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Volumn 4, Issue , 2004, Pages

A homotropic two-state model and auto-antagonism

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; CYCLIC AMP; FORSKOLIN; G PROTEIN COUPLED RECEPTOR; LIGAND; METHACHOLINE; MUSCARINIC M3 RECEPTOR; MUSCARINIC RECEPTOR; PROLACTIN; PROLACTIN RECEPTOR; PROSTACYCLIN; PROSTAGLANDIN E2; TRACER;

EID: 12944265070     PISSN: 14712210     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2210-4-11     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 0027665006 scopus 로고
    • Allosteric proteins: From regulatory enzymes to receptors - Personal recollections
    • Changeux JP: Allosteric proteins: from regulatory enzymes to receptors - personal recollections. Bioessays 1993, 15: 25-634.
    • (1993) Bioessays , vol.15 , pp. 625-634
    • Changeux, J.P.1
  • 2
    • 0034003973 scopus 로고    scopus 로고
    • Allosteric modulators affect the efficacy of partial agonists for recombinant GABA(A) receptors
    • Maksay G, Thompson SA, Wafford KA: Allosteric modulators affect the efficacy of partial agonists for recombinant GABA(A) receptors. Br J Pharmacol 2000, 129:1794-1800.
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 1794-1800
    • Maksay, G.1    Thompson, S.A.2    Wafford, K.A.3
  • 3
    • 0034100346 scopus 로고    scopus 로고
    • Allosteric interactions between the antagonist prazosin and amiloride analogs at the human alpha(1A)-adrenergic receptor
    • Leppik RA, Mynett A, Lazareno S, Birdsall NJ: Allosteric interactions between the antagonist prazosin and amiloride analogs at the human alpha(1A)-adrenergic receptor. Mol Pharmacol 2000, 57: 36-445.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 436-445
    • Leppik, R.A.1    Mynett, A.2    Lazareno, S.3    Birdsall, N.J.4
  • 4
    • 0034821747 scopus 로고    scopus 로고
    • Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase
    • Helmstaedt K, Krappmann S, Braus GH: Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Microbiol Mol Biol Rev 2001, 65:404-421.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 404-421
    • Helmstaedt, K.1    Krappmann, S.2    Braus, G.H.3
  • 5
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos A, Kenakin T: G protein-coupled receptor allosterism and complexing. Pharmacol Rev 2002, 54: 23-374.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 6
    • 0036462446 scopus 로고    scopus 로고
    • Allosteric modulators of group I metabotropic glutamate receptors: Novel subtype-selective ligands and therapeutic perspectives
    • Gasparini F, Kuhn R, Pin JP: Allosteric modulators of group I metabotropic glutamate receptors: novel subtype-selective ligands and therapeutic perspectives. Curr Opin Pharmacol 2002, 2: 3-49.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 43-49
    • Gasparini, F.1    Kuhn, R.2    Pin, J.P.3
  • 7
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux J-P: On the nature of allosteric transitions: A plausible model. J Mol Biol 1965, 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 8
    • 0023655481 scopus 로고
    • Co-operative and allosteric enzymes: 20 years on
    • Ricard J, Cornish-Bowden A: Co-operative and allosteric enzymes: 20 years on. Eur J Biochem 1987, 166:255-272.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 255-272
    • Ricard, J.1    Cornish-Bowden, A.2
  • 10
    • 0037229515 scopus 로고    scopus 로고
    • Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling
    • He YA, Roussel F, Halpert JR: Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling. Arch Biochem Biophys 2003, 409:92-101.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 92-101
    • He, Y.A.1    Roussel, F.2    Halpert, J.R.3
  • 11
    • 0029863212 scopus 로고    scopus 로고
    • Agonist self-inhibitory binding site of the nicotinic acetylcholine receptor
    • Arias HR: Agonist self-inhibitory binding site of the nicotinic acetylcholine receptor. J Neurosci Res 1996, 44: 7-105.
