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Volumn 12, Issue 2, 1998, Pages 121-132

Drugs interacting with G protein α subunits: Selectivity and perspectives

Author keywords

G protein antagonists; G proteins; Mastoparan and related peptides; Receptor independent G protein activation

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MASTOPARAN; NEUROPEPTIDE; PEPTIDE HORMONE; POLYAMINE; PROTEIN SUBUNIT; SUBSTANCE P DERIVATIVE; SURAMIN;

EID: 0031967878     PISSN: 07673981     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1472-8206.1998.tb00932.x     Document Type: Review
Times cited : (40)

References (150)
  • 1
    • 0021355194 scopus 로고
    • Amiodarone-induced hypersensitivity pneumonitis: Evidence of an immunological cell-mediated mechanism
    • Akoun GM, Gauthier-Rahman S, Milleron BJ, Perrot JY, Mayaud CM. Amiodarone-induced hypersensitivity pneumonitis: evidence of an immunological cell-mediated mechanism. Chest 1984 ; 85 : 133-5
    • (1984) Chest , vol.85 , pp. 133-135
    • Akoun, G.M.1    Gauthier-Rahman, S.2    Milleron, B.J.3    Perrot, J.Y.4    Mayaud, C.M.5
  • 3
    • 0025075352 scopus 로고
    • Exocytosis in mast cells by basic secretagogues, evidence for direct activation of GTP-binding proteins
    • Aridor M, Traub L, Sagi-Eisenberg R. Exocytosis in mast cells by basic secretagogues, evidence for direct activation of GTP-binding proteins. J Cell Biol 1990 ; 111 : 909-17
    • (1990) J Cell Biol , vol.111 , pp. 909-917
    • Aridor, M.1    Traub, L.2    Sagi-Eisenberg, R.3
  • 4
    • 0020973455 scopus 로고
    • Facilitation of phospholipase A2 activity by mastoparan, new class of mast cell degranulating peptides from wasp venom
    • Argiolas A, Pisano JJ. Facilitation of phospholipase A2 activity by mastoparan, new class of mast cell degranulating peptides from wasp venom. J Biol Chem 1983 ; 258 : 13697-702
    • (1983) J Biol Chem , vol.258 , pp. 13697-13702
    • Argiolas, A.1    Pisano, J.J.2
  • 5
    • 0018942122 scopus 로고
    • Enhancement of phagocytosis. A newly found activity of substance P residing in its N-terminal tetrapeptide sequence
    • Bar-Shavit Z, Goldman R, Stabinsky Y, Gottelib P, Blumberg S. Enhancement of phagocytosis. A newly found activity of substance P residing in its N-terminal tetrapeptide sequence. Biochem Biophys Res Commun 1980 ; 94 : 14-19
    • (1980) Biochem Biophys Res Commun , vol.94 , pp. 14-19
    • Bar-Shavit, Z.1    Goldman, R.2    Stabinsky, Y.3    Gottelib, P.4    Blumberg, S.5
  • 8
    • 0029861417 scopus 로고    scopus 로고
    • The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis
    • Berman DM, Kozasa T, Gilman AG. The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis. J Biol Chem 1996 ; 271 : 27209-12
    • (1996) J Biol Chem , vol.271 , pp. 27209-27212
    • Berman, D.M.1    Kozasa, T.2    Gilman, A.G.3
  • 9
    • 0026722913 scopus 로고
    • Reconstitution of agonist-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis using purified ml muscarinic receptor, Gq/11, and phospholipase C b1
    • Berstein G, Blank JL, Smrcka AV, Higashijima T, Sternweis PC, Exton JH, Ross EM. Reconstitution of agonist-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis using purified ml muscarinic receptor, Gq/11, and phospholipase C b1. J Biol Chem 1992 ; 267 : 8080-8
    • (1992) J Biol Chem , vol.267 , pp. 8080-8088
    • Berstein, G.1    Blank, J.L.2    Smrcka, A.V.3    Higashijima, T.4    Sternweis, P.C.5    Exton, J.H.6    Ross, E.M.7
  • 11
    • 0024970986 scopus 로고
    • Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits
    • Bidwai AP, Morjana NA, Scarborough GA. Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. J Biol Chem 1989 ; 264 : 11790-5
    • (1989) J Biol Chem , vol.264 , pp. 11790-11795
    • Bidwai, A.P.1    Morjana, N.A.2    Scarborough, G.A.3
  • 12
    • 0025010979 scopus 로고
    • The GTPase super-family: A conserved switch for diverse cell functions
    • Bourne HR, Sanders DA, McCormick F. The GTPase super-family: a conserved switch for diverse cell functions. Nature 1990 ; 348 : 125-32
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 13
    • 0026026818 scopus 로고
    • The GTPase super-family: Conserved strucrure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F. The GTPase super-family: conserved strucrure and molecular mechanism. Nature 1991 ; 349 : 117-27
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 14
    • 0025298681 scopus 로고
    • Effects of three irreversible inhibitors of ornithine decarboxylase on macrophage-mediated tumoricidal activity and antitumor activity in B16F1 tumor-bearing mice
    • Bowlin TL, Hoepper BJ, Rosenberger AL, Davis GF, Sunkara PS. Effects of three irreversible inhibitors of ornithine decarboxylase on macrophage-mediated tumoricidal activity and antitumor activity in B16F1 tumor-bearing mice. Cancer Res 1990 ; 50 : 4510-14
    • (1990) Cancer Res , vol.50 , pp. 4510-4514
    • Bowlin, T.L.1    Hoepper, B.J.2    Rosenberger, A.L.3    Davis, G.F.4    Sunkara, P.S.5
  • 15
    • 0025572696 scopus 로고
    • Activation of Gi-like proteins, a receptor-independent effect of kinins in mast cells
    • Bueb JL, Mousli M, Bronner C, Rouot B, Landry Y. Activation of Gi-like proteins, a receptor-independent effect of kinins in mast cells. Mol Pharmacol 1990 ; 38 : 816
    • (1990) Mol Pharmacol , vol.38 , pp. 816
    • Bueb, J.L.1    Mousli, M.2    Bronner, C.3    Rouot, B.4    Landry, Y.5
  • 16
    • 0027296848 scopus 로고
    • Structure-activity studies of bradykinin analogs on rat mast cell histamine release
    • Bueb JL, Mousli M, Landry Y, Regoli D. Structure-activity studies of bradykinin analogs on rat mast cell histamine release. Peptides 1992 ; 14 : 685-9
    • (1992) Peptides , vol.14 , pp. 685-689
    • Bueb, J.L.1    Mousli, M.2    Landry, Y.3    Regoli, D.4
  • 18
    • 0023992329 scopus 로고
    • Differential effects of suramin on the coupling of receptors to individual species of pertussis toxin-sensitive G proteins
    • Butler SJ, Kelly ECH, Mckenzie FR, Guild SB, Wakelam MJO, Milligan G. Differential effects of suramin on the coupling of receptors to individual species of pertussis toxin-sensitive G proteins. Biochem J 1988 ; 251 : 201-5
    • (1988) Biochem J , vol.251 , pp. 201-205
    • Butler, S.J.1    Kelly, E.C.H.2    Mckenzie, F.R.3    Guild, S.B.4    Wakelam, M.J.O.5    Milligan, G.6
  • 21
    • 0031006273 scopus 로고    scopus 로고
    • A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C
