메뉴 건너뛰기




Volumn 89, Issue 6, 2013, Pages 226-256

Molecular properties of muscarinic acetylcholine receptors

Author keywords

Acetylcholine; Crystal structure; G protein; G protein coupled receptor (GPCR); G protein coupled receptor kinase 2 (GRK2); Muscarinic receptor

Indexed keywords


EID: 84880925637     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.89.226     Document Type: Review
Times cited : (96)

References (148)
  • 1
    • 0001536516 scopus 로고
    • The action of certain esters and ethers of choline, and their relation to muscarine
    • Dale, H.H. (1914) The action of certain esters and ethers of choline, and their relation to muscarine. J. Pharmacol. Exp. Ther. 6, 147-190.
    • (1914) J. Pharmacol. Exp. Ther. , vol.6 , pp. 147-190
    • Dale, H.H.1
  • 2
    • 84964166431 scopus 로고
    • Pharmacology and nerve-endings
    • Dale, H. (1935) Pharmacology and nerve-endings. Proc. R. Soc. Med. 28, 319-332.
    • (1935) Proc. R. Soc. Med. , vol.28 , pp. 319-332
    • Dale, H.1
  • 5
    • 0017129454 scopus 로고
    • Biochemical studies on muscarinic acetylcholine receptors
    • Birdsall, N.J.M. and Hulme, E.C. (1976) Biochemical studies on muscarinic acetylcholine receptors. J. Neurochem. 27, 7-16.
    • (1976) J. Neurochem. , vol.27 , pp. 7-16
    • Birdsall, N.J.M.1    Hulme, E.C.2
  • 6
    • 40949095655 scopus 로고    scopus 로고
    • Guide to Receptors and Channels (GRAC), 3rd ed
    • Alexander, S.P.H., Mathie, A. and Peters, J.A. (2008) Guide to Receptors and Channels (GRAC), 3rd ed. Br. J. Pharmacol. 153 (Suppl. 2), S9-S10.
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.SUPPL.2
    • Alexander, S.P.H.1    Mathie, A.2    Peters, J.A.3
  • 7
    • 0015973544 scopus 로고
    • Muscarinic cholinergic receptor binding: regional distribution in monkey brain
    • Yamamura, H.I., Kuhar, M.J., Greenberg, D. and Snyder, S.H. (1974) Muscarinic cholinergic receptor binding: regional distribution in monkey brain. Brain Res. 66, 541-546.
    • (1974) Brain Res. , vol.66 , pp. 541-546
    • Yamamura, H.I.1    Kuhar, M.J.2    Greenberg, D.3    Snyder, S.H.4
  • 8
    • 0015936071 scopus 로고
    • Choline uptake systems of rat brain synaptosomes
    • Haga, T. and Noda, H. (1973) Choline uptake systems of rat brain synaptosomes. Biochim. Biophys. Acta 291, 564-575.
    • (1973) Biochim. Biophys. Acta , vol.291 , pp. 564-575
    • Haga, T.1    Noda, H.2
  • 9
    • 0015578427 scopus 로고
    • Choline: selective accumulation by central cholinergic neurons
    • Kuhar, M.J., Sethy, V.H., Roth, R.H. and Aghajanian, G.K. (1973) Choline: selective accumulation by central cholinergic neurons. J. Neurochem. 20, 581-593.
    • (1973) J. Neurochem. , vol.20 , pp. 581-593
    • Kuhar, M.J.1    Sethy, V.H.2    Roth, R.H.3    Aghajanian, G.K.4
  • 10
    • 0018835992 scopus 로고
    • Pirenzepine distinguishes between different subclasses of muscarinic receptors
    • Hammer, R., Berrie, C.P., Birdsall, N.J.M., Burgen, A.S.V. and Hulme, E.C. (1980) Pirenzepine distinguishes between different subclasses of muscarinic receptors. Nature 283, 90-92.
    • (1980) Nature , vol.283 , pp. 90-92
    • Hammer, R.1    Berrie, C.P.2    Birdsall, N.J.M.3    Burgen, A.S.V.4    Hulme, E.C.5
  • 12
    • 0018134270 scopus 로고
    • The binding of agonists to brain muscarinic receptors
    • Birdsall, N.J.M., Burgen, A.S.V. and Hulme, E.C. (1979) The binding of agonists to brain muscarinic receptors. Mol. Pharmacol. 14, 723-736.
    • (1979) Mol. Pharmacol. , vol.14 , pp. 723-736
    • Birdsall, N.J.M.1    Burgen, A.S.V.2    Hulme, E.C.3
  • 13
    • 0015954039 scopus 로고
    • Stereospecific binding as a tool in attempts to localize and isolate muscarinic receptors. Part II. Binding of (D)-benzetimide, (!)-benzetimide and atropine to a fraction from bovine tracheal smooth muscle and to bovine caudate nucleus
    • Beld, A.J. and Ariëns, E.J. (1974) Stereospecific binding as a tool in attempts to localize and isolate muscarinic receptors. Part II. Binding of (D)-benzetimide, (!)-benzetimide and atropine to a fraction from bovine tracheal smooth muscle and to bovine caudate nucleus. Eur. J. Pharmacol. 25, 203-209.
    • (1974) Eur. J. Pharmacol. , vol.25 , pp. 203-209
    • Beld, A.J.1    Ariëns, E.J.2
  • 14
    • 0017153387 scopus 로고
    • Solubilization and characterization of the beta-adrenergic receptor binding sites of frog erythrocytes
    • Caron, M.G. and Lefkowitz, R.J. (1976) Solubilization and characterization of the beta-adrenergic receptor binding sites of frog erythrocytes. J. Biol. Chem. 251, 2374-2384.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2374-2384
    • Caron, M.G.1    Lefkowitz, R.J.2
  • 15
    • 0021227134 scopus 로고
    • Hydrodynamic properties of muscarinic acetylcholine receptors solubilized from rat forebrain
    • Berrie, C.P., Birdsall, N.J.M., Haga, K., Haga, T. and Hulme, E.C. (1984) Hydrodynamic properties of muscarinic acetylcholine receptors solubilized from rat forebrain. Br. J. Pharmacol. 82, 839-851.
