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Volumn 287, Issue 6, 2012, Pages 3630-3641

High constitutive activity is an intrinsic feature of ghrelin receptor protein: A study with a functional monomeric GHS-R1a receptor reconstituted in lipid discs

Author keywords

[No Author keywords available]

Indexed keywords

AGONIST-DEPENDENT MANNER; ARRESTINS; CELLULAR ENVIRONMENT; G-PROTEIN COUPLED RECEPTORS; GHRELIN RECEPTOR; GUANOSINES; HETEROLOGOUS SYSTEMS; IN-VIVO; INTRINSIC FEATURES; INTRINSIC FLUORESCENCE; INTRINSIC PROPERTY; MOLECULAR MECHANISM; THERAPEUTIC APPLICATION;

EID: 84856715703     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.288324     Document Type: Article
Times cited : (126)

References (69)
  • 1
    • 0031897256 scopus 로고    scopus 로고
    • Constitutively signaling G-proteincoupled receptors and human disease
    • DOI 10.1016/S1043-2760(98)00007-1, PII S1043276098000071
    • Arvanitakis, L., Geras-Raaka, E., and Gershengorn, M. C. (1998) Constitutively signalingGprotein-coupled receptors and human disease. TrendsEndocrinol. Metab. 9, 27-31 (Pubitemid 28157860)
    • (1998) Trends in Endocrinology and Metabolism , vol.9 , Issue.1 , pp. 27-31
    • Arvanitakis, L.1    Geras-Raaka, E.2    Gershengorn, M.C.3
  • 2
    • 0035083109 scopus 로고    scopus 로고
    • Inverse, protean, and ligand-selective agonism. Matters of receptor conformation
    • Kenakin, T. (2001) Inverse, protean, and ligand-selective agonism. Matters of receptor conformation. FASEB J. 15, 598-611
    • (2001) FASEB J. , vol.15 , pp. 598-611
    • Kenakin, T.1
  • 3
    • 0347627709 scopus 로고    scopus 로고
    • Constitutive activity and inverse agonists ofGproteincoupled receptors.Acurrent perspective
    • Milligan, G. (2003) Constitutive activity and inverse agonists ofGproteincoupled receptors.Acurrent perspective. Mol. Pharmacol. 64, 1271-1276
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1271-1276
    • Milligan, G.1
  • 4
    • 77958039571 scopus 로고    scopus 로고
    • Energy landscapes as a tool to integrate GPCR structure, dynamics, and function
    • Deupi, X., and Kobilka, B. K. (2010) Energy landscapes as a tool to integrate GPCR structure, dynamics, and function. Physiology 25, 293-303
    • (2010) Physiology , vol.25 , pp. 293-303
    • Deupi, X.1    Kobilka, B.K.2
  • 5
    • 33947356279 scopus 로고    scopus 로고
    • G protein-coupled receptor structure and activation
    • Kobilka, B. K. (2007) G protein-coupled receptor structure and activation. Biochim. Biophys. Acta 1768, 794-807
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 794-807
    • Kobilka, B.K.1
  • 6
    • 31844446495 scopus 로고    scopus 로고
    • Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery
    • DOI 10.1016/j.tips.2005.12.007, PII S0165614705003202
    • Bond, R. A., and Ijzerman, A. P. (2006) Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery. Trends Pharmacol. Sci. 27, 92-96 (Pubitemid 43184030)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.2 , pp. 92-96
    • Bond, R.A.1    Ijzerman, A.P.2
  • 9
    • 67650386206 scopus 로고    scopus 로고
    • Understanding the ligand-receptor- G protein ternary complex for GPCR drug discovery
    • Ratnala, V. R., and Kobilka, B. (2009) Understanding the ligand-receptor- G protein ternary complex for GPCR drug discovery. Methods Mol. Biol. 552, 67-77
    • (2009) Methods Mol. Biol. , vol.552 , pp. 67-77
    • Ratnala, V.R.1    Kobilka, B.2
  • 11
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • DOI 10.1074/jbc.M407676200
