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Volumn 60, Issue 1, 2011, Pages 82-92

The complexity of their activation mechanism opens new possibilities for the modulation of mGlu and GABAB class C G protein-coupled receptors

Author keywords

Allosteric communication; Allosteric modulator; Calcium sensing receptor; Dimerization; Taste receptor

Indexed keywords

2,6 DI TERT BUTYL 4 (3 HYDROXY 2,2 DIMETHYLPROPYL)PHENOL; 4 AMINOBUTYRIC ACID; 4 AMINOBUTYRIC ACID C RECEPTOR; 4 AMINOBUTYRIC ACID RECEPTOR STIMULATING AGENT; 5,7 DI TERT BUTYL 3 HYDROXY 3 TRIFLUOROMETHYL 3H BENZOFURAN 2 ONE; AMINO ACID DERIVATIVE; AUTOANTIBODY; BACLOFEN; CALCIUM; CARBOHYDRATE DERIVATIVE; CINACALCET; CPG 7930; G PROTEIN COUPLED RECEPTOR; GLUTAMIC ACID; HETERODIMER; HOMODIMER; ION; METABOTROPIC RECEPTOR; N,N' DICYCLOPENTYL 2 METHYLTHIO 5 NITRO 4,6 PYRIMIDINEDIAMINE; NEUROTRANSMITTER; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 78149497839     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2010.08.009     Document Type: Review
Times cited : (69)

References (129)
  • 1
    • 20344362178 scopus 로고    scopus 로고
    • Amino acid recognition by Venus flytrap domains is encoded in an 8-residue motif
    • Acher F.C., Bertrand H.O. Amino acid recognition by Venus flytrap domains is encoded in an 8-residue motif. Biopolymers 2005, 80:357-366.
    • (2005) Biopolymers , vol.80 , pp. 357-366
    • Acher, F.C.1    Bertrand, H.O.2
  • 3
    • 0028845785 scopus 로고
    • Effects of various valproic acid derivatives on low-calcium spontaneous epileptiform activity in hippocampal slices
    • Armand V., Louvel J., Pumain R., Ronco G., Villa P. Effects of various valproic acid derivatives on low-calcium spontaneous epileptiform activity in hippocampal slices. Epilepsy Res 1995, 22:185-192.
    • (1995) Epilepsy Res , vol.22 , pp. 185-192
    • Armand, V.1    Louvel, J.2    Pumain, R.3    Ronco, G.4    Villa, P.5
  • 4
    • 77951901176 scopus 로고    scopus 로고
    • Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor
    • Assadi-Porter F.M., Maillet E.L., Radek J.T., Quijada J., Markley J.L., Max M. Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor. J. Mol. Biol. 2010, 398:584-599.
    • (2010) J. Mol. Biol. , vol.398 , pp. 584-599
    • Assadi-Porter, F.M.1    Maillet, E.L.2    Radek, J.T.3    Quijada, J.4    Markley, J.L.5    Max, M.6
  • 5
    • 74249121675 scopus 로고    scopus 로고
    • Interactions between the human sweet-sensing T1R2-T1R3 receptor and sweeteners detected by saturation transfer difference NMR spectroscopy
    • Assadi-Porter F.M., Tonelli M., Maillet E.L., Markley J.L., Max M. Interactions between the human sweet-sensing T1R2-T1R3 receptor and sweeteners detected by saturation transfer difference NMR spectroscopy. Biochim. Biophys. Acta 2010, 1798:82-86.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 82-86
    • Assadi-Porter, F.M.1    Tonelli, M.2    Maillet, E.L.3    Markley, J.L.4    Max, M.5
  • 6
    • 0033020243 scopus 로고    scopus 로고
    • Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function
    • Bai M., Trivedi S., Kifor O., Quinn S.J., Brown E.M. Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function. Proc. Natl. Acad. Sci. U S A 1999, 96:2834-2839.
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 2834-2839
    • Bai, M.1    Trivedi, S.2    Kifor, O.3    Quinn, S.J.4    Brown, E.M.5
  • 7
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt T.H., Leitz A.J., Xie G., Oprian D.D., Sligar S.G. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 2007, 282:14875-14881.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 8
    • 0037143619 scopus 로고    scopus 로고
    • Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists
    • Bessis A.S., Rondard P., Gaven F., Brabet I., Triballeau N., Prézeau L., Acher F., Pin J.P. Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists. Proc. Natl. Acad. Sci. U S A 2002, 99:11097-11102.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 11097-11102
    • Bessis, A.S.1    Rondard, P.2    Gaven, F.3    Brabet, I.4    Triballeau, N.5    Prézeau, L.6    Acher, F.7    Pin, J.P.8
  • 9
    • 33646529626 scopus 로고    scopus 로고
    • Molecular diversity, trafficking and subcellular localization of GABAB receptors
    • Bettler B., Tiao J.Y. Molecular diversity, trafficking and subcellular localization of GABAB receptors. Pharmacol. Ther. 2006, 110:533-543.