    • (1984) Br. J. Pharmacol. , vol.82 , pp. 839-851
    • Berrie, C.P.1    Birdsall, N.J.M.2    Haga, K.3    Haga, T.4    Hulme, E.C.5
  • 16
    • 0018898812 scopus 로고
    • Molecular size of muscarinic acetylcholine receptors of rat brain
    • Haga, T. (1980) Molecular size of muscarinic acetylcholine receptors of rat brain. FEBS Lett. 113, 68-72.
    • (1980) FEBS Lett. , vol.113 , pp. 68-72
    • Haga, T.1
  • 17
    • 0018399578 scopus 로고
    • A study of the muscarinic receptor by gel electrophoresis
    • Birdsall, N.J.M., Burgen, A.S.V. and Hulme, E.C. (1979) A study of the muscarinic receptor by gel electrophoresis. Br. J. Pharmacol. 66, 337-342.
    • (1979) Br. J. Pharmacol. , vol.66 , pp. 337-342
    • Birdsall, N.J.M.1    Burgen, A.S.V.2    Hulme, E.C.3
  • 18
    • 84880950012 scopus 로고
    • Affinity chromatography of muscarinic acetylcholine receptors
    • (in Japanese)
    • Haga, K. and Haga, T. (1984) Affinity chromatography of muscarinic acetylcholine receptors. Seitai no Kagaku 35, 296-303 (in Japanese).
    • (1984) Seitai no Kagaku , vol.35 , pp. 296-303
    • Haga, K.1    Haga, T.2
  • 19
    • 0021059388 scopus 로고
    • Affinity chromatography of the muscarinic acetylcholine receptor
    • Haga, K. and Haga, T. (1983) Affinity chromatography of the muscarinic acetylcholine receptor. J. Biol. Chem. 258, 13575-13579.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13575-13579
    • Haga, K.1    Haga, T.2
  • 20
    • 0022391964 scopus 로고
    • Purification of the muscarinic acetylcholine receptor from porcine brain
    • Haga, K. and Haga, T. (1985) Purification of the muscarinic acetylcholine receptor from porcine brain. J. Biol. Chem. 260, 7927-7935.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7927-7935
    • Haga, K.1    Haga, T.2
  • 22
    • 0022976055 scopus 로고
    • The binding of pirenzepine to digitonin-solubilized muscarinic acetylcholine receptors from the rat myocardium
    • Birdsall, N.J.M., Hulme, E.C. and Keen, M. (1986) The binding of pirenzepine to digitonin-solubilized muscarinic acetylcholine receptors from the rat myocardium. Br. J. Pharm. 87, 307-316.
    • (1986) Br. J. Pharm. , vol.87 , pp. 307-316
    • Birdsall, N.J.M.1    Hulme, E.C.2    Keen, M.3
  • 23
    • 0024437837 scopus 로고
    • Comparison between purified cerebral and atrial muscarinic acetylcholine receptors: Pirenzepine binding and the effect of sulfhydryl reagents
    • Nishiyama, T., Berstein, G., Ikegaya, T., Haga, T., Ichiyama, A., Kobayashi, A. and Yamazaki, N. (1989) Comparison between purified cerebral and atrial muscarinic acetylcholine receptors: Pirenzepine binding and the effect of sulfhydryl reagents. Biomed. Res. 10, 251-260.
    • (1989) Biomed. Res. , vol.10 , pp. 251-260
    • Nishiyama, T.1    Berstein, G.2    Ikegaya, T.3    Haga, T.4    Ichiyama, A.5    Kobayashi, A.6    Yamazaki, N.7
  • 24
    • 0024470838 scopus 로고
    • Effect of the lipid environment on the differential affinity of purified cerebral and atrial muscarinic acetylcholine receptors for pirenzepine
    • Berstein, G., Haga, T. and Ichiyama, A. (1989) Effect of the lipid environment on the differential affinity of purified cerebral and atrial muscarinic acetylcholine receptors for pirenzepine. Mol. Pharmacol. 36, 601-607.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 601-607
    • Berstein, G.1    Haga, T.2    Ichiyama, A.3
  • 25
    • 0023944172 scopus 로고
    • Agonist and antagonist binding of muscarinic acetylcholine receptors purified from porcine brain: interconversion of high- and low-affinity sites by sulfhydryl reagents
    • Berstein, G., Haga, K., Haga, T. and Ichiyama, A. (1988) Agonist and antagonist binding of muscarinic acetylcholine receptors purified from porcine brain: interconversion of high- and low-affinity sites by sulfhydryl reagents. J. Neurochem. 50, 1687-1694.
    • (1988) J. Neurochem. , vol.50 , pp. 1687-1694
    • Berstein, G.1    Haga, K.2    Haga, T.3    Ichiyama, A.4
  • 29
    • 0023525878 scopus 로고
    • [3H]Propylbenzilylcholine mustard-labeling of muscarinic cholinergic receptors that selectively couple to phospholipase C or adenylate cyclase in two cultured cell lines
    • Liang, M., Martin, M.W. and Harden, T.K. (1987) [3H]Propylbenzilylcholine mustard-labeling of muscarinic cholinergic receptors that selectively couple to phospholipase C or adenylate cyclase in two cultured cell lines. Mol. Pharmacol. 32, 443- 449.
    • (1987) Mol. Pharmacol. , vol.32
    • Liang, M.1    Martin, M.W.2    Harden, T.K.3
  • 30
    • 0025203815 scopus 로고
    • Interaction of deglycosylated muscarinic receptors with ligands and G proteins
    • Ohara, K., Uchiyama, H., Ohara, K., Haga, T. and Ichiyama, A. (1990) Interaction of deglycosylated muscarinic receptors with ligands and G proteins. Eur. J. Pharmacol. 189, 341-346.