    • Holst, B., Holliday, N. D., Bach, A., Elling, C. E., Cox, H. M., and Schwartz, T. W. (2004) Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 279, 53806-53817 (Pubitemid 40051890)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53806-53817
    • Holst, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 17
    • 38449087113 scopus 로고    scopus 로고
    • In vivo evidence for inverse agonism of Agouti-related peptide in the central nervous system of proopiomelanocortin- deficient mice
    • Tolle, V., and Low, M. J. (2008) In vivo evidence for inverse agonism of Agouti-related peptide in the central nervous system of proopiomelanocortin- deficient mice. Diabetes 57, 86-94
    • (2008) Diabetes , vol.57 , pp. 86-94
    • Tolle, V.1    Low, M.J.2
  • 19
    • 78649810475 scopus 로고    scopus 로고
    • Coexpression systems as models for the analysis of constitutive GPCR activity
    • Schneider, E. H., and Seifert, R. (2010) Coexpression systems as models for the analysis of constitutive GPCR activity. Methods Enzymol. 485, 527-557
    • (2010) Methods Enzymol. , vol.485 , pp. 527-557
    • Schneider, E.H.1    Seifert, R.2
  • 20
    • 78049259128 scopus 로고    scopus 로고
    • Constitutive activity of GPR40/ FFA1 intrinsic or assay dependent?
    • Stoddart, L. A., and Milligan, G. (2010) Constitutive activity of GPR40/ FFA1 intrinsic or assay dependent? Methods Enzymol. 484, 569-590
    • (2010) Methods Enzymol. , vol.484 , pp. 569-590
    • Stoddart, L.A.1    Milligan, G.2
  • 21
    • 78049490903 scopus 로고    scopus 로고
    • Ghrelin receptor. High constitutive activity and methods for developing inverse agonists
    • Els, S., Beck-Sickinger, A. G., and Chollet, C. (2010) Ghrelin receptor. High constitutive activity and methods for developing inverse agonists. Methods Enzymol. 485, 103-121
    • (2010) Methods Enzymol. , vol.485 , pp. 103-121
    • Els, S.1    Beck-Sickinger, A.G.2    Chollet, C.3
  • 22
    • 78049237699 scopus 로고    scopus 로고
    • Modulation of the constitutive activity of the ghrelin receptor by use of pharmacological tools and mutagenesis
    • Mokrosiński, J., and Holst, B. (2010) Modulation of the constitutive activity of the ghrelin receptor by use of pharmacological tools and mutagenesis. Methods Enzymol. 484, 53-73
    • (2010) Methods Enzymol. , vol.484 , pp. 53-73
    • Mokrosiński, J.1    Holst, B.2
  • 23
    • 36849039489 scopus 로고    scopus 로고
    • Importance of constitutive activity and arrestin-independent mechanisms for intracellular trafficking of the ghrelin receptor
    • DOI 10.1210/me.2007-0254
    • Holliday, N. D., Holst, B., Rodionova, E. A., Schwartz, T. W., and Cox, H. M. (2007) Importance of constitutive activity and arrestin-independent mechanisms for intracellular trafficking of the ghrelin receptor. Mol. Endocrinol. 21, 3100-3112 (Pubitemid 350223518)
    • (2007) Molecular Endocrinology , vol.21 , Issue.12 , pp. 3100-3112
    • Holliday, N.D.1    Holst, B.2    Rodionova, E.A.3    Schwartz, T.W.4    Cox, H.M.5
  • 25
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy
    • DOI 10.1074/jbc.M412009200
    • Banères, J. L., Mesnier, D., Martin, A., Joubert, L., Dumuis, A., and Bockaert, J. (2005) Molecular characterization of a purified 5-HT4 receptor. A structural basis for drug efficacy. J. Biol. Chem. 280, 20253-20260 (Pubitemid 40776722)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20253-20260
    • Baneres, J.-L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 27
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • DOI 10.1074/jbc.M701433200
