메뉴 건너뛰기




Volumn 18, Issue 9, 1998, Pages 5208-5218

Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: Molecular mechanisms of kinase regulation

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON; PROTEIN KINASE;

EID: 17144463221     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.9.5208     Document Type: Article
Times cited : (564)

References (79)
  • 1
    • 0028898609 scopus 로고
    • Epidemiology of hepatitis C in the west
    • Alter, M. 1995. Epidemiology of hepatitis C in the west. Semin. Liver Dis. 15:5-14.
    • (1995) Semin. Liver Dis. , vol.15 , pp. 5-14
    • Alter, M.1
  • 2
    • 0029122270 scopus 로고
    • Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase
    • Barber, G. N., R. Jagus, E. F. Meurs, A. G. Hovanessian, and M. G. Katze. 1995. Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase. J. Biol. Chem. 270:17423-17428.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17423-17428
    • Barber, G.N.1    Jagus, R.2    Meurs, E.F.3    Hovanessian, A.G.4    Katze, M.G.5
  • 3
    • 0028211253 scopus 로고
    • The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties
    • Barber, G. N., S. Thompson, T. G. Lee, T. Strom, R. Jagus, A. Darveau, and M. G. Katze. 1994. The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties. Proc. Natl. Acad. Sci. USA 91:4278-4282.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4278-4282
    • Barber, G.N.1    Thompson, S.2    Lee, T.G.3    Strom, T.4    Jagus, R.5    Darveau, A.6    Katze, M.G.7
  • 4
    • 0029061555 scopus 로고
    • Mutants of the RNA-dependent protein kinase (PKR) lacking double- Stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation
    • Barber, G. N., M. Wambach, S. Thompson, R. Jagus, and M. G. Katze. 1995. Mutants of the RNA-dependent protein kinase (PKR) lacking double- stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation. Mol. Cell. Biol. 15:3138-3146.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3138-3146
    • Barber, G.N.1    Wambach, M.2    Thompson, S.3    Jagus, R.4    Katze, M.G.5
  • 6
    • 0000884978 scopus 로고
    • Using the two-hybrid system to detect protein-protein interactions
    • D. A. Hartley (ed.). Oxford University Press, Oxford, England
    • Bartel, P. L., C.-T. Chien, R. Sternglanz, and S. Fields. 1993. Using the two-hybrid system to detect protein-protein interactions, p. 153-179. In D. A. Hartley (ed.), Cellular interactions in development: a practical approach. Oxford University Press, Oxford, England.
    • (1993) Cellular Interactions in Development: A Practical Approach , pp. 153-179
    • Bartel, P.L.1    Chien, C.-T.2    Sternglanz, R.3    Fields, S.4
  • 7
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirant, M., C. Neuveut, R. F. Chun, S. M. Smith, C. E. Samuel, A. Gatignol, and K.-T. Jeang. 1997. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16:611-624.
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirant, M.1    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.-T.7
  • 8
    • 0030941094 scopus 로고    scopus 로고
    • Nonstructural protein 3 of hepatitis C virus blocks the distribution of free catalytic subunit of cyclic AMP-dependent protein kinase
    • Borowski, P., K. Oehlmann, M. Heiland, and R. Laufs. 1997. Nonstructural protein 3 of hepatitis C virus blocks the distribution of free catalytic subunit of cyclic AMP-dependent protein kinase. J. Virol. 71:2838-2843.
    • (1997) J. Virol. , vol.71 , pp. 2838-2843
    • Borowski, P.1    Oehlmann, K.2    Heiland, M.3    Laufs, R.4
  • 9
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution structure between the interferon-induced double-stranded RNA-activated protein kinase and HIV-1 transactivating region RNA
    • Carpick, B. W., V. Graziano, D. Schneider, R. K. Maitra, X. Lee, and B. R. G. Williams. 1997. Characterization of the solution structure between the interferon-induced double-stranded RNA-activated protein kinase and HIV-1 transactivating region RNA. J. Biol. Chem. 272:9510-9516.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9510-9516
    • Carpick, B.W.1    Graziano, V.2    Schneider, D.3    Maitra, R.K.4    Lee, X.5    Williams, B.R.G.6
  • 10
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single-stranded phages
    • J. K. Setlow (ed.). Plenum Press, New York, N.Y.
