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Volumn 52, Issue 25, 2013, Pages 6380-6388

The structural basis of G-protein-coupled receptor signaling (nobel lecture)

Author keywords

2 adrenergic receptor; G protein coupled receptors; Nobel lecture; protein structures; signaling

Indexed keywords

ADRENERGIC RECEPTORS; CHEMICAL MESSENGERS; G PROTEIN COUPLED RECEPTORS; NOBEL LECTURE; NOBEL PRIZES; PROCESS INFORMATION; PROTEIN STRUCTURES; STRUCTURAL BASIS;

EID: 84878896978     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201302116     Document Type: Article
Times cited : (145)

References (51)
  • 2
    • 0141593597 scopus 로고    scopus 로고
    • Arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • "β-Arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors":, M. Azzi, P. G. Charest, S. Angers, G. Rousseau, T. Kohout, M. Bouvier, G. Pineyro, Proc. Natl. Acad. Sci. USA 2003, 100, 11406-11411.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11406-11411
    • Azzi, M.1    Charest, P.G.2    Angers, S.3    Rousseau, G.4    Kohout, T.5    Bouvier, M.6    Pineyro, G.7
  • 4
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • "Roles of G-protein-coupled receptor dimerization":, S. Terrillon, M. Bouvier, EMBO Rep. 2004, 5, 30-34.
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 7
    • 0023889603 scopus 로고
    • 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity
    • 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity":, B. K. Kobilka, T. S. Kobilka, K. Daniel, J. W. Regan, M. G. Caron, R. J. Lefkowitz, Science 1988, 240, 1310-1316.
    • (1988) Science , vol.240 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 8
    • 0025744363 scopus 로고
    • 2 adrenergic receptor increases its affinity for a family of β receptor antagonists
    • 2 adrenergic receptor increases its affinity for a family of β receptor antagonists":, S. Suryanarayana, D. A. Daunt, M. Von Zastrow, B. K. Kobilka, J. Biol. Chem. 1991, 266, 15488-15492.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15488-15492
    • Suryanarayana, S.1    Daunt, D.A.2    Von Zastrow, M.3    Kobilka, B.K.4
  • 9
    • 0026564303 scopus 로고
    • Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide
    • "Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide":, X. M. Guan, T. S. Kobilka, B. K. Kobilka, J. Biol. Chem. 1992, 267, 21995-21998.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21995-21998
    • Guan, X.M.1    Kobilka, T.S.2    Kobilka, B.K.3
  • 10
    • 0027296745 scopus 로고
    • 2-adrenergic receptor modify ligand-binding specificity
    • 2-adrenergic receptor modify ligand-binding specificity":, S. Suryanarayana, B. K. Kobilka, Mol. Pharmacol. 1993, 44, 111-114.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 111-114
    • Suryanarayana, S.1    Kobilka, B.K.2
  • 11
    • 0030028517 scopus 로고    scopus 로고
    • Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin
    • "Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin":, T. Mizobe, M. Maze, V. Lam, S. Suryanarayana, B. K. Kobilka, J. Biol. Chem. 1996, 271, 2387-2389.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2387-2389
    • Mizobe, T.1    Maze, M.2    Lam, V.3    Suryanarayana, S.4    Kobilka, B.K.5
  • 12
    • 0025305260 scopus 로고
    • 2 adrenergic receptor following translocation and glycosylation in a cell-free system
    • 2 adrenergic receptor following translocation and glycosylation in a cell-free system":, B. K. Kobilka, J. Biol. Chem. 1990, 265, 7610-7618.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7610-7618
    • Kobilka, B.K.1
  • 13
    • 0027104740 scopus 로고
    • Identification of a single amino acid residue responsible for the binding of a class of β-adrenergic receptor antagonists to 5-hydroxytryptamine 1A receptors
    • "Identification of a single amino acid residue responsible for the binding of a class of β-adrenergic receptor antagonists to 5-hydroxytryptamine 1A receptors":, X. M. Guan, S. J. Peroutka, B. K. Kobilka, Mol. Pharmacol. 1992, 41, 695-698.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 695-698
    • Guan, X.M.1    Peroutka, S.J.2    Kobilka, B.K.3
  • 14
    • 0028809411 scopus 로고
    • Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor
    • "Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor":, B. K. Kobilka, Anal. Biochem. 1995, 231, 269-271.
    • (1995) Anal. Biochem. , vol.231 , pp. 269-271
    • Kobilka, B.K.1
  • 15
    • 0030448201 scopus 로고    scopus 로고
    • 2 adrenergic receptor: Effect of DTT on receptor conformation monitored by circular dichroism and fluorescence spectroscopy
