	2	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	49858117	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	6223	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	CHEMBL1630806	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	66784890	155497	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	155497	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	68109379	156671	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	156671	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	155548817	173258	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	173258	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	137656301	158124	0	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4093017	158124	0	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL5089623	213433	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	CHEMBL5089623	213433	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	49801371	158183	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	158183	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	11344646	126242	1	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	CHEMBL365368	126242	1	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	1310	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	1369	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	33032	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	44272391	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	88747398	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	CHEMBL575060	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	DB00142	2276	108	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	49858116	56039	0	None	-	1	Human	5.2	pKi	=	5.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	312	2	2	4	2.8	O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2	10.1021/jm101069m
	CHEMBL1630804	56039	0	None	-	1	Human	5.2	pKi	=	5.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	312	2	2	4	2.8	O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2	10.1021/jm101069m
	71137012	122871	0	None	-1	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	122871	0	None	-1	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10198133	204772	10	None	-6	2	Human	7.2	pKi	=	7.2	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	204772	10	None	-6	2	Human	7.2	pKi	=	7.2	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	11484739	122573	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL361051	122573	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11817779	65861	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	259	5	3	4	-0.2	C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL184441	65861	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	259	5	3	4	-0.2	C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	49801368	159099	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	159099	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	11347391	66503	0	None	2	2	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186214	66503	0	None	2	2	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11258119	66968	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	401	7	3	5	2.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188425	66968	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	401	7	3	5	2.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785393	156340	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	156340	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	67705089	151711	0	None	-2	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3969063	151711	0	None	-2	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	49822115	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	49822115	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	2106	17	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	11772601	126973	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	354	6	3	6	0.7	N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL366152	126973	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	354	6	3	6	0.7	N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	49801369	158191	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	158191	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	15392101	99960	0	None	-	1	Rat	5.2	pKi	=	5.2	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/s0960-894x(99)00227-9
	CHEMBL290509	99960	0	None	-	1	Rat	5.2	pKi	=	5.2	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/s0960-894x(99)00227-9
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	162654849	183078	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4755204	183078	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802906	183078	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	134132133	144244	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3909237	144244	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44595851	3730	1	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	3730	1	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	3730	1	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	67633284	183055	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4748699	183055	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802655	183055	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	90098428	122876	0	None	5	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	122876	0	None	5	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11449064	123862	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	287	4	3	4	0.5	N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363940	123862	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	287	4	3	4	0.5	N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	137652320	156720	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	156720	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	11267024	66311	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	315	5	3	5	0.9	N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185335	66311	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	315	5	3	5	0.9	N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	67633340	183129	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4780402	183129	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803381	183129	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	66784262	157674	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	157674	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	49858118	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	6224	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	CHEMBL1630807	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	15518718	99746	0	None	-	1	Rat	5.1	pKi	=	5.1	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	501	6	0	6	6.1	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL288472	99746	0	None	-	1	Rat	5.1	pKi	=	5.1	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	501	6	0	6	6.1	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	10198133	204772	10	None	-6	2	Human	6.1	pKi	=	6.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	204772	10	None	-6	2	Human	6.1	pKi	=	6.