    • Cesareni, G., and J. A. H. Murray. 1987. Plasmid vectors carrying the replication origin of filamentous single-stranded phages, p. 135-154. In J. K. Setlow (ed.), Genetic engineering: principles and methods. Plenum Press, New York, N.Y.
    • (1987) Genetic Engineering: Principles and Methods , pp. 135-154
    • Cesareni, G.1    Murray, J.A.H.2
  • 11
    • 0031901556 scopus 로고    scopus 로고
    • Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene
    • Chang, J., S.-H. Yang, Y.-G. Cho, S. B. Hwang, Y. S. Hahn, and Y. C. Sung. 1998, Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene. J. Virol. 72:3060-3065.
    • (1998) J. Virol. , vol.72 , pp. 3060-3065
    • Chang, J.1    Yang, S.-H.2    Cho, Y.-G.3    Hwang, S.B.4    Hahn, Y.S.5    Sung, Y.C.6
  • 12
    • 0031050892 scopus 로고    scopus 로고
    • Pretreatment virus load and multiple amino acid substitutions in the interferon sensitivity-determining region predict the outcome of interferon treatment in patients with chronic genotype 1b hepatitis C virus infection
    • Chayama, K., A. Tsubota, M. Kobayashi, K. Okamoto, M. Hashimoto, Y. Miyano, H. Koike, I. Koida, Y. Arase, S. Saitoh, Y. Suzuki, N. Murashima, K. Ikeda, and H. Kumada. 1997. Pretreatment virus load and multiple amino acid substitutions in the interferon sensitivity-determining region predict the outcome of interferon treatment in patients with chronic genotype 1b hepatitis C virus infection. Hepatology 25:745-749.
    • (1997) Hepatology , vol.25 , pp. 745-749
    • Chayama, K.1    Tsubota, A.2    Kobayashi, M.3    Okamoto, K.4    Hashimoto, M.5    Miyano, Y.6    Koike, H.7    Koida, I.8    Arase, Y.9    Saitoh, S.10    Suzuki, Y.11    Murashima, N.12    Ikeda, K.13    Kumada, H.14
  • 13
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • Clemens, M. J., and A. Elia. 1997. The double-stranded RNA-dependent protein kinase PKR: structure and function. J. Interferon Cytokine Res. 17:503-524.
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 14
    • 13344261388 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of animal lentivirus infections
    • Clements, J. E., and M. C. Zink. 1996. Molecular biology and pathogenesis of animal lentivirus infections. Clin. Microbiol. Rev. 9:100-117.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 100-117
    • Clements, J.E.1    Zink, M.C.2
  • 16
    • 0029785474 scopus 로고    scopus 로고
    • The kinase insert domain of interferon-induced protein kinase PKR is required for activity but not for interaction with the pseudosubstrate K3L
    • Craig, A. W., G. P. Cosentino, O. Donzé, and N. Sonenberg. 1996. The kinase insert domain of interferon-induced protein kinase PKR is required for activity but not for interaction with the pseudosubstrate K3L. J. Biol. Chem. 271:24526-24533.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24526-24533
    • Craig, A.W.1    Cosentino, G.P.2    Donzé, O.3    Sonenberg, N.4
  • 17
    • 0027942956 scopus 로고
    • Hepatitis C: Progress and problems
    • Cuthbert, J. A. 1994. Hepatitis C: progress and problems. Clin. Microbiol. Rev. 7:505-532.