    • (2006) Pharmacol. Ther. , vol.110 , pp. 533-543
    • Bettler, B.1    Tiao, J.Y.2
  • 10
    • 3142685557 scopus 로고    scopus 로고
    • The heptahelical domain of GABA(B2) is activated directly by CGP7930, a positive allosteric modulator of the GABA(B) receptor
    • Binet V., Brajon C., Le Corre L., Acher F., Pin J.P., Prézeau L. The heptahelical domain of GABA(B2) is activated directly by CGP7930, a positive allosteric modulator of the GABA(B) receptor. J. Biol. Chem. 2004, 279:29085-29091.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29085-29091
    • Binet, V.1    Brajon, C.2    Le Corre, L.3    Acher, F.4    Pin, J.P.5    Prézeau, L.6
  • 11
    • 34249661141 scopus 로고    scopus 로고
    • Common structural requirements for heptahelical domain function in class A and class C G protein-coupled receptors
    • Binet V., Duthey B., Lecaillon J., Vol C., Quoyer J., Labesse G., Pin J.P., Prézeau L. Common structural requirements for heptahelical domain function in class A and class C G protein-coupled receptors. J. Biol. Chem. 2007, 282:12154-12163.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12154-12163
    • Binet, V.1    Duthey, B.2    Lecaillon, J.3    Vol, C.4    Quoyer, J.5    Labesse, G.6    Pin, J.P.7    Prézeau, L.8
  • 12
    • 30844468174 scopus 로고    scopus 로고
    • GABAB receptor: a site of therapeutic benefit
    • Bowery N.G. GABAB receptor: a site of therapeutic benefit. Curr. Opin. Pharmacol. 2006, 6:37-43.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 37-43
    • Bowery, N.G.1
  • 13
    • 33845973375 scopus 로고    scopus 로고
    • Structure, pharmacology and therapeutic prospects of family C G-protein coupled receptors
    • Brauner-Osborne H., Wellendorph P., Jensen A.A. Structure, pharmacology and therapeutic prospects of family C G-protein coupled receptors. Curr. Drug Targets 2007, 8:169-184.
    • (2007) Curr. Drug Targets , vol.8 , pp. 169-184
    • Brauner-Osborne, H.1    Wellendorph, P.2    Jensen, A.A.3
  • 14
    • 28644432057 scopus 로고    scopus 로고
    • Assembly-dependent surface targeting of the heterodimeric GABAB receptor is controlled by COPI but Not 14-3-3
    • Brock C., Boudier L., Maurel D., Blahos J., Pin J.P. Assembly-dependent surface targeting of the heterodimeric GABAB receptor is controlled by COPI but Not 14-3-3. Mol. Biol. Cell 2005, 16:5572-5578.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5572-5578
    • Brock, C.1    Boudier, L.2    Maurel, D.3    Blahos, J.4    Pin, J.P.5
  • 15
    • 36448988595 scopus 로고    scopus 로고
    • Activation of a dimeric metabotropic glutamate receptor by intersubunit rearrangement
    • Brock C., Oueslati N., Soler S., Boudier L., Rondard P., Pin J.P. Activation of a dimeric metabotropic glutamate receptor by intersubunit rearrangement. J. Biol. Chem. 2007, 282:33000-33008.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33000-33008
    • Brock, C.1    Oueslati, N.2    Soler, S.3    Boudier, L.4    Rondard, P.5    Pin, J.P.6
  • 19
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn P., Pin J.-P. Pharmacology and functions of metabotropic glutamate receptors. Annu. Rev. Pharmacol. Toxicol. 1997, 37:205-237.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.1    Pin, J.-P.2
  • 20
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders
    • Conn P.J., Christopoulos A., Lindsley C.W. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat. Rev. Drug Discov. 2009, 8:41-54.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 21
    • 33751505567 scopus 로고    scopus 로고
    • The heterodimeric sweet taste receptor has multiple potential ligand binding sites
    • Cui M., Jiang P., Maillet E., Max M., Margolskee R.F., Osman R. The heterodimeric sweet taste receptor has multiple potential ligand binding sites. Curr. Pharm. Des. 2006, 12:4591-4600.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 4591-4600
    • Cui, M.1    Jiang, P.2    Maillet, E.3    Max, M.4    Margolskee, R.F.5    Osman, R.6
  • 22
    • 33845720603 scopus 로고    scopus 로고
    • Asymmetric conformational changes in a GPCR dimer controlled by G-proteins
    • Damian M., Martin A., Mesnier D., Pin J.P., Banères J.L. Asymmetric conformational changes in a GPCR dimer controlled by G-proteins. Embo J. 2006, 25:5693-5702.