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	71137010	122869	0	None	-1	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	122869	0	None	-1	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	1393	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	1396	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	213056	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	CHEMBL8759	1504	58	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	9885546	110036	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL325140	110036	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	60096178	156327	0	None	-181	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4071962	156327	0	None	-181	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096211	89614	0	None	-5	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381649	89614	0	None	-5	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	69669820	183048	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4746125	183048	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802570	183048	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	66786493	156706	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	156706	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	11749463	65875	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL184504	65875	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11209918	66504	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	337	7	3	4	1.2	N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186215	66504	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	337	7	3	4	1.2	N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71137034	122870	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	122870	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11298568	69018	1	None	-6	2	Human	6.0	pKi	=	6.0	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	CHEMBL192977	69018	1	None	-6	2	Human	6.0	pKi	=	6.0	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	49822115	2106	17	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	8947	2106	17	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	CHEMBL3947764	2106	17	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	59234231	2103	1	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	2103	1	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	2103	1	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	2103	1	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	59234231	2103	1	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	2103	1	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	2103	1	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	2103	1	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	11362035	43	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	6328	43	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	6329	43	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	CHEMBL105296	43	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	1393	1504	58	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1396	1504	58	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	213056	1504	58	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	CHEMBL8759	1504	58	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1378	2374	48	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1399	2374	48	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	9819927	2374	48	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	CHEMBL432038	2374	48	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	None	214572	0	3H-LY354740	-	1	Rat	8.0	pKi	=	8	Binding	NoneNone	PDSP KiDatabase	323	5	5	9	-1.3	C1C(C1C(CN2C=NC3=C2N=C(N=C3O)O)(C(=O)O)N)C(=O)O	None
	12310764	1931	59	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	12310764	1931	59	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	12310764	1931	59	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	1931	59	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	1931	59	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	1931	59	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	1931	59	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	1931	59	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	1931	59	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	1931	59	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	1931	59	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	1931	59	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1310	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	134	2468	19	Functional	-8511	68	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	1775	2468	19	Functional	-8511	68	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	9681	2468	19	Functional	-8511	68	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	CHEMBL1065	2468	19	Functional	-8511	68	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	DB00247	2468	19	Functional	-8511	68	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	15897	2807	0	Functional	-354	37	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	215	2807	0	Functional	-354	37	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	CHEMBL1979333	2807	0	Functional	-354	37	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	1370	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1370	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1372	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1372	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	40539	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	40539	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	6971145	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	6971145	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	CHEMBL279956	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	CHEMBL279956	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	DB02999	3200	62	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	DB02999	3200	62	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	128563	3395	28	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	1666	3395	28	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	CHEMBL445332	3395	28	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	DB12327	3395	28	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	10297	26890	29	Functional	-38	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	C[C@H](N)[C@H](O)c1ccccc1	None
	CHEMBL136560	26890	29	Functional	-38	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	C[C@H](N)[C@H](O)c1ccccc1	None
	2207	99390	54	3H-LY354740	-25	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	183	4	4	3	-1.0	NC(CCP(=O)(O)O)C(=O)O	None
	CHEMBL285843	99390	54	3H-LY354740	-25	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	183	4	4	3	-1.0	NC(CCP(=O)(O)O)C(=O)O	None
	1222	101254	56	Functional	5	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL299683	101254	56	Functional	5	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	111542	39	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	111542	39	3H-GLUTAMATE	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	111542	39	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	111542	39	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	111542	39	3H-GLUTAMATE	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	111542	39	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	446220	132985	13	Functional	-1778	46	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	303	3	0	5	1.9	COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C	None
	CHEMBL370805	132985	13	Functional	-1778	46	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	303	3	0	5	1.9	COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C	None
	19702198	160763	14	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	19702198	160763	14	3H-LY354740	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	19702198	160763	14	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	160763	14	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	160763	14	3H-LY354740	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	160763	14	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	1615	167217	22	Functional	-26	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	193	3	1	3	1.6	CNC(C)Cc1ccc2c(c1)OCO2	None
	CHEMBL43048	167217	22	Functional	-26	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	193	3	1	3	1.6	CNC(C)Cc1ccc2c(c1)OCO2	None