    • (1994) Clin. Microbiol. Rev. , vol.7 , pp. 505-532
    • Cuthbert, J.A.1
  • 18
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der, S. D., Y.-L. Yang, C. Weissman, and B. R. G. Williams. 1997. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 94:3279-3283.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.-L.2    Weissman, C.3    Williams, B.R.G.4
  • 19
    • 0027324505 scopus 로고
    • Mammalian eukaryotic initiation factor eIF2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast
    • Dever, T. E., J.-J. Chen, G. N. Barber, A. M. Cigan, L. Feng, T. F. Donahue, I. M. London, M. G. Katze, and A. G. Hinnebusch. 1993. Mammalian eukaryotic initiation factor eIF2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. Proc. Natl. Acad. Sci. USA 90:4616-4620.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4616-4620
    • Dever, T.E.1    Chen, J.-J.2    Barber, G.N.3    Cigan, A.M.4    Feng, L.5    Donahue, T.F.6    London, I.M.7    Katze, M.G.8    Hinnebusch, A.G.9
  • 20
    • 0028947963 scopus 로고
    • Hepatitis C and hepatocellular carcinoma
    • Di Bisceglie, A. M. 1995. Hepatitis C and hepatocellular carcinoma. Semin. Liver Dis. 15:64-69.
    • (1995) Semin. Liver Dis. , vol.15 , pp. 64-69
    • Di Bisceglie, A.M.1
  • 24
    • 0345164384 scopus 로고    scopus 로고
    • Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon- Induced protein kinase
    • Gale, M., Jr., and M. G. Katze. 1998. Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon- induced protein kinase. Pharmacol. Ther. 78:29-46.
    • (1998) Pharmacol. Ther. , vol.78 , pp. 29-46
    • Gale Jr., M.1    Katze, M.G.2
  • 25
    • 8944219769 scopus 로고    scopus 로고
    • IPK and vaccinia virus K3L is mediated by unique domains: Implications for kinase regulation
    • IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation. Mol. Cell. Biol. 16:4172-4181.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4172-4181
    • Gale Jr., M.1    Tan, S.-L.2    Wambach, M.3    Katze, M.G.4
  • 27
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale, M., Jr., M. J. Korth, N. M. Tang, S. L. Tan, D. A. Hopkins, T. E. Dever, S. J. Polyak, D. R. Gretch, and M. G. Katze. 1997. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230:217-227.
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale Jr., M.1    Korth, M.J.2    Tang, N.M.3    Tan, S.L.4    Hopkins, D.A.5    Dever, T.E.6    Polyak, S.J.7    Gretch, D.R.8    Katze, M.G.9
  • 28
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 29
    • 0031056851 scopus 로고    scopus 로고
    • The interferon sensitivity determining region: All hepatitis C virus isolates are not the same
    • Herion, D., and J. Hoofnagle. 1997. The interferon sensitivity determining region: all hepatitis C virus isolates are not the same. Hepatology 25:769- 771.
    • (1997) Hepatology , vol.25 , pp. 769-771
    • Herion, D.1    Hoofnagle, J.2
  • 30
    • 1842327408 scopus 로고    scopus 로고
    • Mutations in the NS5A gene of hepatitis C virus in North American patients infected with HCV genotype 1a or 1b
    • Hofgärtner, W. T., S. J. Polyak, D. Sullivan, R. L. Carithers, Jr., and D. R. Gretch. 1997. Mutations in the NS5A gene of hepatitis C virus in North American patients infected with HCV genotype 1a or 1b. J. Med. Virol. 53:118-126.
    • (1997) J. Med. Virol. , vol.53 , pp. 118-126
    • Hofgärtner, W.T.1    Polyak, S.J.2    Sullivan, D.3    Carithers Jr., R.L.4    Gretch, D.R.5
  • 31
    • 0025862146 scopus 로고
    • Molecular biology of the hepatitis C viruses: Implications for diagnosis, development and control of viral disease
    • Houghton, M., A. Weiner, J. Han, G. Kuo, and Q.-L. Choo. 1991. Molecular biology of the hepatitis C viruses: implications for diagnosis, development and control of viral disease. Hepatology 14:381-388.
    • (1991) Hepatology , vol.14 , pp. 381-388
    • Houghton, M.1    Weiner, A.2    Han, J.3    Kuo, G.4    Choo, Q.-L.5
  • 32
    • 0029644725 scopus 로고
    • Repressor fusions as a tool to study protein-protein interactions
    • Hu, J. C. 1995. Repressor fusions as a tool to study protein-protein interactions. Structure 3:431-433.
