메뉴 건너뛰기




Volumn 49, Issue 4, 1996, Pages 602-611

Suramin analogues as subtype-selective G protein inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

8 (3 NITROBENZAMIDO) 1,3,5 NAPHTHALENETRISULFONIC ACID; 8 [3 (3 NITROBENZAMIDO)BENZAMIDO] 1,3,5 NAPHTHALENETRISULFONIC ACID; 8,8 [CARBONYLBIS(IMINO 3,1 PHENYLENE)CARBONYLIMINO(3,1 PHENYLENE)]BIS(1,3,5 NAPHTHALENETRISULFONIC ACID); 8,8' [CARBONYLBIS(IMINO 3,1 PHENYLENE)]BIS(1,3,5 NAPHTHALENETRISULFONIC ACID); ADENYLATE CYCLASE; ALPHA 2 ADRENERGIC RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MUSCARINIC RECEPTOR; NF 007; NF 018; NF 023; NF 037; UNCLASSIFIED DRUG; VASOACTIVE INTESTINAL POLYPEPTIDE;

EID: 0029917666     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (147)

References (45)
  • 2
    • 0027936892 scopus 로고
    • Membrane organization in G protein mechanisms
    • Neubig, R. R. Membrane organization in G protein mechanisms. FASEB J. 8:939-946 (1994).
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 3
    • 0028152939 scopus 로고
    • Structural and functional characterization of the interaction between 2′:3′-dialdehyde guanine nucleotide analogues and the stimulatory G protein α subunit
    • Hohenegger, M , C. Nanoff, H. Ahorn, and M. Freissmuth Structural and functional characterization of the interaction between 2′:3′-dialdehyde guanine nucleotide analogues and the stimulatory G protein α subunit J Biol. Chem 269:32008-32015 (1994).
    • (1994) J Biol. Chem , vol.269 , pp. 32008-32015
    • Hohenegger, M.1    Nanoff, C.2    Ahorn, H.3    Freissmuth, M.4
  • 4
    • 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 cell membranes
    • Nanoff, C., S. Boehm, M. Hohenegger, W. Schutz, and M. Freissmuth. 2′:3′-Dialdehyde GTP as an irreversible G protein antagonist: disruption and reconstitution of G protein-mediated signal transduction in cells and cell membranes. J. Biol. Chem. 269:31999-32007 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31999-32007
    • Nanoff, C.1    Boehm, S.2    Hohenegger, M.3    Schutz, W.4    Freissmuth, M.5
  • 5
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., D. A. Sanders, and F. McCormick. The GTPase superfamily: a conserved switch for diverse cell functions. Nature (Lond.) 348:125-132 (1990).
    • (1990) Nature (Lond.) , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 6
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanisms
    • Bourne, H. R., D. A. Sanders, and F. McCormick. The GTPase superfamily: conserved structure and molecular mechanisms. Nature (Lond.) 349:117-127 (1991).
    • (1991) Nature (Lond.) , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0023918551 scopus 로고
    • Mastoparan, a peptide toxin from wasp venom, mimics receptor by activating GTP-binding proteins (G proteins)
    • Higashijima, T., S. Uzu, T. Nakajima, and E. M. Ross. Mastoparan, a peptide toxin from wasp venom, mimics receptor by activating GTP-binding proteins (G proteins). J. Biol Chem. 263:6491-6494 (1988)
    • (1988) J. Biol Chem. , vol.263 , pp. 6491-6494
    • Higashijima, T.1    Uzu, S.2    Nakajima, T.3    Ross, E.M.4
  • 8
    • 0024414931 scopus 로고
    • Mapping of the β-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides
    • Palm, D., G. Munch, C Dees, and M. Hekman. Mapping of the β-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides. FEBS Lett. 254:89-93 (1989).