    • (2006) Embo J. , vol.25 , pp. 5693-5702
    • Damian, M.1    Martin, A.2    Mesnier, D.3    Pin, J.P.4    Banères, J.L.5
  • 24
    • 0036479250 scopus 로고    scopus 로고
    • A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor
    • Duthey B., Caudron S., Perroy J., Bettler B., Fagni L., Pin J.P., Prézeau L. A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor. J. Biol. Chem. 2002, 277:3236-3241.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3236-3241
    • Duthey, B.1    Caudron, S.2    Perroy, J.3    Bettler, B.4    Fagni, L.5    Pin, J.P.6    Prézeau, L.7
  • 25
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst O.P., Gramse V., Kolbe M., Hofmann K.P., Heck M. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl. Acad. Sci. U S A 2007, 104:10859-10864.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 26
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors
    • Felder C.B., Graul R.C., Lee A.Y., Merkle H.P., Sadee W. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS Pharm. Sci. 1999, 1:E2.
    • (1999) AAPS Pharm. Sci. , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 28
    • 30744475204 scopus 로고    scopus 로고
    • Among the twenty classical l-amino acids, only glutamate directly activates metabotropic glutamate receptors
    • Frauli M., Neuville P., Vol C., Pin J.P., Prézeau L. Among the twenty classical l-amino acids, only glutamate directly activates metabotropic glutamate receptors. Neuropharmacology 2006, 50:245-253.
    • (2006) Neuropharmacology , vol.50 , pp. 245-253
    • Frauli, M.1    Neuville, P.2    Vol, C.3    Pin, J.P.4    Prézeau, L.5
  • 29
    • 0035341213 scopus 로고    scopus 로고
    • Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function
    • Galvez T., Duthey B., Kniazeff J., Blahos J., Rovelli G., Bettler B., Prézeau L., Pin J.P. Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function. Embo J. 2001, 20:2152-2159.
    • (2001) Embo J. , vol.20 , pp. 2152-2159
    • Galvez, T.1    Duthey, B.2    Kniazeff, J.3    Blahos, J.4    Rovelli, G.5    Bettler, B.6    Prézeau, L.7    Pin, J.P.8
  • 35
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han Y., Moreira I.S., Urizar E., Weinstein H., Javitch J.A. Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat. Chem. Biol. 2009, 5:688-695.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 36
    • 0035979721 scopus 로고    scopus 로고
    • Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone
    • He X., Chow D., Martick M.M., Garcia K.C. Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science 2001, 293:1657-1662.
    • (2001) Science , vol.293 , pp. 1657-1662
    • He, X.1    Chow, D.2    Martick, M.M.3    Garcia, K.C.4
  • 37
    • 0022586049 scopus 로고
    • Extracellular calcium and potassium concentration changes in chronic epileptic brain tissue
    • Heinemann U., Konnerth A., Pumain R., Wadman W.J. Extracellular calcium and potassium concentration changes in chronic epileptic brain tissue. Adv. Neurol. 1986, 44:641-661.
    • (1986) Adv. Neurol. , vol.44 , pp. 641-661
    • Heinemann, U.1    Konnerth, A.2    Pumain, R.3    Wadman, W.J.4
  • 39
    • 0034716854 scopus 로고    scopus 로고
    • Human Ca2+ receptor cysteine-rich domain. Analysis of function of mutant and chimeric receptors
    • Hu J., Hauache O., Spiegel A.M. Human Ca2+ receptor cysteine-rich domain. Analysis of function of mutant and chimeric receptors. J. Biol. Chem. 2000, 275:16382-16389.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16382-16389
    • Hu, J.1    Hauache, O.2    Spiegel, A.M.3
  • 40
    • 14244269537 scopus 로고    scopus 로고
    • A region in the seven-transmembrane domain of the human Ca2+ receptor critical for response to Ca2+
    • Hu J., McLarnon S.J., Mora S., Jiang J., Thomas C., Jacobson K.A., Spiegel A.M. A region in the seven-transmembrane domain of the human Ca2+ receptor critical for response to Ca2+. J. Biol. Chem. 2005, 280:5113-5120.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5113-5120
    • Hu, J.1    McLarnon, S.J.2    Mora, S.3    Jiang, J.4    Thomas, C.5    Jacobson, K.A.6    Spiegel, A.M.7
  • 41
    • 0037195862 scopus 로고    scopus 로고
    • Identification of acidic residues in the extracellular loops of the seven-transmembrane domain of the human Ca2+ receptor critical for response to Ca2+ and a positive allosteric modulator
    • Hu J., Reyes-Cruz G., Chen W., Jacobson K.A., Spiegel A.M. Identification of acidic residues in the extracellular loops of the seven-transmembrane domain of the human Ca2+ receptor critical for response to Ca2+ and a positive allosteric modulator. J. Biol. Chem. 2002, 277:46622-46631.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46622-46631
    • Hu, J.1    Reyes-Cruz, G.2    Chen, W.3    Jacobson, K.A.4    Spiegel, A.M.5
  • 42
    • 34547131843 scopus 로고    scopus 로고
    • Identification and dissection of Ca(2+)-binding sites in the extracellular domain of Ca(2+)-sensing receptor
    • Huang Y., Zhou Y., Yang W., Butters R., Lee H.W., Li S., Castiblanco A., Brown E.M., Yang J.J. Identification and dissection of Ca(2+)-binding sites in the extracellular domain of Ca(2+)-sensing receptor. J. Biol. Chem. 2007, 282:19000-19010.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19000-19010