    • (1990) Eur. J. Pharmacol. , vol.189 , pp. 341-346
    • Ohara, K.1    Uchiyama, H.2    Ohara, K.3    Haga, T.4    Ichiyama, A.5
  • 31
    • 0025295846 scopus 로고
    • Location in muscarinic acetylcholine receptors of sites for propylbenzilylcholine mustard binding and for phosphorylation with protein kinase C
    • Uchiyama, H., Ohara, K., Haga, K., Haga, T. and Ichiyama, A. (1990) Location in muscarinic acetylcholine receptors of sites for propylbenzilylcholine mustard binding and for phosphorylation with protein kinase C. J. Neurochem. 54, 1870- 1881.
    • (1990) J. Neurochem. , vol.54
    • Uchiyama, H.1    Ohara, K.2    Haga, K.3    Haga, T.4    Ichiyama, A.5
  • 32
    • 85015270300 scopus 로고
    • Muscarinic acetylcholine receptors: peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation
    • Kurtenbach, E., Curtis, C.A.M., Pedder, E.K., Aitken, A., Harris, A.C.M. and Hulme, E.C. (1990) Muscarinic acetylcholine receptors: peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation. J. Biol. Chem. 264, 489-495.
    • (1990) J. Biol. Chem. , vol.264 , pp. 489-495
    • Kurtenbach, E.1    Curtis, C.A.M.2    Pedder, E.K.3    Aitken, A.4    Harris, A.C.M.5    Hulme, E.C.6
  • 33
    • 0023661365 scopus 로고
    • Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors
    • Peralta, E.G., Ashkenazi, A., Winslow, J.W., Smith, D.H., Ramachandran, J. and Capon, D.J. (1987) Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors. EMBO J. 6, 3923-3929.
    • (1987) EMBO J. , vol.6 , pp. 3923-3929
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Smith, D.H.4    Ramachandran, J.5    Capon, D.J.6
  • 34
    • 0024560588 scopus 로고
    • The molecular basis of muscarinic receptor diversity
    • Bonner, T.I. (1989) The molecular basis of muscarinic receptor diversity. Trends Neurosci. 12, 148- 151.
    • (1989) Trends Neurosci. , vol.12
    • Bonner, T.I.1
  • 36
    • 0025231511 scopus 로고
    • Carbachol-induced potentiation and inhibition of acid secretion by guinea pig gastric gland
    • Kajimura, M., Haga, T., Ichiyama, A., Kaneko, E. and Honda, N. (1990) Carbachol-induced potentiation and inhibition of acid secretion by guinea pig gastric gland. Eur. J. Pharmacol. 178, 59-69.
    • (1990) Eur. J. Pharmacol. , vol.178 , pp. 59-69
    • Kajimura, M.1    Haga, T.2    Ichiyama, A.3    Kaneko, E.4    Honda, N.5
  • 37
    • 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, Y.A.1
  • 39
    • 0037024360 scopus 로고    scopus 로고
    • Identification of G proteincoupled receptor genes from the human genome sequence
    • Takeda, S., Kadowaki, S., Haga, T., Takaesu, H. and Mitaku, S. (2002) Identification of G proteincoupled receptor genes from the human genome sequence. FEBS Lett. 520, 97-101.
    • (2002) FEBS Lett. , vol.520 , pp. 97-101
    • Takeda, S.1    Kadowaki, S.2    Haga, T.3    Takaesu, H.4    Mitaku, S.5
  • 40
    • 80052359992 scopus 로고    scopus 로고
    • Emerging paradigms of O-arrestin-dependent seven transmembrane receptor signaling
    • Shukla, A.K., Xiao, K. and Lefkowitz, R.J. (2011) Emerging paradigms of O-arrestin-dependent seven transmembrane receptor signaling. Trends Biochem. Sci. 36, 457-469.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 457-469
    • Shukla, A.K.1    Xiao, K.2    Lefkowitz, R.J.3
  • 41
    • 0000413412 scopus 로고
    • Formation of a cyclic adenosine ribonucleotide by tissue particles
    • Rall, T.W. and Sutherland, E.W. (1958) Formation of a cyclic adenosine 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
  • 43
    • 0017280145 scopus 로고
    • An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor
    • Maguire, M.E., Van Arsdale, P.M. and Gilman, A.G. (1976) An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor. Mol. Pharmacol. 12, 335-339.
    • (1976) Mol. Pharmacol. , vol.12 , pp. 335-339
    • Maguire, M.E.1    Van Arsdale, P.M.2    Gilman, A.G.3
  • 45
    • 0017655195 scopus 로고
    • Hydrodynamic properties of the beta-adrenergic receptor and adenylate cyclase from wild type and varient S49 lymphoma cells
    • Haga, T., Haga, K. and Gilman, A.G. (1977) Hydrodynamic properties of the beta-adrenergic receptor and adenylate cyclase from wild type and varient S49 lymphoma cells. J. Biol. Chem. 252, 5776-5782.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5776-5782
    • Haga, T.1    Haga, K.2    Gilman, A.G.3
  • 46
    • 0017742954 scopus 로고
    • GTP-binding proteins in membranes and the control of adenylate cyclase activity
    • Pfeuffer, T. (1977) GTP-binding proteins in membranes and the control of adenylate cyclase activity. J. Biol. Chem. 252, 7224-7234.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7224-7234
    • Pfeuffer, T.1
  • 47
    • 0008614480 scopus 로고
    • Mechanism of adenylate cyclase activation by cholera toxin: Inhibition of GTP hydrolysis at the regulatory site
    • Cassel, D. and Selinger, Z. (1977) Mechanism of adenylate cyclase activation by cholera toxin: Inhibition of GTP hydrolysis at the regulatory site. Proc. Natl. Acad. Sci. U.S.A. 74, 3307-3311.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3307-3311
    • Cassel, D.1    Selinger, Z.2
  • 48
    • 0347349553 scopus 로고
    • Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system
    • Cassel, D. and Pfeuffer, T. (1978) Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. Proc. Natl. Acad. Sci. U.S.A. 75, 2669-2773.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 2669-2773
    • Cassel, D.1    Pfeuffer, T.2
  • 49
    • 0016669563 scopus 로고
    • Selection of a variant lymphoma cell deficient in adenylate cyclase
    • Bourne, H.R., Coffino, P. and Tomkins, G.M. (1975) Selection of a variant lymphoma cell deficient in adenylate cyclase. Science 187, 750-752.
