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Volumn 46, Issue 26, 2007, Pages 7907-7927

Recovery of oligomers and cooperativity when monomers of the M2 muscarinic cholinergic receptor are reconstituted into phospholipid vesicles

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DATA ACQUISITION; ELECTROPHORESIS; MONOMERS; PHOSPHOLIPIDS; PROTEINS;

EID: 34347354319     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi6026105     Document Type: Article
Times cited : (38)

References (93)
  • 1
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A. G. (1987) G proteins: transducers of receptor-generated signals, Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 3
    • 0035032316 scopus 로고    scopus 로고
    • Oligomerisation of G protein-coupled receptors
    • Milligan, G. (2001) Oligomerisation of G protein-coupled receptors, J. Cell Sci. 114, 1265-1271.
    • (2001) J. Cell Sci , vol.114 , pp. 1265-1271
    • Milligan, G.1
  • 4
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers, S., Salahpour, A., and Bouvier, M. (2002) Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function, Annu. Rev. Pharmacol. Toxicol. 42, 409-435.
    • (2002) Annu. Rev. Pharmacol. Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 5
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • Park, P. S., Filipek, S., Wells, J. W., and Palczewski, K. (2004) Oligomerization of G protein-coupled receptors: past, present, and future, Biochemistry 43, 15643-15656.
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 6
    • 0030963248 scopus 로고    scopus 로고
    • Cardiac muscarinic receptors. Cooperativity as the basis for multiple states of affinity
    • Chidiac, P., Green, M. A., Pawagi, A. B., and Wells, J. W. (1997) Cardiac muscarinic receptors. Cooperativity as the basis for multiple states of affinity, Biochemistry 36, 7361-7379.
    • (1997) Biochemistry , vol.36 , pp. 7361-7379
    • Chidiac, P.1    Green, M.A.2    Pawagi, A.B.3    Wells, J.W.4
  • 7
    • 0008824348 scopus 로고
    • Correlation between the binding properties and pharmacological responses of muscarinic receptors
    • Birdsall, N. J., Burgen, A. S., and Hulme, E. C. (1977) Correlation between the binding properties and pharmacological responses of muscarinic receptors, Adv. Behav. Biol. 24, 25-33.
    • (1977) Adv. Behav. Biol , vol.24 , pp. 25-33
    • Birdsall, N.J.1    Burgen, A.S.2    Hulme, E.C.3
  • 8
    • 0018862848 scopus 로고
    • A quantitative analysis of β-adrenergic receptor interactions: Resolution of high and low affinity states of the receptor by computer modeling of ligand binding data
    • Kent, R. S., De Lean, A., and Lefkowitz, R. J. (1980) A quantitative analysis of β-adrenergic receptor interactions: resolution of high and low affinity 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
  • 9
    • 0022408262 scopus 로고
    • The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium
    • Ehlert, F. J. (1985) The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium, Mol. Pharmacol. 28, 410-421.
    • (1985) Mol. Pharmacol , vol.28 , pp. 410-421
    • Ehlert, F.J.1
  • 10
    • 0021824455 scopus 로고
    • Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo- and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting
    • Mattera, R., Pitts, B. J., Entman, M. L., and Birnbaumer, L. (1985) Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo- and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting, J. Biol. Chem. 260, 7410-7421.
    • (1985) J. Biol. Chem , vol.260 , pp. 7410-7421
    • Mattera, R.1    Pitts, B.J.2    Entman, M.L.3    Birnbaumer, L.4
  • 11
    • 0022475960 scopus 로고
    • β-adrenergic receptors and their mode of coupling to adenylate cyclase
    • Levitzki, A. (1986) β-adrenergic receptors and their mode of coupling to adenylate cyclase, Physiol. Rev. 66, 819-854.
    • (1986) Physiol. Rev , vol.66 , pp. 819-854
    • Levitzki, A.1
  • 12
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean, A., Stadel, J. M., and Lefkowitz, R. J. (1980) A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-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
  • 13
    • 0030961624 scopus 로고    scopus 로고
    • Cardiac muscarinic receptors. Relationship between the G protein and multiple states of affinity
    • Green, M. A., Chidiac, P., and Wells, J. W. (1997) Cardiac muscarinic receptors. Relationship between the G protein and multiple states of affinity, Biochemistry 36, 7380-7394.
    • (1997) Biochemistry , vol.36 , pp. 7380-7394
    • Green, M.A.1    Chidiac, P.2    Wells, J.W.3
  • 14
    • 0022411399 scopus 로고
    • 2-adrenergic receptors in purified membranes from human platelets. Implications of receptor-inhibitory nucleotide-binding protein stoichiometry
    • 2-adrenergic receptors in purified membranes from human platelets. Implications of receptor-inhibitory nucleotide-binding protein stoichiometry, Mol. Pharmacol. 28, 475-486.