    • Huang, Y.1    Zhou, Y.2    Yang, W.3    Butters, R.4    Lee, H.W.5    Li, S.6    Castiblanco, A.7    Brown, E.M.8    Yang, J.J.9
  • 44
    • 26644458124 scopus 로고    scopus 로고
    • Identification of the cyclamate interaction site within the transmembrane domain of the human sweet taste receptor subunit T1R3
    • Jiang P., Cui M., Zhao B., Snyder L.A., Benard L.M., Osman R., Max M., Margolskee R.F. Identification of the cyclamate interaction site within the transmembrane domain of the human sweet taste receptor subunit T1R3. J. Biol. Chem. 2005, 280:34296-34305.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34296-34305
    • Jiang, P.1    Cui, M.2    Zhao, B.3    Snyder, L.A.4    Benard, L.M.5    Osman, R.6    Max, M.7    Margolskee, R.F.8
  • 45
  • 48
    • 73249130654 scopus 로고    scopus 로고
    • Activating autoantibodies against the calcium-sensing receptor detected in two patients with autoimmune polyendocrine syndrome type 1
    • Kemp E.H., Gavalas N.G., Krohn K.J., Brown E.M., Watson P.F., Weetman A.P. Activating autoantibodies against the calcium-sensing receptor detected in two patients with autoimmune polyendocrine syndrome type 1. J. Clin. Endocrinol. Metab. 2009, 94:4749-4756.
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 4749-4756
    • Kemp, E.H.1    Gavalas, N.G.2    Krohn, K.J.3    Brown, E.M.4    Watson, P.F.5    Weetman, A.P.6
  • 51
    • 0036759170 scopus 로고    scopus 로고
    • No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits
    • Kniazeff J., Galvez T., Labesse G., Pin J.P. No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits. J. Neurosci. 2002, 22:7352-7361.
    • (2002) J. Neurosci. , vol.22 , pp. 7352-7361
    • Kniazeff, J.1    Galvez, T.2    Labesse, G.3    Pin, J.P.4
  • 55
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom M.C., Schioth H.B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat. Rev. Drug Discov. 2008, 7:339-357.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 58
    • 1942469528 scopus 로고    scopus 로고
    • Molecular determinants involved in the allosteric control of agonist affinity in GABAB receptor by the GABAB2 subunit
    • Liu J., Maurel D., Etzol S., Brabet I., Pin J.-P., Rondard P. Molecular determinants involved in the allosteric control of agonist affinity in GABAB receptor by the GABAB2 subunit. J. Biol. Chem. 2004, 279:15824-15830.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15824-15830
    • Liu, J.1    Maurel, D.2    Etzol, S.3    Brabet, I.4    Pin, J.-P.5    Rondard, P.6
  • 60
    • 34248393065 scopus 로고    scopus 로고
    • An acquired hypocalciuric hypercalcemia autoantibody induces allosteric transition among active human Ca-sensing receptor conformations
    • Makita N., Sato J., Manaka K., Shoji Y., Oishi A., Hashimoto M., Fujita T., Iiri T. An acquired hypocalciuric hypercalcemia autoantibody induces allosteric transition among active human Ca-sensing receptor conformations. Proc. Natl. Acad. Sci. U S A 2007, 104:5443-5448.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 5443-5448
    • Makita, N.1    Sato, J.2    Manaka, K.3    Shoji, Y.4    Oishi, A.5    Hashimoto, M.6    Fujita, T.7    Iiri, T.8
  • 61
    • 0037424518 scopus 로고    scopus 로고
    • Mutational analysis and molecular modeling of the allosteric binding site of a novel, selective, noncompetitive antagonist of the metabotropic glutamate 1 receptor
    • Malherbe P., Kratochwil N., Knoflach F., Zenner M.T., Kew J.N., Kratzeisen C., Maerki H.P., Adam G., Mutel V. Mutational analysis and molecular modeling of the allosteric binding site of a novel, selective, noncompetitive antagonist of the metabotropic glutamate 1 receptor. J. Biol. Chem. 2003, 278:8340-8347.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8340-8347
    • Malherbe, P.1    Kratochwil, N.2    Knoflach, F.3    Zenner, M.T.4    Kew, J.N.5    Kratzeisen, C.6    Maerki, H.P.7    Adam, G.8    Mutel, V.9
  • 62
    • 0141569326 scopus 로고    scopus 로고
    • Mutational analysis and molecular modeling of the binding pocket of the metabotropic glutamate 5 receptor negative modulator 2-methyl-6-(phenylethynyl)-pyridine
    • Malherbe P., Kratochwil N., Zenner M.T., Piussi J., Diener C., Kratzeisen C., Fischer C., Porter R.H. Mutational analysis and molecular modeling of the binding pocket of the metabotropic glutamate 5 receptor negative modulator 2-methyl-6-(phenylethynyl)-pyridine. Mol. Pharmacol. 2003, 64:823-832.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 823-832
    • Malherbe, P.1    Kratochwil, N.2    Zenner, M.T.3    Piussi, J.4    Diener, C.5    Kratzeisen, C.6    Fischer, C.7    Porter, R.H.8
  • 64
    • 67650494991 scopus 로고    scopus 로고
    • Optical measurement of mGluR1 conformational changes reveals fast activation, slow deactivation, and sensitization
    • Marcaggi P., Mutoh H., Dimitrov D., Beato M., Knopfel T. Optical measurement of mGluR1 conformational changes reveals fast activation, slow deactivation, and sensitization. Proc. Natl. Acad. Sci. U S A 2009, 106:11388-11393.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 11388-11393
    • Marcaggi, P.1    Mutoh, H.2    Dimitrov, D.3    Beato, M.4    Knopfel, T.5
  • 65
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic M., Jan Y.N., Jan L.Y. A trafficking checkpoint controls GABA(B) receptor heterodimerization. Neuron 2000, 27:97-106.