    • (1975) Science , vol.187 , pp. 750-752
    • Bourne, H.R.1    Coffino, P.2    Tomkins, G.M.3
  • 50
    • 0008534153 scopus 로고
    • Adenylate cyclase permanently uncoupled from hormone receptors in a novel variant of S49 mouse lymphoma cells
    • Haga, T., Ross, E.M., Anderson, H.J. and Gilman, A.G. (1977) Adenylate cyclase permanently uncoupled from hormone receptors in a novel variant of S49 mouse lymphoma cells. Proc. Natl. Acad. Sci. U.S.A. 74, 2016-2020.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2016-2020
    • Haga, T.1    Ross, E.M.2    Anderson, H.J.3    Gilman, A.G.4
  • 51
    • 0017716885 scopus 로고
    • Reconstitution of catecholamine-sensitive adenylate cyclase activity: Interactions of solubilized components with receptor-replete membranes
    • Ross, E.M. and Gilman, A.G. (1977) Reconstitution of catecholamine-sensitive adenylate cyclase activity: Interactions of solubilized components with receptor-replete membranes. Proc. Natl. Acad. Sci. U.S.A. 74, 3715-3719.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3715-3719
    • Ross, E.M.1    Gilman, A.G.2
  • 52
    • 0018816350 scopus 로고
    • Biochemical properties of hormone sensitive adenylate cyclase
    • Ross, E.M. and Gilman, A.G. (1980) Biochemical properties of hormone sensitive adenylate cyclase. Annu. Rev. Biochem. 49, 533-546.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 533-546
    • Ross, E.M.1    Gilman, A.G.2
  • 53
    • 0017699791 scopus 로고
    • Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography
    • Vauquelin, G., Geynert, P., Hanoune, J. and Strosberg, A.D. (1977) Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography. Proc. Natl. Acad. Sci. U.S.A. 74, 3710-3714.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3710-3714
    • Vauquelin, G.1    Geynert, P.2    Hanoune, J.3    Strosberg, A.D.4
  • 54
    • 0344126323 scopus 로고
    • Functional reconstitution of beta-adrenergic receptors and the stimulatory GTP-binding protein of adenylate cyclase
    • Pederson, S.E. and Ross, E.M. (1982) Functional reconstitution of beta-adrenergic receptors and the stimulatory GTP-binding protein of adenylate cyclase. Proc. Natl. Acad. Sci. U.S.A. 79, 7228- 7232.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79
    • Pederson, S.E.1    Ross, E.M.2
  • 55
    • 0001465564 scopus 로고
    • Adenyl cyclase III. The effect of catecholamines and choline esters on the formation of adenosine 3B,5B-phosphate by preparations from cardiac muscle and liver
    • Murad, F., Chi, Y.-M., Rall, T.W. and Sutherland, E.W. (1962) Adenyl cyclase III. The effect of catecholamines and choline esters on the formation of adenosine 3B,5B-phosphate by preparations from cardiac muscle and liver. J. Biol. Chem. 237, 1233-1238.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1233-1238
    • Murad, F.1    Chi, Y.-M.2    Rall, T.W.3    Sutherland, E.W.4
  • 56
    • 0017662914 scopus 로고
    • GTP stimulates and inhibits adenylate cyclase in fat cell membrnes through distinct regulatory processes
    • Yamamura, H., Lad, P.M. and Rodbell, M. (1977) GTP stimulates and inhibits adenylate cyclase in fat cell membrnes through distinct regulatory processes. J. Biol. Chem. 252, 7964-7966.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7964-7966
    • Yamamura, H.1    Lad, P.M.2    Rodbell, M.3
  • 57
    • 0018851861 scopus 로고
    • The role of hormone receptors and GTP-regulatory proteins in membrane transduction
    • Rodbell, M. (1980) The role of hormone receptors and GTP-regulatory proteins in membrane transduction. Nature 284, 17-22.
    • (1980) Nature , vol.284 , pp. 17-22
    • Rodbell, M.1
  • 58
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by isletactivating protein due to ADP-ribosylation of a membrane protein
    • Katada, T. and Ui, M. (1982) Direct modification of the membrane adenylate cyclase system by isletactivating protein due to ADP-ribosylation of a membrane protein. Proc. Natl. Acad. Sci. U.S.A. 79, 3129-3133.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 59
    • 0020541131 scopus 로고
    • Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via alpha-adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells
    • Kurose, H., Katada, T., Amano, T. and Ui, M. (1983) Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via alpha-adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells. J. Biol. Chem. 258, 4870-4875.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4870-4875
    • Kurose, H.1    Katada, T.2    Amano, T.3    Ui, M.4
  • 60
    • 0021111692 scopus 로고
    • Identification of the predominant substrate for ADP-ribosylation by islet activating protein
    • Bokoch, G.M., Katada, T., Northup, J.K., Hewlett, E.L. and Gilman, A.G. (1983) Identification of the predominant substrate for ADP-ribosylation by islet activating protein. J. Biol. Chem. 258, 2072- 2075.
    • (1983) J. Biol. Chem. , vol.258
    • Bokoch, G.M.1    Katada, T.2    Northup, J.K.3    Hewlett, E.L.4    Gilman, A.G.5
  • 61
    • 0021748090 scopus 로고
    • Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain
    • Sternweis, P.C. and Robishaw, J.D. (1984) Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain. J. Biol. Chem. 259, 13806-13813.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13806-13813
    • Sternweis, P.C.1    Robishaw, J.D.2
  • 63
    • 0026418426 scopus 로고
    • Type-specific regulation of adenylate cyclase by G protein O
    • Tang, W.J. and Gilman, A.G. (1991) Type-specific regulation of adenylate cyclase by G protein O. subunits. Science 254, 1500-1503.
    • (1991) subunits. Science , vol.254 , pp. 1500-1503
    • Tang, W.J.1    Gilman, A.G.2
  • 67
    • 0023155972 scopus 로고
    • Functional expression of cloned cDNA encoding the alpha-subunit of adenylate cyclase-stimulating G-protein
    • Nukada, T., Mishina, M. and Numa, S. (1987) Functional expression of cloned cDNA encoding the alpha-subunit of adenylate cyclase-stimulating G-protein. FEBS Lett. 211, 5-9.