    • Chatterjee TK, Eapen AK, Fischer RA. A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C. J Biol Chem 1997 ; 272 : 15481-7
    • (1997) J Biol Chem , vol.272 , pp. 15481-15487
    • Chatterjee, T.K.1    Eapen, A.K.2    Fischer, R.A.3
  • 22
    • 0029843409 scopus 로고    scopus 로고
    • RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling
    • Chen CK, Wieland T, Simon MI. RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. Proc Natl Acad Sci USA 1996 ; 93 : 12885-9
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12885-12889
    • Chen, C.K.1    Wieland, T.2    Simon, M.I.3
  • 23
    • 0024501092 scopus 로고
    • Agonist-promoted sequestration of the β2-adrenergic receptor requires regions involved in functional coupling with GS
    • Cheung AH, Sigal IS, Dixon RAF, Strader CD. Agonist-promoted sequestration of the β2-adrenergic receptor requires regions involved in functional coupling with GS. Mol Pharmacol 1989 ; 35 : 132-8
    • (1989) Mol Pharmacol , vol.35 , pp. 132-138
    • Cheung, A.H.1    Sigal, I.S.2    Dixon, R.A.F.3    Strader, C.D.4
  • 24
    • 0025924420 scopus 로고
    • Specific activation of Gs by synthetic peptides corresponding to an intracellular loop of the β-adrenergic receptor
    • Cheung AH, Huang RC, Graziano MP, Strader CD. Specific activation of Gs by synthetic peptides corresponding to an intracellular loop of the β-adrenergic receptor. FEBS Lett 1991 ; 279 : 277-80
    • (1991) FEBS Lett , vol.279 , pp. 277-280
    • Cheung, A.H.1    Huang, R.C.2    Graziano, M.P.3    Strader, C.D.4
  • 25
    • 0027318238 scopus 로고
    • Structural elements of Gα-subunits that interact with G βγ-subunits, receptors and effectors
    • Conklin BR, Bourne HR. Structural elements of Gα-subunits that interact with G βγ-subunits, receptors and effectors. Cell 1993 ; 73 : 631-41
    • (1993) Cell , vol.73 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 26
    • 0026608113 scopus 로고
    • Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: Thermodynamic interpretation of negative antagonisme and of receptor activity in the absence of ligand
    • Costa T, Ogino Y, Munson PJ, Onaran O, Rodbard D. Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: thermodynamic interpretation of negative antagonisme and of receptor activity in the absence of ligand. Mol Pharamcol 1992 ; 41 : 549-60
    • (1992) Mol Pharamcol , vol.41 , pp. 549-560
    • Costa, T.1    Ogino, Y.2    Munson, P.J.3    Onaran, O.4    Rodbard, D.5
  • 27
    • 0006041356 scopus 로고
    • Toxicity and cystemic effects of local anesthetic agents
    • Berlin: Springer
    • Covino BG. Toxicity and cystemic effects of local anesthetic agents. In: Experimental Pharmacology. Berlin: Springer; 1987.p 187-212
    • (1987) Experimental Pharmacology , pp. 187-212
    • Covino, B.G.1
  • 28
    • 0023896925 scopus 로고
    • Histamine release from rat peritoneal mast cells by kinin antagonists
    • Devillier P, Renoux M, Drapeau G, Regoli D. Histamine release from rat peritoneal mast cells by kinin antagonists. Eur J Pharmacol 1988 ; 149 : 137-40
    • (1988) Eur J Pharmacol , vol.149 , pp. 137-140
    • Devillier, P.1    Renoux, M.2    Drapeau, G.3    Regoli, D.4
  • 29
    • 0024414818 scopus 로고
    • Role of the N-terminal arginine in the histamine-releasing activity of substance P, bradykinin, and related peptides
    • Devillier P, Drapeau G, Renoux M, Regoli D. Role of the N-terminal arginine in the histamine-releasing activity of substance P, bradykinin, and related peptides. Eur J Pharmacol 1989 ; 168 : 53-60
    • (1989) Eur J Pharmacol , vol.168 , pp. 53-60
    • Devillier, P.1    Drapeau, G.2    Renoux, M.3    Regoli, D.4
  • 30
    • 0029767982 scopus 로고    scopus 로고
    • Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: Expression, localization, and genetic interaction and physical association with Gpal (the G protein α subunit)
    • Dohlman HG, Song J, Ma D, Courchesne WE, Thorner J. Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization, and genetic interaction and physical association with Gpal (the G protein α subunit). Mol Cell Biol 1996 ; 16 : 5194-209
    • (1996) Mol Cell Biol , vol.16 , pp. 5194-5209
    • Dohlman, H.G.1    Song, J.2    Ma, D.3    Courchesne, W.E.4    Thorner, J.5
  • 31
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey KM, Blumer KJ, Kang VH, Kehrl JH. Inhibition of G protein-mediated MAP kinase activation by a new mammalian gene family. Nature 1996 ; 379 : 742-6
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 32
    • 0026011647 scopus 로고
    • Mortality and morbidity in patients receiving encaininde, flecainide, or placebo: The cardiac arrhythmia suppression trial
    • Echt DS, Liebson PR, Mitchell LB, Baker A, Richardson DW, the CAST investigators. Mortality and morbidity in patients receiving encaininde, flecainide, or placebo: the cardiac arrhythmia suppression trial. N Engl J Med 1991 ; 324 : 781-8
    • (1991) N Engl J Med , vol.324 , pp. 781-788
    • Echt, D.S.1    Liebson, P.R.2    Mitchell, L.B.3    Baker, A.4    Richardson, D.W.5
  • 33
    • 0028265789 scopus 로고
    • Complement peptides C3a- and C5a-induced mediator release from dissiciated human skin mast cells
    • El-Lati SG, Dahinden CA, Church MK. Complement peptides C3a- and C5a-induced mediator release from dissiciated human skin mast cells. J Invest Dermatol 1994 ; 102 : 803-6
    • (1994) J Invest Dermatol , vol.102 , pp. 803-806
    • El-Lati, S.G.1    Dahinden, C.A.2    Church, M.K.3
  • 34
    • 0028936297 scopus 로고
    • Human and rat cutaneous mast cells : Involvement of G protein in the response to peptidergic stimuli
    • Emadi-Khiav B, Mousli M, Bronner C, Landry Y. Human and rat cutaneous mast cells : involvement of G protein in the response to peptidergic stimuli. Eur J Pharmacol 1995 ; 272 : 97-102
    • (1995) Eur J Pharmacol , vol.272 , pp. 97-102
    • Emadi-Khiav, B.1    Mousli, M.2    Bronner, C.3    Landry, Y.4
  • 35
    • 0027399005 scopus 로고
    • The mechanism of inhibition of alkylamines on the mast-cell peptidergic pathway
    • Fischer T, Bronner C, Landry Y, Mousli M. The mechanism of inhibition of alkylamines on the mast-cell peptidergic pathway. Biochim Biophys Acta 1993 ; 1176 : 305-12
    • (1993) Biochim Biophys Acta , vol.1176 , pp. 305-312
    • Fischer, T.1    Bronner, C.2    Landry, Y.3    Mousli, M.4
  • 36
    • 0020647577 scopus 로고
    • Structure-activity relationships for some substance P-related peptides that cause wheal and flare reactions in human skin
