메뉴 건너뛰기




Volumn , Issue , 2010, Pages 251-278

GPCRs: Past, present, and future

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84879235698     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-7091-0045-5_14     Document Type: Chapter
Times cited : (1)

References (101)
  • 1
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated beta-Adrenergic receptor by the beta-Adrenergic receptor kinase: Potential role of an analog of the retinal protein arrestin (48-kda protein)
    • Benovic JL, Kn H, Weyand I, Codina J, Caron MG, Lefkowitz RJ (1987) Functional desensitization of the isolated beta-Adrenergic receptor by the beta-Adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc Natl Acad Sci USA 84: 8879-8882
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8879-8882
    • Benovic, J.L.1    Kn, H.2    Weyand, I.3    Codina, J.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 2
    • 31844446495 scopus 로고    scopus 로고
    • Recent developments in constitutive receptor activity and inverse agonism, and their potential for gpcr drug discovery
    • Bond RA and Ijzerman AP (2006) Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery. Trends Pharmacol Sci 27: 92-96
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 92-96
    • Bond, R.A.1    Ijzerman, A.P.2
  • 4
    • 0035824276 scopus 로고    scopus 로고
    • Distribution of an orphan g-protein coupled receptor (jp05) mrna in the human brain
    • Brillon S, Detheux M, Parmentier M, Hfelt T, Hurd YL (2001) Distribution of an orphan G-protein coupled receptor (JP05) mRNA in the human brain. Brain Res 921: 21-30
    • (2001) Brain Res , vol.921 , pp. 21-30
    • Brillon, S.1    Detheux, M.2    Parmentier, M.3    Hfelt, T.4    Hurd, Y.L.5
  • 6
    • 11244255332 scopus 로고    scopus 로고
    • Location and nature of the residues important for ligand recognition in g-protein coupled receptors
    • Bywater RP (2005) Location and nature of the residues important for ligand recognition in G-protein coupled receptors. J Mol Recognit 18: 60-72
    • (2005) J Mol Recognit , vol.18 , pp. 60-72
    • Bywater, R.P.1
  • 8
    • 0020503940 scopus 로고
    • Reconstitution of beta-Adrenergic receptors in lipid vesicles: Affi nity chromatography-purifi ed receptors confer catecholamine responsiveness on a heterologous adenylate cyclase system
    • Cerione RA , Strulovici B, Benovic JL, Strader CD, Caron MG, Lefkowitz RJ (1983) Reconstitution of beta-Adrenergic receptors in lipid vesicles: affi nity chromatography-purifi ed receptors confer catecholamine responsiveness on a heterologous adenylate cyclase system. Proc Natl Acad Sci USA 80: 4899-4903
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4899-4903
    • Cerione, R.A.1    Strulovici, B.2    Benovic, J.L.3    Strader, C.D.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 9
    • 0021212048 scopus 로고
    • Reconstitution of a hormone-sensitive adenylate cyclase system. The pure beta-Adrenergic receptor and guanine nucleotide regulatory protein confer hormone responsiveness on the resolved catalytic unit
    • Cerione RA , Sibley DR, Codina J, Benovic JL, Winslow J, Neer EJ, Birnbaumer L, Caron MG, Lefkowitz RJ (1984) Reconstitution of a hormone-sensitive adenylate cyclase system. The pure beta-Adrenergic receptor and guanine nucleotide regulatory protein confer hormone responsiveness on the resolved catalytic unit. J Biol Chem 259: 9979-9982
    • (1984) J Biol Chem , vol.259 , pp. 9979-9982
    • Cerione, R.A.1    Sibley, D.R.2    Codina, J.3    Benovic, J.L.4    Winslow, J.5    Neer, E.J.6    Birnbaumer, L.7    Caron, M.G.8    Lefkowitz, R.J.9
  • 11
    • 0020162299 scopus 로고
    • Potency enhancement of a gnrh agonist: Gnrh-receptor microaggregation stimulates gonadotropin release