	1297	169674	33	Functional	-1	4	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	1297	169674	33	Functional	-1	4	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	CHEMBL444589	169674	33	Functional	-1	4	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	CHEMBL444589	169674	33	Functional	-1	4	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	162265	200578	19	Functional	-239	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	4786	200578	19	Functional	-239	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	CHEMBL61006	200578	19	Functional	-239	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	139054390	203205	101	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	139054390	203205	101	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	139054390	203205	101	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	203205	101	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	203205	101	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	203205	101	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	203205	101	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	203205	101	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	203205	101	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	11954224	214164	0	Functional	-141253	60	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	581	4	3	6	2.0	CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C	None
	6971132	214225	0	3H-LY341495	-2570	14	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	268	1	2	2	2.1	CN1CC(C=C2C1CC3=CNC4=CC=CC2=C34)C(=O)O	None
	None	214402	0	Functional	-2	7	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	214402	0	Functional	1	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	25137849	214415	0	Functional	-4	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	165	3	2	2	1.3	CC(C(C1=CC=CC=C1)O)NC	None
	71290	214415	0	Functional	-4	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	165	3	2	2	1.3	CC(C(C1=CC=CC=C1)O)NC	None
	3337	214431	0	Functional	-1513	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)CC1=CC(=CC=C1)C(F)(F)F	None
	65801	214431	0	Functional	-1513	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)CC1=CC(=CC=C1)C(F)(F)F	None
	66264	214431	0	Functional	-1513	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)CC1=CC(=CC=C1)C(F)(F)F	None
	91452	214431	0	Functional	-1513	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)CC1=CC(=CC=C1)C(F)(F)F	None
	None	214555	0	Functional	-1	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	153	3	3	3	-1.4	C(C(C(=O)O)N)S(=O)O	None
	None	214556	0	Functional	-1	39	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	169	3	3	4	-1.7	C(C(C(=O)O)N)S(=O)(=O)O	None
	None	214564	0	Functional	-13	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	149	2	1	2	1.2	CC(C(=O)C1=CC=CC=C1)N	None
	1576	214565	0	Functional	-16	41	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	163	3	1	2	1.5	CC(C(=O)C1=CC=CC=C1)NC	None
	177120	214575	0	3H-LY354740	-	1	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	169	3	4	3	-1.4	C(C(C(=O)O)N)P(=O)(O)O	None
	194385	214584	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	172	3	3	4	-1.1	C1=C(ONC1=O)CC(C(=O)O)N	None
	194385	214584	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	172	3	3	4	-1.1	C1=C(ONC1=O)CC(C(=O)O)N	None
	6604769	214601	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	145	2	3	3	-1.1	C1C(NC1C(=O)O)C(=O)O	None
	6604769	214601	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	145	2	3	3	-1.1	C1C(NC1C(=O)O)C(=O)O	None
	None	214602	0	Functional	1	3	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	245	3	3	4	0.2	CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N	None
	None	214602	0	Functional	-1	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	245	3	3	4	0.2	CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N	None
	None	214603	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	233	3	2	6	-0.1	CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N	None
	None	214603	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	233	3	2	6	-0.1	CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N	None
	None	214604	0	Functional	1	3	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	197	4	4	3	-0.6	CC(CCP(=O)(O)O)(C(=O)O)N	None
	None	214604	0	Functional	-1	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	197	4	4	3	-0.6	CC(CCP(=O)(O)O)(C(=O)O)N	None
	None	214643	0	Functional	-	1	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	396	2	0	4	4.7	CC(=O)C1(C(=C)CC2C1(CCC3C2CC(=C)C4=CC(=O)CCC34C)C)OC(=O)C	None
	None	214651	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	250	3	3	4	-0.3	C(C1=C(C(=O)NO1)Br)C(C(=O)O)N	None
	None	214651	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	250	3	3	4	-0.3	C(C1=C(C(=O)NO1)Br)C(C(=O)O)N	None
	None	214738	0	Functional	1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	144	2	2	2	-0.7	CC(C(=O)NC)NC(=O)C	None
	None	214739	0	Functional	1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	161	5	3	3	-0.3	C(CC(C(=O)O)N)CC(=O)O	None
	1376	318	50	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	2071	318	50	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	CHEMBL313938	318	50	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	1310	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1310	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	None	214402	0	3H-LY354740	1	7	Rat	5.7	pKi	=	5.7	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	214402	0	Functional	1	7	Rat	5.7	pKi	=	5.7	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	214573	0	Functional	-5	3	Human	6.5	pKi	=	6.5	Binding	NoneNone	PDSP KiDatabase	203	4	4	4	-1.6	C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N	None
	None	214642	0	Functional	-	1	Human	5.5	pKi	=	5.5	Binding	NoneNone	PDSP KiDatabase	174	2	4	4	-1.8	C1C(NCC1(C(=O)O)N)C(=O)O	None
	1310	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	None	214573	0	3H-LY354740	3	3	Rat	7.2	pKi	=	7.2	Binding	NoneNone	PDSP KiDatabase	203	4	4	4	-1.6	C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N	None
	None	214574	0	3H-LY354740	-	1	Rat	7.2	pKi	=	7.2	Binding	NoneNone	PDSP KiDatabase	159	3	3	3	-0.9	C1C(C1C(=O)O)C(C(=O)O)N	None
	114827	214571	0	3H-LY341495	3	3	Rat	7.1	pKi	=	7.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	114827	214571	0	3H-LY341495	-3	3	Human	7.1	pKi	=	7.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	1310	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	2276	108	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	114827	214571	0	3H-LY354740	3	3	Rat	8.1	pKi	=	8.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	49822115	2106	17	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	8947	2106	17	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	CHEMBL3947764	2106	17	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	49836087	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	6222	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	CHEMBL1630805	1041	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	49858118	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	6224	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	CHEMBL1630807	1087	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	49858117	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	6223	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	CHEMBL1630806	1068	3	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	11310142	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	11614	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	CHEMBL192051	2379	16	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	11158623	3287	7	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	3287	7	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	3287	7	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	49765871	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	6317	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	CHEMBL2179319	2105	40	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	11158623	3287	7	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	3287	7	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	3287	7	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6325	3294	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	474	3	2	4	5.4	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O	21470207