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 66
    • 0035807889 scopus 로고    scopus 로고
    • Ligand-induced signal transduction within heterodimeric GABA(B) receptors
    • Margeta-Mitrovic M., Jan Y.N., Jan L.Y. Ligand-induced signal transduction within heterodimeric GABA(B) receptors. Proc. Natl. Acad. Sci. U S A 2001, 98:14643-14648.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 14643-14648
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 67
    • 0035807875 scopus 로고    scopus 로고
    • Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors
    • Margeta-Mitrovic M., Jan Y.N., Jan L.Y. Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors. Proc. Natl. Acad. Sci. U S A 2001, 98:14649-14654.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 14649-14654
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 69
    • 30844432624 scopus 로고    scopus 로고
    • Glutamate-based therapeutic approaches: allosteric modulators of metabotropic glutamate receptors
    • Marino M.J., Conn P.J. Glutamate-based therapeutic approaches: allosteric modulators of metabotropic glutamate receptors. Curr. Opin. Pharmacol. 2006, 6:98-102.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 98-102
    • Marino, M.J.1    Conn, P.J.2
  • 71
    • 0037363728 scopus 로고    scopus 로고
    • Positive allosteric modulation of the human metabotropic glutamate receptor 4 (hmGluR4) by SIB-1893 and MPEP
    • Mathiesen J.M., Svendsen N., Brauner-Osborne H., Thomsen C., Ramirez M.T. Positive allosteric modulation of the human metabotropic glutamate receptor 4 (hmGluR4) by SIB-1893 and MPEP. Br. J. Pharmacol. 2003, 138:1026-1030.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1026-1030
    • Mathiesen, J.M.1    Svendsen, N.2    Brauner-Osborne, H.3    Thomsen, C.4    Ramirez, M.T.5
  • 73
    • 48749100421 scopus 로고    scopus 로고
    • Sweet taste in man: a review
    • Meyers B., Brewer M.S. Sweet taste in man: a review. J. Food Sci. 2008, 73:R81-90.
    • (2008) J. Food Sci. , vol.73
    • Meyers, B.1    Brewer, M.S.2
  • 74
    • 1342346546 scopus 로고    scopus 로고
    • Homology modeling of the transmembrane domain of the human calcium sensing receptor and localization of an allosteric binding site
    • Miedlich S.U., Gama L., Seuwen K., Wolf R.M., Breitwieser G.E. Homology modeling of the transmembrane domain of the human calcium sensing receptor and localization of an allosteric binding site. J. Biol. Chem. 2004, 279:7254-7263.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7254-7263
    • Miedlich, S.U.1    Gama, L.2    Seuwen, K.3    Wolf, R.M.4    Breitwieser, G.E.5
  • 76
    • 23944498549 scopus 로고    scopus 로고
    • From small sweeteners to sweet proteins: anatomy of the binding sites of the human T1R2_T1R3 receptor
    • Morini G., Bassoli A., Temussi P.A. From small sweeteners to sweet proteins: anatomy of the binding sites of the human T1R2_T1R3 receptor. J. Med. Chem. 2005, 48:5520-5529.