    • (1985) Mol. Pharmacol , vol.28 , pp. 475-486
    • Neubig, R.R.1    Gantzos, R.D.2    Brasier, R.S.3
  • 15
    • 0023017887 scopus 로고
    • Assessment of a ternary model for the binding of agonists to neurohumoral receptors
    • Lee, T. W., Sole, M. J., and Wells, J. W. (1986) Assessment of a ternary model for the binding of agonists to neurohumoral receptors, Biochemistry 25, 7009-7020.
    • (1986) Biochemistry , vol.25 , pp. 7009-7020
    • Lee, T.W.1    Sole, M.J.2    Wells, J.W.3
  • 16
    • 0022973445 scopus 로고
    • Assessment of mechanistic proposals for the binding of agonists to cardiac muscarinic receptors
    • Wong, H. M., Sole, M. J., and Wells, J. W. (1986) Assessment of mechanistic proposals for the binding of agonists to cardiac muscarinic receptors, Biochemistry 25, 6995-7008.
    • (1986) Biochemistry , vol.25 , pp. 6995-7008
    • Wong, H.M.1    Sole, M.J.2    Wells, J.W.3
  • 17
    • 0029083945 scopus 로고
    • Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors
    • Wreggett, K. A., and Wells, J. W. (1995) Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors, J. Biol. Chem. 270, 22488-22499.
    • (1995) J. Biol. Chem , vol.270 , pp. 22488-22499
    • Wreggett, K.A.1    Wells, J.W.2
  • 18
    • 0031001608 scopus 로고    scopus 로고
    • Does subunit dissociation necessarily accompany the activation of all heterotrimeric G proteins?
    • Rebois, R. V., Warner, D. R., and Basi, N. S. (1997) Does subunit dissociation necessarily accompany the activation of all heterotrimeric G proteins? Cell. Signalling 9, 141-151.
    • (1997) Cell. Signalling , vol.9 , pp. 141-151
    • Rebois, R.V.1    Warner, D.R.2    Basi, N.S.3
  • 19
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receptor-G protein-effector interactions
    • Chidiac, P. (1998) Rethinking receptor-G protein-effector interactions, Biochem. Pharmacol. 55, 549-556.
    • (1998) Biochem. Pharmacol , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 22
    • 0026469361 scopus 로고
    • Effects of adenyl nucleotides and carbachol on cooperative interactions among G proteins
    • Chidiac, P., and Wells, J. W. (1992) Effects of adenyl nucleotides and carbachol on cooperative interactions among G proteins, Biochemistry 31, 10908-10921.
    • (1992) Biochemistry , vol.31 , pp. 10908-10921
    • Chidiac, P.1    Wells, J.W.2
  • 23
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G protein-linked receptors
    • Maggio, R., Vogel, Z., and Wess, J. (1993) Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G protein-linked receptors, Proc. Natl. Acad. Sci. U.S.A. 90, 3103-3107.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 3103-3107
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 28
    • 0242424107 scopus 로고    scopus 로고
    • 2 muscarinic cholinergic receptor purified from Sf9 cells
    • 2 muscarinic cholinergic receptor purified from Sf9 cells, Biochemistry 42, 12960-12971.
    • (2003) Biochemistry , vol.42 , pp. 12960-12971
    • Park, P.S.1    Wells, J.W.2
  • 29
    • 0037197663 scopus 로고    scopus 로고
    • Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors
    • Park, P. S., Sum, C. S., Pawagi, A. B., and Wells, J. W. (2002) Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors, Biochemistry 41, 5588-5604.
    • (2002) Biochemistry , vol.41 , pp. 5588-5604
    • Park, P.S.1    Sum, C.S.2    Pawagi, A.B.3    Wells, J.W.4
  • 30
    • 0035933747 scopus 로고    scopus 로고
    • 2 receptor dimer formation: Evidence from ligand binding
    • 2 receptor dimer formation: evidence from ligand binding, J. Biol. Chem. 276, 22621-22629.
    • (2001) J. Biol. Chem , vol.276 , pp. 22621-22629
    • Armstrong, D.1    Strange, P.G.2
  • 32
    • 6944237210 scopus 로고    scopus 로고
    • The ants go marching two by two: Oligomeric structure of G protein-coupled receptors
    • Javitch, J. A. (2004) The ants go marching two by two: oligomeric structure of G protein-coupled receptors, Mol. Pharmacol. 66, 1077-1082.