    • (1989) FEBS Lett. , vol.254 , pp. 89-93
    • Palm, D.1    Munch, G.2    Dees, C.3    Hekman, M.4
  • 9
    • 0025193034 scopus 로고
    • Regulation of Gi and Go by mastoparan related amphiphilic peptides and hydrophobic amines: Mechanism and structural determinants
    • Higashijima, T., J. Burnier, and E. M. Ross. Regulation of Gi and Go by mastoparan related amphiphilic peptides and hydrophobic amines: mechanism and structural determinants. J. Biol. Chem. 265:14176-14186 (1990)
    • (1990) J. Biol. Chem. , vol.265 , pp. 14176-14186
    • Higashijima, T.1    Burnier, J.2    Ross, E.M.3
  • 10
    • 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 peptides
    • Munch, G., C. Dees, M, Hekman, and D. Palm. 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 peptides. Eur. J. Biochem. 198:357-364 (1991).
    • (1991) Eur. J. Biochem. , vol.198 , pp. 357-364
    • Munch, G.1    Dees, C.2    Hekman, M.3    Palm, D.4
  • 11
    • 0026781221 scopus 로고
    • Attenuation of GTPase activity of recombinant G(o) alpha by peptides representing sequence permutations of mastoparan
    • Oppi, C., T. Wagner, A. Crisari, B. Camerini, and G. P. Tocchini Valentini. Attenuation of GTPase activity of recombinant G(o) alpha by peptides representing sequence permutations of mastoparan. Proc. Natl. Acad. Sci. USA 89:8268-8273 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8268-8273
    • Oppi, C.1    Wagner, T.2    Crisari, A.3    Camerini, B.4    Tocchini Valentini, G.P.5
  • 12
    • 0027456328 scopus 로고
    • An amphipathic α-helical structure does not predict the ability of receptor-derived peptides to interact with G proteins
    • Voss, T., E. Wallner, A. P. Csernilofsky, and M. Freissmuth. An amphipathic α-helical structure does not predict the ability of receptor-derived peptides to interact with G proteins. J. Biol. Chem. 268:4637-4642 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4637-4642
    • Voss, T.1    Wallner, E.2    Csernilofsky, A.P.3    Freissmuth, M.4
  • 13
    • 0028775602 scopus 로고
    • 5-Hydroxytryptamine-1A receptor synthetic peptides: Mechanisms of adenylyl cyclase inhibition
    • Varrault, A., D. LeNguyen, S. McClue, B. Harris, P. Jouin, and J. Bockaert. 5-Hydroxytryptamine-1A receptor synthetic peptides: mechanisms of adenylyl cyclase inhibition. J. Biol. Chem. 269:16720-16725 (1994).
    • (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
  • 14
    • 0026728169 scopus 로고
    • G protein antagonists: A novel hydrophobic peptide competes with receptor for G protein binding
    • Mukai, H., E. Munekata, and T. Higashijima. G protein antagonists: a novel hydrophobic peptide competes with receptor for G protein binding. J. Biol. Chem. 267:16237-16243 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16237-16243
    • Mukai, H.1    Munekata, E.2    Higashijima, T.3
  • 17
    • 0023992329 scopus 로고
    • Differential effects of suramin on the coupling of receptors to individual species of pertussis toxin-sensitive guanine nucleotide binding proteins
    • Butler, S., E. C. H. Kelly, F. McKenzie, S. Guild, M O. Wakelam, and G. Milligan. Differential effects of suramin on the coupling of receptors to individual species of pertussis toxin-sensitive guanine nucleotide binding proteins. Biochem. J. 251:201-205 (1988).
    • (1988) Biochem. J. , vol.251 , pp. 201-205
    • Butler, S.1    Kelly, E.C.H.2    McKenzie, F.3    Guild, S.4    Wakelam, M.O.5    Milligan, G.6
  • 18
    • 0025099596 scopus 로고
    • Identification of allosteric antagonists of receptor-guanine nucleotide binding protein interactions
    • Huang, R.-R. C., R. N. Dehaven, A. H. Cheung, R. E. Diehl, R. A. F. Dixon, and C. D. Strader. Identification of allosteric antagonists of receptor-guanine nucleotide binding protein interactions. Mol. Pharmacol. 37:304-310 (1990).