    • (1995) Structure , vol.3 , pp. 431-433
    • Hu, J.C.1
  • 33
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: Analysis with lambda repressor-GCN4 leucine zipper fusions
    • Hu, J. C., E. K. O'Shea, P. S. Kim, and R. T. Saur. 1990. Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science 250:1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Saur, R.T.4
  • 34
    • 0030784599 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein is phosphorylated in vitro by a stably bound protein kinase from HeLa cells and by cAMP-dependent protein kinase A-alpha catalytic subunit
    • Ide, Y., A. Tanimoto, Y. Sasaguri, and R. Padmanabhan. 1997. Hepatitis C virus NS5A protein is phosphorylated in vitro by a stably bound protein kinase from HeLa cells and by cAMP-dependent protein kinase A-alpha catalytic subunit. Gene 201:151-158.
    • (1997) Gene , vol.201 , pp. 151-158
    • Ide, Y.1    Tanimoto, A.2    Sasaguri, Y.3    Padmanabhan, R.4
  • 37
    • 0026909526 scopus 로고
    • The war against the interferon-induced dsRNA-activated protein kinase: Can viruses win?
    • Katze, M. G. 1992. The war against the interferon-induced dsRNA-activated protein kinase: can viruses win? J. Interferon Res. 12:241-248.
    • (1992) J. Interferon Res. , vol.12 , pp. 241-248
    • Katze, M.G.1
  • 39
    • 0030927170 scopus 로고    scopus 로고
    • Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF-2α
    • Kawagishi-Kobayashi, M., J. B. Silverman, T. L. Ung, and T. E. Dever. 1997. Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF-2α. Mol. Cell. Biol. 17:4146-4158.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4146-4158
    • Kawagishi-Kobayashi, M.1    Silverman, J.B.2    Ung, T.L.3    Dever, T.E.4
  • 40
    • 18344402297 scopus 로고    scopus 로고
    • Mutations of hepatitis C virus 1b NS5A 2209-2248 amino acid sequence do not predict the response to recombinant interferon-alpha therapy in French patients
    • Khorsi, H., S. Castelain, A. Wyseur, J. Izopet, V. Canva, A. Rombout, D. Capron, J.-P. Capron, F. Lunel, L. Stuyver, and G. Duverlie. 1997. Mutations of hepatitis C virus 1b NS5A 2209-2248 amino acid sequence do not predict the response to recombinant interferon-alpha therapy in French patients. J. Hepatol. 27:72-77.
    • (1997) J. Hepatol. , vol.27 , pp. 72-77
    • Khorsi, H.1    Castelain, S.2    Wyseur, A.3    Izopet, J.4    Canva, V.5    Rombout, A.6    Capron, D.7    Capron, J.-P.8    Lunel, F.9    Stuyver, L.10    Duverlie, G.11
  • 42
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas, A. E., S. Roy, G. N. Barber, M. G. Katze, and N. Sonenberg. 1992. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257:1685-1689.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 43
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB
    • Kumar, A., J. Haque, J. Lacoste, J. Hiscott, and B. R. G. Williams. 1994. Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB. Proc. Natl. Acad. Sci. USA 91:6288- 6292.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6288-6292
    • Kumar, A.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Williams, B.R.G.5
  • 44
    • 17444449609 scopus 로고    scopus 로고
    • Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: Role of IRF-1 and NF-κB
    • Kumar, A., Y.-L. Yang, V. Flati, S. Der, S. Kadereit. A. Deb, J. Haque, L. Reis, C. Weissmann, and B. R. G. Williams. 1997. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-κB. EMBO J. 16:406-416.
    • (1997) EMBO J. , vol.16 , pp. 406-416
    • Kumar, A.1    Yang, Y.-L.2    Flati, V.3    Der, S.4    Kadereit, S.5    Deb, A.6    Haque, J.7    Reis, L.8    Weissmann, C.9    Williams, B.R.G.10
  • 45
    • 0031042869 scopus 로고    scopus 로고
    • Analysis of genotypes and amino acid residues 2209 to 2248 of the NS5A region of hepatitis C virus in relation to the response to interferon-β therapy
    • Kurosaki, M., N. Enomoto, T. Murakami, I. Sakuma, Y. Asahina, C. Yamamoto, T. Ikeda, S. Tozuka, N. Izumi, F. Marumo, and C. Sato. 1997. Analysis of genotypes and amino acid residues 2209 to 2248 of the NS5A region of hepatitis C virus in relation to the response to interferon-β therapy. Hepatology 25:750-753.