    • (2004) Mol. Pharmacol , vol.66 , pp. 1077-1082
    • Javitch, J.A.1
  • 35
    • 0041935939 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Bethesda, MD, USA
    • Rasband, W. S. ImageJ, U.S. National Institutes of Health, Bethesda, MD, USA, http://rsb.info.nih.gov/ij, 1997-2006.
    • (1997) ImageJ
    • Rasband, W.S.1
  • 38
    • 0021268730 scopus 로고
    • Mammalian β-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains
    • Stiles, G. L., Benovic, J. L., Caron, M. G., and Lefkowitz, R. J. (1984) Mammalian β-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains, J. Biol. Chem. 259, 8655-8663.
    • (1984) J. Biol. Chem , vol.259 , pp. 8655-8663
    • Stiles, G.L.1    Benovic, J.L.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 39
    • 0035480002 scopus 로고    scopus 로고
    • Apparent capacity of cardiac muscarinic receptors for different radiolabeled antagonists
    • Sum, C. S., Pyo, N., and Wells, J. W. (2001) Apparent capacity of cardiac muscarinic receptors for different radiolabeled antagonists, Biochem. Pharmacol. 62, 829-851.
    • (2001) Biochem. Pharmacol , vol.62 , pp. 829-851
    • Sum, C.S.1    Pyo, N.2    Wells, J.W.3
  • 40
    • 0037183981 scopus 로고    scopus 로고
    • Effects of N-ethylmaleimide on conformational equilibria in purified cardiac muscarinic receptors
    • Sum, C. S., Park, P. S., and Wells, J. W. (2002) Effects of N-ethylmaleimide on conformational equilibria in purified cardiac muscarinic receptors, J. Biol. Chem. 277, 36188-36203.
    • (2002) J. Biol. Chem , vol.277 , pp. 36188-36203
    • Sum, C.S.1    Park, P.S.2    Wells, J.W.3
  • 41
    • 3343026033 scopus 로고    scopus 로고
    • 2 muscarinic cholinergic receptor
    • 2 muscarinic cholinergic receptor, J. Neurochem. 90, 537-548.
    • (2004) J. Neurochem , vol.90 , pp. 537-548
    • Park, P.S.1    Wells, J.W.2
  • 42
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells
    • Parker, E. M., Kameyama, K., Higashijima, T., and Ross, E. M. (1991) Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells, J. Biol. Chem. 266, 519-527.
    • (1991) J. Biol. Chem , vol.266 , pp. 519-527
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 44
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer, B. H., Segura, J. M., Martinez, K. L., Hovius, R., George, N., Johnsson, K., and Vogel, H. (2006) FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells, Proc. Natl. Acad. Sci. U.S.A. 103, 2138-2143.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.M.2    Martinez, K.L.3    Hovius, R.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 45
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor as a functional unit
    • Chabre, M., and le Maire, M. (2005) Monomeric G protein-coupled receptor as a functional unit, Biochemistry 44, 9395-9403.
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    le Maire, M.2
  • 47
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • Botelho, A. V., Huber, T., Sakmar, T. P., and Brown, M. F. (2006) Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes, Biophys. J. 91, 4464-4477.
    • (2006) Biophys. J , vol.91 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 48
    • 0037144581 scopus 로고    scopus 로고
    • Constitutive agonist-independent CCR5 oligomerization and antibody-mediated clustering occurring at physiological levels of receptors
    • Issafras, H., Angers, S., Bulenger, S., Blanpain, C., Parmentier, M., Labbe-Jullie, C., Bouvier, M., and Marullo, S. (2002) Constitutive agonist-independent CCR5 oligomerization and antibody-mediated clustering occurring at physiological levels of receptors, J. Biol. Chem. 277, 34666-34673.
    • (2002) J. Biol. Chem , vol.277 , pp. 34666-34673
    • Issafras, H.1    Angers, S.2    Bulenger, S.3    Blanpain, C.4    Parmentier, M.5    Labbe-Jullie, C.6    Bouvier, M.7    Marullo, S.8
  • 50
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor
    • Overton, M. C., Chinault, S. L., and Blumer, K. J. (2003) Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor, J. Biol. Chem. 278, 49369-49377.
    • (2003) J. Biol. Chem , vol.278 , pp. 49369-49377
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 51
    • 0041315583 scopus 로고    scopus 로고
    • C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast
    • Floyd, D. H., Geva, A., Bruinsma, S. P., Overton, M. C., Blumer, K. J., and Baranski, T. J. (2003) C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast, J. Biol. Chem. 278, 35354-35361.