    • Conn PM, Rogers DC, McNeil R (1982a) Potency enhancement of a GnRH agonist: GnRH-receptor microaggregation stimulates gonadotropin release. Endocrinology 111: 335-337
    • (1982) Endocrinology , vol.111 , pp. 335-337
    • Conn, P.M.1    Rogers, D.C.2    McNeil, R.3
  • 12
    • 0020328255 scopus 로고
    • Conversion of a gonadotropin-releasing hormone antagonist to an agonist
    • Conn PM, Rogers DC, Stewart JM, Niedel J, Sheffi eld T (1982b) Conversion of a gonadotropin-releasing hormone antagonist to an agonist. Nature 296: 653-655
    • (1982) Nature , vol.296 , pp. 653-655
    • Conn, P.M.1    Rogers, D.C.2    Stewart, J.M.3    Niedel, J.4    Sheffield, T.5
  • 13
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of gpcrs: A novel approach for the treatment of cns disorders
    • Conn PJ, Christopoulos A, Lindsley CW (2009) Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat Rev Drug Discov 8: 41-54
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 14
    • 0001169515 scopus 로고
    • Antagonists with negative intrinsic activity at delta opioid receptors coupled to gtp-binding proteins
    • Costa T and Herz A (1989) Antagonists with negative intrinsic activity at delta opioid receptors coupled to GTP-binding proteins. Proc Natl Acad Sci USA 86: 7321-7325
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7321-7325
    • Costa, T.1    Herz, A.2
  • 15
    • 0026608113 scopus 로고
    • Drug effi cacy at guanine nucleotidebinding regulatory protein-linked receptors: Thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand
    • Costa T, Ogino Y, Munson PJ, Onaran HO, Rodbard D (1992) Drug effi cacy at guanine nucleotidebinding regulatory protein-linked receptors: thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand. Mol Pharmacol 41: 549-560
    • (1992) Mol Pharmacol , vol.41 , pp. 549-560
    • Costa, T.1    Ogino, Y.2    Munson, P.J.3    Onaran, H.O.4    Rodbard, D.5
  • 16
    • 0026575003 scopus 로고
    • Discrete amino acid sequences of the alpha 1-Adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis
    • Cotecchia S, Ostrowski J, Kjelsberg MA, Caron MG, Lefkowitz RJ (1992) Discrete amino acid sequences of the alpha 1-Adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis. J Biol Chem 267: 1633-1639
    • (1992) J Biol Chem , vol.267 , pp. 1633-1639
    • Cotecchia, S.1    Ostrowski, J.2    Kjelsberg, M.A.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 17
    • 0025868465 scopus 로고
    • Molecular dynamics of dopamine at the d2 receptor
    • Dahl SG, Edvardsen O, Sylte I (1991) Molecular dynamics of dopamine at the D2 receptor. Proc Natl Acad Sci USA 88: 8111-8115
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8111-8115
    • Dahl, S.G.1    Edvardsen, O.2    Sylte, I.3
  • 18
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specifi c binding properties of the adenylate cyclase-coupled beta-Adrenergic receptor
    • De Lean A, Stadel JM, Lefkowitz RJ (1980) A ternary complex model explains the agonist-specifi c binding properties of the adenylate cyclase-coupled beta-Adrenergic receptor. J Biol Chem 255: 7108-7117
    • (1980) J Biol Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 21
    • 0027959026 scopus 로고
    • Seven-helix receptors: Structure and modelling
    • Donnelly D and Findlay JB (1994) Seven-helix receptors: structure and modelling. Curr Opin Struct Biol 4: 582-589
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 582-589
    • Donnelly, D.1    Findlay, J.B.2
  • 22
    • 0032740152 scopus 로고    scopus 로고
    • Theoretical study of the electrostatically driven step of receptor-g-protein recognition
