메뉴 건너뛰기




Volumn 85, Issue 2, 2017, Pages 332-341

The anatomy of mammalian sweet taste receptors

Author keywords

chemical senses; class C; GPCR; structure function relationships; sweet taste; T1R

Indexed keywords

G PROTEIN COUPLED RECEPTOR; METABOTROPIC RECEPTOR 1; METABOTROPIC RECEPTOR 5; GRM5 PROTEIN, HUMAN; LIGAND; METABOTROPIC GLUTAMATE RECEPTOR TYPE 1; METABOTROPIC RECEPTOR; PROTEIN BINDING; SWEETENING AGENT; TASTE RECEPTORS, TYPE 1;

EID: 85010378578     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.25228     Document Type: Article
Times cited : (40)

References (71)
  • 1
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum DM, Rasmussen SGF, Kobilka BK. The structure and function of G-protein-coupled receptors. Nature 2009;459:356–363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 2
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch V, Cherezov V, Stevens RC. Structure-function of the G protein-coupled receptor superfamily. Annu Rev Pharmacol Toxicol 2013;53:531–556.
    • (2013) Annu Rev Pharmacol Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 3
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka BK, Deupi X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 2007;28:397–406.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 4
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerström MC, Lundin L-G, Schiöth HB. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 2003;63:1256–1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerström, M.C.2    Lundin, L.-G.3    Schiöth, H.B.4
  • 10
    • 84902271945 scopus 로고    scopus 로고
    • Functional roles of the sweet taste receptor in oral and extraoral tissues
    • Laffitte A, Neiers F, Briand L. Functional roles of the sweet taste receptor in oral and extraoral tissues. Curr Opin Clin Nutr Metab Care 2014;17:379–385.
    • (2014) Curr Opin Clin Nutr Metab Care , vol.17 , pp. 379-385
    • Laffitte, A.1    Neiers, F.2    Briand, L.3
  • 11
    • 67650628028 scopus 로고    scopus 로고
    • Molecular basis for amino acid sensing by family C G-protein-coupled receptors
    • Wellendorph P, Bräuner-Osborne H. Molecular basis for amino acid sensing by family C G-protein-coupled receptors. Br J Pharmacol 2009;156:869–884.
    • (2009) Br J Pharmacol , vol.156 , pp. 869-884
    • Wellendorph, P.1    Bräuner-Osborne, H.2
  • 12
    • 4644308014 scopus 로고    scopus 로고
    • Different functional roles of T1R subunits in the heteromeric taste receptors
    • Xu H, Staszewski L, Tang H, Adler E, Zoller M, Li X. Different functional roles of T1R subunits in the heteromeric taste receptors. Proc Natl Acad Sci USA 2004;101:14258–14263.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14258-14263
    • Xu, H.1    Staszewski, L.2    Tang, H.3    Adler, E.4    Zoller, M.5    Li, X.6
  • 15
    • 33947424283 scopus 로고    scopus 로고
    • Mechanistic events underlying odorant binding protein chemoreception
    • Golebiowski J, Antonczak S, Fiorucci S, Cabrol-Bass D. Mechanistic events underlying odorant binding protein chemoreception. Proteins 2007;67:448–458.
    • (2007) Proteins , vol.67 , pp. 448-458
    • Golebiowski, J.1    Antonczak, S.2    Fiorucci, S.3    Cabrol-Bass, D.4
  • 16
    • 84859986450 scopus 로고    scopus 로고
    • Characterization of the modes of binding between human sweet taste receptor and low-molecular-weight sweet compounds
    • Masuda K, Koizumi A, Nakajima K, Tanaka T, Abe K, Misaka T, Ishiguro M. Characterization of the modes of binding between human sweet taste receptor and low-molecular-weight sweet compounds. PLoS One 2012;7:e35380.
    • (2012) PLoS One , vol.7
    • Masuda, K.1    Koizumi, A.2    Nakajima, K.3    Tanaka, T.4    Abe, K.5    Misaka, T.6    Ishiguro, M.7
  • 19
    • 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 LA, Benard LMJ, Osman R, Max M, Margolskee RF. 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.J.5    Osman, R.6    Max, M.7    Margolskee, R.F.8
  • 20
    • 36749099088 scopus 로고    scopus 로고
    • The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor
    • Winnig M, Bufe B, Kratochwil NA, Slack JP, Meyerhof W. The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor. BMC Struct Biol 2007;7:66.