    • (1987) FEBS Lett. , vol.211 , pp. 5-9
    • Nukada, T.1    Mishina, M.2    Numa, S.3
  • 68
    • 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
  • 69
    • 0026785920 scopus 로고
    • Adenylate cyclases
    • Tang, W.J. and Gilman, A.G. (1992) Adenylate cyclases. Cell 70, 869-872.
    • (1992) Cell , vol.70 , pp. 869-872
    • Tang, W.J.1    Gilman, A.G.2
  • 70
    • 0035040818 scopus 로고    scopus 로고
    • Regulation and role of adenylyl cyclase isoforms
    • Hanoune, J. and Defer, N. (2001) Regulation and role of adenylyl cyclase isoforms. Annu. Rev. Pharmacol. Toxicol. 41, 145-174.
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 145-174
    • Hanoune, J.1    Defer, N.2
  • 72
    • 0021041785 scopus 로고
    • Muscarinic receptors in porcine caudate nucleus. II. Different effects of N-ethylmaleimide on cismethyldioxolane binding to heat-labile (guanyl nucleotide-sensitive) sites and heat-stable (guanyl nucleotide-insensitive) sites
    • Nukada, T., Haga, T. and Ichiyama, A. (1983) Muscarinic receptors in porcine caudate nucleus. II. Different effects of N-ethylmaleimide on cismethyldioxolane binding to heat-labile (guanyl nucleotide-sensitive) sites and heat-stable (guanyl nucleotide-insensitive) sites. Mol. Pharmacol. 24, 374-379.
    • (1983) Mol. Pharmacol. , vol.24 , pp. 374-379
    • Nukada, T.1    Haga, T.2    Ichiyama, A.3
  • 73
    • 0022367080 scopus 로고
    • Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein
    • Haga, K., Haga, T., Ichiyama, A., Katada, T., Kurose, H. and Ui, M. (1985) Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein. Nature 316, 731-733.
    • (1985) Nature , vol.316 , pp. 731-733
    • Haga, K.1    Haga, T.2    Ichiyama, A.3    Katada, T.4    Kurose, H.5    Ui, M.6
  • 74
    • 0022838315 scopus 로고
    • Reconstitution of the muscarinic acetylcholine receptor.Guanine nucleotide-sensitive high affinity binding of agonists to purified muscarinic receptors reconstituted with GTP-binding proteins (Gi and Go).
    • Haga, K., Haga, T. and Ichiyama, A. (1986) Reconstitution of the muscarinic acetylcholine receptor. Guanine nucleotide-sensitive high affinity binding of agonists to purified muscarinic receptors reconstituted with GTP-binding proteins (Gi and Go). J. Biol. Chem. 261, 10133- 10140.
    • (1986) J. Biol. Chem. , vol.261
    • Haga, K.1    Haga, T.2    Ichiyama, A.3
  • 75
    • 0024605048 scopus 로고
    • Cerebral muscarinic acetylcholine receptors interact with three kinds of GTP-binding proteins in a reconstitution system of purified components
    • Haga, K., Uchiyama, H., Haga, T., Ichiyama, A., Kangawa, K. and Matsuo, H. (1989) Cerebral muscarinic acetylcholine receptors interact with three kinds of GTP-binding proteins in a reconstitution system of purified components. Mol. Pharmacol. 35, 286-294.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 286-294
    • Haga, K.1    Uchiyama, H.2    Haga, T.3    Ichiyama, A.4    Kangawa, K.5    Matsuo, H.6
  • 76
    • 0023630641 scopus 로고
    • Interaction of the muscarinic acetylcholine receptor and GTPbinding proteins
    • Haga, T. and Haga, K. (1987) Interaction of the muscarinic acetylcholine receptor and GTPbinding proteins. Biomed. Res. 8, 149-156.
    • (1987) Biomed. Res. , vol.8 , pp. 149-156
    • Haga, T.1    Haga, K.2
  • 78
    • 0026466773 scopus 로고
    • Effects of magnesium on the interaction of atrial muscarinic acetylcholine receptors and GTP-binding regulatory proteins
    • Shiozaki, K. and Haga, T. (1992) Effects of magnesium on the interaction of atrial muscarinic acetylcholine receptors and GTP-binding regulatory proteins. Biochemistry 31, 10634-10642.
    • (1992) Biochemistry , vol.31 , pp. 10634-10642
    • Shiozaki, K.1    Haga, T.2
  • 80
    • 0242323014 scopus 로고    scopus 로고
    • Identification of a G protein-coupled receptor for 5-oxo-eicosatetraenoic acid
    • Takeda, S., Yamamoto, A. and Haga, T. (2002) Identification of a G protein-coupled receptor for 5-oxo-eicosatetraenoic acid. Biomed. Res. 23, 101-108.
    • (2002) Biomed. Res. , vol.23 , pp. 101-108
    • Takeda, S.1    Yamamoto, A.2    Haga, T.3
  • 81
    • 34547471030 scopus 로고    scopus 로고
    • Ligand screening system using fusion proteins of G protein-coupled receptors with G protein , subunits
    • Suga, H. and Haga, T. (2007) Ligand screening system using fusion proteins of G protein-coupled receptors with G protein , subunits. Neurochem. Int. 51, 140-164.
    • (2007) Neurochem. Int. , vol.51 , pp. 140-164
    • Suga, H.1    Haga, T.2
  • 82
    • 0005521383 scopus 로고
    • Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices
    • Hokin, L.E. and Hokin, M.R. (1955) Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices. Biochim. Biophys. Acta 18, 102-110.