    • (2003) J. Biol. Chem , vol.278 , pp. 35354-35361
    • Floyd, D.H.1    Geva, A.2    Bruinsma, S.P.3    Overton, M.C.4    Blumer, K.J.5    Baranski, T.J.6
  • 54
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • Zhu, X., and Wess, J. (1998) Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function, Biochemistry 37, 15773-15784.
    • (1998) Biochemistry , vol.37 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2
  • 56
    • 0034704906 scopus 로고    scopus 로고
    • G protein-coupled receptors function as oligomers in vivo
    • Overton, M. C., and Blumer, K. J. (2000) G protein-coupled receptors function as oligomers in vivo, Curr. Biol. 10, 341-344.
    • (2000) Curr. Biol , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 58
    • 0023657239 scopus 로고
    • Reconstitution of the purified porcine atrial muscarinic acetylcholine receptor with purified porcine atrial inhibitory guanine nucleotide binding protein
    • Tota, M. R., Kahler, K. R., and Schimerlik, M. I. (1987) Reconstitution of the purified porcine atrial muscarinic acetylcholine receptor with purified porcine atrial inhibitory guanine nucleotide binding protein, Biochemistry 26, 8175-8182.
    • (1987) Biochemistry , vol.26 , pp. 8175-8182
    • Tota, M.R.1    Kahler, K.R.2    Schimerlik, M.I.3
  • 63
    • 0027583723 scopus 로고
    • 3H]histamine in guinea pig cerebral cortex. II. Mechanistic basis for multiple states of affinity
    • 3H]histamine in guinea pig cerebral cortex. II. Mechanistic basis for multiple states of affinity, Mol. Pharmacol. 43, 583-594.
    • (1993) Mol. Pharmacol , vol.43 , pp. 583-594
    • Sinkins, W.G.1    Wells, J.W.2
  • 64
    • 0023424967 scopus 로고
    • The effects of agonists on the components of the cardiac muscarinic receptor
    • Burgen, A. S. (1987) The effects of agonists on the components of the cardiac muscarinic receptor, Br. J. Pharmacol. 92, 327-332.
    • (1987) Br. J. Pharmacol , vol.92 , pp. 327-332
    • Burgen, A.S.1
  • 65
    • 0020027848 scopus 로고
    • Rat cardiac muscarinic receptors. I. Effects of guanine nucleotides on high- and low-affinity binding sites
    • Waelbroeck, M., Robberecht, P., Chatelain, P., and Christophe, J. (1982) Rat cardiac muscarinic receptors. I. Effects of guanine nucleotides on high- and low-affinity binding sites, Mol. Pharmacol. 21, 581-588.
    • (1982) Mol. Pharmacol , vol.21 , pp. 581-588
    • Waelbroeck, M.1    Robberecht, P.2    Chatelain, P.3    Christophe, J.4
  • 66
    • 0021166286 scopus 로고
    • Solubilization and characterization of guanine nucleotide-sensitive muscarinic agonist binding sites from rat myocardium
    • Berrie, C. P., Birdsall, N. J., Hulme, E. C., Keen, M., and Stockton, J. M. (1984) Solubilization and characterization of guanine nucleotide-sensitive muscarinic agonist binding sites from rat myocardium, Br. J. Pharmacol. 82, 853-861.
    • (1984) Br. J. Pharmacol , vol.82 , pp. 853-861
    • Berrie, C.P.1    Birdsall, N.J.2    Hulme, E.C.3    Keen, M.4    Stockton, J.M.5
  • 67
    • 0021998712 scopus 로고
    • 3H]acetylcholine to muscarinic receptors. Regional distribution and modulation by guanine nucleotides
    • 3H]acetylcholine to muscarinic receptors. Regional distribution and modulation by guanine nucleotides, Mol. Pharmacol. 28, 297-305.
    • (1985) Mol. Pharmacol , vol.28 , pp. 297-305
    • Gurwitz, D.1    Kloog, Y.2    Sokolovsky, M.3
  • 69
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ-opioid receptor: Implication for a role in receptor internalization
    • Cvejic, S., and Devi, L. A. (1997) Dimerization of the δ-opioid receptor: implication for a role in receptor internalization, J. Biol. Chem. 272, 26959-26964.
    • (1997) J. Biol. Chem , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 72
    • 0033516576 scopus 로고    scopus 로고
    • 3 muscarinic receptor dimers
    • 3 muscarinic receptor dimers, J. Biol. Chem. 274, 19487-19497.
    • (1999) J. Biol. Chem , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 73
    • 4344571483 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of human somatostatin receptor 2 dimers: A role in receptor trafficking
    • Grant, M., Collier, B., and Kumar, U. (2004) Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking, J. Biol. Chem. 279, 36179-36183.