    • Foreman JC, Jordan CC, Oehme P, Renner H. Structure-activity relationships for some substance P-related peptides that cause wheal and flare reactions in human skin. J Physiol 1983 ; 335 : 449-65
    • (1983) J Physiol , vol.335 , pp. 449-465
    • Foreman, J.C.1    Jordan, C.C.2    Oehme, P.3    Renner, H.4
  • 37
    • 0023270456 scopus 로고
    • Peptides and neurogenic inflammation
    • Foreman JC. Peptides and neurogenic inflammation. Br Med Bull 1987; 43 : 386-400
    • (1987) Br Med Bull , vol.43 , pp. 386-400
    • Foreman, J.C.1
  • 38
    • 6844250463 scopus 로고
    • The pharmacology of neuropeptides in mast cells and skin: Its implication for the physiology of blood flow in normal and diseased human skin
    • Foreman JC. The pharmacology of neuropeptides in mast cells and skin: its implication for the physiology of blood flow in normal and diseased human skin. Asia Pac J Pharmacol 1991 ; 6 : S1-9
    • (1991) Asia Pac J Pharmacol , vol.6
    • Foreman, J.C.1
  • 39
    • 0025947347 scopus 로고
    • Interaction of the bovine brain A1-adenosine receptor with recombinant G protein a subunits
    • Freissmuth M, Schütz W, Linder ME. Interaction of the bovine brain A1-adenosine receptor with recombinant G protein a subunits. J Biol Chem 1991 ; 266 : 17778-83
    • (1991) J Biol Chem , vol.266 , pp. 17778-17783
    • Freissmuth, M.1    Schütz, W.2    Linder, M.E.3
  • 41
    • 0025010595 scopus 로고
    • Anaphylatoxin binding and degranulation by rat peritoneal mast cells
    • Fukuoka Y, Hugli TE. Anaphylatoxin binding and degranulation by rat peritoneal mast cells. J Immunol 1990 ; 145 : 1851-7
    • (1990) J Immunol , vol.145 , pp. 1851-1857
    • Fukuoka, Y.1    Hugli, T.E.2
  • 42
    • 0026604734 scopus 로고
    • Amiodarone: An overview of its pharmacological properties, and review of its therapeutic use in cardiac arrhythmias
    • Gill J, Heel RC, Fitton A. Amiodarone: an overview of its pharmacological properties, and review of its therapeutic use in cardiac arrhythmias. Drugs 1992 ; 43 : 69-110
    • (1992) Drugs , vol.43 , pp. 69-110
    • Gill, J.1    Heel, R.C.2    Fitton, A.3
  • 43
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG. G proteins: Transducers of receptor-generated signals. Annu Rev Biochem 1987 ; 56 : 615-49
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 44
    • 0025731115 scopus 로고
    • Effects of mastoparan and related peptides on phosphoinositide breakdown in HL-60 cells and cell-free preperation
    • Gusovsky F, Soergel DG, Daly JW. Effects of mastoparan and related peptides on phosphoinositide breakdown in HL-60 cells and cell-free preperation. Eur J Pharmacol 1991 ; 206 : 309-14
    • (1991) Eur J Pharmacol , vol.206 , pp. 309-314
    • Gusovsky, F.1    Soergel, D.G.2    Daly, J.W.3
  • 45
    • 0028175796 scopus 로고
    • Lipophilic β-adrenoceptor antagonists and local anesthetics are effective direct activators of G proteins
    • Hagelüken A, Grünbaum L, Nürnberg B, Harhammer R, Seifert R. Lipophilic β-adrenoceptor antagonists and local anesthetics are effective direct activators of G proteins. Biochem Pharmacol 1994 ; 47 : 1789-95
    • (1994) Biochem Pharmacol , vol.47 , pp. 1789-1795
    • Hagelüken, A.1    Grünbaum, L.2    Nürnberg, B.3    Harhammer, R.4    Seifert, R.5
  • 46
    • 0028914956 scopus 로고
    • The class III antiarrhythmic drug amiodarone directly activates pertussis toxin-sensitive G proteins
    • Hagelüken A, Nürnberg B, Harhammer R, Grünbaum L, Seifert R. The class III antiarrhythmic drug amiodarone directly activates pertussis toxin-sensitive G proteins. Mol Pharmacol 1995 ; 47: 234-40
    • (1995) Mol Pharmacol , vol.47 , pp. 234-240
    • Hagelüken, A.1    Nürnberg, B.2    Harhammer, R.3    Grünbaum, L.4    Seifert, R.5
  • 47
    • 0022617106 scopus 로고
    • Substance P binding properties and studies on cellular response in guinea-pig macrophages
    • Hartung HP, Wolters K, Toyka KV. Substance P binding properties and studies on cellular response in guinea-pig macrophages. J Immunol 1986 ; 136 : 3856-61
    • (1986) J Immunol , vol.136 , pp. 3856-3861
    • Hartung, H.P.1    Wolters, K.2    Toyka, K.V.3
  • 48
    • 0023580413 scopus 로고
    • Substance P induces chemotaxis of neutrophils in normal and capsaicin-treated rats
    • Helme RD, Eglezos A, Hosking CS. Substance P induces chemotaxis of neutrophils in normal and capsaicin-treated rats. Immunol Cell Biol 1987 ; 65 : 267-71
    • (1987) Immunol Cell Biol , vol.65 , pp. 267-271
    • Helme, R.D.1    Eglezos, A.2    Hosking, C.S.3
  • 50
    • 0023918551 scopus 로고
    • Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins)
    • Higashjima T, Uzu S, Nakajima T, Ross EM. Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins). J Biol Chem 1988 ; 263 : 6491-4
    • (1988) J Biol Chem , vol.263 , pp. 6491-6494
    • Higashjima, T.1    Uzu, S.2    Nakajima, T.3    Ross, E.M.4
  • 51
    • 0025193034 scopus 로고
    • Regulation of Gi and Go by mastoparan, related amphiphilic peptides, and Hydrophobic amines
    • Higashijima T, Bumier J, Ross EM. Regulation of Gi and Go by mastoparan, related amphiphilic peptides, and Hydrophobic amines. J Biol Chem 1990 ; 265 : 14176-86
    • (1990) J Biol Chem , vol.265 , pp. 14176-14186
    • Higashijima, T.1    Bumier, J.2    Ross, E.M.3
  • 52
    • 0025883272 scopus 로고
    • Mapping of the mastoparan-binding site on G proteins
    • Higashijima T, Ross EM. Mapping of the mastoparan-binding site on G proteins. J Biol Chem 1991 ; 266 : 12655-61
    • (1991) J Biol Chem , vol.266 , pp. 12655-12661
    • Higashijima, T.1    Ross, E.M.2
  • 53
    • 0018706184 scopus 로고
    • A new mast cell degranulating peptide "mastoparan" in the venom of Vaspula lewisii
    • Hirai Y, Yasuhara T, Yoshida H, Fujino M, Kitada C. A new mast cell degranulating peptide "mastoparan" in the venom of Vaspula lewisii. Chem Pharmacol Bull 1979 ; 27 : 1942-4
    • (1979) Chem Pharmacol Bull , vol.27 , pp. 1942-1944
    • Hirai, Y.1    Yasuhara, T.2    Yoshida, H.3    Fujino, M.4    Kitada, C.5
  • 54
    • 0026562628 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum via the catalytic adenosine-nucleotide-binding site
    • 2+-ATPase of sarcoplasmic reticulum via the catalytic adenosine-nucleotide-binding site. Eur J Biochem 1992 ; 205 : 173-9
    • (1992) Eur J Biochem , vol.205 , pp. 173-179
    • Hohenegger, M.1    Makinose, M.2
  • 55
    • 0028152939 scopus 로고
    • Structural and functional characterization of the interaction between 2′:3′-dialdehyde guanine nucleotide analogues and the stimulatory G protein a subunits