    • (1955) Biochim. Biophys. Acta , vol.18 , pp. 102-110
    • Hokin, L.E.1    Hokin, M.R.2
  • 83
    • 0021750054 scopus 로고
    • Inositol triphosphate, a novel second messenger in cellular signal transduction
    • Berridge, M.J. and Irvine, R.F. (1984) Inositol triphosphate, a novel second messenger in cellular signal transduction. Nature 312, 315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 84
    • 0025786971 scopus 로고
    • Identification of two novel GTP-binding protein alpha-subunits that lack apparent ADP-ribosylation sites for pertussis toxin
    • Nakamura, F., Ogata, K., Shiozaki, K., Kameyama, K., Ohara, K., Haga, T. and Nukada, T. (1991) Identification of two novel GTP-binding protein alpha-subunits that lack apparent ADP-ribosylation sites for pertussis toxin. J. Biol. Chem. 266, 12676-12681.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12676-12681
    • Nakamura, F.1    Ogata, K.2    Shiozaki, K.3    Kameyama, K.4    Ohara, K.5    Haga, T.6    Nukada, T.7
  • 85
    • 0025695580 scopus 로고
    • G protein diversity: A distinct class of , subunits is present in vertebrates and invertebrates
    • Strathmann, M. and Simon, M.I. (1990) G protein diversity: A distinct class of , subunits is present in vertebrates and invertebrates. Proc. Natl. Acad. Sci. U.S.A. 87, 9113-9117.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9113-9117
    • Strathmann, M.1    Simon, M.I.2
  • 86
    • 0028988310 scopus 로고
    • Characterization of Gq family G proteins GL1alpha (G14alpha), GL2alpha(G11- alpha), and Gqalpha expressed in the baculovirusinsect cell system
    • Nakamura, F., Kato, M., Kameyama, K., Nukada, T., Haga, T., Kato, H., Takenawa, T. and Kikkawa, U. (1995) Characterization of Gq family G proteins GL1alpha (G14alpha), GL2alpha(G11- alpha), and Gqalpha expressed in the baculovirusinsect cell system. J. Biol. Chem. 270, 6246-6253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6246-6253
    • Nakamura, F.1    Kato, M.2    Kameyama, K.3    Nukada, T.4    Haga, T.5    Kato, H.6    Takenawa, T.7    Kikkawa, U.8
  • 88
    • 69249208550 scopus 로고    scopus 로고
    • Regulation of RhoGEF protein by G12/13-coupled receptors
    • Siehler, S. (2009) Regulation of RhoGEF protein by G12/13-coupled receptors. Br. J. Pharmacol. 158, 41-49.
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 41-49
    • Siehler, S.1
  • 89
    • 0025214371 scopus 로고
    • Phosphorylation by protein kinase C of the muscarinic acetylcholine receptor
    • Haga, K., Haga, T. and Ichiyama, A. (1990) Phosphorylation by protein kinase C of the muscarinic acetylcholine receptor. J. Neurochem. 54, 1639-1644.
    • (1990) J. Neurochem. , vol.54 , pp. 1639-1644
    • Haga, K.1    Haga, T.2    Ichiyama, A.3
  • 91
    • 0018145339 scopus 로고
    • Light-dependent binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes
    • Kuhn, H. (1978) Light-dependent binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes. Biochemistry 17, 4389- 4395.
    • (1978) Biochemistry , vol.17
    • Kuhn, H.1
  • 92
    • 0344812247 scopus 로고
    • Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor
    • Benovic, J.L., Strasser, R.H., Caron, M.G. and Lefkowitz, R.J. (1986) Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. Proc. Natl. Acad. Sci. U.S.A. 83, 2797-2801.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2797-2801
    • Benovic, J.L.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 93
    • 0027981478 scopus 로고
    • G protein-coupled receptor kinases
    • Haga, T., Haga, K. and Kameyama, K. (1994) G protein-coupled receptor kinases. J. Neurochem. 63, 400-412.
    • (1994) J. Neurochem. , vol.63 , pp. 400-412
    • Haga, T.1    Haga, K.2    Kameyama, K.3
  • 94
    • 0022971472 scopus 로고
    • Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist
    • Kwatra, M.M. and Hosey, M.M. (1986) Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist. J. Biol. Chem. 261, 12429- 12432.
    • (1986) J. Biol. Chem. , vol.261
    • Kwatra, M.M.1    Hosey, M.M.2
  • 95
    • 0024453632 scopus 로고
    • Agonist-dependent phosphorylation of cerebral and atrial muscarinic receptors: blockade of the phosphorylation by GTP-binding regulatory proteins and its reversal by guanine nucleotides
    • Haga, K. and Haga, T. (1989) Agonist-dependent phosphorylation of cerebral and atrial muscarinic receptors: blockade of the phosphorylation by GTP-binding regulatory proteins and its reversal by guanine nucleotides. Biomed. Res. 10, 293- 299.
    • (1989) Biomed. Res. , vol.10
    • Haga, K.1    Haga, T.2
  • 96
    • 0025315797 scopus 로고
    • Dual regulation by G proteins of agonist-dependent phosphorylation of muscarinic acetylcholine receptors
    • Haga, K. and Haga, T. (1990) Dual regulation by G proteins of agonist-dependent phosphorylation of muscarinic acetylcholine receptors. FEBS Lett. 268, 43-47.
    • (1990) FEBS Lett. , vol.268 , pp. 43-47
    • Haga, K.1    Haga, T.2
  • 97
    • 0026793617 scopus 로고
    • Activation by G protein beta gamma subunits of agonist- or lightdependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin
    • Haga, K. and Haga, T. (1992) Activation by G protein beta gamma subunits of agonist- or lightdependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin. J. Biol. Chem. 267, 2222-2227.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2222-2227
    • Haga, K.1    Haga, T.2
  • 98
    • 0022641020 scopus 로고
    • Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase
    • Benovic, J.L., Mayor, F. Jr., Somers, R.L., Caron, M.G. and Lefkowitz, R.J. (1986) Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase. Nature 321, 869-872.
    • (1986) Nature , vol.321 , pp. 869-872
    • Benovic, J.L.1    Mayor, F.Jr.2    Somers, R.L.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 99
    • 0024372284 scopus 로고
    • Phosphorylation of chick heart muscarinic cholinergic receptors by the O-adrenergic receptor kinase
    • Kwatra, M.M., Benovic, J.L., Caron, M.G., Lefkowitz, R.J. and Hosey, M.M. (1989) Phosphorylation of chick heart muscarinic cholinergic receptors by the O-adrenergic receptor kinase. Biochemistry 28, 4543-4547.