    • (1990) Mol. Pharmacol. , vol.37 , pp. 304-310
    • Huang, R.-R.C.1    Dehaven, R.N.2    Cheung, A.H.3    Diehl, R.E.4    Dixon, R.A.F.5    Strader, C.D.6
  • 20
    • 0024476804 scopus 로고
    • sα in Escherichia coli: Purification and characterization of two forms of the protein
    • sα in Escherichia coli: purification and characterization of two forms of the protein. J. Biol. Chem. 264:409-418 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 409-418
    • Graziano, M.P.1    Freissmuth, M.2    Gilman, A.G.3
  • 21
    • 0028142193 scopus 로고
    • Myristoylation of G protein α subunits
    • Mumby, S. M., and M. E. Linder. Myristoylation of G protein α subunits. Methods Eraymol. 237:254-268 (1994).
    • (1994) Methods Eraymol. , vol.237 , pp. 254-268
    • Mumby, S.M.1    Linder, M.E.2
  • 23
    • 0022435177 scopus 로고
    • Adenylate cyclase from bovine brain cortex, purification and characterization of the catalytic unit
    • Pfeuffer, E., S. Mollner, and T. Pfeuffer. Adenylate cyclase from bovine brain cortex, purification and characterization of the catalytic unit. EMBO J. 4:3675-3679 (1985).
    • (1985) EMBO J. , vol.4 , pp. 3675-3679
    • Pfeuffer, E.1    Mollner, S.2    Pfeuffer, T.3
  • 24
    • 0025793604 scopus 로고
    • Assay of adenylyl cyclase catalytic activity
    • Johnson, R. A., and Y Salomon. Assay of adenylyl cyclase catalytic activity. Methods Enzymol. 195:32-41 (1991).
    • (1991) Methods Enzymol. , vol.195 , pp. 32-41
    • Johnson, R.A.1    Salomon, Y.2
  • 25
  • 26
    • 0025878182 scopus 로고
    • Synthetic peptide antisera with determined specificity for G protein α or β subunits
    • Mumby, S. M, and A. G. Gilman. Synthetic peptide antisera with determined specificity for G protein α or β subunits. Methods Enzymol. 195: 215-233 (1991).
    • (1991) Methods Enzymol. , vol.195 , pp. 215-233
    • Mumby, S.M.1    Gilman, A.G.2
  • 28
    • 0028104711 scopus 로고
    • Noradrenaline release from rat sympathetic neurons evoked by P2-purinoceptor activation
    • Boehm, S. Noradrenaline release from rat sympathetic neurons evoked by P2-purinoceptor activation. Naunyn-Schmiedeberg's Arch. Pharmacol. 350:454-458 (1994).
    • (1994) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.350 , pp. 454-458
    • Boehm, S.1
  • 29
    • 0019441262 scopus 로고
    • Improved patch-clamp technique for high resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., A. Marty, E. Neher, E., B. Sakman, and F. J. Sigworth. Improved patch-clamp technique for high resolution current recording from cells and cell-free membrane patches Pfluegers Arch. 391:85-100 (1981).
    • (1981) Pfluegers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakman, E.B.4    Sigworth, F.J.5
  • 31
    • 0020050452 scopus 로고
    • Kinetics of interaction between β-receptor, GTP-binding protein, and catalytic unit of turkey erythrocyte adenylate cyclase
    • Tolkovsky, A. M., S. Braun, and A. Levitzki. Kinetics of interaction between β-receptor, GTP-binding protein, and catalytic unit of turkey erythrocyte adenylate cyclase. Proc. Natl. Acad. Sci. USA 79:213-217 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 213-217
    • Tolkovsky, A.M.1    Braun, S.2    Levitzki, A.3
  • 32
    • 0022405658 scopus 로고
    • The interactions between the activatory guanine nucleotide binding protein and the catalytic subunit of adenylate cyclase in rat liver plasma membranes
    • Wong, S. K.-F., and B. R. Martin. The interactions between the activatory guanine nucleotide binding protein and the catalytic subunit of adenylate cyclase in rat liver plasma membranes. Biochem. J. 231:39-46 (1985).