    • (2007) BMC Struct Biol , vol.7 , pp. 66
    • Winnig, M.1    Bufe, B.2    Kratochwil, N.A.3    Slack, J.P.4    Meyerhof, W.5
  • 24
    • 0037423395 scopus 로고    scopus 로고
    • Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1
    • Sato T, Shimada Y, Nagasawa N, Nakanishi S, Jingami H. Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. J Biol Chem 2003;278:4314–4321.
    • (2003) J Biol Chem , vol.278 , pp. 4314-4321
    • Sato, T.1    Shimada, Y.2    Nagasawa, N.3    Nakanishi, S.4    Jingami, H.5
  • 25
    • 77958514966 scopus 로고    scopus 로고
    • Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1α (mGluR1α) that controls receptor activation
    • Jiang Y, Huang Y, Wong H-C, Zhou Y, Wang X, Yang J, Hall RA, Brown EM, Yang JJ. Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1α (mGluR1α) that controls receptor activation. J Biol Chem 2010;285:33463–33474.
    • (2010) J Biol Chem , vol.285 , pp. 33463-33474
    • Jiang, Y.1    Huang, Y.2    Wong, H.-C.3    Zhou, Y.4    Wang, X.5    Yang, J.6    Hall, R.A.7    Brown, E.M.8    Yang, J.J.9
  • 26
    • 84908191816 scopus 로고    scopus 로고
    • Selectivity and evolutionary divergence of metabotropic glutamate receptors for endogenous ligands and G proteins coupled to phospholipase C or TRP channels
    • Kang HJ, Menlove K, Ma J, Wilkins A, Lichtarge O, Wensel TG. Selectivity and evolutionary divergence of metabotropic glutamate receptors for endogenous ligands and G proteins coupled to phospholipase C or TRP channels. J Biol Chem 2014;289:29961–29974.
    • (2014) J Biol Chem , vol.289 , pp. 29961-29974
    • Kang, H.J.1    Menlove, K.2    Ma, J.3    Wilkins, A.4    Lichtarge, O.5    Wensel, T.G.6
  • 28
    • 0042230756 scopus 로고    scopus 로고
    • Molecular modeling and mutagenesis of the ligand-binding pocket of the mGlu3 subtype of metabotropic glutamate receptor
    • Yao Y, Pattabiraman N, Michne WF, Huang X-P, Hampson DR. Molecular modeling and mutagenesis of the ligand-binding pocket of the mGlu3 subtype of metabotropic glutamate receptor. J Neurochem 2003;86:947–957.
    • (2003) J Neurochem , vol.86 , pp. 947-957
    • Yao, Y.1    Pattabiraman, N.2    Michne, W.F.3    Huang, X.-P.4    Hampson, D.R.5
  • 30
    • 0036510646 scopus 로고    scopus 로고
    • Molecular determinants of high affinity binding to group III metabotropic glutamate receptors
    • Rosemond E, Peltekova V, Naples M, Thøgersen H, Hampson DR. Molecular determinants of high affinity binding to group III metabotropic glutamate receptors. J Biol Chem 2002;277:7333–7340.
    • (2002) J Biol Chem , vol.277 , pp. 7333-7340
    • Rosemond, E.1    Peltekova, V.2    Naples, M.3    Thøgersen, H.4    Hampson, D.R.5
  • 31
    • 4544287627 scopus 로고    scopus 로고
    • Mutation-induced quisqualic acid and ibotenic acid affinity at the metabotropic glutamate receptor subtype 4
    • Hermit MB, Greenwood JR, Bräuner-Osborne H. Mutation-induced quisqualic acid and ibotenic acid affinity at the metabotropic glutamate receptor subtype 4. J Biol Chem 2004;279:34811–34817.
    • (2004) J Biol Chem , vol.279 , pp. 34811-34817
    • Hermit, M.B.1    Greenwood, J.R.2    Bräuner-Osborne, H.3
  • 34
    • 33748927491 scopus 로고    scopus 로고
    • Point mutations in either subunit of the GABAB receptor confer constitutive activity to the heterodimer
    • Mukherjee RS, McBride EW, Beinborn M, Dunlap K, Kopin AS. Point mutations in either subunit of the GABAB receptor confer constitutive activity to the heterodimer. Mol Pharmacol 2006;70:1406–1413.