    • (1989) Biochemistry , vol.28 , pp. 4543-4547
    • Kwatra, M.M.1    Benovic, J.L.2    Caron, M.G.3    Lefkowitz, R.J.4    Hosey, M.M.5
  • 100
    • 0027418322 scopus 로고
    • Activation by G protein beta-gamma subunits of beta adrenergic and muscarinic receptor kinase
    • Kameyama, K., Haga, K., Haga, T., Kotani, K., Katada, T. and Fukada, Y. (1993) Activation by G protein beta-gamma subunits of beta adrenergic and muscarinic receptor kinase. J. Biol. Chem. 268, 7753-7758.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7753-7758
    • Kameyama, K.1    Haga, K.2    Haga, T.3    Kotani, K.4    Katada, T.5    Fukada, Y.6
  • 101
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and GO
    • Lodowski, D.T., Pitcher, J.A., Capel, W.D., Lefkowitz, R.J. and Tesmer, J.J.G. (2003) Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and GO.. Science 300, 1256-1262.
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.G.5
  • 103
    • 0028199059 scopus 로고
    • Synergistic activation of a G protein-coupled receptor kinase by G protein beta gamma subunits and mastoparan or related peptides
    • Haga, K., Kameyama, K. and Haga, T. (1994) Synergistic activation of a G protein-coupled receptor kinase by G protein beta gamma subunits and mastoparan or related peptides. J. Biol. Chem. 269, 12594-12599.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12594-12599
    • Haga, K.1    Kameyama, K.2    Haga, T.3
  • 105
    • 0028568644 scopus 로고
    • 2 subtypes: Facilitation by G protein-coupled receptor kinase (GRK2) and attenuation by a dominant-negative mutant of GRK2
    • 2 subtypes: Facilitation by G protein-coupled receptor kinase (GRK2) and attenuation by a dominant-negative mutant of GRK2. J. Biol. Chem. 269, 32522-32527.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32522-32527
    • Tsuga, H.1    Kameyama, K.2    Haga, T.3    Kurose, H.4    Nagao, T.5
  • 107
    • 0031910017 scopus 로고    scopus 로고
    • 5 subtypes: Effect of G protein-coupled receptor kinases GRK2, GRK4, GRK5 and GRK6
    • 5 subtypes: Effect of G protein-coupled receptor kinases GRK2, GRK4, GRK5 and GRK6. J. Pharmacol. Exp. Ther. 284, 1218-1226.
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 1218-1226
    • Tsuga, H.1    Okuno, E.2    Kameyama, K.3    Haga, T.4
  • 110
    • 0030614382 scopus 로고    scopus 로고
    • Ca2Ddependent inhibition of G protein-coupled receptor kinase 2 by calmodulin
    • Haga, K., Tsuga, H. and Haga, T. (1997) Ca2Ddependent inhibition of G protein-coupled receptor kinase 2 by calmodulin. Biochemistry 36, 1315-1321.
    • (1997) Biochemistry , vol.36 , pp. 1315-1321
    • Haga, K.1    Tsuga, H.2    Haga, T.3
  • 111
    • 0032528248 scopus 로고    scopus 로고
    • GTP-binding-protein-coupled receptor kinase 2 (GRK2) binds and phosphorylates tubulin
    • Haga, K., Ogawa, H., Haga, T. and Murofushi, H. (1998) GTP-binding-protein-coupled receptor kinase 2 (GRK2) binds and phosphorylates tubulin. Eur. J. Biochem. 255, 363-368.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 363-368
    • Haga, K.1    Ogawa, H.2    Haga, T.3    Murofushi, H.4
  • 112
    • 0037349646 scopus 로고    scopus 로고
    • Identification of sites of phosphorylation by Gprotein- coupled receptor kinase 2 in O-tubulin
    • Yoshida, N., Haga, K. and Haga, T. (2003) Identification of sites of phosphorylation by Gprotein- coupled receptor kinase 2 in O-tubulin. Eur. J. Biochem. 270, 1154-1163.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1154-1163
    • Yoshida, N.1    Haga, K.2    Haga, T.3
  • 113
    • 0015984844 scopus 로고
    • Polymerization and depolymerization of microtubules in vitro as studied by flow birefringence
    • Haga, T., Abe, T. and Kurokawa, M. (1974) Polymerization and depolymerization of microtubules in vitro as studied by flow birefringence. FEBS Lett. 39, 291-295.
    • (1974) FEBS Lett. , vol.39 , pp. 291-295
    • Haga, T.1    Abe, T.2    Kurokawa, M.3
  • 115
    • 0031569809 scopus 로고    scopus 로고
    • 2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail
    • 2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail. Arch. Biochem. Biophys. 340, 376-382.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 376-382
    • Hayashi, M.K.1    Haga, T.2
  • 116
    • 0029866609 scopus 로고    scopus 로고
    • 4 muscarinic acetylcholine receptor gene contains a cell typespecific silencer element
    • 4 muscarinic acetylcholine receptor gene contains a cell typespecific silencer element. J. Biol. Chem. 271, 5177-5182.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5177-5182
    • Mieda, M.1    Haga, T.2    Saffen, D.W.3
  • 117
    • 0031055065 scopus 로고    scopus 로고
    • 4 muscarinic acetylcholine receptor gene is regulated by the neuron-restrictive silencer element/repressor element 1
    • 4 muscarinic acetylcholine receptor gene is regulated by the neuron-restrictive silencer element/repressor element 1. J. Biol. Chem. 272, 5854-5860.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5854-5860
    • Mieda, M.1    Haga, T.2    Saffen, D.W.3
  • 119
    • 0019305679 scopus 로고
    • Solubilization of muscarinic acetylcholine receptors by L-,-lysophosphatidylcholine
    • Haga, T. (1980) Solubilization of muscarinic acetylcholine receptors by L-,-lysophosphatidylcholine. Biomed. Res. 1, 265-268.
    • (1980) Biomed. Res. , vol.1 , pp. 265-268
    • Haga, T.1
  • 120
    • 0023769532 scopus 로고
    • Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl O-D-maltoside
    • Peterson, G.L., Rosenbaum, L.C. and Schimerlik, M.I. (1988) Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl O-D-maltoside. Biochem. J. 255, 553-560.