    • (1996) J. Neurosci. Res. , vol.44 , pp. 97-105
    • Arias, H.R.1
  • 13
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P, Elferink RO: Mammalian ABC transporters in health and disease. Annu Rev Biochem 2002, 71:537-592.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 14
    • 0141562158 scopus 로고    scopus 로고
    • Short-term activation by low 17beta-estradiol concentrations of the Na+/H+ exchanger in rat aortic smooth muscle cells: Physiopathological implications
    • Incerpi S, D'Arezzo S, Marino M, Musanti R, Pallottini V, Pascolini A, Trentalance A: Short-term activation by low 17beta-estradiol concentrations of the Na+/H+ exchanger in rat aortic smooth muscle cells: physiopathological implications. Endocrinology 2003, 144:4315-4324.
    • (2003) Endocrinology , vol.144 , pp. 4315-4324
    • Incerpi, S.1    D'Arezzo, S.2    Marino, M.3    Musanti, R.4    Pallottini, V.5    Pascolini, A.6    Trentalance, A.7
  • 16
    • 0022477916 scopus 로고
    • Interpretation of dose-response curves for luteinizing hormone release by gonadotropinreleasing hormone, related peptides, and leukotriene C4 according to a hormone/receptor/effector model
    • Leiser J, Conn PM, Blum JJ: Interpretation of dose-response curves for luteinizing hormone release by gonadotropinreleasing hormone, related peptides, and leukotriene C4 according to a hormone/receptor/effector model. Proc Natl Acad Sci U S A 1986, 83:5963-7.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 5963-5967
    • Leiser, J.1    Conn, P.M.2    Blum, J.J.3
  • 17
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger J: Signal transduction by allosteric receptor oligomerization. Trends Biochem Sci 1988, 13:443-447.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 443-447
    • Schlessinger, J.1
  • 18
    • 0027529259 scopus 로고
    • Desensitization and reactivation of ACh-regulated exocrine secretion in hen tracheal epithelium
    • Winding B, Bindslev N: Desensitization and reactivation of ACh-regulated exocrine secretion in hen tracheal epithelium. Am J Physiol 1993, 264:C342-C351.
    • (1993) Am. J. Physiol. , vol.264
    • Winding, B.1    Bindslev, N.2
  • 19
    • 0029787046 scopus 로고    scopus 로고
    • Agonist-induced modulation of inverse agonist efficacy at the beta 2-adrenergic receptor
    • Chidiac P, Nouet S, Bouvier M: Agonist-induced modulation of inverse agonist efficacy at the beta 2-adrenergic receptor. Mol Pharmacol 1996, 50:662-669.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 662-669
    • Chidiac, P.1    Nouet, S.2    Bouvier, M.3
  • 20
    • 0033621458 scopus 로고    scopus 로고
    • A dual component analysis explains the distinctive kinetics of cAMP accumulation in brown adipocytes
    • Bronnikov GE, Zhang SJ, Cannon B, Nedergaard J: A dual component analysis explains the distinctive kinetics of cAMP accumulation in brown adipocytes. J Biol Chem 1999, 274:37770-37780.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37770-37780
    • Bronnikov, G.E.1    Zhang, S.J.2    Cannon, B.3    Nedergaard, J.4
  • 21
    • 0038630416 scopus 로고    scopus 로고
    • Benzoquinolines and chloride secretion in murine colonic epithelium
    • Cuthbert AW: Benzoquinolines and chloride secretion in murine colonic epithelium. Br J Pharmacol 2003, 138: 528-1534.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1528-1534
    • Cuthbert, A.W.1
  • 22
    • 0037739740 scopus 로고    scopus 로고
    • Evidence for cross-talk between M2 and M3 muscarinic acetylcholine receptors in the regulation of second messenger and extracellular signal-regulated kinase signalling pathways in Chinese hamster ovary cells
    • Hornigold DC, Mistry R, Raymond PD, Blank JL, Challiss RA: Evidence for cross-talk between M2 and M3 muscarinic acetylcholine receptors in the regulation of second messenger and extracellular signal-regulated kinase signalling pathways in Chinese hamster ovary cells. Br J Pharmacol 2003, 138:1340-1350.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1340-1350
    • Hornigold, D.C.1    Mistry, R.2    Raymond, P.D.3    Blank, J.L.4    Challiss, R.A.5
  • 23
    • 0037446481 scopus 로고    scopus 로고
    • Comparison of the pharmacological antagonism of M2 and M3 muscarinic receptors expressed in isolation and in combination
    • Griffin MT, Hsu JC, Shehnaz D, Ehlert FJ: Comparison of the pharmacological antagonism of M2 and M3 muscarinic receptors expressed in isolation and in combination. Biochem Pharmacol 2003, 65:1227-1241.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1227-1241
    • Griffin, M.T.1    Hsu, J.C.2    Shehnaz, D.3    Ehlert, F.J.4
  • 25
    • 0032494119 scopus 로고    scopus 로고
    • Pharmacodynamic aspects of peptide administration biological response modifiers
    • Talmadge JE: Pharmacodynamic aspects of peptide administration biological response modifiers. Adv Drug Deliv Rev 1998, 33:241-252.
