메뉴 건너뛰기




Volumn 52, Issue , 2012, Pages 1-19

Silver spoons and other personal reflections

Author keywords

Adenylyl cyclase; Cyclic AMP; G proteins; Receptor

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; BETA ADRENERGIC RECEPTOR; CYCLIC GMP; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE;

EID: 84855886095     PISSN: 03621642     EISSN: 15454304     Source Type: Book Series    
DOI: 10.1146/annurev-pharmtox-010611-134652     Document Type: Review
Times cited : (6)

References (49)
  • 1
    • 0013674190 scopus 로고
    • Puromycin inhibition of enzyme induction by 3-methylcholanthrene and phenobarbital
    • Conney AH, Gilman AG. 1963. Puromycin inhibition of enzyme induction by 3-methylcholanthrene and phenobarbital. J. Biol. Chem. 238:3682-85
    • (1963) J. Biol. Chem. , vol.238 , pp. 3682-3685
    • Conney, A.H.1    Gilman, A.G.2
  • 2
    • 84965091312 scopus 로고
    • The relationship of epinephrine and glucagon to liver phosphorylase: IV. Effect of epinephrine and glucagon on the reactivation of phosphorylase in liver homogenates
    • Rall TW, Sutherland EW, Berthet J. 1957. The relationship of epinephrine and glucagon to liver phosphorylase: IV. Effect of epinephrine and glucagon on the reactivation of phosphorylase in liver homogenates. J. Biol. Chem. 224:463-75
    • (1957) J. Biol. Chem. , vol.224 , pp. 463-475
    • Rall, T.W.1    Sutherland, E.W.2    Berthet, J.3
  • 3
    • 0010291733 scopus 로고
    • The relationship of epinephrine and glucagon to liver phosphorylase: III. Reactivation of liver phosphorylase in slices and in extracts
    • Rall TW, Sutherland EW, Wosilait WD. 1956. The relationship of epinephrine and glucagon to liver phosphorylase: III. Reactivation of liver phosphorylase in slices and in extracts. J. Biol. Chem. 218:483-95
    • (1956) J. Biol. Chem. , vol.218 , pp. 483-495
    • Rall, T.W.1    Sutherland, E.W.2    Wosilait, W.D.3
  • 4
    • 0642346948 scopus 로고    scopus 로고
    • Ten commandments of enzymology, amended
    • DOI 10.1016/j.tibs.2003.08.007, PII S0968000403002160
    • Kornberg A. 2003. Ten commandments of enzymology, amended. Trends Biochem. Sci. 28:515-17 (Pubitemid 38366273)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.10 , pp. 515-517
    • Kornberg, A.1
  • 5
    • 0014409394 scopus 로고
    • An adenosine 3′5′-monophosphate-dependent protein kinase from rabbit skeletal muscle
    • Walsh DA, Perkins JB, Krebs EG. 1968. An adenosine 3′5′- monophosphate-dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243:3763-65
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.B.2    Krebs, E.G.3
  • 6
    • 0014854395 scopus 로고
    • A protein binding assay for adenosine 3′:5′-cyclic monophosphate
    • Gilman AG. 1970. A protein binding assay for adenosine 3′:5′-cyclic monophosphate. Proc. Natl. Acad. Sci. USA 67:305-12
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 305-312
    • Gilman, A.G.1
  • 8
    • 0016137789 scopus 로고
    • The reaction of [3H]norepinephrine with particulate fractions of cells responsive to catecholamines
    • Maguire ME, Goldmann PH, Gilman AG. 1974. The reaction of [3H]norepinephrine with particulate fractions of cells responsive to catecholamines. Mol. Pharmacol. 10:563-81
    • (1974) Mol. Pharmacol. , vol.10 , pp. 563-581
    • Maguire, M.E.1    Goldmann, P.H.2    Gilman, A.G.3
  • 9
    • 0017290335 scopus 로고
    • β-Adrenergic receptor interactions: Characterization of iodohydroxybenzylpindolol as a specific ligand
    • Brown EM, Aurbach GD, Hauser D, Troxler F. 1976. β-Adrenergic receptor interactions: characterization of iodohydroxybenzylpindolol as a specific ligand. J. Biol. Chem. 251:1232-38
    • (1976) J. Biol. Chem. , vol.251 , pp. 1232-1238
    • Brown, E.M.1    Aurbach, G.D.2    Hauser, D.3    Troxler, F.4
  • 10
    • 0016669563 scopus 로고
    • Selection of a variant lymphoma cell line deficient in adenylate cyclase
    • Bourne HR, Coffino P, Tomkins GM. 1975. Selection of a variant lymphoma cell line deficient in adenylate cyclase. Science 187:750-52
    • (1975) Science , vol.187 , pp. 750-752
    • Bourne, H.R.1    Coffino, P.2    Tomkins, G.M.3
  • 12
    • 0017716885 scopus 로고
    • Reconstitution of catecholamine-sensitive adenylate cyclase activity: interaction of solubilized components with receptor-replete membranes
    • DOI 10.1073/pnas.74.9.3715