    • Bayburt, T. H., Leitz, A. J., Xie, G., Oprian, D. D., and Sligar, S. G. (2007) Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 282, 14875-14881 (Pubitemid 47093370)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 29
    • 40849130624 scopus 로고    scopus 로고
    • Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles
    • Banerjee, S., Huber, T., and Sakmar, T. P. (2008) Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles. J. Mol. Biol. 377, 1067-1081
    • (2008) J. Mol. Biol. , vol.377 , pp. 1067-1081
    • Banerjee, S.1    Huber, T.2    Sakmar, T.P.3
  • 31
    • 0029830110 scopus 로고    scopus 로고
    • qand inverse agonism of 5HT2c receptor antagonists
    • q and inverse agonism of 5HT2c receptor antagonists. J. Biol. Chem. 271, 22591-22597
    • (1996) J. Biol. Chem. , vol.271 , pp. 22591-22597
    • Hartman IV, J.L.1    Northup, J.K.2
  • 32
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function. Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • Banères, J. L., and Parello, J. (2003) Structure-based analysis of GPCR function. Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol. 329, 815-829
    • (2003) J. Mol. Biol. , vol.329 , pp. 815-829
    • Banères, J.L.1    Parello, J.2
  • 35
    • 67650080503 scopus 로고    scopus 로고
    • Amphipol-assisted in vitro folding of G protein-coupled receptors
    • Dahmane, T., Damian, M., Mary, S., Popot, J. L., and Banères, J. L. (2009) Amphipol-assisted in vitro folding of G protein-coupled receptors. Biochemistry 48, 6516-6521
    • (2009) Biochemistry , vol.48 , pp. 6516-6521
    • Dahmane, T.1    Damian, M.2    Mary, S.3    Popot, J.L.4    Banères, J.L.5
  • 36
    • 9644255747 scopus 로고    scopus 로고
    • 4 receptor BLT1
    • DOI 10.1074/jbc.M404941200
    • Mesnier, D., and Banères, J. L. (2004) Cooperative conformational changes in a G protein-coupled receptor dimer, the leukotriene B(4) receptor BLT1. J. Biol. Chem. 279, 49664-49670 (Pubitemid 39577769)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 49664-49670
    • Mesnier, D.1    Baneres, J.-L.2
  • 38
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • DOI 10.1006/abio.1994.1112
    • Schägger, H., Cramer, W. A., and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by twodimensional native electrophoresis. Anal. Biochem. 217, 220-230 (Pubitemid 24080754)
    • (1994) Analytical Biochemistry , vol.217 , Issue.2 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 39
    • 23644434688 scopus 로고    scopus 로고
    • Measurement of internal movements within the 30 S ribosomal subunit using Förster resonance energy transfer
    • DOI 10.1016/j.jmb.2005.09.010, PII S0022283605010661
    • Hickerson, R., Majumdar, Z. K., Baucom, A., Clegg, R. M., and Noller, H. F. (2005) Measurement of internal movements within the 30 S ribosomal subunit using Förster resonance energy transfer. J. Mol. Biol. 354, 459-472 (Pubitemid 41579858)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.2 , pp. 459-472
    • Hickerson, R.1    Majumdar, Z.K.2    Baucom, A.3    Clegg, R.M.4    Noller, H.F.5
  • 40
    • 0035311495 scopus 로고    scopus 로고
    • Fluorescent BODIPY-GTP analogs: Real-time measurement of nucleotide binding to G proteins
    • DOI 10.1006/abio.2001.5011
    • McEwen, D. P., Gee, K. R., Kang, H. C., and Neubig, R. R. (2001) Fluorescent BODIPY-GTP analogs. Real-time measurement of nucleotide binding to G proteins. Anal. Biochem. 291, 109-117 (Pubitemid 32324531)
    • (2001) Analytical Biochemistry , vol.291 , Issue.1 , pp. 109-117