    • (1997) Hepatology , vol.25 , pp. 750-753
    • Kurosaki, M.1    Enomoto, N.2    Murakami, T.3    Sakuma, I.4    Asahina, Y.5    Yamamoto, C.6    Ikeda, T.7    Tozuka, S.8    Izumi, N.9    Marumo, F.10    Sato, C.11
  • 47
    • 0345064267 scopus 로고
    • Monoclonal antibodies to interferon induced 68,000 Mr protein and their use for the detection of double-stranded RNA dependent protein kinase in human cells
    • Laurent, A. G., B. Krust, J. Galabru, J. Svab, and A. G. Hovanessian. 1985. Monoclonal antibodies to interferon induced 68,000 Mr protein and their use for the detection of double-stranded RNA dependent protein kinase in human cells. Proc. Natl. Acad. Sci. USA 82:4341-4345.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4341-4345
    • Laurent, A.G.1    Krust, B.2    Galabru, J.3    Svab, J.4    Hovanessian, A.G.5
  • 48
    • 0027949937 scopus 로고
    • The 58,000-Dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee, T. G., N. Tang, S. Thompson, J. Miller, and M. G. Katze. 1994. The 58,000-Dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol. Cell. Biol. 14:2331-2342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 49
    • 0028929014 scopus 로고
    • Epidemiology of hepatitis C in the east
    • Mansell, C., and S. Locarnini. 1995. Epidemiology of hepatitis C in the east. Semin. Liver Dis. 15:15-32.
    • (1995) Semin. Liver Dis. , vol.15 , pp. 15-32
    • Mansell, C.1    Locarnini, S.2
  • 51
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • J. Hershey, M. Mathews, and N. Sonenberg (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, N.Y.
    • Merrick, W. C., and J. W. B. Hershey. 1996. The pathway and mechanism of eukaryotic protein synthesis, p. 31-70. In J. Hershey, M. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, N.Y.
    • (1996) Translational Control , pp. 31-70
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 52
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs, E., K. L. Chong, J. Galabru, N. Thomas, I. Kerr, B. R. G. Williams, and A. G. Hovanessian. 1990. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62:379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.L.2    Galabru, J.3    Thomas, N.4    Kerr, I.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 53
    • 0026929934 scopus 로고
    • Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phos- Phorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth
    • Meurs, E., Y. Watanabe, G. N. Barber, M. G. Katze, K. L. Chong, B. R. G. Williams, and A. G. Hovanessian. 1992. Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phos- phorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth. J. Virol. 66:5805-5814.
    • (1992) J. Virol. , vol.66 , pp. 5805-5814
    • Meurs, E.1    Watanabe, Y.2    Barber, G.N.3    Katze, M.G.4    Chong, K.L.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 54
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs, E. F., J. Galabru, G. N. Barber, M. G. Katze, and A. G. Hovanessian. 1993. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 90:232-236.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 232-236
    • Meurs, E.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 55
    • 0030030724 scopus 로고    scopus 로고
    • Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells
    • Ortega, L. G., M. D. McCotter, G. L. Henry, S. J. McCormack, D. C. Thomis, and C. E. Samuel. 1996. Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells. Virology 215:31-39.