    • (1998) Adv. Drug Deliv. Rev. , vol.33 , pp. 241-252
    • Talmadge, J.E.1
  • 26
    • 0027952717 scopus 로고
    • Excess-substrate inhibition in enzymology and highdose inhibition in pharmacology: A reinterpretation
    • [corrected]
    • Kühl PW: Excess-substrate inhibition in enzymology and highdose inhibition in pharmacology: a reinterpretation [corrected]. Biochem J 1994, 298:171-180.
    • (1994) Biochem. J. , vol.298 , pp. 171-180
    • Kühl, P.W.1
  • 27
    • 0019024103 scopus 로고
    • Substrate inhibition as a problem of non-linear steady state kinetics with monomeric enzymes
    • Kaiser PM: Substrate inhibition as a problem of non-linear steady state kinetics with monomeric enzymes. J Mol Catal 1980, 8:431-442.
    • (1980) J. Mol. Catal. , vol.8 , pp. 431-442
    • Kaiser, P.M.1
  • 28
    • 0029550774 scopus 로고
    • Mechanism of insulin and IGF-I receptor activation and signal transduction specificity. Receptor dimer cross-linking, bell-shaped curves, and sustained versus transient signaling
    • De Meyts P, Urso B, Christoffersen CT, Shymko RM: Mechanism of insulin and IGF-I receptor activation and signal transduction specificity. Receptor dimer cross-linking, bell-shaped curves, and sustained versus transient signaling. Ann N Y Acad Sci 1995, 766:388-401.
    • (1995) Ann. N. Y. Acad. Sci. , vol.766 , pp. 388-401
    • De Meyts, P.1    Urso, B.2    Christoffersen, C.T.3    Shymko, R.M.4
  • 29
    • 0036630357 scopus 로고    scopus 로고
    • Molecular versatility of antibodies
    • Metzger H: Molecular versatility of antibodies. Immunol Rev 2002, 185:186-205.
    • (2002) Immunol. Rev. , vol.185 , pp. 186-205
    • Metzger, H.1
  • 30
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA: G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol Ther 2001, 92:71-87.
    • (2001) Pharmacol. Ther. , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 31
    • 0028840330 scopus 로고
    • Competition between positive and negative allosteric effectors on muscarinic receptors
    • Proška J, Tuček S: Competition between positive and negative allosteric effectors on muscarinic receptors. Mol Pharmacol 1995, 48:696-702.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 696-702
    • Proška, J.1    Tuček, S.2
  • 32
    • 0031009786 scopus 로고    scopus 로고
    • Allosteric binding sites on muscarinic receptors
    • Ellis J: Allosteric binding sites on muscarinic receptors. Drug Dev Res 1997, 40:193-204.
    • (1997) Drug Dev. Res. , vol.40 , pp. 193-204
    • Ellis, J.1
  • 34
    • 0033669603 scopus 로고    scopus 로고
    • Modeling the functional effects of allosteric modulators at pharmacological receptors: An extension of the two-state model of receptor activation
    • Hall DA: Modeling the functional effects of allosteric modulators at pharmacological receptors: an extension of the two-state model of receptor activation. Mol Pharmacol 2000, 58: 412-1423.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1412-1423
    • Hall, D.A.1
  • 35
    • 0029935383 scopus 로고    scopus 로고
    • The Cubic Ternary Complex Receptor-Occupancy Model I. Model Description
    • Weiss JM, Morgan PH, Lutz MW, Kenakin TP: The Cubic Ternary Complex Receptor-Occupancy Model I. Model Description. J Theor Biol 1996, 178:151-167.