    • McEwen, D.P.1    Gee, K.R.2    Kang, H.C.3    Neubig, R.R.4
  • 41
    • 0034006773 scopus 로고    scopus 로고
    • Arrestin, mutagenesis, expression, purification, and functional characterization
    • Gurevich, V. V., and Benovic, J. L. (2000) Arrestin, mutagenesis, expression, purification, and functional characterization. Methods Enzymol. 315, 422-437
    • (2000) Methods Enzymol. , vol.315 , pp. 422-437
    • Gurevich, V.V.1    Benovic, J.L.2
  • 42
    • 14844307607 scopus 로고    scopus 로고
    • Dynamics of arrestin-rhodopsin interactions: Arrestin and retinal release are directly linked events
    • DOI 10.1074/jbc.M411341200
    • Sommer, M. E., Smith, W. C., and Farrens, D. L. (2005) Dynamics of arrestin-rhodopsin interactions. Arrestin and retinal release are directly linked events. J. Biol. Chem. 280, 6861-6871 (Pubitemid 40341241)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6861-6871
    • Sommer, M.E.1    Smith, W.C.2    Farrens, D.L.3
  • 43
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D. J., and Evans, P. R. (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282, 1327-1332 (Pubitemid 28524497)
    • (1998) Science , vol.282 , Issue.5392 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 45
    • 79959294939 scopus 로고    scopus 로고
    • New advances in production and functional folding of G protein-coupled receptors
    • Banères, J. L., Popot, J. L., and Mouillac, B. (2011) New advances in production and functional folding of G protein-coupled receptors. Trends Biotechnol. 29, 314-322
    • (2011) Trends Biotechnol. , vol.29 , pp. 314-322
    • Banères, J.L.1    Popot, J.L.2    Mouillac, B.3
  • 47
    • 35148874303 scopus 로고    scopus 로고
    • Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer: Implications for in vitro studies of amphipol-stabilized membrane proteins
    • DOI 10.1021/bi7007596
    • Zoonens, M., Giusti, F., Zito, F., and Popot, J. L. (2007) Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46, 10392-10404 (Pubitemid 350067632)
    • (2007) Biochemistry , vol.46 , Issue.36 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.-L.4
  • 49
    • 1642382983 scopus 로고    scopus 로고
    • Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
    • DOI 10.1021/ja0393574
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126, 3477-3487 (Pubitemid 38366738)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 50
    • 0242330291 scopus 로고    scopus 로고
    • High Constitutive Signaling of the Ghrelin Receptor - Identification of a Potent Inverse Agonist
    • DOI 10.1210/me.2003-0069
    • Holst, B., Cygankiewicz, A., Jensen, T. H., Ankersen, M., and Schwartz, T. W. (2003) High constitutive signaling of the ghrelin receptor. Identification of a potent inverse agonist. Mol. Endocrinol. 17, 2201-2210 (Pubitemid 37352532)
    • (2003) Molecular Endocrinology , vol.17 , Issue.11 , pp. 2201-2210
    • Holst, B.1    Cygankiewicz, A.2    Jensen, T.H.3    Ankersen, M.4    Schwartz, T.W.5
  • 51
    • 34548487757 scopus 로고    scopus 로고
    • Stimulation by ghrelin of p42/p44 mitogen-activated protein kinase through the GHS-R1a receptor: Role of G-proteins and β-arrestins
    • DOI 10.1002/jcp.21109
    • Camiña, J. P., Lodeiro, M., Ischenko, O., Martini, A. C., and Casanueva, F. F. (2007) Stimulation by ghrelin of p42/p44 mitogen-activated protein kinase through the GHS-R1a receptor. Role of G-proteins and β-arrestins. J. Cell Physiol. 213, 187-200 (Pubitemid 47378807)