	73755206	3294	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	474	3	2	4	5.4	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O	21470207
	6324	3289	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	73755205	3289	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	1373	2430	46	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	139055582	2430	46	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	446355	2430	46	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	CHEMBL257626	2430	46	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	DB04256	2430	46	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	104766	34	36	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	1365	34	36	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	CHEMBL34453	34	36	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	1400	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	1400	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	5311079	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	5311079	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	CHEMBL1450466	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	CHEMBL1450466	1503	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	1373	2430	46	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	139055582	2430	46	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	446355	2430	46	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	CHEMBL257626	2430	46	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	DB04256	2430	46	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	1374	2042	31	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	5311455	2042	31	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	CHEMBL39372	2042	31	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	1310	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	1369	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	33032	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	44272391	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	88747398	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	CHEMBL575060	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	DB00142	2276	108	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	1392	73	42	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	5310984	73	42	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	CHEMBL40086	73	42	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	104766	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	104766	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	1365	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	1365	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	CHEMBL34453	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	CHEMBL34453	34	36	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	1398	362	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	3964633	362	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	CHEMBL1437137	362	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	1310	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	1310	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	1369	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	1369	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	33032	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	33032	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	44272391	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	44272391	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	88747398	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	88747398	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	CHEMBL575060	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	CHEMBL575060	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	DB00142	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	DB00142	2276	108	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	1368	2248	31	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	5310956	2248	31	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	CHEMBL280563	2248	31	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	1377	1308	19	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	5310979	1308	19	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	CHEMBL284193	1308	19	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	1368	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	1368	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	5310956	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	5310956	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	CHEMBL280563	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	CHEMBL280563	2248	31	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	1393	1504	58	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	1396	1504	58	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	213056	1504	58	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	CHEMBL8759	1504	58	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	1377	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	1377	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	5310979	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	5310979	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	CHEMBL284193	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	CHEMBL284193	1308	19	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	1393	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1393	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	1396	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1396	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	213056	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	213056	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	CHEMBL8759	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	CHEMBL8759	1504	58	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	10197984	2378	37	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	1394	2378	37	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	CHEMBL275079	2378	37	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	1378	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	1378	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	1399	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	1399	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	9819927	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	9819927	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	CHEMBL432038	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	CHEMBL432038	2374	48	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	1378	2374	48	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1399	2374	48	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	9819927	2374	48	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	CHEMBL432038	2374	48	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1397	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	1397	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	9886034	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	9886034	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	CHEMBL186453	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	CHEMBL186453	2483	11	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	1395	2482	9	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999
	9837317	2482	9	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999
	CHEMBL121053	2482	9	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999

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Ligand source activities (1 row/activity)