메뉴 건너뛰기




Volumn 78, Issue 1, 1998, Pages 29-46

Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase

Author keywords

Inhibitor; Interferons; PKR; Protein kinase; Translational control; Virus

Indexed keywords

INTERFERON; PROTEIN KINASE; VIRUS PROTEIN; VIRUS RNA;

EID: 0345164384     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0163-7258(97)00165-4     Document Type: Review
Times cited : (340)

References (211)
  • 1
    • 0025288638 scopus 로고
    • Expression of cellular genes in CD4-positive lymphoid cells infected by the human immunodeficiency virus, HIV-1: Evidence for a host protein synthesis shutoff induced by cellular mRNA degradation
    • Agy M. B., Wambach M., Foy K., Katze M. G. Expression of cellular genes in CD4-positive lymphoid cells infected by the human immunodeficiency virus, HIV-1. evidence for a host protein synthesis shutoff induced by cellular mRNA degradation Virology. 177:1990;251-258.
    • (1990) Virology , vol.177 , pp. 251-258
    • Agy, M.B.1    Wambach, M.2    Foy, K.3    Katze, M.G.4
  • 2
    • 0029619153 scopus 로고
    • Interferon treatment inhibits virus replication in HIV-1- And SIV-infected CD4+ T-cells by distinct mechanisms: Evidence for decreased stability and aberrant processing of HIV-1 proteins
    • Agy M. B., Acker R. L., Sherbert C. H., Katze M. G. Interferon treatment inhibits virus replication in HIV-1- and SIV-infected CD4+ T-cells by distinct mechanisms. evidence for decreased stability and aberrant processing of HIV-1 proteins Virology. 214:1995;379-386.
    • (1995) Virology , vol.214 , pp. 379-386
    • Agy, M.B.1    Acker, R.L.2    Sherbert, C.H.3    Katze, M.G.4
  • 3
    • 0024394966 scopus 로고
    • Specific kinase inhibitory factor of vaccinia virus prevents translational inhibition in rabbit reticulocytes
    • Akkaraju G. R., Whitaker-Dowling P., Youngner J. S. Y., Jagus R. Specific kinase inhibitory factor of vaccinia virus prevents translational inhibition in rabbit reticulocytes. J. Biol. Chem. 264:1989;10321-10325.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10321-10325
    • Akkaraju, G.R.1    Whitaker-Dowling, P.2    Youngner, J.S.Y.3    Jagus, R.4
  • 4
    • 0025890062 scopus 로고
    • Early events in Epstein-Barr virus infection of human B lymphocytes
    • Alfieri C., Birkenbach M., Kief E. Early events in Epstein-Barr virus infection of human B lymphocytes. Virology. 181:1991;595-608.
    • (1991) Virology , vol.181 , pp. 595-608
    • Alfieri, C.1    Birkenbach, M.2    Kief, E.3
  • 5
    • 0026537278 scopus 로고
    • Nucleocytoplasmic transport: The influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA
    • Alonso-Caplen F. V., Nemeroff M. E., Qiu Y., Krug R. M. Nucleocytoplasmic transport. the influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA Genes Dev. 6:1992;255-267.
    • (1992) Genes Dev. , vol.6 , pp. 255-267
    • Alonso-Caplen, F.V.1    Nemeroff, M.E.2    Qiu, Y.3    Krug, R.M.4
  • 6
    • 0028898609 scopus 로고
    • Epidemiology of hepatitis C in the west
    • Alter M. Epidemiology of hepatitis C in the west. Semin. Liver Dis. 15:1995;5-14.
    • (1995) Semin. Liver Dis. , vol.15 , pp. 5-14
    • Alter, M.1
  • 7
    • 0027428105 scopus 로고
    • The mouse antiphosphotyrosine immunoreactive kinase, TIK, is indistinguishable from the double-stranded RNA-dependent, interferon-induced protein kinase, PKR
    • Baier L. J., Shors T., Shors S. T., Jacobs B. L. The mouse antiphosphotyrosine immunoreactive kinase, TIK, is indistinguishable from the double-stranded RNA-dependent, interferon-induced protein kinase, PKR. Nucl. Acids Res. 21:1993;4830-4835.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 4830-4835
    • Baier, L.J.1    Shors, T.2    Shors, S.T.3    Jacobs, B.L.4
  • 8
    • 0025746604 scopus 로고
    • Functional expression and characterization of the interferon-induced double-stranded RNA activated P68 protein kinase from Escherichia coli
