메뉴 건너뛰기




Volumn 50, Issue 4, 1996, Pages 789-798

Covalent modification of transmembrane span III of the A1 adenosine receptor with an antagonist photoaffinity probe

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE RECEPTOR; CYANOGEN BROMIDE;

EID: 0029995690     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (48)
  • 10
    • 0026633147 scopus 로고
    • Molecular cloning of a novel adenosine receptor gene from rat brain
    • Chern, Y., K. King, H.-L. Lai, and H.-T. Lai. Molecular cloning of a novel adenosine receptor gene from rat brain. Biochem. Biophys. Res. Commun. 185:304-309 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 304-309
    • Chern, Y.1    King, K.2    Lai, H.-L.3    Lai, H.-T.4
  • 14
    • 0026726695 scopus 로고
    • Molecular cloning and expression of an adenosine A2b receptor from human brain
    • Pierce, K. D., T. J. Furlong, L. A. Selbie, and J. Shine. Molecular cloning and expression of an adenosine A2b receptor from human brain. Biochem. Biophys. Res. Commun. 187:86-93 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 86-93
    • Pierce, K.D.1    Furlong, T.J.2    Selbie, L.A.3    Shine, J.4
  • 17
    • 0025825121 scopus 로고
    • Molecular cloning of a novel putative G-protein coupled receptor expressed during rat spermiogenesis
    • Meyerhof, W., R. Muller-Brechlin, and D. Richter. Molecular cloning of a novel putative G-protein coupled receptor expressed during rat spermiogenesis. FEBS Lett. 284:155-160 (1991).
    • (1991) FEBS Lett. , vol.284 , pp. 155-160
    • Meyerhof, W.1    Muller-Brechlin, R.2    Richter, D.3
  • 18
  • 20
    • 0027489851 scopus 로고
    • cDNA cloning and sequence analysis of the human A3 adenosine receptor
    • Sajjadi, F. G., and G. S. Firestein. cDNA cloning and sequence analysis of the human A3 adenosine receptor. Biochim. Biophys. Acta 1179:105-107 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 105-107
    • Sajjadi, F.G.1    Firestein, G.S.2
  • 22
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmembrane-segment receptors
    • Dohlman, H. G., J. Thorner, M. G. Caron, and R. J. Lefkowitz. Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 60:653-688 (1991).
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 23
    • 0023945272 scopus 로고
    • Identification and sequence of a binding site peptide of the beta 2-adrenergic receptor
    • Dohlman, H. G., M. G. Caron, C. D. Strader, N. Amlaiky, and R. J. Lefkowitz. Identification and sequence of a binding site peptide of the beta 2-adrenergic receptor. Biochemistry 27:813-1817 (1988).
    • (1988) Biochemistry , vol.27 , pp. 813-1817
    • Dohlman, H.G.1    Caron, M.G.2    Strader, C.D.3    Amlaiky, N.4    Lefkowitz, R.J.5
  • 24
    • 0023941859 scopus 로고
    • The catecholamine binding site of the beta-adrenergic receptor is formed by juxtaposed membrane-spanning domains
    • Wong, S. K-F., C. Slaughter, A. E. Ruoho, and E. M. Ross. The catecholamine binding site of the beta-adrenergic receptor is formed by juxtaposed membrane-spanning domains. J. Biol. Chem. 263:7925-7928 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 7925-7928
    • Wong, S.K.-F.1    Slaughter, C.2    Ruoho, A.E.3    Ross, E.M.4
  • 26
    • 0028902886 scopus 로고
    • Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators
    • Yamada, M., A. Kuliopulos, N. P. Nelson, D. A. Roth, B. Furie, B. C. Furie, and C. T. Walsh. Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators. Biochemistry 34:481-489 (1995).
    • (1995) Biochemistry , vol.34 , pp. 481-489
    • Yamada, M.1    Kuliopulos, A.2    Nelson, N.P.3    Roth, D.A.4    Furie, B.5    Furie, B.C.6    Walsh, C.T.7
  • 29
    • 85047678432 scopus 로고
    • Cloned receptors and cardiovascular responses to adenosine
    • Tucker, A. L., and J. Linden. Cloned receptors and cardiovascular responses to adenosine. Cardiovasc. Res. 27:62-67 (1993).
    • (1993) Cardiovasc. Res. , vol.27 , pp. 62-67
    • Tucker, A.L.1    Linden, J.2
  • 30
    • 0024475076 scopus 로고
    • 1 adenosine receptors of rat brain membranes
    • 1 adenosine receptors of rat brain membranes. Mol. Pharmacol. 35:780-786 (1989).
    • (1989) Mol. Pharmacol. , vol.35 , pp. 780-786
    • Nakata, H.1
  • 31
    • 0020562171 scopus 로고
    • A rapid filtration assay for soluble receptors using polyethylenimine-treated filters
    • Bruns, R. F., K. Lawson-Wendling, and T. A. Pugsley. A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal. Biochem. 132:74-81 (1983).