    • (2005) J. Med. Chem. , vol.48 , pp. 5520-5529
    • Morini, G.1    Bassoli, A.2    Temussi, P.A.3
  • 77
    • 23844491861 scopus 로고    scopus 로고
    • A double mutation in the extracellular Ca2+-sensing receptor's venus flytrap domain that selectively disables l-amino acid sensing
    • Mun H.C., Culverston E.L., Franks A.H., Collyer C.A., Clifton-Bligh R.J., Conigrave A.D. A double mutation in the extracellular Ca2+-sensing receptor's venus flytrap domain that selectively disables l-amino acid sensing. J. Biol. Chem. 2005, 280:29067-29072.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29067-29072
    • Mun, H.C.1    Culverston, E.L.2    Franks, A.H.3    Collyer, C.A.4    Clifton-Bligh, R.J.5    Conigrave, A.D.6
  • 78
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • Muto T., Tsuchiya D., Morikawa K., Jingami H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc. Natl. Acad. Sci. U S A 2007, 104:3759-3764.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 79
    • 77949516412 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: physiology, pharmacology, and disease
    • Niswender C.M., Conn P.J. Metabotropic glutamate receptors: physiology, pharmacology, and disease. Annu. Rev. Pharmacol. Toxicol. 2010, 50:295-322.
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 295-322
    • Niswender, C.M.1    Conn, P.J.2
  • 82
    • 3142582002 scopus 로고    scopus 로고
    • Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction
    • Ogawa H., Qiu Y., Ogata C.M., Misono K.S. Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. J. Biol. Chem. 2004, 279:28625-28631.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28625-28631
    • Ogawa, H.1    Qiu, Y.2    Ogata, C.M.3    Misono, K.S.4
  • 85
    • 0034721795 scopus 로고    scopus 로고
    • The non-competitive antagonists 2-methyl-6-(phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group-I metabotropic glutamate receptors
    • Pagano A., Ruegg D., Litschig S., Stoehr N., Stierlin C., Heinrich M., Floersheim P., Prézeau L., Carroll F., Pin J.P., Cambria A., Vranesic I., Flor P.J., Gasparini F., Kuhn R. The non-competitive antagonists 2-methyl-6-(phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group-I metabotropic glutamate receptors. J. Biol. Chem. 2000, 275:33750-33758.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33750-33758
    • Pagano, A.1    Ruegg, D.2    Litschig, S.3    Stoehr, N.4    Stierlin, C.5    Heinrich, M.6    Floersheim, P.7    Prézeau, L.8    Carroll, F.9    Pin, J.P.10    Cambria, A.11    Vranesic, I.12    Flor, P.J.13    Gasparini, F.14    Kuhn, R.15
  • 87
    • 2442548717 scopus 로고    scopus 로고
    • Positive and negative allosteric modulators of the Ca2+-sensing receptor interact within overlapping but not identical binding sites in the transmembrane domain
    • Petrel C., Kessler A., Dauban P., Dodd R.H., Rognan D., Ruat M. Positive and negative allosteric modulators of the Ca2+-sensing receptor interact within overlapping but not identical binding sites in the transmembrane domain. J. Biol. Chem. 2004, 279:18990-18997.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18990-18997
    • Petrel, C.1    Kessler, A.2    Dauban, P.3    Dodd, R.H.4    Rognan, D.5    Ruat, M.6
  • 88
    • 1442358771 scopus 로고    scopus 로고
    • Modeling and mutagenesis of the binding site of Calhex 231, a novel negative allosteric modulator of the extracellular Ca(2+)-sensing receptor
    • Petrel C., Kessler A., Maslah F., Dauban P., Dodd R.H., Rognan D., Ruat M. Modeling and mutagenesis of the binding site of Calhex 231, a novel negative allosteric modulator of the extracellular Ca(2+)-sensing receptor. J. Biol. Chem. 2003, 278:49487-49494.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49487-49494
    • Petrel, C.1    Kessler, A.2    Maslah, F.3    Dauban, P.4    Dodd, R.H.5    Rognan, D.6    Ruat, M.7
  • 90
    • 0001050066 scopus 로고    scopus 로고
    • The metabotropic glutamate receptors: structure, activation mechanism and pharmacology
    • Pin J.-P., Acher F. The metabotropic glutamate receptors: structure, activation mechanism and pharmacology. Curr. Drug Targets 2002, 1:297-317.
    • (2002) Curr. Drug Targets , vol.1 , pp. 297-317
    • Pin, J.-P.1    Acher, F.2
  • 91
    • 0038662595 scopus 로고    scopus 로고
    • Evolution, structure and activation mechanism of family 3/C G-protein coupled receptors
    • Pin J.-P., Galvez T., Prézeau L. Evolution, structure and activation mechanism of family 3/C G-protein coupled receptors. Pharmacol. Ther. 2003, 98:325-354.
    • (2003) Pharmacol. Ther. , vol.98 , pp. 325-354
    • Pin, J.-P.1    Galvez, T.2    Prézeau, L.3
  • 93
    • 0025716317 scopus 로고
    • Atomic structure of periplasmic binding proteins and the high-affinity active transport system in bacteria
    • Quiocho F.A. Atomic structure of periplasmic binding proteins and the high-affinity active transport system in bacteria. Phil. Trans. R. Soc. Lond. (B) 1990, 326:341-351.