    • (1996) J. Theor. Biol. , vol.178 , pp. 151-167
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 36
    • 0029983553 scopus 로고    scopus 로고
    • The Cubic Ternary Complex Receptor-Occupancy Model II. Understanding Apparent Affinity
    • Weiss JM, Morgan PH, Lutz MW, Kenakin TP: The Cubic Ternary Complex Receptor-Occupancy Model II. Understanding Apparent Affinity. J Theor Biol 1996, 178:169-182.
    • (1996) J. Theor. Biol. , vol.178 , pp. 169-182
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 37
    • 0030596736 scopus 로고    scopus 로고
    • The cubic ternary complex receptor-occupancy model. III. Resurrecting efficacy
    • Weiss JM, Morgan PH, Lutz MW, Kenakin TP: The cubic ternary complex receptor-occupancy model. III. Resurrecting efficacy. J Theor Biol 1996, 181:381-397.
    • (1996) J. Theor. Biol. , vol.181 , pp. 381-397
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 38
    • 0033543571 scopus 로고    scopus 로고
    • Biological properties of human prolactin analogs depend not only on global hormone affinity, but also on the relative affinities of both receptor binding sites
    • Kinet S, Bernichtein S, Kelly PA, Martial JA, Goffin V: Biological properties of human prolactin analogs depend not only on global hormone affinity, but also on the relative affinities of both receptor binding sites. J Biol Chem 1999, 274:26033-26043.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26033-26043
    • Kinet, S.1    Bernichtein, S.2    Kelly, P.A.3    Martial, J.A.4    Goffin, V.5
  • 39
    • 0037111176 scopus 로고    scopus 로고
    • Bell-shaped curves for prostaglandin-induced modulation of adenylate cyclase: Two mutually opposing effects
    • Accomazzo MR, Cattaneo S, Nicosia S, Rovati GE: Bell-shaped curves for prostaglandin-induced modulation of adenylate cyclase: two mutually opposing effects. Eur J Pharmacol 2002, 454:107-114.
    • (2002) Eur. J. Pharmacol. , vol.454 , pp. 107-114
    • Accomazzo, M.R.1    Cattaneo, S.2    Nicosia, S.3    Rovati, G.E.4
  • 40
    • 0029083945 scopus 로고
    • Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors
    • Wreggett KA, Wells JW: Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors. J Biol Chem 1995, 270:22488-22499.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22488-22499
    • Wreggett, K.A.1    Wells, J.W.2
  • 41
    • 1342323325 scopus 로고    scopus 로고
    • Application of a kinetic model to the apparently complex behavior of negative and positive allosteric modulators of muscarinic acetylcholine receptors
    • Avlani V, May LT, Sexton PM, Christopoulos A: Application of a kinetic model to the apparently complex behavior of negative and positive allosteric modulators of muscarinic acetylcholine receptors. J Pharmacol Exp Ther 2004, 308:1062-72.
    • (2004) J. Pharmacol. Exp. Ther. , vol.308 , pp. 1062-1072
    • Avlani, V.1    May, L.T.2    Sexton, P.M.3    Christopoulos, A.4
  • 42
    • 0033801789 scopus 로고    scopus 로고
    • Molecular aspects of muscarinic receptor dimerization
    • Zeng F, Wess J: Molecular aspects of muscarinic receptor dimerization. Neuropsycho-pharmacology 2000, 23:S19-31.
    • (2000) Neuropsycho-pharmacology , vol.23
    • Zeng, F.1    Wess, J.2
  • 43
    • 0028305892 scopus 로고
    • Differential regulation of cAMP-mediated gene transcription by m1 and m4 muscarinic acetylcholine receptors. Preferential coupling of m4 receptors to Gi alpha-2
    • Migeon JC, Nathanson NM: Differential regulation of cAMP-mediated gene transcription by m1 and m4 muscarinic acetylcholine receptors. Preferential coupling of m4 receptors to Gi alpha-2. J Biol Chem 1994, 269:9767-9773.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9767-9773
    • Migeon, J.C.1    Nathanson, N.M.2
  • 45
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun D: Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br J Pharmacol 1998, 125: 24-947.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 46
    • 0020443638 scopus 로고
    • A three-state model of the benzodiazepine receptor explains the interactions between the benzodiazepine antagonist Ro 15-1788, benzodiazepine tranquilizers, beta-carbolines, and phenobarbitone
    • Polc P, Bonetti EP, Schaffner R, Haefely W: A three-state model of the benzodiazepine receptor explains the interactions between the benzodiazepine antagonist Ro 15-1788, benzodiazepine tranquilizers, beta-carbolines, and phenobarbitone. Naunyn - Schmiedebergs Arch Pharmacol 1982, 321:260-264.