    • (1983) Anal. Biochem. , vol.132 , pp. 74-81
    • Bruns, R.F.1    Lawson-Wendling, K.2    Pugsley, T.A.3
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379 (1987).
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 34
    • 0028044973 scopus 로고
    • Proteolysis of a membrane-bound protein in polyacrylamide gel slices using freeze-pulverization and gel electrophoresis techniques
    • Pong, A. S., and J. N. Wells. Proteolysis of a membrane-bound protein in polyacrylamide gel slices using freeze-pulverization and gel electrophoresis techniques. Anal. Biochem. 217:163-165 (1994).
    • (1994) Anal. Biochem. , vol.217 , pp. 163-165
    • Pong, A.S.1    Wells, J.N.2
  • 35
    • 0018717153 scopus 로고
    • Protein fingerprinting by SDS-gel electrooresis after partial fragmentation with CNBr
    • Nikodem, V., and J. R. Fresco. Protein fingerprinting by SDS-gel electrooresis after partial fragmentation with CNBr. Anal. Biochem. 97:382-386 (1979).
    • (1979) Anal. Biochem. , vol.97 , pp. 382-386
    • Nikodem, V.1    Fresco, J.R.2
  • 36
    • 0014962696 scopus 로고
    • The specific nonenzymatic cleavage of bovine ribonuclease with hydroxylamine
    • Bornstein, P., and G. Balian. The specific nonenzymatic cleavage of bovine ribonuclease with hydroxylamine. J. Biol. Chem. 245:4854-4856 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 4854-4856
    • Bornstein, P.1    Balian, G.2
  • 37
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E., and D. Lane. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1988).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 38
    • 0025679063 scopus 로고
    • Purification and characterization of bovine cerebral cortex A1 adenosine receptor
    • Olah, M. E., K. A. Jacobson, and G. L. Stiles. Purification and characterization of bovine cerebral cortex A1 adenosine receptor. Arch. Biochem. Biophys. 283:440-446 (1990).
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 440-446
    • Olah, M.E.1    Jacobson, K.A.2    Stiles, G.L.3
  • 39
    • 0015452895 scopus 로고
    • Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds
    • Houmard, J., and G. R. Drapeau. Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc. Natl. Acad. Sci. USA 69:3506-3509 (1972).
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3506-3509
    • Houmard, J.1    Drapeau, G.R.2
  • 40
    • 0025984862 scopus 로고
    • Fragmentation of proteins by S. aureus strain V8 protease
    • Sørensen, S. B., T. L. Sørensen, and K. Breddam. Fragmentation of proteins by S. aureus strain V8 protease. FEBS Lett. 294:195-197 (1991).
    • (1991) FEBS Lett. , vol.294 , pp. 195-197
    • Sørensen, S.B.1    Sørensen, T.L.2    Breddam, K.3
  • 41
    • 0021105027 scopus 로고
    • Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis
    • Jekel, P. A., W. J. Weijer, and J. J. Beintema. Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis. Anal. Biochem. 134:347-354 (1983).
    • (1983) Anal. Biochem. , vol.134 , pp. 347-354
    • Jekel, P.A.1    Weijer, W.J.2    Beintema, J.J.3
  • 43
    • 0018848604 scopus 로고
    • Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi
    • Drapeau, G. R. Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi. J. Biol. Chem. 255:839-840 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 839-840
    • Drapeau, G.R.1
  • 44
    • 10244249396 scopus 로고
    • Characterization of ghitamyl cleavage activity of endoproteinase Asp-N "sequencing grade."
    • Geuß, U., M. Schäffer, J. Tschakert, S. Fischer, and G.-B. Kresse. Characterization of ghitamyl cleavage activity of endoproteinase Asp-N "sequencing grade." J. Protein Chem. 9:299-300 (1990).
    • (1990) J. Protein Chem. , vol.9 , pp. 299-300
    • Geuß, U.1    Schäffer, M.2    Tschakert, J.3    Fischer, S.4    Kresse, G.-B.5
  • 45
    • 0022994052 scopus 로고
    • 1 adenosine receptor-binding subunits
    • 1 adenosine receptor-binding subunits. J. Biol. Chem. 261:10839-10843 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 10839-10843
    • Stiles, G.L.1
  • 46
    • 0028050692 scopus 로고
    • Role of the second extracellular loop of adenosine receptors in agonist and antagonist binding
    • Olah, M. E., K. A. Jacobson, and G. L. Stiles. Role of the second extracellular loop of adenosine receptors in agonist and antagonist binding. J. Biol. Chem. 269:24692-24698 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 24692-24698
    • Olah, M.E.1    Jacobson, K.A.2    Stiles, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.