    • (1990) Phil. Trans. R. Soc. Lond. (B) , vol.326 , pp. 341-351
    • Quiocho, F.A.1
  • 94
    • 0034602293 scopus 로고    scopus 로고
    • Cys-140 is critical for metabotropic glutamate receptor-1 dimerization [In Process Citation]
    • Ray K., Hauschild B.C. Cys-140 is critical for metabotropic glutamate receptor-1 dimerization [In Process Citation]. J. Biol. Chem. 2000, 275:34245-34251.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34245-34251
    • Ray, K.1    Hauschild, B.C.2
  • 95
    • 0033600911 scopus 로고    scopus 로고
    • Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor
    • Ray K., Hauschild B.C., Steinbach P.J., Goldsmith P.K., Hauache O., Spiegel A.M. Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor. J. Biol. Chem. 1999, 274:27642-27650.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27642-27650
    • Ray, K.1    Hauschild, B.C.2    Steinbach, P.J.3    Goldsmith, P.K.4    Hauache, O.5    Spiegel, A.M.6
  • 96
    • 27744560413 scopus 로고    scopus 로고
    • Calindol, a positive allosteric modulator of the human Ca(2+) receptor, activates an extracellular ligand-binding domain-deleted rhodopsin-like seven-transmembrane structure in the absence of Ca(2+)
    • Ray K., Tisdale J., Dodd R.H., Dauban P., Ruat M., Northup J.K. Calindol, a positive allosteric modulator of the human Ca(2+) receptor, activates an extracellular ligand-binding domain-deleted rhodopsin-like seven-transmembrane structure in the absence of Ca(2+). J. Biol. Chem. 2005, 280:37013-37020.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37013-37020
    • Ray, K.1    Tisdale, J.2    Dodd, R.H.3    Dauban, P.4    Ruat, M.5    Northup, J.K.6
  • 100
    • 33747739191 scopus 로고    scopus 로고
    • Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors
    • Rondard P., Liu J., Huang S., Malhaire F., Vol C., Pinault A., Labesse G., Pin J.P. Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors. J. Biol. Chem. 2006, 281:24653-24661.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24653-24661
    • Rondard, P.1    Liu, J.2    Huang, S.3    Malhaire, F.4    Vol, C.5    Pinault, A.6    Labesse, G.7    Pin, J.P.8
  • 105
    • 27844587815 scopus 로고    scopus 로고
    • Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor
    • Silve C., Petrel C., Leroy C., Bruel H., Mallet E., Rognan D., Ruat M. Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor. J. Biol. Chem. 2005, 280:37917-37923.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37917-37923
    • Silve, C.1    Petrel, C.2    Leroy, C.3    Bruel, H.4    Mallet, E.5    Rognan, D.6    Ruat, M.7
  • 106
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky A.I., Rosconi M.P., Gouaux E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 2009, 462:745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 108
    • 2942574363 scopus 로고    scopus 로고
    • Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin
    • Tancredi T., Pastore A., Salvadori S., Esposito V., Temussi P.A. Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin. Eur. J. Biochem. 2004, 271:2231-2240.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2231-2240
    • Tancredi, T.1    Pastore, A.2    Salvadori, S.3    Esposito, V.4    Temussi, P.A.5
  • 109
    • 3042551375 scopus 로고    scopus 로고
    • Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha
    • Tateyama M., Abe H., Nakata H., Saito O., Kubo Y. Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha. Nat. Struct. Mol. Biol. 2004, 11:637-642.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 637-642
    • Tateyama, M.1    Abe, H.2    Nakata, H.3    Saito, O.4    Kubo, Y.5
  • 110
    • 32244436435 scopus 로고    scopus 로고
    • Dual signaling is differentially activated by different active states of the metabotropic glutamate receptor 1alpha
    • Tateyama M., Kubo Y. Dual signaling is differentially activated by different active states of the metabotropic glutamate receptor 1alpha. Proc. Natl. Acad. Sci. U S A 2006, 103:1124-1128.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 1124-1128
    • Tateyama, M.1    Kubo, Y.2
  • 111
    • 34748919072 scopus 로고    scopus 로고
    • The sweet taste receptor: a single receptor with multiple sites and modes of interaction
    • Temussi P. The sweet taste receptor: a single receptor with multiple sites and modes of interaction. Adv. Food Nutr. Res. 2007, 53:199-239.
    • (2007) Adv. Food Nutr. Res. , vol.53 , pp. 199-239
    • Temussi, P.1
  • 112
    • 18244363907 scopus 로고    scopus 로고
    • The calcium-sensing receptor in normal physiology and pathophysiology: a review
    • Tfelt-Hansen J., Brown E.M. The calcium-sensing receptor in normal physiology and pathophysiology: a review. Crit. Rev. Clin. Lab. Sci. 2005, 42:35-70.