    • (1988) Biochem. J. , vol.255 , pp. 553-560
    • Peterson, G.L.1    Rosenbaum, L.C.2    Schimerlik, M.I.3
  • 121
    • 0027255390 scopus 로고
    • Solubilization and characterization of atrial muscarinic acetylcholine receptors in sucrose monolaurate
    • Rinken, A. and Haga, T. (1983) Solubilization and characterization of atrial muscarinic acetylcholine receptors in sucrose monolaurate. Arch. Biochem. Biophys. 301, 158-164.
    • (1983) Arch. Biochem. Biophys. , vol.301 , pp. 158-164
    • Rinken, A.1    Haga, T.2
  • 122
    • 0020352914 scopus 로고
    • Solubilization of the muscarinic acetylcholine receptor by sodium cholate: Stabilization of the receptor by muscarinic ligands
    • Haga, T., Nukada, T. and Haga, K. (1982) Solubilization of the muscarinic acetylcholine receptor by sodium cholate: Stabilization of the receptor by muscarinic ligands. Biomed. Res. 3, 695-698.
    • (1982) Biomed. Res. , vol.3 , pp. 695-698
    • Haga, T.1    Nukada, T.2    Haga, K.3
  • 125
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E.M. and Rosenbusch, J.P. (1996) Lipidic cubic phases: A novel concept for the crystallization of membrane proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 14532-14535.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 126
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. and Cherezov, V. (2009) Crystallizing membrane proteins using lipidic mesophases. Nat. Protoc. 4, 706-731.
    • (2009) Nat. Protoc. , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 131
    • 36349016730 scopus 로고    scopus 로고
    • Roof and floor of the muscarinic binding pocket: variations in the binding modes of orthosteric ligands
    • Goodwin, J.A., Hulme, E.C., Jangmead, C.J. and Tehen, B.G. (2007) Roof and floor of the muscarinic binding pocket: variations in the binding modes of orthosteric ligands. Mol. Pharmacol. 72, 1484-1496.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1484-1496
    • Goodwin, J.A.1    Hulme, E.C.2    Jangmead, C.J.3    Tehen, B.G.4
  • 133
    • 0027496941 scopus 로고
    • Mutational analysis of muscarinic acetylcholine receptors: structural basis of ligand/ receptor/G protein interactions
    • Wess, J. (1993) Mutational analysis of muscarinic acetylcholine receptors: structural basis of ligand/ receptor/G protein interactions. Life Sci. 53, 1447-1463.
    • (1993) Life Sci. , vol.53 , pp. 1447-1463
    • Wess, J.1
  • 134
    • 19944401545 scopus 로고    scopus 로고
    • Allosterism at muscarinic receptors: ligands and mechanisms
    • Birdsall, N.J.M. and Lazareno, S. (2005) Allosterism at muscarinic receptors: ligands and mechanisms. Mini-Reviews. Med. Chem. 5, 523-543.
    • (2005) Mini-Reviews. Med. Chem. , vol.5 , pp. 523-543
    • Birdsall, N.J.M.1    Lazareno, S.2
  • 135
    • 0028231689 scopus 로고
    • Mechanisms of steric and cooperative actions of alcuronium on cardiac muscarinic acetylcholine receptors
    • Proska, J. and Tucek, S. (1994) Mechanisms of steric and cooperative actions of alcuronium on cardiac muscarinic acetylcholine receptors. Mol. Pharmacol. 45, 709-717.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 709-717
    • Proska, J.1    Tucek, S.2
  • 141
    • 0002163185 scopus 로고
    • Molecular basis of pharmacologic selectivity
    • (eds. Pratt, W.B. and Palmer, T.), 3rd ed.Churchill Livingstone Inc., New York
    • Taylor, P. and Insel, P.A. (1990) Molecular basis of pharmacologic selectivity. In Principle of Drug Action (eds. Pratt, W.B. and Palmer, T.), 3rd ed., Churchill Livingstone Inc., New York, pp. 1-74.
    • (1990) In Principle of Drug Action , pp. 1-74
    • Taylor, P.1    Insel, P.A.2
  • 143
    • 84871812592 scopus 로고    scopus 로고
    • GPCR activation: a mutagenic spotlight on crystal structures
    • Hulme, E.C. (2013) GPCR activation: a mutagenic spotlight on crystal structures. Trends Pharmacol. Sci. 34, 67-84.
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 67-84
    • Hulme, E.C.1
  • 145
    • 34548362105 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development
    • Wess, J., Eglen, R.M. and Gautan, D. (2007) Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development. Nat. Rev. Drug Discov. 6, 721-733.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 721-733
    • Wess, J.1    Eglen, R.M.2    Gautan, D.3
  • 146
    • 61349093537 scopus 로고    scopus 로고
    • Subtype-selective allosteric modulators of muscarinic receptors for the treatment of CNS disorders
    • Conn, P.J., Jones, C.K. and Lindsley, C.W. (2009) Subtype-selective allosteric modulators of muscarinic receptors for the treatment of CNS disorders. Trends Pharmacol. Sci. 30, 148-155.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 148-155
    • Conn, P.J.1    Jones, C.K.2    Lindsley, C.W.3
  • 147
    • 77957282651 scopus 로고    scopus 로고
    • Allosteric modulation of muscarinic acetylcholine receptors
    • Jakubik, J. and El-Fakahany, E. (2010) Allosteric modulation of muscarinic acetylcholine receptors. Pharmaceuticals 3, 2838-2860.
    • (2010) Pharmaceuticals , vol.3 , pp. 2838-2860
    • Jakubik, J.1    El-Fakahany, E.2
  • 148
    • 78149496159 scopus 로고    scopus 로고
    • Allosteric modulation of G protein-coupled receptors: a pharmacological perspective
    • Keov, P., Sexton, P.M. and Christopoulos, A. (2011) Allosteric modulation of G protein-coupled receptors: a pharmacological perspective. Neuropharm. 60, 24-35.
    • (2011) Neuropharm. , vol.60 , pp. 24-35
    • Keov, P.1    Sexton, P.M.2    Christopoulos, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.