메뉴 건너뛰기




Volumn 237, Issue 3, 1996, Pages 611-618

Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase

Author keywords

CAMP dependent protein kinase; Chaperone; Non structural protein 3; Protein phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; CYCLIC AMP DEPENDENT PROTEIN KINASE; PROTEIN KINASE INHIBITOR; VIRUS PROTEIN;

EID: 0029992405     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0611p.x     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0025217987 scopus 로고
    • Hepatitis C virus: The major causative agent of viral non-A, non-B hepatitis
    • Choo, Q.-L., Weiner, A. J., Overby, L. R., Kuo, G. & Houghton, M. (1990) Hepatitis C virus: the major causative agent of viral non-A, non-B hepatitis, Br. Med Bull. 46, 423-441.
    • (1990) Br. Med Bull. , vol.46 , pp. 423-441
    • Choo, Q.-L.1    Weiner, A.J.2    Overby, L.R.3    Kuo, G.4    Houghton, M.5
  • 2
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Choo, Q.-L., Kuo, G., Weiner, A. J., Bradley, D. W. & Houghton, M. (1989) Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome, Science 244, 359-362.
    • (1989) Science , vol.244 , pp. 359-362
    • Choo, Q.-L.1    Kuo, G.2    Weiner, A.J.3    Bradley, D.W.4    Houghton, M.5
  • 3
    • 0026517752 scopus 로고
    • Participation of tyrosine phosphorylation in the cytopathic effect of human immunodeficiency virus-1
    • Cohen, D. I., Tani, Y., Tian, H., Boone, E., Samelson, L. E. & Lane, H. C. (1992) Participation of tyrosine phosphorylation in the cytopathic effect of human immunodeficiency virus-1, Science 256, 542-545.
    • (1992) Science , vol.256 , pp. 542-545
    • Cohen, D.I.1    Tani, Y.2    Tian, H.3    Boone, E.4    Samelson, L.E.5    Lane, H.C.6
  • 4
    • 0025034748 scopus 로고
    • The HIV protein, gp120, activates nuclear protein kinase C in nuclei from lymphocytes and brain
    • Zorn, N. E., Weill, C. L. & Russell, D. H. (1990) The HIV protein, gp120, activates nuclear protein kinase C in nuclei from lymphocytes and brain, Biochem. Biophys. Res. Commun. 166, 1133-1139.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1133-1139
    • Zorn, N.E.1    Weill, C.L.2    Russell, D.H.3
  • 6
    • 0027409855 scopus 로고
    • Hepatitis B virus transactivator Hbx uses a tumour promoter signalling pathway
    • Kekule, A. S., Lauer, U., Weiss, L., Luber, B. & Hofschneider, P. H. (1993) Hepatitis B virus transactivator Hbx uses a tumour promoter signalling pathway, Nature 361, 742-745.
    • (1993) Nature , vol.361 , pp. 742-745
    • Kekule, A.S.1    Lauer, U.2    Weiss, L.3    Luber, B.4    Hofschneider, P.H.5
  • 8
    • 0026069052 scopus 로고
    • Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming protein
    • Petti, L., Nilson, L. A. & DiMaio, D. (1991) Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming protein, EMBO J. 10, 845-855.
    • (1991) EMBO J. , vol.10 , pp. 845-855
    • Petti, L.1    Nilson, L.A.2    DiMaio, D.3
  • 9
    • 0028338904 scopus 로고
    • Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein
    • Meyer, A. N., Xu, Y.-F., Webster, M. K., Smith, A. E. & Donoghue, D. J. (1994) Cellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein, Proc. Natl Acad. Sci. USA 91, 4634-4638.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4634-4638
    • Meyer, A.N.1    Xu, Y.-F.2    Webster, M.K.3    Smith, A.E.4    Donoghue, D.J.5
  • 10
    • 0026683466 scopus 로고
    • Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells
    • Petti, L. & DiMaio, D. (1992) Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells. Proc. Natl Acad. Sci. USA 89, 6736-6740.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6736-6740
    • Petti, L.1    DiMaio, D.2
  • 14
    • 0025249362 scopus 로고
    • Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups
    • Miller, R. H. & Purcell, R. H. (1990) Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups. Proc. Natl Acad. Sci. USA 87, 2057-2061.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2057-2061
    • Miller, R.H.1    Purcell, R.H.2
  • 15
    • 0027176287 scopus 로고
    • NS3 is a serine protease required for processing of Hepatitis C virus polyprotein
    • Tomei, L., Failla, C., Santolini, E., DeFrancesco, R. & LaMonica, N. (1993) NS3 is a serine protease required for processing of Hepatitis C virus polyprotein. J. Virol. 67, 4017-4026.
    • (1993) J. Virol. , vol.67 , pp. 4017-4026
    • Tomei, L.1    Failla, C.2    Santolini, E.3    DeFrancesco, R.4    LaMonica, N.5
  • 16
    • 0025171037 scopus 로고
    • Cleavage of dengue virus NS1-NS2A requires an octapeptide sequence at the C terminus of NS1
    • Hori, H. & Lai, C. J. (1990) Cleavage of dengue virus NS1-NS2A requires an octapeptide sequence at the C terminus of NS1, J. Virol. 64, 4573-4577.
    • (1990) J. Virol. , vol.64 , pp. 4573-4577
    • Hori, H.1    Lai, C.J.2