    • (2007) Journal of Cellular Physiology , vol.213 , Issue.1 , pp. 187-200
    • Camina, J.P.1    Lodeiro, M.2    Ischenko, O.3    Martini, A.C.4    Casanueva, F.F.5
  • 52
    • 70349336145 scopus 로고    scopus 로고
    • Growth hormone secretagogues and growth hormone releasing peptides act as orthosteric super-agonists but not allosteric regulators for activation of the G protein Gα(o1) by the ghrelin receptor
    • Bennett, K. A., Langmead, C. J., Wise, A., and Milligan, G. (2009) Growth hormone secretagogues and growth hormone releasing peptides act as orthosteric super-agonists but not allosteric regulators for activation of the G protein Gα(o1) by the ghrelin receptor. Mol. Pharmacol. 76, 802-811
    • (2009) Mol. Pharmacol. , vol.76 , pp. 802-811
    • Bennett, K.A.1    Langmead, C.J.2    Wise, A.3    Milligan, G.4
  • 53
    • 77954760056 scopus 로고    scopus 로고
    • Monomeric rhodopsin is the minimal functional unit required for arrestin binding
    • Tsukamoto, H., Sinha, A., DeWitt, M., and Farrens, D. L. (2010) Monomeric rhodopsin is the minimal functional unit required for arrestin binding. J. Mol. Biol. 399, 501-511
    • (2010) J. Mol. Biol. , vol.399 , pp. 501-511
    • Tsukamoto, H.1    Sinha, A.2    DeWitt, M.3    Farrens, D.L.4
  • 56
    • 33644864081 scopus 로고    scopus 로고
    • Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization
    • Paing, M. M., Johnston, C. A., Siderovski, D. P., and Trejo, J. (2006) Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization. Mol. Cell. Biol. 26, 3231-3242
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3231-3242
    • Paing, M.M.1    Johnston, C.A.2    Siderovski, D.P.3    Trejo, J.4
  • 58
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • Bayburt, T. H., and Sligar, S. G. (2010) Membrane protein assembly into nanodiscs. FEBS Lett. 584, 1721-1727
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 59
    • 33644658516 scopus 로고    scopus 로고
    • Ghrelin receptor mutations - Too little height and too much hunger
    • DOI 10.1172/JCI27999
    • Holst, B., and Schwartz, T. W. (2006) Ghrelin receptor mutations. Too little height and too much hunger. J. Clin. Invest. 116, 637-641 (Pubitemid 43326872)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.3 , pp. 637-641
    • Holst, B.1    Schwartz, T.W.2
  • 60
    • 58649097003 scopus 로고    scopus 로고
    • The constitutive activity of the ghrelin receptor attenuates apoptosis via a protein kinase C-dependent pathway
    • Lau, P. N., Chow, K. B., Chan, C. B., Cheng, C. H., and Wise, H. (2009) The constitutive activity of the ghrelin receptor attenuates apoptosis via a protein kinase C-dependent pathway. Mol. Cell Endocrinol. 299, 232-239
    • (2009) Mol. Cell Endocrinol. , vol.299 , pp. 232-239
    • Lau, P.N.1    Chow, K.B.2    Chan, C.B.3    Cheng, C.H.4    Wise, H.5
  • 61
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino, J. S., and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447 (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 62
    • 0038121047 scopus 로고    scopus 로고
    • Endocytosis of the viral chemokine receptor US28 does not require beta-arrestins but is dependent on the clathrin-mediated pathway
    • Fraile-Ramos, A., Kohout, T. A., Waldhoer, M., and Marsh, M. (2003) Endocytosis of the viral chemokine receptor US28 does not require β-arrestins but is dependent on the clathrin-mediated pathway. Traffic 4, 243-253 (Pubitemid 36665385)
    • (2003) Traffic , vol.4 , Issue.4 , pp. 243-253
    • Fraile-Ramos, A.1    Kohout, T.A.2    Waldhoer, M.3    Marsh, M.4