    • Hohenegger M, Nanoff C, Ahron H, Freissmuth M. Structural and functional characterization of the interaction between 2′:3′-dialdehyde guanine nucleotide analogues and the stimulatory G protein a subunits. J Biol Chem 1994 ; 269 : 32008-15
    • (1994) J Biol Chem , vol.269 , pp. 32008-32015
    • Hohenegger, M.1    Nanoff, C.2    Ahron, H.3    Freissmuth, M.4
  • 56
    • 0023898089 scopus 로고
    • Local effector functions of capsaicin-sensitive sensory nerve endings: Involvement of tachykinins, calcitonin gene-related peptide and other neuropeptides
    • Holzer P. Local effector functions of capsaicin-sensitive sensory nerve endings: involvement of tachykinins, calcitonin gene-related peptide and other neuropeptides. Neuroscience 1988 ; 24 : 739-68
    • (1988) Neuroscience , vol.24 , pp. 739-768
    • Holzer, P.1
  • 58
    • 0030610240 scopus 로고    scopus 로고
    • Attenuation of Gi- and Gq-mediated signalling by expression of RGS4 or GAIP in mammalian cells
    • Huang C, Hepler JR, Gilman AG, Mumby SM. Attenuation of Gi- and Gq-mediated signalling by expression of RGS4 or GAIP in mammalian cells. Pro Natl Acad Sci USA 1997 ; 94 : 6159-63
    • (1997) Pro Natl Acad Sci USA , vol.94 , pp. 6159-6163
    • Huang, C.1    Hepler, J.R.2    Gilman, A.G.3    Mumby, S.M.4
  • 59
    • 6844254917 scopus 로고
    • Structure and function of C3a anaphylatoxin
    • Hugli TE. Structure and function of C3a anaphylatoxin. Curr Top Microbiol Immunol 1989 ; 135 : 151-63
    • (1989) Curr Top Microbiol Immunol , vol.135 , pp. 151-163
    • Hugli, T.E.1
  • 60
    • 0029830014 scopus 로고    scopus 로고
    • RGS 10 is a selective activator of Gαi GTPase activity
    • Hunt TW, Fields TA, Casey PJ, Peralta EJ. RGS 10 is a selective activator of Gαi GTPase activity. Nature 1996 ; 383 : 175-7
    • (1996) Nature , vol.383 , pp. 175-177
    • Hunt, T.W.1    Fields, T.A.2    Casey, P.J.3    Peralta, E.J.4
  • 61
    • 0021733824 scopus 로고
    • Homologies between signal transducing G proteins and ras gene product
    • Hurley JB, Simon MI, Teplow D, Robishaw JD, Gilman AG. Homologies between signal transducing G proteins and ras gene product. Science 1984 ; 226 : 860-2
    • (1984) Science , vol.226 , pp. 860-862
    • Hurley, J.B.1    Simon, M.I.2    Teplow, D.3    Robishaw, J.D.4    Gilman, A.G.5
  • 62
    • 0018693835 scopus 로고
    • Further studies on the structural requirements for plypeptide-mediated histamine release from rat mast cells
    • Jasani B, Kreil G, Mackler BF, Stanworth DR. Further studies on the structural requirements for plypeptide-mediated histamine release from rat mast cells. Biochem J 1979 ; 181 : 623-32
    • (1979) Biochem J , vol.181 , pp. 623-632
    • Jasani, B.1    Kreil, G.2    Mackler, B.F.3    Stanworth, D.R.4
  • 63
    • 0022394955 scopus 로고
    • Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene protein
    • Jurnak F. Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene protein. Science 1985 ; 230 : 32-6
    • (1985) Science , vol.230 , pp. 32-36
    • Jurnak, F.1
  • 64
    • 0026774105 scopus 로고
    • Activation of nucleoside diphosphate kinase by mastoparan, a peptide isolated from wasp venom
    • Kikkawa S, Takahashi K, Shimada N, Ui M, Katada T. Activation of nucleoside diphosphate kinase by mastoparan, a peptide isolated from wasp venom. FEBS Lett 1992 ; 305 : 237-40
    • (1992) FEBS Lett , vol.305 , pp. 237-240
    • Kikkawa, S.1    Takahashi, K.2    Shimada, N.3    Ui, M.4    Katada, T.5
  • 65
    • 0023545364 scopus 로고
    • Calcitonin gene-related peptide increases survival of a musculocutaneous critical flap in the rat
    • Kjartansson J, Dalsgaard CJ. Calcitonin gene-related peptide increases survival of a musculocutaneous critical flap in the rat. Eur J Pharmacol 1987 ; 142 : 355-8
    • (1987) Eur J Pharmacol , vol.142 , pp. 355-358
    • Kjartansson, J.1    Dalsgaard, C.J.2
  • 66
    • 0030907376 scopus 로고    scopus 로고
    • A new family of G-protein regulators, the RGS proteins
    • Koelle MR. A new family of G-protein regulators, the RGS proteins. Curr Opin Cell Biol 1997 ; 9 : 143-7
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 143-147
    • Koelle, M.R.1
  • 68
    • 0025821645 scopus 로고
    • Functional interactions of recombinant α2-adrenergic receptor subtypes and G proteins in reconstituted phospholipid vesicles
    • Kurose H, Regan J, Caron MG, Lefkowitz RJ. Functional interactions of recombinant α2-adrenergic receptor subtypes and G proteins in reconstituted phospholipid vesicles. Biochemistry 1991 ; 30 : 3335-41
    • (1991) Biochemistry , vol.30 , pp. 3335-3341
    • Kurose, H.1    Regan, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 69
    • 0029908908 scopus 로고    scopus 로고
    • Secretion of protease nexin-1 by C6 glioma cells is under the control of a heterotrimeric G protein, Go1
    • Lagriffoul A, Charpentier N, Carrette J, Tougard C, Bockaert J, Homburger V. Secretion of protease nexin-1 by C6 glioma cells is under the control of a heterotrimeric G protein, Go1. J Biol Chem 1996 ; 271 : 31508-16
    • (1996) J Biol Chem , vol.271 , pp. 31508-31516
    • Lagriffoul, A.1    Charpentier, N.2    Carrette, J.3    Tougard, C.4    Bockaert, J.5    Homburger, V.6
  • 71
    • 0026535633 scopus 로고
    • Affinity labeling of GTP-binding proteins in cellular extracts
    • Löw A, Faulhammer HG, Sprinzl M. Affinity labeling of GTP-binding proteins in cellular extracts. FEBS Lett 1992 ; 303 : 64-8
    • (1992) FEBS Lett , vol.303 , pp. 64-68
    • Löw, A.1    Faulhammer, H.G.2    Sprinzl, M.3
  • 72
    • 0027181337 scopus 로고
    • Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP
    • Löw A, Sprinzl M, Faulhammer HG. Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. Eur J Biochem 1993 ; 215 : 473-9
    • (1993) Eur J Biochem , vol.215 , pp. 473-479
    • Löw, A.1    Sprinzl, M.2    Faulhammer, H.G.3
  • 73
    • 0019825169 scopus 로고
    • Substance P binds to formylpeptide chemotaxis receptor on the rabbit neutrophil
    • Marasco WA, Showell HJ, Becker EL. Substance P binds to formylpeptide chemotaxis receptor on the rabbit neutrophil. Biochem Biophys Res Commun 1981 ; 99 : 1065
    • (1981) Biochem Biophys Res Commun , vol.99 , pp. 1065
    • Marasco, W.A.1    Showell, H.J.2    Becker, E.L.3
  • 74
    • 0026378713 scopus 로고
    • Capsaicin inhibits hyperresponsiveness but not lipooxygenase activity or eisinophilia after repeated aerosolized antigen in guinea pigs