    • Fanelli F, Menziani C, Scheer A, Cotecchia S, De Benedett i PG (1999) Theoretical study of the electrostatically driven step of receptor-G-protein recognition. Proteins 37: 145-156
    • (1999) Proteins , vol.37 , pp. 145-156
    • Fanelli, F.1    Menziani, C.2    Scheer, A.3    Cotecchia, S.4    De Benedetti, P.G.5
  • 23
    • 0023786564 scopus 로고
    • The genomic clone g-21 which resembles a beta-Adrenergic receptor sequence encodes the 5-ht1a receptor
    • Fargin A, Raymond JR, Lohse MJ, Kobilka BK, Caron MG, Lefkowitz RJ (1988) The genomic clone G-21 which resembles a beta-Adrenergic receptor sequence encodes the 5-HT1A receptor. Nature 335: 358-360
    • (1988) Nature , vol.335 , pp. 358-360
    • Fargin, A.1    Raymond, J.R.2    Lohse, M.J.3    Kobilka, B.K.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 24
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274: 768-770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 27
    • 0023062991 scopus 로고
    • G-proteins: Transducers of receptor-generated signals
    • Gilman AG (1987) G-proteins: transducers of receptor-generated signals. Ann Rev Biochem 56: 615-649
    • (1987) Ann Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 28
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of g-protein signaling
    • Hamm HE (1998) The many faces of G-protein signaling. J Biol Chem 273: 669-672
    • (1998) J Biol Chem , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 30
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of gpcrs by endocytic membrane traffi cking and its potential implications
    • Hanyaloglu AC and von Zastrow M (2008) Regulation of GPCRs by endocytic membrane traffi cking and its potential implications. Ann Rev Pharmacol Toxicol 48: 537-568
    • (2008) Ann Rev Pharmacol Toxicol , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    Von Zastrow, M.2
  • 32
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-Adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Hebert TE, Moffett S, Morello JP, Loisel TP, Bichet DG, Barret C, Bouvier M (1996) A peptide derived from a beta2-Adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J Biol Chem 271: 16384-16392
    • (1996) J Biol Chem , vol.271 , pp. 16384-16392
    • Hebert, T.E.1    Moffett, S.2    Morello, J.P.3    Loisel, T.P.4    Bichet, D.G.5    Barret, C.6    Bouvier, M.7
  • 33
    • 0016842810 scopus 로고
    • Th ree-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R and Unwin PN (1975) Th ree-dimensional model of purple membrane obtained by electron microscopy. Nature 257: 28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 34
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213: 899-929
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 35
    • 0038646059 scopus 로고    scopus 로고
    • Structural and functional aspects of g-protein-coupled receptor oligomerization
    • Hert TE and Bouvier M (1998) Structural and functional aspects of G-protein-coupled receptor oligomerization. Biochem Cell Biol 76: 1-11
    • (1998) Biochem Cell Biol , vol.76 , pp. 1-11
    • Hert, T.E.1    Bouvier, M.2
  • 36
    • 0025881062 scopus 로고
    • Th ree-dimensional models of neurotransmitt er g-binding protein-coupled receptors
    • Hibert MF, Trumpp-Kallmeyer S, Bruinvels A, Hofl ack J (1991) Th ree-dimensional models of neurotransmitt er G-binding protein-coupled receptors. Mol Pharmacol 40: 8-15
    • (1991) Mol Pharmacol , vol.40 , pp. 8-15
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 39
    • 77949321753 scopus 로고    scopus 로고
    • Light activation of rhodopsin: Insights from molecular dynamics simulations guided by solid-state nmr distance restraints