    • (1996) Virology , vol.215 , pp. 31-39
    • Ortega, L.G.1    McCotter, M.D.2    Henry, G.L.3    McCormack, S.J.4    Thomis, D.C.5    Samuel, C.E.6
  • 56
    • 0028241859 scopus 로고
    • Role of the amino-lerminal residues of the interferon-induced protein kinase in its activation by double- Stranded RNA and heparin
    • Patel, R. C-. P. Stanton, and G. C. Sen. 1994. Role of the amino-lerminal residues of the interferon-induced protein kinase in its activation by double- stranded RNA and heparin. J. Biol. Chem. 269:18593-18598.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18593-18598
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 57
    • 0029841348 scopus 로고    scopus 로고
    • Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties
    • Patel. R. C., P. Stanton, and G. C. Sen. 1996. Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties. J. Biol. Chem. 271:25657-25663.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 58
    • 0031958419 scopus 로고    scopus 로고
    • Evolution of hepatitis C virus quasispecies in hypervariable region 1 and the putative interieron sensitivity-determining region during interferon therapy and natural infection
    • Polyak, S. J., S. McCardle, S.-L. Lui, D. Sullivan, M. Chung, W. T. Hofgärtner, R. Carithers, B. J. McMahon, J. I. Mullins, L. Corey, and D. R. Gretch. 1998. Evolution of hepatitis C virus quasispecies in hypervariable region 1 and the putative interieron sensitivity-determining region during interferon therapy and natural infection. J. Virol. 72:4288-4296.
    • (1998) J. Virol. , vol.72 , pp. 4288-4296
    • Polyak, S.J.1    McCardle, S.2    Lui, S.-L.3    Sullivan, D.4    Chung, M.5    Hofgärtner, W.T.6    Carithers, R.7    McMahon, B.J.8    Mullins, J.I.9    Corey, L.10    Gretch, D.R.11
  • 59
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • Proud, C. G. 1995. PKR: a new name and new roles. Trends Biochem. Sci. 20:241-246.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 60
    • 0030589563 scopus 로고    scopus 로고
    • Suppression of apoptotic cell death by hepatitis C virus core protein
    • Ray. R. B., K. Meyer, and R. Ray. 1996. Suppression of apoptotic cell death by hepatitis C virus core protein. Virology 226:176-182.
    • (1996) Virology , vol.226 , pp. 176-182
    • Ray, R.B.1    Meyer, K.2    Ray, R.3
  • 61
    • 8944262349 scopus 로고    scopus 로고
    • Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype
    • Ray, R. B., L. M. Lagging, K. Meyer, and R. Ray. 1996. Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype. J. Virol. 70:4438-4443.
    • (1996) J. Virol. , vol.70 , pp. 4438-4443
    • Ray, R.B.1    Lagging, L.M.2    Meyer, K.3    Ray, R.4
  • 62
    • 0030828466 scopus 로고    scopus 로고
    • Phosphorylation of the hepatitis C virus NS5A protein in vitro and in vivo: Properties of the NS5A-associated kinase
    • Reed, K. E., J. Xu, and C. M. Rice. 1997. Phosphorylation of the hepatitis C virus NS5A protein in vitro and in vivo: properties of the NS5A-associated kinase. J. Virol. 71:7187-7197.
    • (1997) J. Virol. , vol.71 , pp. 7187-7197
    • Reed, K.E.1    Xu, J.2    Rice, C.M.3
  • 63
    • 0028924758 scopus 로고
    • Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in Saccharomyces cerevisiae
    • Romano, P. R., S. R, Green, G. N. Barber, M. B. Mathews, and A. G. Hinnebusch. 1995. Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:365-378.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 365-378
    • Romano, P.R.1    Green, S.R.2    Barber, G.N.3    Mathews, M.B.4    Hinnebusch, A.G.5
  • 64
    • 0031550806 scopus 로고    scopus 로고
    • Sensitization to Fas-mediated apoptosis by hepatitis C virus core protein
    • Ruggieri, A., T. Harada, Y. Matsuura, and T. Miyamura. 1997. Sensitization to Fas-mediated apoptosis by hepatitis C virus core protein. Virology 229: 68-76.
    • (1997) Virology , vol.229 , pp. 68-76
    • Ruggieri, A.1    Harada, T.2    Matsuura, Y.3    Miyamura, T.4
  • 65
    • 0029063640 scopus 로고
    • Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells
    • Sakamuro, D., T. Furukawa, and T. Takegami. 1995. Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells. J. Virol. 69:3893-3896.