    • (1985) Biochem. J. , vol.231 , pp. 39-46
    • Wong, S.K.-F.1    Martin, B.R.2
  • 33
    • 0021682740 scopus 로고
    • s and the catalytic unit of adenylate cyclase are tightly associated: Mechanistic consequences
    • s and the catalytic unit of adenylate cyclase are tightly associated: mechanistic consequences. Proc. Natl. Acad. Sci. USA 81:6579-6583 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6579-6583
    • Arad, H.1    Rosenbusch, J.P.2    Levitzki, A.3
  • 34
    • 0027318238 scopus 로고
    • Structural elements of G α subunits that interact with G βγ subunits, receptors and effectors
    • Conklin, B R., and H. R. Bourne. Structural elements of G α subunits that interact with G βγ subunits, receptors and effectors. Cell 73:631-641 (1993).
    • (1993) Cell , vol.73 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 35
    • 0027132717 scopus 로고
    • The 2.2 a crystal structure of transducin-α complexed with GTPγS
    • Noel, J. P., H. E, Hamm, and P. B. Sigler. The 2.2 A crystal structure of transducin-α complexed with GTPγS. Nature (Lond.) 366:654-663 (1993).
    • (1993) Nature (Lond.) , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 38
    • 9244250114 scopus 로고
    • The GTP-analogue 2′:3′-dialdehyde GTP abolishes the modulation of neuronal calcium currents by various neurotransmitters
    • Boehm, S., C. Nanoff, M. Hohenegger, M. Freissmuth, and S. Huck. The GTP-analogue 2′:3′-dialdehyde GTP abolishes the modulation of neuronal calcium currents by various neurotransmitters. Soc. Neurosci. Abstr. 19: 1263 (1993).
    • (1993) Soc. Neurosci. Abstr. , vol.19 , pp. 1263
    • Boehm, S.1    Nanoff, C.2    Hohenegger, M.3    Freissmuth, M.4    Huck, S.5
  • 39
    • 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 13:657-669 (1994).
    • (1994) Neuron , vol.13 , pp. 657-669
    • Zhu, Y.1    Ikeda, R.2
  • 40
    • 0026452219 scopus 로고
    • G protein βγ subunits synthesized in SF9-cells: Functional characterization and the significance of prenylation of γ
    • Inuiguez-Lluhi, J. A., M I. Simon, J. D. Robishaw, and A G. Gilman. G protein βγ subunits synthesized in SF9-cells: functional characterization and the significance of prenylation of γ. J. Biol. Chem. 267:23409-23417 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 23409-23417
    • Inuiguez-Lluhi, J.A.1    Simon, M.I.2    Robishaw, J.D.3    Gilman, A.G.4
  • 41
    • 0027491658 scopus 로고
    • o subunit: Mutation of conserved cysteines identifies a subunit contact surface and alters GDP affinity
    • o subunit: mutation of conserved cysteines identifies a subunit contact surface and alters GDP affinity. Proc. Natl. Acad. Sci. USA 90:10295-10298 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10295-10298
    • Thomas, T.C.1    Schmidt, C.J.2    Neer, E.J.3
  • 42
    • 0027495918 scopus 로고
    • Tryptophane W207 in transducin Tα is the fluorescence sensor of the G protein activation switch and is involved in effector binding
    • Faurobert, E., A. Otto-Bruc, P. Chardin, and M. Chabre. Tryptophane W207 in transducin Tα is the fluorescence sensor of the G protein activation switch and is involved in effector binding. EMBO J. 12:4191-4198 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4191-4198
    • Faurobert, E.1    Otto-Bruc, A.2    Chardin, P.3    Chabre, M.4
  • 43
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α subunit of a heterotrimeric G protein
    • Lambright, D. G., J P. Noel, H. E. Hamm, and P. B. Sigler. Structural determinants for activation of the α subunit of a heterotrimeric G protein. Nature (Lond.) 369:621-628 (1994).
    • (1994) Nature (Lond.) , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.