    • Matsuse T, Thomson RJ., Chen XR, Salari H, Schellenberg RR. Capsaicin inhibits hyperresponsiveness but not lipooxygenase activity or eisinophilia after repeated aerosolized antigen in guinea pigs. Am Rev Respir Dis 1991 ; 144 : 368-72
    • (1991) Am Rev Respir Dis , vol.144 , pp. 368-372
    • Matsuse, T.1    Thomson, R.J.2    Chen, X.R.3    Salari, H.4    Schellenberg, R.R.5
  • 75
    • 0029019334 scopus 로고
    • Effects of mastoparan upon the late stage of the ACTH secretory pathway of AtT-20 cells
    • McFerran BW, Guild SB. Effects of mastoparan upon the late stage of the ACTH secretory pathway of AtT-20 cells. Br J Pharmacol 1995 ; 115 : 696-702
    • (1995) Br J Pharmacol , vol.115 , pp. 696-702
    • McFerran, B.W.1    Guild, S.B.2
  • 76
    • 0025237383 scopus 로고
    • Affinity labeling of spinach leaf phosphoribulokinase by ATP analogs. Modification of an active site lysine
    • Miziorko HM, Brodt CA, Krieger TJ. Affinity labeling of spinach leaf phosphoribulokinase by ATP analogs. Modification of an active site lysine. J Biol Chem 1990 ; 265 : 3642-7
    • (1990) J Biol Chem , vol.265 , pp. 3642-3647
    • Miziorko, H.M.1    Brodt, C.A.2    Krieger, T.J.3
  • 78
    • 0029143313 scopus 로고
    • Mastoparan-induced phosphatidylcholine hydrolysis by phospholipase D activation in human astrocytoma cells
    • Mizuno K, Nakahata N, Ohizumi Y. Mastoparan-induced phosphatidylcholine hydrolysis by phospholipase D activation in human astrocytoma cells. Br J Pharmacol 1995 ; 116 : 2090-6
    • (1995) Br J Pharmacol , vol.116 , pp. 2090-2096
    • Mizuno, K.1    Nakahata, N.2    Ohizumi, Y.3
  • 80
    • 0025162326 scopus 로고
    • G protein activation: A receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
    • Mousli M, Bueb JL, Bronner C, Rouot B, Landry Y. G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides. Trends Pharmacol Sci 1990 ; 11 : 358-62
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 358-362
    • Mousli, M.1    Bueb, J.L.2    Bronner, C.3    Rouot, B.4    Landry, Y.5
  • 81
    • 0025190182 scopus 로고
    • Direct activation of GTP-binding regulatory proteins (G proteins) by substance P and compound 48/80
    • Mousli M, Bronner C, Landry Y, Bockaert J, Rouot B. Direct activation of GTP-binding regulatory proteins (G proteins) by substance P and compound 48/80. FEBS Lett 1990 ; 259 : 260-2
    • (1990) FEBS Lett , vol.259 , pp. 260-262
    • Mousli, M.1    Bronner, C.2    Landry, Y.3    Bockaert, J.4    Rouot, B.5
  • 82
    • 0025826882 scopus 로고
    • Evidence for the interaction of mast cell-degranulating peptide (MCD) with pertussis toxin-sensitive G proteins in mast cells
    • Mousli M, Bronner C, Bueb JL, Landry Y. Evidence for the interaction of mast cell-degranulating peptide (MCD) with pertussis toxin-sensitive G proteins in mast cells. Eur J Pharmacol 1991 ; 207 : 249-55
    • (1991) Eur J Pharmacol , vol.207 , pp. 249-255
    • Mousli, M.1    Bronner, C.2    Bueb, J.L.3    Landry, Y.4
  • 83
    • 0026594019 scopus 로고
    • A mechanism of action for anaphylatoxin C3a stimulation of mast cells
    • Mousli M, Hugli TE, Landry Y, Bronner C. A mechanism of action for anaphylatoxin C3a stimulation of mast cells. J Immunol 1992 ; 148 : 2456-61
    • (1992) J Immunol , vol.148 , pp. 2456-2461
    • Mousli, M.1    Hugli, T.E.2    Landry, Y.3    Bronner, C.4
  • 84
    • 0028105828 scopus 로고
    • Peptidergic pathway in human skin and rat peritoneal mast cells
    • Mousli M, Hugli TE, Landry Y, Bronner C. Peptidergic pathway in human skin and rat peritoneal mast cells. Immunopharmacology 1993 ; 1 : 1-11
    • (1993) Immunopharmacology , vol.1 , pp. 1-11
    • Mousli, M.1    Hugli, T.E.2    Landry, Y.3    Bronner, C.4
  • 85
    • 0028985702 scopus 로고
    • Structural requirements for neuropeptide Y in mast cell and G protein activation
    • Mousli M, Trifilieff A, Pelton JT, Gies JP, Landry Y. Structural requirements for neuropeptide Y in mast cell and G protein activation. Eur J Pharmacol 1995 ; 289 : 125-33
    • (1995) Eur J Pharmacol , vol.289 , pp. 125-133
    • Mousli, M.1    Trifilieff, A.2    Pelton, J.T.3    Gies, J.P.4    Landry, Y.5
  • 87
    • 0025882303 scopus 로고
    • Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine-nucleotide-binding regulatory protein. Structural and functional studies by β-receptor-site-specific synthetic peptides
    • Münch G, Dees C, Hekman M, Palm D. Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine-nucleotide-binding regulatory protein. Structural and functional studies by β-receptor-site-specific synthetic peptides. Eur J Biochem 1991 ; 198 : 357-64
    • (1991) Eur J Biochem , vol.198 , pp. 357-364
    • Münch, G.1    Dees, C.2    Hekman, M.3    Palm, D.4
  • 88
    • 0028080007 scopus 로고
    • 2′:3′-dialdehyde GTP as an irreversible G protein antagonist: Disruption and reconstitution of G protein-mediated signal transduction in cells and in cell membranes
    • Nanoff C, Boehm S, Hohenegger M, Schütz W, Freissmuth M. 2′:3′-dialdehyde GTP as an irreversible G protein antagonist: disruption and reconstitution of G protein-mediated signal transduction in cells and in cell membranes. J Biol Chem 1994, 269 : 31999-2007
    • (1994) J Biol Chem , vol.269 , pp. 31999-32007
    • Nanoff, C.1    Boehm, S.2    Hohenegger, M.3    Schütz, W.4    Freissmuth, M.5
  • 89
    • 0028011112 scopus 로고
    • G proteins: Critical control points for transmembrane signals
    • Neer EJ. G proteins: critical control points for transmembrane signals. Protein Sci 1994 ; 3 : 3-14
    • (1994) Protein Sci , vol.3 , pp. 3-14
    • Neer, E.J.1
  • 90
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins : Organizers of transmembrane signals
    • Neer EJ. Heterotrimeric G proteins : organizers of transmembrane signals. Cell 1995 ; 80 : 249-57
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 91
    • 0031025382 scopus 로고    scopus 로고
    • Intracellular signalling: Turning down G-protein signals
    • Neer EJ. Intracellular signalling: turning down G-protein signals. Curr Biol 1997 ; 7 : R31-3
    • (1997) Curr Biol , vol.7
    • Neer, E.J.1
  • 92
    • 0031053536 scopus 로고    scopus 로고
    • Potential role for a regulator of G protein signaling (RGS 3) in gonadotropin-releasing hormone (GnRH) stimulated desensitization
    • Neill JD, Duck LW, Sellers JC, Musgrove LC, Scheschonka A, Druey KM, Kehrl JH. Potential role for a regulator of G protein signaling (RGS 3) in gonadotropin-releasing hormone (GnRH) stimulated desensitization. Endocrinology 1997 ; 138 : 843-6
    • (1997) Endocrinology , vol.138 , pp. 843-846