    • Ross EM, Gilman AG. 1977. Reconstitution of catecholamine-sensitive adenylate cyclase activity: interaction of solubilized components with receptor-repletemembranes. Proc.Natl. Acad. Sci.USA74:3715-19 (Pubitemid 8189953)
    • (1977) Proceedings of the National Academy of Sciences of the United States of America , vol.74 , Issue.9 , pp. 3715-3719
    • Ross, E.M.1    Gilman, A.G.2
  • 13
    • 0018177278 scopus 로고
    • Reconstitution of hormone-sensitive adenylate cyclase activity with resolved components of the enzyme
    • Ross EM,Howlett AC, Ferguson KM,Gilman AG. 1978. Reconstitution of hormone-sensitive adenylate cyclase activity with resolved components of the enzyme. J. Biol. Chem. 253:6401-12 (Pubitemid 9025319)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.18 , pp. 6401-6412
    • Ross, E.M.1    Howlett, A.C.2    Ferguson, K.M.3    Gilman, A.G.4
  • 14
    • 0015239313 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver: V. An obligatory role of guanylnucleotides in glucagon action
    • Rodbell M, Birnbaumer L, Pohl SL, Krans HM. 1971. The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver: V. An obligatory role of guanylnucleotides in glucagon action. J. Biol. Chem. 246:1877-82
    • (1971) J. Biol. Chem. , vol.246 , pp. 1877-1882
    • Rodbell, M.1    Birnbaumer, L.2    Pohl, S.L.3    Krans, H.M.4
  • 18
    • 0020595220 scopus 로고
    • The regulatory components of adenylate cyclase and transducin. A family of structurally homologous guanine nucleotide-binding proteins
    • Manning DR, Gilman AG. 1983. The regulatory components of adenylate cyclase and transducin: a family of structurally homologous guanine nucleotide binding proteins. J. Biol. Chem. 258:7059-63 (Pubitemid 13059959)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.11 , pp. 7059-7063
    • Manning, D.R.1    Gilman, A.G.2
  • 19
    • 0021733824 scopus 로고
    • Homologies between signal transducing G proteins and ras gene products
    • Hurley JB, Simon MI, Teplow DB, Robishaw JD, Gilman AG. 1984. Homologies between signal transducing G proteins and ras gene products. Science 226:860-62 (Pubitemid 15200686)
    • (1984) Science , vol.226 , Issue.4676 , pp. 860-862
    • Hurley, J.B.1    Simon, M.I.2    Teplow, D.B.3
  • 20
    • 0021812775 scopus 로고
    • Molecular cloning of complementary DNA for the alpha subunit of the G protein that stimulates adenylate cyclase
    • Harris BA, Robishaw JD, Mumby SM, Gilman AG. 1985. Molecular cloning of cDNA for the αsubunit of the G protein that stimulates adenylate cyclase. Science 229:1274-77 (Pubitemid 15021680)
    • (1985) Science , vol.229 , Issue.4719 , pp. 1274-1277
    • Harris, B.A.1    Robishaw, J.D.2    Mumby, S.M.3    Gilman, A.G.4
  • 23
    • 0023655760 scopus 로고
    • Expression of cDNAs for G proteins in Escherichia coli: Two forms of Gsα stimulate adenylyl cyclase
    • Graziano MP, Casey PJ, Gilman AG. 1987. Expression of cDNAs for G proteins in Escherichia coli: two forms of Gsα stimulate adenylyl cyclase. J. Biol. Chem. 262:11375-81
    • (1987) J. Biol. Chem. , vol.262 , pp. 11375-11381
    • Graziano, M.P.1    Casey, P.J.2    Gilman, A.G.3
  • 26
    • 0028838122 scopus 로고
    • Mammalian membrane-bound adenylyl cyclases
    • Taussig R, Gilman AG. 1995. Mammalian membrane-bound adenylyl cyclases. J. Biol. Chem. 270:1-4
    • (1995) J. Biol. Chem. , vol.270 , pp. 1-4
    • Taussig, R.1    Gilman, A.G.2
  • 27
    • 0029000308 scopus 로고
    • Construction of a soluble adenylyl cyclase activated by Gsα and forskolin
    • Tang W-J, Gilman AG. 1995. Construction of a soluble adenylyl cyclase activated by Gsα and forskolin. Science 268:1769-72
    • (1995) Science , vol.268 , pp. 1769-1772
    • Tang, W.-J.1    Gilman, A.G.2
  • 30
    • 0030832040 scopus 로고    scopus 로고
    • Interactions of forskolin and ATP with the cytosolic domains of mammalian adenylyl cyclase
    • DOI 10.1074/jbc.272.35.22272
    • Dessauer CW, Scully TT, Gilman AG. 1997. Interactions of forskolin and ATP with the cytosolic domains of mammalian adenylyl cyclase. J. Biol. Chem. 272:22272-77 (Pubitemid 27382861)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 22272-22277
    • Dessauer, C.W.1    Scully, T.T.2    Gilman, A.G.3
  • 31
    • 0030736715 scopus 로고    scopus 로고
    • The catalytic mechanism of mammalian adenylyl cyclase: Equilibrium binding and kinetic analysis of P-site inhibition