    • 2 adrenergic receptor: effect of DTT on receptor conformation monitored by circular dichroism and fluorescence spectroscopy":, S. Lin, U. Gether, B. K. Kobilka, Biochemistry 1996, 35, 14445-14451.
    • (1996) Biochemistry , vol.35 , pp. 14445-14451
    • Lin, S.1    Gether, U.2    Kobilka, B.K.3
  • 16
    • 0028856707 scopus 로고
    • 2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • 2 adrenergic receptor. Evidence for ligand-specific conformational changes":, U. Gether, S. Lin, B. K. Kobilka, J. Biol. Chem. 1995, 270, 28268-28275.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 17
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • "Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility":, U. Gether, J. A. Ballesteros, R. Seifert, E. Sanders-Bush, H. Weinstein, B. K. Kobilka, J. Biol. Chem. 1997, 272, 2587-2590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 21
    • 20444499405 scopus 로고    scopus 로고
    • 2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • 2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists":, G. Swaminath, X. Deupi, T. W. Lee, W. Zhu, F. S. Thian, T. S. Kobilka, B. Kobilka, J. Biol. Chem. 2005, 280, 22165-22171.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22165-22171
    • Swaminath, G.1    Deupi, X.2    Lee, T.W.3    Zhu, W.4    Thian, F.S.5    Kobilka, T.S.6    Kobilka, B.7
  • 22
    • 34548438468 scopus 로고    scopus 로고
    • Activation of G protein-coupled receptors
    • "Activation of G protein-coupled receptors":, X. Deupi, B. Kobilka, Adv. Protein Chem. 2007, 74, 137-166.
    • (2007) Adv. Protein Chem. , vol.74 , pp. 137-166
    • Deupi, X.1    Kobilka, B.2
  • 23
    • 77958039571 scopus 로고    scopus 로고
    • Energy landscapes as a tool to integrate GPCR structure, dynamics, and function
    • "Energy landscapes as a tool to integrate GPCR structure, dynamics, and function":, X. Deupi, B. K. Kobilka, Physiology 2010, 25, 293-303.
    • (2010) Physiology , vol.25 , pp. 293-303
    • Deupi, X.1    Kobilka, B.K.2
  • 24
  • 26
    • 0343081370 scopus 로고    scopus 로고
    • X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles
    • "X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles":, T. Okada, I. Le Trong, B. A. Fox, C. A. Behnke, R. E. Stenkamp, K. Palczewski, J. Struct. Biol. 2000, 130, 73-80.
    • (2000) J. Struct. Biol. , vol.130 , pp. 73-80
    • Okada, T.1    Le Trong, I.2    Fox, B.A.3    Behnke, C.A.4    Stenkamp, R.E.5    Palczewski, K.6
  • 27
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • "Crystal structure of the ligand-free G-protein-coupled receptor opsin":, J. H. Park, P. Scheerer, K. P. Hofmann, H. W. Choe, O. P. Ernst, Nature 2008, 454, 183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 31
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • "Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure":, S. Faham, J. U. Bowie, J. Mol. Biol. 2002, 316, 1-6.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 33
    • 0032422462 scopus 로고    scopus 로고
    • A simple mechanical mixer for small viscous lipid-containing samples
    • "A simple mechanical mixer for small viscous lipid-containing samples":, A. Cheng, B. Hummel, H. Qiu, M. Caffrey, Chem. Phys. Lipids 1998, 95, 11-21.
    • (1998) Chem. Phys. Lipids , vol.95 , pp. 11-21
    • Cheng, A.1    Hummel, B.2    Qiu, H.3    Caffrey, M.4
  • 41
    • 84872832090 scopus 로고    scopus 로고
    • Identification of GPCR-interacting cytosolic proteins using HDL particles and mass spectrometry-based proteomic approach
    • "Identification of GPCR-interacting cytosolic proteins using HDL particles and mass spectrometry-based proteomic approach":, K. Y. Chung, P. W. Day, G. Velez-Ruiz, R. K. Sunahara, B. K. Kobilka, PLoS One 2013, 8, e 54942.
    • (2013) PLoS One , vol.8 , pp. 54942
    • Chung, K.Y.1    Day, P.W.2    Velez-Ruiz, G.3    Sunahara, R.K.4    Kobilka, B.K.5
  • 42
    • 84867131783 scopus 로고    scopus 로고
    • N-terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor
    • "N-terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor":, Y. Zou, W. I. Weis, B. K. Kobilka, PLoS One 2012, 7, e 46039.
    • (2012) PLoS One , vol.7 , pp. 46039
    • Zou, Y.1    Weis, W.I.2    Kobilka, B.K.3
  • 44
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • "Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation":, G. Lebon, T. Warne, P. C. Edwards, K. Bennett, C. J. Langmead, A. G. Leslie, C. G. Tate, Nature 2011, 474, 521-525.
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1    Warne, T.2    Edwards, P.C.3    Bennett, K.4    Langmead, C.J.5    Leslie, A.G.6    Tate, C.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.