    • Neill, J.D.1    Duck, L.W.2    Sellers, J.C.3    Musgrove, L.C.4    Scheschonka, A.5    Druey, K.M.6    Kehrl, J.H.7
  • 93
    • 0023815680 scopus 로고
    • Site-directed mutagenesis of the cytoplasmic domains of the human β2-adrenergic receptor. Localization of regions involved in G protein-receptor coupling
    • O'Dowd BF, Hnatowich M, Regan JW, Leader WM, Caron MG, Lefkowitz RJ. Site-directed mutagenesis of the cytoplasmic domains of the human β2-adrenergic receptor. Localization of regions involved in G protein-receptor coupling. J Biol Chem 1988 ; 263 : 15985-92
    • (1988) J Biol Chem , vol.263 , pp. 15985-15992
    • O'Dowd, B.F.1    Hnatowich, M.2    Regan, J.W.3    Leader, W.M.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 94
    • 0022199824 scopus 로고
    • A wasp venom mastoparan-induced polyphosphoinositide breakdown in rat peritoneal mast cells
    • Okano Y, Takagi H, Tohmatsu T, Saito K, Nozawa Y. A wasp venom mastoparan-induced polyphosphoinositide breakdown in rat peritoneal mast cells. FEBS Lett 1985 ; 188 : 363-6
    • (1985) FEBS Lett , vol.188 , pp. 363-366
    • Okano, Y.1    Takagi, H.2    Tohmatsu, T.3    Saito, K.4    Nozawa, Y.5
  • 95
    • 0026781221 scopus 로고
    • Attenuation of GTPase activity of recombinant Go by peptides representing sequence permutations of mastoparan
    • Oppi CT, Wagner T, Crisari A, Camerini B, Valentini GPT. Attenuation of GTPase activity of recombinant Go by peptides representing sequence permutations of mastoparan. Proc Natl Acad Sci USA 1992 ; 89 : 8268-73
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8268-8273
    • Oppi, C.T.1    Wagner, T.2    Crisari, A.3    Camerini, B.4    Valentini, G.P.T.5
  • 97
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: Implication for the mechanism of GTP hydrolysis
    • Pai EF, Krengl U, Holmes KC, John J, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implication for the mechanism of GTP hydrolysis. EMBO J 1990 ; 9 : 2351-9
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengl, U.2    Holmes, K.C.3    John, J.4    Wittinghofer, A.5
  • 99
    • 0020964719 scopus 로고
    • Specific stimulation of human T lymphocytes by substance P
    • Payan DG. Brewster DR, Goetzl EG. Specific stimulation of human T lymphocytes by substance P. J Immunol 1983 ; 131 : 1613-15
    • (1983) J Immunol , vol.131 , pp. 1613-1615
    • Payan, D.G.1    Brewster, D.R.2    Goetzl, E.G.3
  • 100
    • 0020215250 scopus 로고
    • Polyamine metabolism and function
    • Pegg AE, McCann PP. Polyamine metabolism and function. Am J Physiol 1982 ; 243 : C212-21
    • (1982) Am J Physiol , vol.243
    • Pegg, A.E.1    McCann, P.P.2
  • 101
    • 0024298582 scopus 로고
    • Affinity labeling of the GDP/GTP binding site in thermus thermophilus elongation factor Tu
    • Peter ME, Wittmann-Liebold B, Sprinzl M. Affinity labeling of the GDP/GTP binding site in thermus thermophilus elongation factor Tu. Biochemistry 1988 ; 27 : 9132-9
    • (1988) Biochemistry , vol.27 , pp. 9132-9139
    • Peter, M.E.1    Wittmann-Liebold, B.2    Sprinzl, M.3
  • 102
    • 0026639097 scopus 로고
    • Benefecial effect of amiodarone on cardiac mortality in patients with asymptomatic complex ventricular arrhythmias after acute myocardial infarction and preserved but not impaired left ventricular function
    • Pfisterer MW, Kiowski D, Follath F, Burkart F. Benefecial effect of amiodarone on cardiac mortality in patients with asymptomatic complex ventricular arrhythmias after acute myocardial infarction and preserved but not impaired left ventricular function. Am J Cardiol 1992 ; 69 : 1399-402
    • (1992) Am J Cardiol , vol.69 , pp. 1399-1402
    • Pfisterer, M.W.1    Kiowski, D.2    Follath, F.3    Burkart, F.4
  • 103
    • 0025375985 scopus 로고
    • Neuropeptides in skin from patients with atopic dermatitis: An immunohistochemical study
    • Pincelli C, Fantini F, Massimi P, Girolomoni G, Gianetti A. Neuropeptides in skin from patients with atopic dermatitis: an immunohistochemical study. Br J Dermatol 1990 ; 122 : 745-51
    • (1990) Br J Dermatol , vol.122 , pp. 745-751
    • Pincelli, C.1    Fantini, F.2    Massimi, P.3    Girolomoni, G.4    Gianetti, A.5
  • 105
    • 6844260862 scopus 로고
    • β-adrenoceptor blocking agents
    • Abshagen U, eds. Berlin: Springer
    • Prichard BNC. β-adrenoceptor blocking agents. In: Abshagen U, eds. Experimental Pharmacology. Berlin: Springer, 1985 ; 385-458
    • (1985) Experimental Pharmacology , pp. 385-458
    • Prichard, B.N.C.1
  • 106
    • 0025855113 scopus 로고
    • Membrane interaction of amphiphilic polypeptides mastoparan, melittin, polymyxin B, and cardiotoxin
    • Raynor RL, Zherng B, Kuo JF. Membrane interaction of amphiphilic polypeptides mastoparan, melittin, polymyxin B, and cardiotoxin. J Biol Chem 1991 ; 266 : 2753-8
    • (1991) J Biol Chem , vol.266 , pp. 2753-2758
    • Raynor, R.L.1    Zherng, B.2    Kuo, J.F.3
  • 107
    • 0018636996 scopus 로고
    • Benzalkonium chloride: A selective inhibitor of histamine release induced by compound 48/80 and other polyamines
    • Read GW, Kiefer EF. Benzalkonium chloride: a selective inhibitor of histamine release induced by compound 48/80 and other polyamines. J Pharmacol Exp Ther 1979 ; 211 : 711-15
    • (1979) J Pharmacol Exp Ther , vol.211 , pp. 711-715
    • Read, G.W.1    Kiefer, E.F.2
  • 108
    • 0018995127 scopus 로고
    • Pharmacology of bradykinin and related kinins
    • Regoli D, Barabé J. Pharmacology of bradykinin and related kinins. Pharmacol Rev 1980 ; 32 : 1-46
    • (1980) Pharmacol Rev , vol.32 , pp. 1-46
    • Regoli, D.1    Barabé, J.2
  • 109
    • 0025239942 scopus 로고
    • New selective bradykinin receptor antagonists and bradykinin B2 receptor characterization
    • Regoli D, Rhaleb NE, Dion S, Drapeau G. New selective bradykinin receptor antagonists and bradykinin B2 receptor characterization. Trends Pharmacol Sci 1990 ; 11 : 156-61
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 156-161
    • Regoli, D.1    Rhaleb, N.E.2    Dion, S.3    Drapeau, G.4
  • 110
    • 0027296623 scopus 로고
    • Constitutively active mutants of the α2-adrenergic receptor
    • Ren Q, Kurose H, Lefkowitz RJ, Cotecchia S. Constitutively active mutants of the α2-adrenergic receptor. J Biol Chem 1993 ; 268 : 16483-7
    • (1993) J Biol Chem , vol.268 , pp. 16483-16487
    • Ren, Q.1    Kurose, H.2    Lefkowitz, R.J.3    Cotecchia, S.4
  • 111
    • 0023247404 scopus 로고
    • Histamine release induced by Arg-Pro-Lys-Pro(CH2)11CH3 from rat peritoneal mast cells