    • (1982) Naunyn - Schmiedebergs Arch. Pharmacol. , vol.321 , pp. 260-264
    • Polc, P.1    Bonetti, E.P.2    Schaffner, R.3    Haefely, W.4
  • 47
    • 0036453601 scopus 로고    scopus 로고
    • GPCR drug discovery through the exploitation of allosteric drug binding sites
    • Rees S, Morrow D, Kenakin T: GPCR drug discovery through the exploitation of allosteric drug binding sites. Receptors Channels 2002, 8:261-268.
    • (2002) Receptors Channels , vol.8 , pp. 261-268
    • Rees, S.1    Morrow, D.2    Kenakin, T.3
  • 48
    • 0004214524 scopus 로고
    • London: Longmans, Green & Co
    • Haldane JBS: Enzymes London: Longmans, Green & Co; 1930:84-85.
    • (1930) Enzymes , pp. 84-85
    • Haldane, J.B.S.1
  • 49
    • 12944324332 scopus 로고
    • The inhibition of esterases by excess substrate
    • Murray DRP: The inhibition of esterases by excess substrate. Biochem J 1930, 24:1890-96.
    • (1930) Biochem. J. , vol.24 , pp. 1890-1896
    • Murray, D.R.P.1
  • 50
    • 0001518571 scopus 로고
    • The molecular kinetics of the urea-urease system. I. The kinetic laws
    • Laidler KJ, Hoare JP: The molecular kinetics of the urea-urease system. I. The kinetic laws. J Am Chem Soc 1949, 71:2699-2702.
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 2699-2702
    • Laidler, K.J.1    Hoare, J.P.2
  • 51
    • 0011876812 scopus 로고
    • Affinity and intrinsic-activity in the theory of competitive- and non-competitive inhibition and an analysis of some forms of dualism in action
    • Ariëns EJ, Simonis AM, De Groot WM: Affinity and intrinsic-activity in the theory of competitive- and non-competitive inhibition and an analysis of some forms of dualism in action. Arch int pharmacodyn 1955, 100:298-322.
    • (1955) Arch. Int. Pharmacodyn. , vol.100 , pp. 298-322
    • Ariëns, E.J.1    Simonis, A.M.2    De Groot, W.M.3
  • 52
    • 0035677432 scopus 로고    scopus 로고
    • Patterns of cyclic AMP formation by coexpressed D1 and D2L dopamine receptors in HEK 293 cells
    • Sakolsky DJ, Ashby B: Patterns of cyclic AMP formation by coexpressed D1 and D2L dopamine receptors in HEK 293 cells. Receptors Channels 2001, 7:479-489.
    • (2001) Receptors Channels , vol.7 , pp. 479-489
    • Sakolsky, D.J.1    Ashby, B.2
  • 53
    • 1842866515 scopus 로고    scopus 로고
    • Quinidine and haloperidol as modifiers of CYP3A4 activity: Multisite kinetic model approach
    • Galetin A, Clarke SE, Houston JB: Quinidine and haloperidol as modifiers of CYP3A4 activity: multisite kinetic model approach. Drug Metab Dispos 2002, 30:1512-1522.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1512-1522
    • Galetin, A.1    Clarke, S.E.2    Houston, J.B.3
  • 54
    • 84965075853 scopus 로고
    • A study of the 'desensitization' produced by acetylcholine at the motor end-plate
    • Katz B, Thesleff S: A study of the 'desensitization' produced by acetylcholine at the motor end-plate. J Physiol 1957, 138:63-80.
    • (1957) J. Physiol. , vol.138 , pp. 63-80
    • Katz, B.1    Thesleff, S.2
  • 55
    • 0028950255 scopus 로고
    • The two-state model of receptor activation
    • Leff P: The two-state model of receptor activation. Trends Pharmacol Sci 1995, 16:89-97.