    • Hornak V, Ahuja S, Eilers M, Goncalves JA, Sheves M, Reeves PJ, Smith SO (2010) Light activation of rhodopsin: insights from molecular dynamics simulations guided by solid-state NMR distance restraints. J Mol Biol 396(3): 510-527
    • (2010) J Mol Biol , vol.396 , Issue.3 , pp. 510-527
    • Hornak, V.1    Ahuja, S.2    Eilers, M.3    Goncalves, J.A.4    Sheves, M.5    Reeves, P.J.6    Smith, S.O.7
  • 40
    • 0023214801 scopus 로고
    • Interactions of amiloride with alpha-And beta-Adrenergic receptors: Amiloride reveals an allosteric site on alpha 2-Adrenergic receptors
    • Howard MJ, Hughes RJ, Motulsky HJ, Mullen MD, Insel PA (1987) Interactions of amiloride with alpha-And beta-Adrenergic receptors: amiloride reveals an allosteric site on alpha 2-Adrenergic receptors. Mol Pharmacol 32: 53-58
    • (1987) Mol Pharmacol , vol.32 , pp. 53-58
    • Howard, M.J.1    Hughes, R.J.2    Motulsky, H.J.3    Mullen, M.D.4    Insel, P.A.5
  • 42
    • 67650239912 scopus 로고    scopus 로고
    • Analysis of full and partial agonists binding to beta2-Adrenergic receptor suggests a role of transmembrane helix v in agonist-specifi c conformational changes
    • Katritch V, Reynolds KA , Cherezov V, Hanson MA, Roth CB, Yeager M, Abagyan R (2009) Analysis of full and partial agonists binding to beta2-Adrenergic receptor suggests a role of transmembrane helix V in agonist-specifi c conformational changes. J Mol Recognit 22: 307-318
    • (2009) J Mol Recognit , vol.22 , pp. 307-318
    • Katritch, V.1    Reynolds, K.A.2    Cherezov, V.3    Hanson, M.A.4    Roth, C.B.5    Yeager, M.6    Abagyan, R.7
  • 43
    • 0035083109 scopus 로고    scopus 로고
    • Inverse, protean, and ligand-selective agonism: Matt ers of receptor conformation
    • Kenakin T (2001) Inverse, protean, and ligand-selective agonism: matt ers of receptor conformation. FASEB J 15: 598-611
    • (2001) FASEB J , vol.15 , pp. 598-611
    • Kenakin, T.1
  • 44
    • 0036463901 scopus 로고    scopus 로고
    • Effi cacy at g-protein-coupled receptors
    • Kenakin T (2002) Effi cacy at G-protein-coupled receptors. Nat Rev Drug Discov 1: 103-110
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 103-110
    • Kenakin, T.1
  • 45
    • 0018862848 scopus 로고
    • A quantitative analysis of beta-Adrenergic receptor interactions: Resolution of high and low affi nity states of the receptor by computer modeling of ligand binding data
    • Kent RS, De Lean A, Lefkowitz RJ (1980) A quantitative analysis of beta-Adrenergic receptor interactions: resolution of high and low affi nity states of the receptor by computer modeling of ligand binding data. Mol Pharmacol 17: 14-23
    • (1980) Mol Pharmacol , vol.17 , pp. 14-23
    • Kent, R.S.1    De Lean, A.2    Lefkowitz, R.J.3
  • 46
    • 0029960789 scopus 로고    scopus 로고
    • Glutamate residues in the second extracellular loop of the human a2a adenosine receptor are required for ligand recognition
    • Kim J, Jiang Q, Glashofer M, Yehle S, Wess J, Jacobson KA (1996) Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition. Mol Pharmacol 49: 683-691
    • (1996) Mol Pharmacol , vol.49 , pp. 683-691
    • Kim, J.1    Jiang, Q.2    Glashofer, M.3    Yehle, S.4    Wess, J.5    Jacobson, K.A.6
  • 47
  • 48
    • 0026592357 scopus 로고
    • Constitutive activation of the alpha 1b-Adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation
    • Kjelsberg MA, Cotecchia S, Ostrowski J, Caron MG, Lefkowitz RJ (1992) Constitutive activation of the alpha 1B-Adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation. J Biol Chem 267: 1430-1433
    • (1992) J Biol Chem , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 49
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of g-protein-coupled receptors
    • Kobilka BK and Deupi X (2007) Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 28: 397-406