  • 63
    • 80052082999 scopus 로고    scopus 로고
    • Structural insights into agonist-induced activation of G-protein-coupled receptors
    • Deupi, X., and Standfuss, J. (2011) Structural insights into agonist-induced activation of G-protein-coupled receptors. Curr. Opin. Struct. Biol. 21, 541-551
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 64
    • 73649109875 scopus 로고    scopus 로고
    • Activation of the ghrelin receptor is described by a privileged collective motion. A model for constitutive and agonist-induced activation of a subclass A G-protein coupled receptor (GPCR)
    • Floquet, N., M'Kadmi, C., Perahia, D., Gagne, D., Bergé, G., Marie, J., Banères, J. L., Galleyrand, J. C., Fehrentz, J. A., and Martinez, J. (2010) Activation of the ghrelin receptor is described by a privileged collective motion. A model for constitutive and agonist-induced activation of a subclass A G-protein coupled receptor (GPCR). J. Mol. Biol. 395, 769-784
    • (2010) J. Mol. Biol. , vol.395 , pp. 769-784
    • Floquet, N.1    M'Kadmi, C.2    Perahia, D.3    Gagne, D.4    Bergé, G.5    Marie, J.6    Banères, J.L.7    Galleyrand, J.C.8    Fehrentz, J.A.9    Martinez, J.10
  • 65
    • 0037648337 scopus 로고    scopus 로고
    • 4 binding to recombinant BLT1
    • DOI 10.1016/S0022-2836(03)00438-8
    • Baneres, J. L., Martin, A., Hullot, P., Girard, J. P., Rossi, J. C., and Parello, J. (2003) Structure-based analysis of GPCR function. Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329, 801-814 (Pubitemid 36629372)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.4 , pp. 801-814
    • Baneres, J.-L.1    Martin, A.2    Hullot, P.3    Girard, J.-P.4    Rossi, J.-C.5    Parello, J.6
  • 66
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor heterodimerization. Contribution to pharmacology and function
    • Milligan, G. (2009) G protein-coupled receptor heterodimerization. Contribution to pharmacology and function. Br. J. Pharmacol. 158, 5-14
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 5-14
    • Milligan, G.1
  • 67
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • DOI 10.1021/bi050720o
    • Chabre, M., and le Maire, M. (2005) Monomeric G protein-coupled receptor as a functional unit. Biochemistry 44, 9395-9403 (Pubitemid 40962038)
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9395-9403
    • Chabre, M.1    Le, M.M.2
  • 68
    • 62949087122 scopus 로고    scopus 로고
    • The apparent cooperativity of some GPCRs does not necessarily imply dimerization
    • Chabre, M., Deterre, P., and Antonny, B. (2009) The apparent cooperativity of some GPCRs does not necessarily imply dimerization. Trends Pharmacol. Sci. 30, 182-187
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 182-187
    • Chabre, M.1    Deterre, P.2    Antonny, B.3
  • 69
    • 24344479915 scopus 로고    scopus 로고
    • Nonpeptide and peptide growth hormone secretagogues act both as ghrelin receptor agonist and as positive or negative allosteric modulators of ghrelin signaling
    • DOI 10.1210/me.2005-0059
    • Holst, B., Brandt, E., Bach, A., Heding, A., and Schwartz, T. W. (2005) Nonpeptide and peptide growth hormone secretagogues act both as ghrelin receptor agonist and as positive or negative allosteric modulators of ghrelin signaling. Mol. Endocrinol. 19, 2400-2411 (Pubitemid 41252832)
    • (2005) Molecular Endocrinology , vol.19 , Issue.9 , pp. 2400-2411
    • Holst, B.1    Brandt, E.2    Bach, A.3    Heding, A.4    Schwartz, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.