    • (2005) Crit. Rev. Clin. Lab. Sci. , vol.42 , pp. 35-70
    • Tfelt-Hansen, J.1    Brown, E.M.2
  • 113
    • 17144385534 scopus 로고    scopus 로고
    • Virtual screening workflow development guided by the " receiver operating characteristic" curve approach. Application to high-throughput docking on metabotropic glutamate receptor subtype 4
    • Triballeau N., Acher F., Brabet I., Pin J.P., Bertrand H.O. Virtual screening workflow development guided by the " receiver operating characteristic" curve approach. Application to high-throughput docking on metabotropic glutamate receptor subtype 4. J. Med. Chem. 2005, 48:2534-2547.
    • (2005) J. Med. Chem. , vol.48 , pp. 2534-2547
    • Triballeau, N.1    Acher, F.2    Brabet, I.3    Pin, J.P.4    Bertrand, H.O.5
  • 114
    • 0037022586 scopus 로고    scopus 로고
    • Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+
    • Tsuchiya D., Kunishima N., Kamiya N., Jingami H., Morikawa K. Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+. Proc. Natl. Acad. Sci. U S A 2002, 99:2660-2665.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 116
    • 0141742370 scopus 로고    scopus 로고
    • N, N'-Dicyclopentyl-2-methylsulfanyl-5-nitro-pyrimidine-4,6-diamine (GS39783) and structurally related compounds: novel allosteric enhancers of gamma-aminobutyric acidB receptor function
    • Urwyler S., Pozza M.F., Lingenhoehl K., Mosbacher J., Lampert C., Froestl W., Koller M., Kaupmann K. N, N'-Dicyclopentyl-2-methylsulfanyl-5-nitro-pyrimidine-4,6-diamine (GS39783) and structurally related compounds: novel allosteric enhancers of gamma-aminobutyric acidB receptor function. J. Pharmacol. Exp. Ther. 2003, 307:322-330.
    • (2003) J. Pharmacol. Exp. Ther. , vol.307 , pp. 322-330
    • Urwyler, S.1    Pozza, M.F.2    Lingenhoehl, K.3    Mosbacher, J.4    Lampert, C.5    Froestl, W.6    Koller, M.7    Kaupmann, K.8
  • 117
    • 0034612573 scopus 로고    scopus 로고
    • Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor
    • van den Akker F., Zhang X., Miyagi M., Huo X., Misono K.S., Yee V.C. Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor. Nature 2000, 406:101-104.
    • (2000) Nature , vol.406 , pp. 101-104
    • van den Akker, F.1    Zhang, X.2    Miyagi, M.3    Huo, X.4    Misono, K.S.5    Yee, V.C.6
  • 118
    • 69549111756 scopus 로고    scopus 로고
    • Molecular pharmacology of promiscuous seven transmembrane receptors sensing organic nutrients
    • Wellendorph P., Johansen L.D., Brauner-Osborne H. Molecular pharmacology of promiscuous seven transmembrane receptors sensing organic nutrients. Mol. Pharmacol. 2009, 76:453-465.
    • (2009) Mol. Pharmacol. , vol.76 , pp. 453-465
    • Wellendorph, P.1    Johansen, L.D.2    Brauner-Osborne, H.3
  • 122
    • 36749099088 scopus 로고    scopus 로고
    • The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor
    • Winnig M., Bufe B., Kratochwil N.A., Slack J.P., Meyerhof W. The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor. BMC Struct. Biol. 2007, 7:66-78.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 66-78
    • Winnig, M.1    Bufe, B.2    Kratochwil, N.A.3    Slack, J.P.4    Meyerhof, W.5
  • 123
    • 26444538550 scopus 로고    scopus 로고
    • Valine 738 and lysine 735 in the fifth transmembrane domain of rTas1r3 mediate insensitivity towards lactisole of the rat sweet taste receptor
    • Winnig M., Bufe B., Meyerhof W. Valine 738 and lysine 735 in the fifth transmembrane domain of rTas1r3 mediate insensitivity towards lactisole of the rat sweet taste receptor. BMC Neurosci. 2005, 6:22.
    • (2005) BMC Neurosci. , vol.6 , pp. 22
    • Winnig, M.1    Bufe, B.2    Meyerhof, W.3
  • 126
    • 0034063038 scopus 로고    scopus 로고
    • Umami and food palatability
    • Yamaguchi S., Ninomiya K. Umami and food palatability. J. Nutr. 2000, 130:921S-926S.
    • (2000) J. Nutr. , vol.130
    • Yamaguchi, S.1    Ninomiya, K.2
  • 129
    • 0037072797 scopus 로고    scopus 로고
    • Three adjacent serines in the extracellular domains of the CaR are required for l-amino acid-mediated potentiation of receptor function
    • Zhang Z., Qiu W., Quinn S.J., Conigrave A.D., Brown E.M., Bai M. Three adjacent serines in the extracellular domains of the CaR are required for l-amino acid-mediated potentiation of receptor function. J. Biol. Chem. 2002, 277:33727-33735.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33727-33735
    • Zhang, Z.1    Qiu, W.2    Quinn, S.J.3    Conigrave, A.D.4    Brown, E.M.5    Bai, M.6


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