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 50
    • 0023643263 scopus 로고
    • An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins
    • Kobilka BK, Frielle T, Collins S, Yang-Feng T, Kobilka TS, Francke U, Lefkowitz RJ, Caron MG (1987a) An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins. Nature 329: 75-79
    • (1987) Nature , vol.329 , pp. 75-79
    • Kobilka, B.K.1    Frielle, T.2    Collins, S.3    Yang-Feng, T.4    Kobilka, T.S.5    Francke, U.6    Lefkowitz, R.J.7    Caron, M.G.8
  • 51
    • 0023194433 scopus 로고
    • Delineation of the intronless nature of the genes for the human and hamster beta 2-Adrenergic receptor and their putative promoter regions
    • Kobilka BK, Frielle T, Dohlman HG, Bolanowski MA, Dixon RA , Keller P, Caron MG, Lefkowitz RJ (1987b) Delineation of the intronless nature of the genes for the human and hamster beta 2-Adrenergic receptor and their putative promoter regions. J Biol Chem 262: 7321-7327
    • (1987) J Biol Chem , vol.262 , pp. 7321-7327
    • Kobilka, B.K.1    Frielle, T.2    Dohlman, H.G.3    Bolanowski, M.A.4    Dixon, R.A.5    Keller, P.6    Caron, M.G.7    Lefkowitz, R.J.8
  • 53
    • 70349986967 scopus 로고    scopus 로고
    • Arrestin development: Emerging roles for beta-Arrestins in developmental signaling pathways
    • Kovacs JJ, Hara MR, Davenport CL, Kim J, Lefkowitz RJ (2009) Arrestin development: emerging roles for beta-Arrestins in developmental signaling pathways. Dev Cell 17: 443-458
    • (2009) Dev Cell , vol.17 , pp. 443-458
    • Kovacs, J.J.1    Hara, M.R.2    Davenport, C.L.3    Kim, J.4    Lefkowitz, R.J.5
  • 54
    • 28244486354 scopus 로고
    • On the reaction of cells and of nerve-endings to certain poisons, chiefl y as regards the reaction of striated muscle to nicotine and to curari
    • Langley JN (1905) On the reaction of cells and of nerve-endings to certain poisons, chiefl y as regards the reaction of striated muscle to nicotine and to curari. J Physiol 33: 374-413
    • (1905) J Physiol , vol.33 , pp. 374-413
    • Langley, J.N.1
  • 55
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz RJ, Cotecchia S, Samama P, Costa T (1993) Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol Sci 14: 303-307
    • (1993) Trends Pharmacol Sci , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 57
  • 59
    • 0025352299 scopus 로고
    • Beta-Arrestin: A protein that regulates beta-Adrenergic receptor function
    • Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (1990) beta-Arrestin: a protein that regulates beta-Adrenergic receptor function. Science 248: 1547-1550
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 60
    • 2142832180 scopus 로고    scopus 로고
    • Receptive substances" john newport langley 1852-1925) and his path to a receptor theory of drug action
    • Maehle A (2004) "Receptive substances": John Newport Langley (1852-1925) and his path to a receptor theory of drug action. Med Hist 48: 153-174
    • (2004) Med Hist , vol.48 , pp. 153-174
    • Maehle, A.1
  • 61
    • 0022372997 scopus 로고
    • Reconstitution of catecholamine-stimulated adenylate cyclase activity using three purifi ed proteins
    • May DC, Ross EM, Gilman AG, Smigel MD (1985) Reconstitution of catecholamine-stimulated adenylate cyclase activity using three purifi ed proteins. J Biol Chem 260: 15829-15833
    • (1985) J Biol Chem , vol.260 , pp. 15829-15833
    • May, D.C.1    Ross, E.M.2    Gilman, A.G.3    Smigel, M.D.4
  • 62
    • 0016739036 scopus 로고
    • Subsensitivity of adenylate cyclase and decreased beta-Adrenergic receptor binding aft er chronic exposure to (minus)-isoproterenol in vitro