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 89-97
    • Leff, P.1
  • 56
    • 12944325417 scopus 로고
    • Mechanism of muscular contraction. II. Kinetic studies on muscle ATP-ase
    • Watanabe S, Tonomura Y, Shiokawa H: Mechanism of muscular contraction. II. Kinetic studies on muscle ATP-ase. J Biochem 1953, 40:387-402.
    • (1953) J. Biochem. , vol.40 , pp. 387-402
    • Watanabe, S.1    Tonomura, Y.2    Shiokawa, H.3
  • 57
    • 0006244627 scopus 로고
    • The enzymatic interaction between myosin and nucleotides
    • Blum JJ: The enzymatic interaction between myosin and nucleotides. Arch Biochem Biophys 1955, 55:486-511.
    • (1955) Arch. Biochem. Biophys. , vol.55 , pp. 486-511
    • Blum, J.J.1
  • 58
    • 12944306990 scopus 로고
    • An illustration of a kinetic analysis: The myosin B-ATP-EDTA system
    • Edited by: The committee of muscle chemistry of Japan. Tokyo: Igaku Shoin
    • Botts J, Drain GF: An illustration of a kinetic analysis: The myosin B-ATP-EDTA system. In Conference on the chemistry of muscular contraction 1957 Edited by: The committee of muscle chemistry of Japan. Tokyo: Igaku Shoin; 1958:33-41.
    • (1958) Conference on the Chemistry of Muscular Contraction 1957 , pp. 33-41
    • Botts, J.1    Drain, G.F.2
  • 59
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE Jr, Nemethy G, Filmer D: Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 1966, 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 60
    • 0017183499 scopus 로고
    • The non-stoichiometric floating receptor model for hormone sensitive adenylyl cyclase
    • De Haën C: The non-stoichiometric floating receptor model for hormone sensitive adenylyl cyclase. J Theor Biol 1976, 58:383-400.
    • (1976) J. Theor. Biol. , vol.58 , pp. 383-400
    • De Haën, C.1
  • 61
    • 0002859426 scopus 로고
    • A theory of drug action based on the rate of drug-receptor combination
    • Paton WDM: A theory of drug action based on the rate of drug-receptor combination. Proc Roy Soc Lond 1961, 154: 1-69.
    • (1961) Proc. Roy. Soc. Lond. , vol.154 , pp. 21-69
    • Paton, W.D.M.1
  • 63
    • 0019888557 scopus 로고
    • The regulatory component of adenylate cyclase. Purification and properties
    • Sternweis PC, Northup JK, Smigel MD, Gilman AG: The regulatory component of adenylate cyclase. Purification and properties. J Biol Chem 1981, 256:11517-11526.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11517-11526
    • Sternweis, P.C.1    Northup, J.K.2    Smigel, M.D.3    Gilman, A.G.4
  • 64
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor
    • De Lean A, Stadel JM, Lefkowitz RJ: A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor. J Biol Chem 1980, 255:7108-7117.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 65
    • 0001169515 scopus 로고
    • Antagonists with negative intrinsic activity at delta opioid receptors coupled to GTP-binding proteins
    • Costa T, Herz A: Antagonists with negative intrinsic activity at delta opioid receptors coupled to GTP-binding proteins. Proc Natl Acad Sci 1989, 86:7321-7325.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 7321-7325
    • Costa, T.1    Herz, A.2
  • 66
    • 0027513982 scopus 로고
    • A mutationinduced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P, Cotecchia S, Costa T, Lefkowitz RJ: A mutationinduced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 1993, 268 4625-4636.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 67
    • 0000984916 scopus 로고    scopus 로고
    • The evolution of drugreceptor models: The cubic ternary complex model for G protein-coupled receptors
    • Edited by: Kenakin T, Angus JA. Berlin: Springer Verlag
    • Kenakin T, Morgan P, Lutz M, Weiss J: The evolution of drugreceptor models: The cubic ternary complex model for G protein-coupled receptors. In The pharmacology of functional, biochemical, and recombinant receptor systems Edited by: Kenakin T, Angus JA. Berlin: Springer Verlag; 2000:147-165.
    • (2000) The Pharmacology of Functional, Biochemical, and Recombinant Receptor Systems , pp. 147-165
    • Kenakin, T.1    Morgan, P.2    Lutz, M.3    Weiss, J.4


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