    • (2006) Mol Pharmacol , vol.70 , pp. 1406-1413
    • Mukherjee, R.S.1    McBride, E.W.2    Beinborn, M.3    Dunlap, K.4    Kopin, A.S.5
  • 36
    • 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, Prezeau L, Carroll F, Pin J-P, Cambria A, Vranesic I, Flor PJ, 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    Prezeau, 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
  • 37
    • 0035818605 scopus 로고    scopus 로고
    • Positive allosteric modulators of metabotropic glutamate 1 receptor: characterization, mechanism of action, and binding site
    • Knoflach F, Mutel V, Jolidon S, Kew JN, Malherbe P, Vieira E, Wichmann J, Kemp JA. Positive allosteric modulators of metabotropic glutamate 1 receptor: characterization, mechanism of action, and binding site. Proc Natl Acad Sci USA 2001;98:13402–13407.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13402-13407
    • Knoflach, F.1    Mutel, V.2    Jolidon, S.3    Kew, J.N.4    Malherbe, P.5    Vieira, E.6    Wichmann, J.7    Kemp, J.A.8
  • 38
    • 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 JNC, Kratzeisen C, Maerki HP, 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.C.5    Kratzeisen, C.6    Maerki, H.P.7    Adam, G.8    Mutel, V.9
  • 39
    • 34248667888 scopus 로고    scopus 로고
    • Pharmacological characterization of a new, orally active and potent allosteric metabotropic glutamate receptor 1 antagonist, 4-[1-(2-fluoropyridin-3-yl)−5-methyl-1H-1,2,3-triazol-4-yl]-N-isopropyl-N-methyl-3,6-dihydropyridine-1(2H)-carboxamide (FTIDC)
    • Suzuki G, Kimura T, Satow A, Kaneko N, Fukuda J, Hikichi H, Sakai N, Maehara S, Kawagoe-Takaki H, Hata M, Azuma T, Ito S, Kawamoto H, Ohta H. Pharmacological characterization of a new, orally active and potent allosteric metabotropic glutamate receptor 1 antagonist, 4-[1-(2-fluoropyridin-3-yl)−5-methyl-1H-1,2,3-triazol-4-yl]-N-isopropyl-N-methyl-3,6-dihydropyridine-1(2H)-carboxamide (FTIDC). J Pharmacol Exp Ther 2007;321:1144–1153.
    • (2007) J Pharmacol Exp Ther , vol.321 , pp. 1144-1153
    • Suzuki, G.1    Kimura, T.2    Satow, A.3    Kaneko, N.4    Fukuda, J.5    Hikichi, H.6    Sakai, N.7    Maehara, S.8    Kawagoe-Takaki, H.9    Hata, M.10    Azuma, T.11    Ito, S.12    Kawamoto, H.13    Ohta, H.14
  • 40
    • 68749094966 scopus 로고    scopus 로고
    • Identification of a novel transmembrane domain involved in the negative modulation of mGluR1 using a newly discovered allosteric mGluR1 antagonist, 3-cyclohexyl-5-fluoro-6-methyl-7-(2-morpholin-4-ylethoxy)−4H-chromen-4-one
    • Fukuda J, Suzuki G, Kimura T, Nagatomi Y, Ito S, Kawamoto H, Ozaki S, Ohta H. Identification of a novel transmembrane domain involved in the negative modulation of mGluR1 using a newly discovered allosteric mGluR1 antagonist, 3-cyclohexyl-5-fluoro-6-methyl-7-(2-morpholin-4-ylethoxy)−4H-chromen-4-one. Neuropharmacology 2009;57:438–445.
    • (2009) Neuropharmacology , vol.57 , pp. 438-445
    • Fukuda, J.1    Suzuki, G.2    Kimura, T.3    Nagatomi, Y.4    Ito, S.5    Kawamoto, H.6    Ozaki, S.7    Ohta, H.8
  • 41
    • 0141569348 scopus 로고    scopus 로고
    • Pharmacological characterization and identification of amino acids involved in the positive modulation of metabotropic glutamate receptor subtype 2
    • Schaffhauser H. Pharmacological characterization and identification of amino acids involved in the positive modulation of metabotropic glutamate receptor subtype 2. Mol Pharmacol 2003;64:798–810.