    • Mickey J, Tate R, Lefkowitz RJ (1975) Subsensitivity of adenylate cyclase and decreased beta-Adrenergic receptor binding aft er chronic exposure to (minus)-isoproterenol in vitro. J Biol Chem 250: 5727-5729
    • (1975) J Biol Chem , vol.250 , pp. 5727-5729
    • Mickey, J.1    Tate, R.2    Lefkowitz, R.J.3
  • 63
    • 0028196652 scopus 로고
    • Orphan seven transmembrane domain receptors: Reversing pharmacology
    • Mills A and Duggan MJ (1994) Orphan seven transmembrane domain receptors: reversing pharmacology. Trends Biotechnol 12: 47-49
    • (1994) Trends Biotechnol , vol.12 , pp. 47-49
    • Mills, A.1    Duggan, M.J.2
  • 64
    • 0016769472 scopus 로고
    • Identifi cation of adenylate cyclase-coupled beta-Adrenergic receptors in frog erythrocytes with (minus)-[3-h] alprenolol
    • Mukherjee C, Caron MG, Coverstone M, Lefkowitz RJ (1975) Identifi cation of adenylate cyclase-coupled beta-Adrenergic receptors in frog erythrocytes with (minus)-[3-H] alprenolol. J Biol Chem 250: 4869-4876
    • (1975) J Biol Chem , vol.250 , pp. 4869-4876
    • Mukherjee, C.1    Caron, M.G.2    Coverstone, M.3    Lefkowitz, R.J.4
  • 65
    • 0028276459 scopus 로고
    • A common step for signal transduction in g-proteincoupled receptors
    • Oliveira L, Paiva AC, Sander C, Vriend G (1994) A common step for signal transduction in G-proteincoupled receptors. Trends Pharmacol Sci 15: 170-172
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 170-172
    • Oliveira, L.1    Paiva, A.C.2    Sander, C.3    Vriend, G.4
  • 66
    • 0033452126 scopus 로고    scopus 로고
    • A low resolution model for the interaction of g-proteins with g-protein-coupled receptors
    • Oliveira L, Paiva AC, Vriend G (1999) A low resolution model for the interaction of G-proteins with G-protein-coupled receptors. Protein Eng 12: 1087-1095
    • (1999) Protein Eng , vol.12 , pp. 1087-1095
    • Oliveira, L.1    Paiva, A.C.2    Vriend, G.3
  • 69
    • 0020373509 scopus 로고
    • Rhodopsin and bacteriorhodopsin: Structure-function relationships
    • Ovchinnikov YuA (1982) Rhodopsin and bacteriorhodopsin: structure-function relationships. FEBS Lett 148: 179-191
    • (1982) FEBS Lett , vol.148 , pp. 179-191
    • Ovchinnikov, YuA.1
  • 72
    • 0026517309 scopus 로고
    • On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors
    • Pardo L, Ballesteros JA, Osman R, Weinstein H (1992) On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors. Proc Natl Acad Sci USA 89: 4009-4012
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4009-4012
    • Pardo, L.1    Ballesteros, J.A.2    Osman, R.3    Weinstein, H.4
  • 74
    • 0030742986 scopus 로고    scopus 로고
    • Structure of the m1 muscarinic acetylcholine receptor gene and its promoter
    • Pepitoni S, Wood IC, Buckley NJ (1997) Structure of the m1 muscarinic acetylcholine receptor gene and its promoter. J Biol Chem 272: 17112-17117
    • (1997) J Biol Chem , vol.272 , pp. 17112-17117
    • Pepitoni, S.1    Wood, I.C.2    Buckley, N.J.3
  • 75
    • 0015918260 scopus 로고
    • Opiate receptor: Demonstration in nervous tissue
    • Pert CB and Snyder SH (1973) Opiate receptor: demonstration in nervous tissue. Science 179: 1011-1014
    • (1973) Science , vol.179 , pp. 1011-1014
    • Pert, C.B.1    Snyder, S.H.2
  • 77
    • 0000413412 scopus 로고
    • Formation of a cyclic adenine ribonucleotide by tissue particles
    • Rall TW and Sutherland EW (1958) Formation of a cyclic adenine ribonucleotide by tissue particles. J Biol Chem 232: 1065-1076
    • (1958) J Biol Chem , vol.232 , pp. 1065-1076
    • Rall, T.W.1    Sutherland, E.W.2
  • 79
    • 70450263435 scopus 로고    scopus 로고
    • Fine-tuning of gpcr activity by receptor-interacting-proteins