    • Repke H, Piotrowski W, Bienert M, Foreman JC. Histamine release induced by Arg-Pro-Lys-Pro(CH2)11CH3 from rat peritoneal mast cells. J Pharmacol Ther Exp 1987 ; 243 : 317-21
    • (1987) J Pharmacol Ther Exp , vol.243 , pp. 317-321
    • Repke, H.1    Piotrowski, W.2    Bienert, M.3    Foreman, J.C.4
  • 113
    • 0022474887 scopus 로고
    • Deduced primary structure of the α-subunit of the GTP-binding stimulatory protein of adenylyl cyclase
    • Robishaw JD, Russell DW, Harris BA, Gilman AG. Deduced primary structure of the α-subunit of the GTP-binding stimulatory protein of adenylyl cyclase. Proc Natl Acad Sci USA 1986 ; 83 : 1251-5
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1251-1255
    • Robishaw, J.D.1    Russell, D.W.2    Harris, B.A.3    Gilman, A.G.4
  • 114
    • 0024709982 scopus 로고
    • Signal sorting and amplification through G protein-coupled receptors
    • Ross EM. Signal sorting and amplification through G protein-coupled receptors. Neuron 1989 ; 3 : 141-52
    • (1989) Neuron , vol.3 , pp. 141-152
    • Ross, E.M.1
  • 115
    • 0022346134 scopus 로고
    • Substance P receptor-mediated chemotaxis of human monocytes
    • Ruff MR, Wahl SM, Pert CB. Substance P receptor-mediated chemotaxis of human monocytes. Peptides 1985 ; 6 : 107-11
    • (1985) Peptides , vol.6 , pp. 107-111
    • Ruff, M.R.1    Wahl, S.M.2    Pert, C.B.3
  • 116
    • 0027102562 scopus 로고
    • Cell signaling. A molecular growth industry
    • Ruvkun G. Cell signaling. a molecular growth industry. Nature 1992 ; 360 : 711-12
    • (1992) Nature , vol.360 , pp. 711-712
    • Ruvkun, G.1
  • 117
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor : Extending the ternary complex model
    • Samama P, Cotecchia S, Costa T, Lefkowitz RJ. A mutation-induced activated state of the β2-adrenergic receptor : extending the ternary complex model. J Biol Chem 1993 ; 268 : 4625-36
    • (1993) J Biol Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 118
    • 0028209348 scopus 로고
    • Negative antagonists promote an inactive conformation of the β2-adrenergic receptor
    • Samama P, Gang P, Costa T, Cotecchia S, Lefkowitz RJ. Negative antagonists promote an inactive conformation of the β2-adrenergic receptor. Mol Pharmacol 1993 ; 45 : 390-4
    • (1993) Mol Pharmacol , vol.45 , pp. 390-394
    • Samama, P.1    Gang, P.2    Costa, T.3    Cotecchia, S.4    Lefkowitz, R.J.5
  • 119
    • 0011036509 scopus 로고
    • Basic and clinical pharmacology of local anesthetic drugs
    • Miller MD, eds. New York: Churchill Livingstone
    • Savarese JJ, Covino BG. Basic and clinical pharmacology of local anesthetic drugs. In: Miller MD, eds. Anesthesia. New York: Churchill Livingstone; 1986. p. 985-1013
    • (1986) Anesthesia , pp. 985-1013
    • Savarese, J.J.1    Covino, B.G.2
  • 120
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for the structure-function relationships among G protein-coupled receptors
    • Savarese TM, Fraser CM. In vitro mutagenesis and the search for the structure-function relationships among G protein-coupled receptors. Biochem J 1992 ; 283 : 1-19
    • (1992) Biochem J , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 121
    • 0025871666 scopus 로고
    • Effect of thermus thermophilus elongation factor Ts on the conformation of elongation factor Tu
    • Schirmer NK, Reiser C, Sprinzl M. Effect of thermus thermophilus elongation factor Ts on the conformation of elongation factor Tu. Eur J Biochem 1991 ; 200 : 295-300
    • (1991) Eur J Biochem , vol.200 , pp. 295-300
    • Schirmer, N.K.1    Reiser, C.2    Sprinzl, M.3
  • 122
    • 0024382725 scopus 로고
    • Influence of polyamines on membrane functions
    • Schuber F. Influence of polyamines on membrane functions. Biochem J 1989 ; 260 : 1-10
    • (1989) Biochem J , vol.260 , pp. 1-10
    • Schuber, F.1
  • 123
    • 0028039751 scopus 로고
    • The H1 receptor agonist 2-(3-chlorophenyl)histamine activates Gi proteins in HL-60 cells through a mechanism that is independent of known histamine receptor subtypes
    • Seifert R, Hagelüken A, Höer A, Höer D, Grünbaum L, Offermanns S, Schultz G. The H1 receptor agonist 2-(3-chlorophenyl)histamine activates Gi proteins in HL-60 cells through a mechanism that is independent of known histamine receptor subtypes. Mol Pharmacol 1994 ; 45 : 578-86
    • (1994) Mol Pharmacol , vol.45 , pp. 578-586
    • Seifert, R.1    Hagelüken, A.2    Höer, A.3    Höer, D.4    Grünbaum, L.5    Offermanns, S.6    Schultz, G.7
  • 124
    • 0025237409 scopus 로고
    • Specificity of receptor G protein interactions: Discrimination of subtypes by the D2-dopamine receptor in a reconstituted system
    • Senogles SE, Spiegel AM, Padrell F, Caron MG. Specificity of receptor G protein interactions: discrimination of subtypes by the D2-dopamine receptor in a reconstituted system. J Biol Chem 1990 ; 265 : 4507-14
    • (1990) J Biol Chem , vol.265 , pp. 4507-4514
    • Senogles, S.E.1    Spiegel, A.M.2    Padrell, F.3    Caron, M.G.4
  • 126
    • 0024450129 scopus 로고
    • Deletion analysis of the mouse m1 muscarinic acethylcholine receptor: Effect of phosphoinositide metabolism and down-regulation
    • Shapiro RA, Nathanson NM. Deletion analysis of the mouse m1 muscarinic acethylcholine receptor: effect of phosphoinositide metabolism and down-regulation. Biochemistry 1989 ; 28 : 8946-50
    • (1989) Biochemistry , vol.28 , pp. 8946-8950
    • Shapiro, R.A.1    Nathanson, N.M.2
  • 127
    • 0027372340 scopus 로고
    • A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty
    • Shenker A, Laue L, Kosugi S, Merendino JJ Jr, Minegishi T, Culter GB. A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature 1993 ; 365 : 652-4
    • (1993) Nature , vol.365 , pp. 652-654
    • Shenker, A.1    Laue, L.2    Kosugi, S.3    Merendino Jr., J.J.4    Minegishi, T.5    Culter, G.B.6
  • 129
    • 0027325610 scopus 로고
    • Abnormalities in G protein-coupled signal transduction pathways in human disease
    • Spiegel AM, Weinstein LS, Shenker A. Abnormalities in G protein-coupled signal transduction pathways in human disease. J Clin Invest 1993 ; 92 : 1119-25
    • (1993) J Clin Invest , vol.92 , pp. 1119-1125
    • Spiegel, A.M.1    Weinstein, L.S.2    Shenker, A.3
  • 130
    • 0024519931 scopus 로고
    • Structural basis of β-adrenergic receptor function
    • Strader CD, Sigal IS, Dixon RAF. Structural basis of β-adrenergic receptor function. FASEB J 1989 ; 3 : 1825-32
    • (1989) FASEB J , vol.3 , pp. 1825-1832
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.F.3
  • 131