  • 18
    • 0027301548 scopus 로고
    • Localisation of hepatitis C virus proteins in infected liver tissue by immunofluorescence
    • Blight, K., Lesniewski, R., LaBrooy, J., Trowbridge, R. & Gowans, E. (1993) Localisation of hepatitis C virus proteins in infected liver tissue by immunofluorescence, Gastroenterol. Jpn. 28, 55-58.
    • (1993) Gastroenterol. Jpn. , vol.28 , pp. 55-58
    • Blight, K.1    Lesniewski, R.2    LaBrooy, J.3    Trowbridge, R.4    Gowans, E.5
  • 19
    • 0028894711 scopus 로고
    • Study on reliability of commercially available Hepatitis C virus antibody tests
    • Feucht, H., Zöllner, B., Polywka, S. & Laufs, R. (1995) Study on reliability of commercially available Hepatitis C virus antibody tests, J. Clin. Microbiol. 33, 620-624.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 620-624
    • Feucht, H.1    Zöllner, B.2    Polywka, S.3    Laufs, R.4
  • 20
    • 0019332528 scopus 로고
    • Studies on functional domains of the regulatory subunit of bovine heart adenosine 3′,5′-monophosphale-dependent protein kinase
    • Flockhart, D. A., Watterson, D. M. & Corbin, J. D. (1980) Studies on functional domains of the regulatory subunit of bovine heart adenosine 3′,5′-monophosphale-dependent protein kinase, J. Biol. Chem. 255, 4435-4440.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4435-4440
    • Flockhart, D.A.1    Watterson, D.M.2    Corbin, J.D.3
  • 21
    • 0015217645 scopus 로고
    • Purification and characterisation of a protein inhibitor of adenosine 3′,5′-monophosphate-dependent protein kinases
    • Walsh, D. A., Ashby, C. D., Gonzalez, C., Calkins, D., Fischer, E. H. & Krebs, E. G. (1971) Purification and characterisation of a protein inhibitor of adenosine 3′,5′-monophosphate-dependent protein kinases, J. Biol. Chem. 246, 1977-1985.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1977-1985
    • Walsh, D.A.1    Ashby, C.D.2    Gonzalez, C.3    Calkins, D.4    Fischer, E.H.5    Krebs, E.G.6
  • 23
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinated impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer, B. J., Jackson, P. K., Van Etten, R. A. & Baltimore, D. (1992) Point mutations in the abl SH2 domain coordinated impair phosphotyrosine binding in vitro and transforming activity in vivo, Mol. Cell. Biol. 12, 609-618.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 24
    • 0022364057 scopus 로고
    • Identification of an inhibitory region of the heat-stable protein inhibitor of the cAMP-dependent protein kinase
    • Scott, J. D., Fischer, E. H., Demaille, J. G. & Krebs, F. G. (1985) Identification of an inhibitory region of the heat-stable protein inhibitor of the cAMP-dependent protein kinase, Proc. Natl Acad. Sci. USA 82, 4379-4383.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4379-4383
    • Scott, J.D.1    Fischer, E.H.2    Demaille, J.G.3    Krebs, F.G.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0023025483 scopus 로고
    • Phorbol ester binding and activation of protein kinase C on Triton X-100 mixed micelles containing phosphatidylserine
    • Hannun, Y. A. & Bell, R. M. (1986) Phorbol ester binding and activation of protein kinase C on Triton X-100 mixed micelles containing phosphatidylserine, J. Biol. Chem. 261, 9341-9347.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9341-9347
    • Hannun, Y.A.1    Bell, R.M.2
  • 27
    • 0023019104 scopus 로고
    • Histone H1 kinase in exponential and synchronous populations of Chinese hamster fibroblasts
    • Woodford, T. A. & Pardee, A. B. (1986) Histone H1 kinase in exponential and synchronous populations of Chinese hamster fibroblasts, J. Biol. Chem. 261, 4669-4676.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4669-4676
    • Woodford, T.A.1    Pardee, A.B.2
  • 28
    • 0023662524 scopus 로고
    • Limited proteolysis alters the photo-affinity labeling of adenosine 3′,5′-monophosphate dependent protein kinase II with 8-azidoadenosine 3′,5′-monophosphate
    • Bubis, J. & Taylor, S. S. (1987) Limited proteolysis alters the photo-affinity labeling of adenosine 3′,5′-monophosphate dependent protein kinase II with 8-azidoadenosine 3′,5′-monophosphate, Biochemistry 26, 5997-6004.
    • (1987) Biochemistry , vol.26 , pp. 5997-6004
    • Bubis, J.1    Taylor, S.S.2
  • 30
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven, J. & Dernick, R. (1985) Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining, Electrophoresis 6, 103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 31
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • Krebs, F. G. & Beavo, J. A. (1979) Phosphorylation-dephosphorylation of enzymes, Annu. Rev. Biochem. 48, 923-959.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 923-959
    • Krebs, F.G.1    Beavo, J.A.2
  • 32
    • 0017406326 scopus 로고