    • Ritt er SL and Hall RA (2009) Fine-tuning of GPCR activity by receptor-interactinG-proteins. Nat Rev Mol Cell Biol 10: 819-830
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 80
    • 0015239313 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action
    • Rodbell M, Birnbaumer L, Pohl SL, Krans HM (1971) The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action. J Biol Chem 246: 1877-1882
    • (1971) J Biol Chem , vol.246 , pp. 1877-1882
    • Rodbell, M.1    Birnbaumer, L.2    Pohl, S.L.3    Krans, H.M.4
  • 81
    • 84889868556 scopus 로고    scopus 로고
    • Ligand design for g-protein-coupled receptors. Wiley-vch ross em and gilman ag 1977) resolution of some components of adenylate cyclase necessary for catalytic activity
    • Rognan D (2006) Ligand design for G-protein-coupled receptors. Wiley-VCH Ross EM and Gilman AG (1977) Resolution of some components of adenylate cyclase necessary for catalytic activity. J Biol Chem 252: 6966-6969
    • (2006) J Biol Chem , vol.252 , pp. 6966-6969
    • Rognan, D.1
  • 82
    • 0026639831 scopus 로고
    • Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor. Role of conserved cysteines in receptor function
    • Savarese TM, Wang CD, Fraser CM (1992) Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor. Role of conserved cysteines in receptor function. J Biol Chem 267: 11439-11448
    • (1992) J Biol Chem , vol.267 , pp. 11439-11448
    • Savarese, T.M.1    Wang, C.D.2    Fraser, C.M.3
  • 84
    • 0034578519 scopus 로고    scopus 로고
    • Serine and alanine mutagenesis of the nine native cysteine residues of the human a(1) adenosine receptor
    • Scholl DJ and Wells JN (2000) Serine and alanine mutagenesis of the nine native cysteine residues of the human A(1) adenosine receptor. Biochem Pharmacol 60: 1647-1654
    • (2000) Biochem Pharmacol , vol.60 , pp. 1647-1654
    • Scholl, D.J.1    Wells, J.N.2
  • 85
    • 0036033424 scopus 로고    scopus 로고
    • Constitutive activity of g-protein-coupled receptors: Cause of disease and common property of wild-type receptors
    • Seifert R and Wenzel-Seifert K (2002) Constitutive activity of G-protein-coupled receptors: cause of disease and common property of wild-type receptors. Naunyn Schmiedeberg's Arch Pharmacol 366: 381-416
    • (2002) Naunyn Schmiedeberg's Arch Pharmacol , vol.366 , pp. 381-416
    • Seifert, R.1    Wenzel-Seifert, K.2
  • 86
    • 0036169280 scopus 로고    scopus 로고
    • The binding site of aminergic g-protein-coupled receptors: The transmembrane segments and second extracellular loop
    • Shi L and Javitch JA (2002) The binding site of aminergic G-protein-coupled receptors: the transmembrane segments and second extracellular loop. Ann Rev Pharmacol Toxicol 42: 437-467
    • (2002) Ann Rev Pharmacol Toxicol , vol.42 , pp. 437-467
    • Shi, L.1    Javitch, J.A.2
  • 87
    • 0347717582 scopus 로고    scopus 로고
    • The second extracellular loop of the dopamine d2 receptor lines the binding-site crevice
    • Shi L and Javitch JA (2004) The second extracellular loop of the dopamine D2 receptor lines the binding-site crevice. Proc Natl Acad Sci USA 101: 440-445
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 440-445
    • Shi, L.1    Javitch, J.A.2
  • 88
    • 0037174606 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • Shi L, Liapakis G, Xu R, Guarnieri F, Ballesteros JA, Javitch JA (2002) Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J Biol Chem 277: 40989-40996
    • (2002) J Biol Chem , vol.277 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 89
    • 0020620777 scopus 로고
    • Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor
    • Stadel JM, Nambi P, Shorr RG, Sawyer DF, Caron MG, Lefkowitz RJ (1983) Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor. Proc Natl Acad Sci USA 80: 3173-3177