    • 0001127336 scopus 로고
    • The action of local anesthetics on ion channels of excitable tissues
    • Strichartz GR, eds. Berlin: Springer
    • Strichartz GR, Ritchie JM. The action of local anesthetics on ion channels of excitable tissues. In: Strichartz GR, eds. Experimental Pharmacology. Berlin: Springer; 1987. p 21-52
    • (1987) Experimental Pharmacology , pp. 21-52
    • Strichartz, G.R.1    Ritchie, J.M.2
  • 132
    • 0026787417 scopus 로고
    • G protein-bound conformation of mastoparan-X, a receptor memitic peptide
    • Sukumar M, Higashijima T. G protein-bound conformation of mastoparan-X, a receptor memitic peptide. J Biol Chem 1992 ; 267 : 21421
    • (1992) J Biol Chem , vol.267 , pp. 21421
    • Sukumar, M.1    Higashijima, T.2
  • 134
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor CW, Tabor H. Polyamines in microorganisms. Microbiol Rev 1985 ; 49 : 81-99
    • (1985) Microbiol Rev , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 135
    • 0026785546 scopus 로고
    • Suramin affects differentiated and undifferentiated throid epithelial cells in vitro
    • Treib K, Dorfinger K, Selzer E, Neuhold N, Wilfing A, Czernin S et al. Suramin affects differentiated and undifferentiated throid epithelial cells in vitro. J Endocrinol 1992 ; 134 : 505-11
    • (1992) J Endocrinol , vol.134 , pp. 505-511
    • Treib, K.1    Dorfinger, K.2    Selzer, E.3    Neuhold, N.4    Wilfing, A.5    Czernin, S.6
  • 136
    • 0021759089 scopus 로고
    • ADP-ribosylation of transducin by pertussis toxin blocks the light-stimulated hydrolysis of GTP and cGMP in retinal photoreceptors
    • Van Dop C, Yamanaka G, Steinberg F, Sekura RD, Manclark CR, Stryer L, Bourne HR. ADP-ribosylation of transducin by pertussis toxin blocks the light-stimulated hydrolysis of GTP and cGMP in retinal photoreceptors. J Biol Chem 1984 ; 259 : 23-6
    • (1984) J Biol Chem , vol.259 , pp. 23-26
    • Van Dop, C.1    Yamanaka, G.2    Steinberg, F.3    Sekura, R.D.4    Manclark, C.R.5    Stryer, L.6    Bourne, H.R.7
  • 137
    • 0028775602 scopus 로고
    • 5-Hydroxytryptamine-1A receptor synthetic peptides : Mechanisms of adenylyl inhibition
    • Varrault A, LeNguyen D, McClue S, Harris B, Jouin P, Bockaert J. 5-Hydroxytryptamine-1A receptor synthetic peptides : mechanisms of adenylyl inhibition. J Biol Chem 1994 ; 269 : 16720-5
    • (1994) J Biol Chem , vol.269 , pp. 16720-16725
    • Varrault, A.1    LeNguyen, D.2    McClue, S.3    Harris, B.4    Jouin, P.5    Bockaert, J.6
  • 139
    • 0027456328 scopus 로고
    • An amphipathic α-helical structure does not predict the ability of receptor-derived peptides to interact with G proteins
    • Voss T, Wallner E, Csernilofsky AP, Freissmuth M. An amphipathic α-helical structure does not predict the ability of receptor-derived peptides to interact with G proteins. J Biol Chem 1993 ; 268 : 4637-42
    • (1993) J Biol Chem , vol.268 , pp. 4637-4642
    • Voss, T.1    Wallner, E.2    Csernilofsky, A.P.3    Freissmuth, M.4
  • 140
    • 0025059293 scopus 로고
    • Luminal polyamines stimulate repair of gastric mucosal stress ulcers
    • Wang JY, Johnson LR. Luminal polyamines stimulate repair of gastric mucosal stress ulcers. Am J Physiol 1990 ; 259 : G584-92
    • (1990) Am J Physiol , vol.259
    • Wang, J.Y.1    Johnson, L.R.2
  • 141
    • 0030937708 scopus 로고    scopus 로고
    • Ocular inflammation induced by electroconvulsive treatments
    • Wang ZY, Waldeck K, Grundemar L, Hakanson R. Ocular inflammation induced by electroconvulsive treatments. Br J Pharmacol 1997 ; 120 : 1491-6
    • (1997) Br J Pharmacol , vol.120 , pp. 1491-1496
    • Wang, Z.Y.1    Waldeck, K.2    Grundemar, L.3    Hakanson, R.4
  • 143
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members : GTPase activating proteins for heterotrimeric G-protein alpha-subunits
    • Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ. RGS family members : GTPase activating proteins for heterotrimeric G-protein alpha-subunits. Nature 1996 ; 383 : 172-5
    • (1996) Nature , vol.383 , pp. 172-175
    • Watson, N.1    Linder, M.E.2    Druey, K.M.3    Kehrl, J.H.4    Blumer, K.J.5
  • 144
    • 0025173098 scopus 로고
    • A role for polyamines in glucose-stimulated insulin-gene expression
    • Welsh N. A role for polyamines in glucose-stimulated insulin-gene expression. Biochem J 1990 ; 271 : 393-7
    • (1990) Biochem J , vol.271 , pp. 393-397
    • Welsh, N.1
  • 145
    • 0030853492 scopus 로고    scopus 로고
    • Interactions of polyamines with ion channels
    • Williams K. Interactions of polyamines with ion channels. Biochem J 1997 ; 325 : 289-97
    • (1997) Biochem J , vol.325 , pp. 289-297
    • Williams, K.1
  • 146
    • 0030992381 scopus 로고    scopus 로고
    • Mastoparan-stimulated prolactin secretion in rat pituitary GH3 cells involves activation of Gq/11 proteins
    • Yajima Y, Uchino K, Ito H, Kawashima S. Mastoparan-stimulated prolactin secretion in rat pituitary GH3 cells involves activation of Gq/11 proteins. Endocrinology 1997 ; 138 : 1949-58
    • (1997) Endocrinology , vol.138 , pp. 1949-1958
    • Yajima, Y.1    Uchino, K.2    Ito, H.3    Kawashima, S.4
  • 147
    • 0030611749 scopus 로고    scopus 로고
    • RGS4 inhibits Gq-mediated activation of mitogene-activated protein kinase and phosphoinositide synthesis
    • Van Y, Chi PP, Bourne HR. RGS4 inhibits Gq-mediated activation of mitogene-activated protein kinase and phosphoinositide synthesis. J Biol Chem 1997 ; 272 : 11924-7
    • (1997) J Biol Chem , vol.272 , pp. 11924-11927
    • Van, Y.1    Chi, P.P.2    Bourne, H.R.3
  • 148
    • 0024548963 scopus 로고
    • Mastoparan, a wasp venom, stimulates insulin release by pancreatic islets through pertussis toxin sensitive GTP-binding protein
    • Yokokawa N, Komatsu M, Takeda T, Aizawa T, yamada T. Mastoparan, a wasp venom, stimulates insulin release by pancreatic islets through pertussis toxin sensitive GTP-binding protein. Biochem Biophys Res Commun 1989 ; 158 : 712-16
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 712-716
    • Yokokawa, N.1    Komatsu, M.2    Takeda, T.3    Aizawa, T.4    Yamada, T.5
  • 149
  • 150
    • 0028095503 scopus 로고
    • 2+ channels of sympathetic neurons via a pertussis toxin-insensitive but cholera toxin-sensitive pathway
    • 2+ channels of sympathetic neurons via a pertussis toxin-insensitive but cholera toxin-sensitive pathway. Neuron 1994 ; 13 : 657-69
    • (1994) Neuron , vol.13 , pp. 657-669
    • Zhu, Y.1    Ikeda, R.2


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