    • (2003) Mol Pharmacol , vol.64 , pp. 798-810
    • Schaffhauser, H.1
  • 43
    • 45749143169 scopus 로고    scopus 로고
    • Transposition of three amino acids transforms the human metabotropic glutamate receptor (mGluR)−3-positive allosteric modulation site to mGluR2, and additional characterization of the mGluR2-positive allosteric modulation site
    • Rowe BA, Schaffhauser H, Morales S, Lubbers LS, Bonnefous C, Kamenecka TM, McQuiston J, Daggett LP. Transposition of three amino acids transforms the human metabotropic glutamate receptor (mGluR)−3-positive allosteric modulation site to mGluR2, and additional characterization of the mGluR2-positive allosteric modulation site. J Pharmacol Exp Ther 2008;326:240–251.
    • (2008) J Pharmacol Exp Ther , vol.326 , pp. 240-251
    • Rowe, B.A.1    Schaffhauser, H.2    Morales, S.3    Lubbers, L.S.4    Bonnefous, C.5    Kamenecka, T.M.6    McQuiston, J.7    Daggett, L.P.8
  • 44
    • 84867805089 scopus 로고    scopus 로고
    • Pharmacological characterization and modeling of the binding sites of novel 1,3-bis(pyridinylethynyl)benzenes as metabotropic glutamate receptor 5-selective negative allosteric modulators
    • Molck C, Harpsoe K, Gloriam DE, Clausen RP, Madsen U, Pedersen LO, Jimenez HN, Nielsen SM, Mathiesen JM, Brauner-Osborne H. Pharmacological characterization and modeling of the binding sites of novel 1,3-bis(pyridinylethynyl)benzenes as metabotropic glutamate receptor 5-selective negative allosteric modulators. Mol Pharmacol 2012;82:929–937.
    • (2012) Mol Pharmacol , vol.82 , pp. 929-937
    • Molck, C.1    Harpsoe, K.2    Gloriam, D.E.3    Clausen, R.P.4    Madsen, U.5    Pedersen, L.O.6    Jimenez, H.N.7    Nielsen, S.M.8    Mathiesen, J.M.9    Brauner-Osborne, H.10
  • 45
    • 51649102148 scopus 로고    scopus 로고
    • Conformational change of the transmembrane helices II and IV of metabotropic glutamate receptor involved in G protein activation
    • Yamashita T, Terakita A, Kai T, Shichida Y. Conformational change of the transmembrane helices II and IV of metabotropic glutamate receptor involved in G protein activation. J Neurochem 2008;106:850–859.
    • (2008) J Neurochem , vol.106 , pp. 850-859
    • Yamashita, T.1    Terakita, A.2    Kai, T.3    Shichida, Y.4
  • 47
    • 0034703014 scopus 로고    scopus 로고
    • Functional importance of the Ala(116)-Pro(136) region in the calcium-sensing receptor. Constitutive activity and inverse agonism in a family C G-protein-coupled receptor
    • Jensen AA, Spalding TA, Burstein ES, Sheppard PO, O'Hara PJ, Brann MR, Krogsgaard-Larsen P, Bräuner-Osborne H. Functional importance of the Ala(116)-Pro(136) region in the calcium-sensing receptor. Constitutive activity and inverse agonism in a family C G-protein-coupled receptor. J Biol Chem 2000;275:29547–29555.
    • (2000) J Biol Chem , vol.275 , pp. 29547-29555
    • Jensen, A.A.1    Spalding, T.A.2    Burstein, E.S.3    Sheppard, P.O.4    O'Hara, P.J.5    Brann, M.R.6    Krogsgaard-Larsen, P.7    Bräuner-Osborne, H.8
  • 49
    • 67649619319 scopus 로고    scopus 로고
    • Pharmacochaperone-mediated rescue of calcium-sensing receptor loss-of-function mutants
    • White E, McKenna J, Cavanaugh A, Breitwieser GE. Pharmacochaperone-mediated rescue of calcium-sensing receptor loss-of-function mutants. Mol Endocrinol 2009;23:1115–1123.
    • (2009) Mol Endocrinol , vol.23 , pp. 1115-1123
    • White, E.1    McKenna, J.2    Cavanaugh, A.3    Breitwieser, G.E.4
  • 52
    • 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
  • 53
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234:779–815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 55
    • 67649422714 scopus 로고    scopus 로고
    • Fpocket: an open source platform for ligand pocket detection
    • Guilloux VL, Schmidtke P, Tuffery P. Fpocket: an open source platform for ligand pocket detection. BMC Bioinformatics 2009;10:168.