    • (2004) J. Biol. Chem , vol.279 , pp. 36179-36183
    • Grant, M.1    Collier, B.2    Kumar, U.3
  • 74
    • 4544235707 scopus 로고    scopus 로고
    • The hydrodynamic properties of dark- and light-activated states of n-dodecyl β-D-maltoside- solubilized bovine rhodopsin support the dimeric structure of both conformations
    • Medina, R., Perdomo, D., and Bubis, J. (2004) The hydrodynamic properties of dark- and light-activated states of n-dodecyl β-D-maltoside- solubilized bovine rhodopsin support the dimeric structure of both conformations, J. Biol. Chem. 279, 39565-39573.
    • (2004) J. Biol. Chem , vol.279 , pp. 39565-39573
    • Medina, R.1    Perdomo, D.2    Bubis, J.3
  • 77
    • 0037160105 scopus 로고    scopus 로고
    • 2- adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • 2- adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer, J. Biol. Chem. 277, 44925-44931.
    • (2002) J. Biol. Chem , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 78
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • Raicu, V., Jansma, D. B., Miller, R. J., and Friesen, J. D. (2005) Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer, Biochem. J. 385, 265-277.
    • (2005) Biochem. J , vol.385 , pp. 265-277
    • Raicu, V.1    Jansma, D.B.2    Miller, R.J.3    Friesen, J.D.4
  • 79
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y., Fotiadis, D., Filipek, S., Saperstein, D. A., Palczewski, K., and Engel, A. (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes, J. Biol. Chem. 278, 21655-21662.
    • (2003) J. Biol. Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 82
    • 0025143740 scopus 로고
    • 1-adenosine receptors with guanine nucleotide-binding proteins of human platelet membranes following reconstitution
    • 1-adenosine receptors with guanine nucleotide-binding proteins of human platelet membranes following reconstitution, Mol. Pharmacol. 38, 170-176.
    • (1990) Mol. Pharmacol , vol.38 , pp. 170-176
    • Munshi, R.1    Linden, J.2
  • 83
    • 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
    • Baneres, 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
    • Baneres, J.L.1    Parello, J.2
  • 85
    • 28844437680 scopus 로고    scopus 로고
    • 2C receptor function through heterodimerization: Receptor dimers bind two molecules of ligand and one G protein
    • 2C receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G protein, J. Biol. Chem. 280, 40144-40151.
    • (2005) J. Biol. Chem , vol.280 , pp. 40144-40151
    • Herrick-Davis, K.1    Grinde, E.2    Harrigan, T.J.3    Mazurkiewicz, J.E.4
  • 86
    • 22944468181 scopus 로고    scopus 로고
    • Plasmon resonance methods in GPCR signaling and other membrane events
    • Alves, I. D., Park, C. K., and Hruby, V. J. (2005) Plasmon resonance methods in GPCR signaling and other membrane events, Curr. Protein Pept. Sci. 6, 293-312.
    • (2005) Curr. Protein Pept. Sci , vol.6 , pp. 293-312
    • Alves, I.D.1    Park, C.K.2    Hruby, V.J.3
  • 88
    • 0022536212 scopus 로고
    • Physical properties of the purified cardiac muscarinic acetylcholine receptor
    • Peterson, G. L., Rosenbaum, L. C., Broderick, D. J., and Schimerlik, M. I. (1986) Physical properties of the purified cardiac muscarinic acetylcholine receptor, Biochemistry 25, 3189-3202.
    • (1986) Biochemistry , vol.25 , pp. 3189-3202
    • Peterson, G.L.1    Rosenbaum, L.C.2    Broderick, D.J.3    Schimerlik, M.I.4
  • 89
    • 0023893103 scopus 로고
    • 2 adrenergic receptors: Evidence for a precoupled receptor-guanine nucleotide protein complex
    • 2 adrenergic receptors: evidence for a precoupled receptor-guanine nucleotide protein complex, Biochemistry 27, 2374-2384.
    • (1988) Biochemistry , vol.27 , pp. 2374-2384
    • Neubig, R.R.1    Gantzos, R.D.2    Thomsen, W.J.3
  • 92
    • 0000329823 scopus 로고
    • Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments
    • Kwok-Keung, F. B., and Stryer, L. (1980) Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments, Proc. Natl. Acad. Sci. U.S.A. 77, 2500-2504.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 2500-2504
    • Kwok-Keung, F.B.1    Stryer, L.2
  • 93
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik, V., and Berg, H. C. (2004) Functional interactions between receptors in bacterial chemotaxis, Nature 428, 437-441.
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.