    • DOI 10.1074/jbc.272.44.27787
    • Dessauer CW, Gilman AG. 1997. The catalytic mechanism of mammalian adenylyl cyclase: equilibrium binding and kinetic analysis of P-site inhibition. J. Biol. Chem. 272:27787-95 (Pubitemid 27473578)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.44 , pp. 27787-27795
    • Dessauer, C.W.1    Gilman, A.G.2
  • 32
    • 0021325727 scopus 로고
    • Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase
    • Bokoch GM, Katada T, Northup JK, Ui M, Gilman AG. 1984. Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. J. Biol. Chem. 259:3560-67 (Pubitemid 14170085)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.6 , pp. 3560-3567
    • Bokoch, G.M.1    Katada, T.2    Northup, J.K.3
  • 33
    • 0026418426 scopus 로고
    • Type-specific regulation of adenylyl cyclase by G protein βγ subunits
    • Tang W-J, Gilman AG. 1991. Type-specific regulation of adenylyl cyclase by G protein βγ subunits. Science 254:1500-3 (Pubitemid 21917488)
    • (1991) Science , vol.254 , Issue.5037 , pp. 1500-1503
    • Tang, W.-J.1    Gilman, A.G.2
  • 37
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits
    • DOI 10.1016/S0092-8674(00)80117-8
    • Berman DM, Wilkie TM, Gilman AG. 1996. GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein αsubunits. Cell 86:445-52 (Pubitemid 26272084)
    • (1996) Cell , vol.86 , Issue.3 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 38
    • 0029861417 scopus 로고    scopus 로고
    • The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis
    • DOI 10.1074/jbc.271.44.27209
    • BermanDM,KozasaT,Gilman AG. 1996. TheGTPase-activating proteinRGS4stabilizes the transition state for nucleotide hydrolysis. J. Biol. Chem. 271:27209-12 (Pubitemid 26367266)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27209-27212
    • Berman, D.M.1    Kozasa, T.2    Gilman, A.G.3
  • 39
    • 0027132717 scopus 로고
    • The 2.2 A crystal structure of transducin-αcomplexedwithGTPγS
    • Noel JP,HammHE, Sigler P. 1993. The 2.2 A crystal structure of transducin-αcomplexedwithGTPγS. Nature 366:654-63
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.3
  • 40
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • DOI 10.1038/369621a0
    • Lambright DG, Noel JP, Hamm HE, Sigler PB. 1994. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369:621-28 (Pubitemid 24199466)
    • (1994) Nature , vol.369 , Issue.6482 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 41
    • 0028027596 scopus 로고
    • GTPase mechanism of Gproteins from the 1.7-Angstroms crystal structure of transducin alpha.GDP.AIF4
    • DOI 10.1038/372276a0
    • Sondek J, Lambright DG, Noel JP, Hamm HE, Sigler PB. 1994. GTPase mechanism of G proteins from the 1.7-A crystal structure of transducin α-GDP-AlF4. Nature 372:276-79 (Pubitemid 2152279)
    • (1994) Nature , vol.372 , Issue.6503 , pp. 276-279
    • Sondek, J.1    Lambright, D.G.2    Noel, J.P.3    Hamm, H.E.4    Sigler, P.B.5
  • 45
    • 0030982264 scopus 로고    scopus 로고
    • --activated G(iα1): Stabilization of the transition state for GTP hydrolysis
    • Tesmer JJG, Berman DM, Gilman AG, Sprang SR. 1997. Structure of RGS4 bound to AlF4 β-activated Giα1: stabilization of the transition state for GTP hydrolysis. Cell 89:251-61 (Pubitemid 27199897)
    • (1997) Cell , vol.89 , Issue.2 , pp. 251-261
    • Tesmer, J.J.G.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 46
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα)·GTPγΣ
    • DOI 10.1126/science.278.5345.1907
    • Tesmer JJG, Sunahara RK, Gilman AG, Sprang SR. 1997. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsα·GTPγS. Science 278:1907-16 (Pubitemid 28013225)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1907-1916
    • Tesmer, J.J.G.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 49
    • 33744809296 scopus 로고    scopus 로고
    • A global analysis of cross-talk in a mammalian cellular signalling network
    • DOI 10.1038/ncb1418, PII N1418
    • Natarajan M, Lin KM, Hsueh RC, Sternweis PC, Ranganathan R. 2006. A global analysis of cross-talk in a mammalian cellular signaling network. Nat. Cell Biol. 8:571-80 (Pubitemid 43827349)
    • (2006) Nature Cell Biology , vol.8 , Issue.6 , pp. 571-580
    • Natarajan, M.1    Lin, K.-M.2    Hsueh, R.C.3    Sternweis, P.C.4    Ranganathan, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.