    • (2009) BMC Bioinformatics , vol.10 , pp. 168
    • Guilloux, V.L.1    Schmidtke, P.2    Tuffery, P.3
  • 57
    • 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 USA 2007;104:3759–3764.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 58
    • 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 USA 2002;99:2660–2665.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 60
    • 84862704637 scopus 로고    scopus 로고
    • Non-Caloric Sweeteners, Sweetness Modulators, and Sweetener Enhancers
    • DuBois GE, Prakash I. Non-Caloric Sweeteners, Sweetness Modulators, and Sweetener Enhancers. Annu Rev Food Sci Technol 2012;3:353–380.
    • (2012) Annu Rev Food Sci Technol , vol.3 , pp. 353-380
    • DuBois, G.E.1    Prakash, I.2
  • 61
    • 79952056045 scopus 로고    scopus 로고
    • Sweet and umami taste: natural products, their chemosensory targets, and beyond
    • Behrens M, Meyerhof W, Hellfritsch C, Hofmann T. Sweet and umami taste: natural products, their chemosensory targets, and beyond. Angew Chem Int Ed Engl 2011;50:2220–2242.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 2220-2242
    • Behrens, M.1    Meyerhof, W.2    Hellfritsch, C.3    Hofmann, T.4
  • 62
    • 80054787148 scopus 로고    scopus 로고
    • New insights into the characteristics of sweet and bitter taste receptors
    • Temussi PA. New insights into the characteristics of sweet and bitter taste receptors. Inte Rev Cell Mol Biol 2011;291:191–226.
    • (2011) Inte Rev Cell Mol Biol , vol.291 , pp. 191-226
    • Temussi, P.A.1
  • 63
    • 78149499652 scopus 로고    scopus 로고
    • A critical pocket close to the glutamate binding site of mGlu receptors opens new possibilities for agonist design
    • Acher FC, Selvam C, Pin J-P, Goudet C, Bertrand H-O. A critical pocket close to the glutamate binding site of mGlu receptors opens new possibilities for agonist design. Neuropharmacology 2011;60:102–107.
    • (2011) Neuropharmacology , vol.60 , pp. 102-107
    • Acher, F.C.1    Selvam, C.2    Pin, J.-P.3    Goudet, C.4    Bertrand, H.-O.5
  • 65
    • 84963576856 scopus 로고    scopus 로고
    • Molecular mechanism of sweetness sensation
    • DuBois GE. Molecular mechanism of sweetness sensation. Physiol Behav 2016;164:453–463.
    • (2016) Physiol Behav , vol.164 , pp. 453-463
    • DuBois, G.E.1
  • 67
    • 80052082999 scopus 로고    scopus 로고
    • Structural insights into agonist-induced activation of G-protein-coupled receptors
    • Deupi X, Standfuss J. Structural insights into agonist-induced activation of G-protein-coupled receptors. Curr Opin Struct Biol 2011;21:541–551.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 68
    • 0034604451 scopus 로고    scopus 로고
    • Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
    • Palczewski K. Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor. Science 2000;289:739–745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 70
    • 84919704267 scopus 로고    scopus 로고
    • Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer
    • Xue L, Rovira X, Scholler P, Zhao H, Liu J, Pin J-P, Rondard P. Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer. Nat Chem Biol 2015;11:134–140.
    • (2015) Nat Chem Biol , vol.11 , pp. 134-140
    • Xue, L.1    Rovira, X.2    Scholler, P.3    Zhao, H.4    Liu, J.5    Pin, J.-P.6    Rondard, P.7
  • 71
    • 84905567322 scopus 로고    scopus 로고
    • Genetic Architecture of Sweet Taste
    • In, Weerasinghe DK, DuBois GE, editors., Washington, DC, American Chemical Society, pp
    • Bachmanov AA. Genetic Architecture of Sweet Taste. In: Weerasinghe DK, DuBois GE, editors. Sweetness and Sweeteners. Washington, DC: American Chemical Society; 2008. pp 18–47.
    • (2008) Sweetness and Sweeteners , pp. 18-47
    • Bachmanov, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.