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3173-3177
    • Stadel, J.M.1    Nambi, P.2    Shorr, R.G.3    Sawyer, D.F.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 92
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
    • Sutherland EW and Rall TW (1958) Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J Biol Chem 232: 1077-1091
    • (1958) J Biol Chem , vol.232 , pp. 1077-1091
    • Sutherland, E.W.1    Rall, T.W.2
  • 93
    • 40349088827 scopus 로고    scopus 로고
    • G-protein-coupled receptor phosphorylation: Where, when and by whom
    • Tobin AB (2008) G-protein-coupled receptor phosphorylation: where, when and by whom. Br J Pharm 153 (Suppl 1): S167-S176
    • (2008) Br J Pharm , vol.153 , Issue.SUPPL. 1
    • Tobin, A.B.1
  • 94
    • 0028024910 scopus 로고
    • A threonine residue in the seventh transmembrane domain of the human a1 adenosine receptor mediates specifi c agonist binding
    • Townsend-Nicholson A and Schofi eld PR (1994) A threonine residue in the seventh transmembrane domain of the human A1 adenosine receptor mediates specifi c agonist binding. J Biol Chem 269: 2373-2376
    • (1994) J Biol Chem , vol.269 , pp. 2373-2376
    • Townsend-Nicholson, A.1    Schofield, P.R.2
  • 95
    • 0014409394 scopus 로고
    • An adenosine 3-,5-monophosphate-dependant protein kinase from rabbit skeletal muscle
    • Walsh DA, Perkins JP, Krebs EG (1968) An adenosine 3-,5-monophosphate- dependant protein kinase from rabbit skeletal muscle. J Biol Chem 243: 3763-3765
    • (1968) J Biol Chem , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 97
    • 0019956634 scopus 로고
    • Light-dependent phosphorylation of rhodopsin: Number of phosphorylation sites
    • Wilden U and Kn H (1982) Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry 21: 3014-3022
    • (1982) Biochemistry , vol.21 , pp. 3014-3022
    • Wilden, U.1    Kn, H.2
  • 98
    • 0000025689 scopus 로고
    • Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kda protein of rod outer segments
    • Wilden U, Hall SW, Kn H (1986) Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci USA 83: 1174-1178
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1174-1178
    • Wilden, U.1    Hall, S.W.2    Kn, H.3
  • 99
    • 0033840363 scopus 로고    scopus 로고
    • Coupling of canine serotonin 5-ht(1b) and 5-ht(1d) receptor subtypes to the formation of inositol phosphates by dual interactions with endogenous g(i/o) and recombinant g(alpha15) proteins
    • Wurch T and Pauwels PJ (2000) Coupling of canine serotonin 5-HT(1B) and 5-HT(1D) receptor subtypes to the formation of inositol phosphates by dual interactions with endogenous G(i/o) and recombinant G(alpha15) proteins. J Neurochem 75: 1180-1189
    • (2000) J Neurochem , vol.75 , pp. 1180-1189
    • Wurch, T.1    Pauwels, P.J.2
  • 100
    • 0016159582 scopus 로고
    • Muscarinic cholinergic binding in rat brain
    • Yamamura HI and Snyder SH (1974) Muscarinic cholinergic binding in rat brain. Proc Natl Acad Sci USA 71: 1725-1729
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1725-1729
    • Yamamura, H.I.1    Snyder, S.H.2
  • 101
    • 0029847408 scopus 로고    scopus 로고
    • Identifi cation of critical extracellular loop residues involved in alpha 1-adrenergic receptor subtype-selective antagonist binding
    • Zhao MM, Hwa J, Perez DM (1996) Identifi cation of critical extracellular loop residues involved in alpha 1-adrenergic receptor subtype-selective antagonist binding. Mol Pharmacol 50: 1118-1126
    • (1996) Mol Pharmacol , vol.50 , pp. 1118-1126
    • Zhao, M.M.1    Hwa, J.2    Perez, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.