    • Isolation and properties of the rabbit skeletal muscle protein inhibitor of adenosine 3′,5′-monophosphate dependent protein kinases
    • Demaille, J. G., Peters, K. A. & Fischcher, E. H. (1977) Isolation and properties of the rabbit skeletal muscle protein inhibitor of adenosine 3′,5′-monophosphate dependent protein kinases, Biochemistry 16, 3080-3086.
    • (1977) Biochemistry , vol.16 , pp. 3080-3086
    • Demaille, J.G.1    Peters, K.A.2    Fischcher, E.H.3
  • 33
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. (1952) The determination of enzyme inhibitor constants. Biochem. J. 55, 170-171.
    • (1952) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 34
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden, A. (1974) A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors, Biochem. J. 137, 143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 35
    • 0020567474 scopus 로고
    • The kinetics of tyrosine phosphorylation by the purified epidermal growth factor receptor kinase of A-431 cells
    • Erneux, C., Cohen, S. & Garbers, D. L. (1983) The kinetics of tyrosine phosphorylation by the purified epidermal growth factor receptor kinase of A-431 cells, J. Biol. Chem. 258, 4137-4142.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4137-4142
    • Erneux, C.1    Cohen, S.2    Garbers, D.L.3
  • 36
    • 0024401290 scopus 로고
    • Protein kinase inhibitor-(6-22)-amide peptide analogs with standard and nonstandard amino acid substitutions for phenylalanine10
    • Glass, D. B., Lundquist, L. J., Katz, B. M. & Walsh, D. A. (1989) Protein kinase inhibitor-(6-22)-amide peptide analogs with standard and nonstandard amino acid substitutions for phenylalanine10, J. Biol. Chem. 264, 14579-14584.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14579-14584
    • Glass, D.B.1    Lundquist, L.J.2    Katz, B.M.3    Walsh, D.A.4
  • 37
    • 0025088506 scopus 로고
    • Specifities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function
    • Smith, M. K., Colbran, R. J. & Soderling, T. R. (1990) Specifities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function, J. Biol. Chem. 265, 1837-1840.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1837-1840
    • Smith, M.K.1    Colbran, R.J.2    Soderling, T.R.3
  • 38
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus spccifity motifs: Tabulation
    • Pearson, R. B. & Kemp, B. E. (1991) Protein kinase phosphorylation site sequences and consensus spccifity motifs: tabulation, Methods Enzymol. 200, 62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 39
    • 0025049134 scopus 로고
    • Control of src kinase activity by activators, inhibitors and substrate chaperones
    • Abdel-Ghany, M., El-Gendy, K., Zhang, S. & Racker, E. (1990) Control of src kinase activity by activators, inhibitors and substrate chaperones, Proc. Natl Acad. Sci. USA 87, 7061-7065.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 7061-7065
    • Abdel-Ghany, M.1    El-Gendy, K.2    Zhang, S.3    Racker, E.4
  • 40
    • 0028247283 scopus 로고
    • Regulation of epidermal growth factor receptor kinase activity by polyions
    • Borowski, P., Medem, S. & Laufs, R. (1994) Regulation of epidermal growth factor receptor kinase activity by polyions, J. Biochem. 115, 825-829.
    • (1994) J. Biochem. , vol.115 , pp. 825-829
    • Borowski, P.1    Medem, S.2    Laufs, R.3
  • 41
    • 0025874473 scopus 로고
    • Heparin stimulates epidermal growth factor receptor-mediated phosphorylation of tyrosine and threonine residues
    • Revis-Gupta, S., Abdel-Ghany, M., Koland, J. & Racker, E. (1991) Heparin stimulates epidermal growth factor receptor-mediated phosphorylation of tyrosine and threonine residues, Proc. Natl Acad. Sci. USA 88, 5954-5958.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5954-5958
    • Revis-Gupta, S.1    Abdel-Ghany, M.2    Koland, J.3    Racker, E.4
  • 46
    • 0028049245 scopus 로고
    • Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity
    • Gotoh, N., Tojo, A., Muroya, K., Hashimoto, Y., Hattori, S., Nakamura, S., Ta-kenawa, T., Yazaki, Y. & Shibuya, M. (1994) Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity, Proc. Natl Acad. Sci. USA 91, 167-171.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 167-171
    • Gotoh, N.1    Tojo, A.2    Muroya, K.3    Hashimoto, Y.4    Hattori, S.5    Nakamura, S.6    Ta-kenawa, T.7    Yazaki, Y.8    Shibuya, M.9
  • 47
    • 0018798540 scopus 로고
    • The protein inhibitor of adeno-sinc 3′,5′-monophosphate-dependent protein kinases
    • Demaille, J. G., Ferraz, C. & Fischer, E. H. (1979) The protein inhibitor of adeno-sinc 3′,5′-monophosphate-dependent protein kinases, Biochim. Biophys. Acta 586, 374-383.
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 374-383
    • Demaille, J.G.1    Ferraz, C.2    Fischer, E.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.