    • (1995) J. Virol. , vol.69 , pp. 3893-3896
    • Sakamuro, D.1    Furukawa, T.2    Takegami, T.3
  • 67
    • 0025739093 scopus 로고
    • Antiviral actions of interferon: Interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel, C. E. 1991. Antiviral actions of interferon: interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology 183:1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 68
    • 0026739463 scopus 로고
    • The interferon system: A bird's eye view of its biochemistry
    • Sen, G. C., and P. Lengyel. 1992. The interferon system: a bird's eye view of its biochemistry. J. Biol. Chem. 267:5017-5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 69
    • 0027352378 scopus 로고
    • Interferon-induced antiviral actions and their regulation
    • Sen, G. C., and R. M. Ransohoff. 1993. Interferon-induced antiviral actions and their regulation. Adv. Virus Res. 42:57-102.
    • (1993) Adv. Virus Res. , vol.42 , pp. 57-102
    • Sen, G.C.1    Ransohoff, R.M.2
  • 70
    • 0028833484 scopus 로고
    • Evaluation of complete genome sequences and sequences of individual gene products for the clas sification of hepatitis C viruses
    • Shukla, D. D., P. A. Hoyne, and C. W. Ward. 1995. Evaluation of complete genome sequences and sequences of individual gene products for the clas sification of hepatitis C viruses. Arch. Virol. 140:1747-1761.
    • (1995) Arch. Virol. , vol.140 , pp. 1747-1761
    • Shukla, D.D.1    Hoyne, P.A.2    Ward, C.W.3
  • 71
    • 0028905430 scopus 로고
    • Variability of hepatitis C virus
    • Simmonds, P. 1995. Variability of hepatitis C virus. Hepatology 21:570-583.
    • (1995) Hepatology , vol.21 , pp. 570-583
    • Simmonds, P.1
  • 72
    • 0023806075 scopus 로고
    • Single-step purification of polypep- Tides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypep- tides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 74
    • 0029855773 scopus 로고    scopus 로고
    • The 58-kDa cellular inhibitor of the double stranded RNA-dependent protein kinase requires the tetra- Tricopeptide repeat 6 and DnaJ motifs to stimulate protein synthesis in vivo
    • Tang, N. M., C. Y. Ho, and M. G. Katze. 1996. The 58-kDa cellular inhibitor of the double stranded RNA-dependent protein kinase requires the tetra- tricopeptide repeat 6 and DnaJ motifs to stimulate protein synthesis in vivo. J. Biol. Chem. 271:28660-28666.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28660-28666
    • Tang, N.M.1    Ho, C.Y.2    Katze, M.G.3
  • 75
    • 0028978937 scopus 로고
    • Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A
    • Tanji, Y., T. Kaneko, S. Satoh, and K. Shimotohno. 1995. Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A. J. Virol. 69:3980- 3986.
    • (1995) J. Virol. , vol.69 , pp. 3980-3986
    • Tanji, Y.1    Kaneko, T.2    Satoh, S.3    Shimotohno, K.4
  • 77
    • 0028797781 scopus 로고
    • The role of the dsRNA-activated kinase, PKR, in signal transduction
    • Williams, B. R. G. 1995. The role of the dsRNA-activated kinase, PKR, in signal transduction. Semin. Virol. 6:191-202.
    • (1995) Semin. Virol. , vol.6 , pp. 191-202
    • Williams, B.R.G.1
  • 78
    • 0031056446 scopus 로고    scopus 로고
    • Mutations in the nonstructural 5A gene of European hepatitis C virus isolates and response to interferon alfa
    • Zeuzem, S., J.-H. Lee, and W. K. Roth. 1997. Mutations in the nonstructural 5A gene of European hepatitis C virus isolates and response to interferon alfa. Hepatology 25:740-744.
    • (1997) Hepatology , vol.25 , pp. 740-744
    • Zeuzem, S.1    Lee, J.-H.2    Roth, W.K.3
  • 79
    • 0031957325 scopus 로고    scopus 로고
    • Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF- Induced apoptosis
    • Zhu, N., A. Khoshan, R. Schneider, M. Matsumoto, G. Dennert, C. F. Ware, and M. C. Lai. 1998. Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF- induced apoptosis. J. Virol. 72:3691-3697.
    • (1998) J. Virol. , vol.72 , pp. 3691-3697
    • Zhu, N.1    Khoshan, A.2    Schneider, R.3    Matsumoto, M.4    Dennert, G.5    Ware, C.F.6    Lai, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.