    • Barber G. N., Tomita J., Hovanessian A. G., Meurs E., Katze M. G. Functional expression and characterization of the interferon-induced double-stranded RNA activated P68 protein kinase from Escherichia coli. Biochemistry. 30:1991;10356-10361.
    • (1991) Biochemistry , vol.30 , pp. 10356-10361
    • Barber, G.N.1    Tomita, J.2    Hovanessian, A.G.3    Meurs, E.4    Katze, M.G.5
  • 10
    • 85083605524 scopus 로고
    • Regulation of viral and cellular gene expression in cells infected by animal viruses, including influenza virus and human immunodeficiency virus type 1
    • Adolph, K. (ed.) Academic Press, Inc., Orlando
    • Barber, G. N., Agy, M. B. and Katze, M. G. (1994) Regulation of viral and cellular gene expression in cells infected by animal viruses, including influenza virus and human immunodeficiency virus type 1. In: Methods in Virology, pp. 141-168. Adolph, K. (ed.) Academic Press, Inc., Orlando.
    • (1994) In: Methods in Virology , pp. 141-168
    • Barber, G.N.1    Agy, M.B.2    Katze, M.G.3
  • 11
    • 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., Wambach M., Thompson S., Jagus R., Katze M. G. 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. 15:1995;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
  • 12
    • 0025815146 scopus 로고
    • Vaccinia virus-encoded eIF-2 alpha homolog abrogates the antiviral effect of interferon
    • Beattie E., Tartaglia J., Paoletti E. Vaccinia virus-encoded eIF-2 alpha homolog abrogates the antiviral effect of interferon. Virology. 183:1991;419-422.
    • (1991) Virology , vol.183 , pp. 419-422
    • Beattie, E.1    Tartaglia, J.2    Paoletti, E.3
  • 13
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • a
    • Beattie E., Denzler K. L., Tartaglia J., Perkus M. E., Paoletti E., Jacobs B. L. Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J. Virol. 69:1995;499-505. a.
    • (1995) J. Virol. , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 16
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirane M., Neuveut C., Chun R. F., Smith S. M., Samuel C. E., Gatignol A., Jeang K.-T. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16:1997;611-624.
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirane, M.1    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.-T.7
  • 17
    • 0022244511 scopus 로고
    • Mechanism of interferon action: Purification and substrate specificities of the double-stranded RNA dependent protein kinase from untreated and interferon-treated mouse fibroblasts
    • Berry M. J., Knutson G. S., Lasky S. R., Munemitsu S. M., Samuel C. E. Mechanism of interferon action. purification and substrate specificities of the double-stranded RNA dependent protein kinase from untreated and interferon-treated mouse fibroblasts J. Biol. Chem. 260:1985;11240-11247.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11240-11247
    • Berry, M.J.1    Knutson, G.S.2    Lasky, S.R.3    Munemitsu, S.M.4    Samuel, C.E.5
  • 18
    • 0020803450 scopus 로고
    • Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5
    • Bhat R. A., Thimmappaya B. Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5. Proc. Natl. Acad. Sci. USA. 80:1983;4789-4793.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4789-4793
    • Bhat, R.A.1    Thimmappaya, B.2
  • 19
    • 0022350788 scopus 로고
    • Construction and analysis of additional adenovirus substitution mutants confirm the complementation of VAI RNA function by two small RNAs encoded by Epstein-Barr virus
    • Bhat R. A., Thimmappaya B. Construction and analysis of additional adenovirus substitution mutants confirm the complementation of VAI RNA function by two small RNAs encoded by Epstein-Barr virus. J. Virol. 56:1985;750-756.
    • (1985) J. Virol. , vol.56 , pp. 750-756
    • Bhat, R.A.1    Thimmappaya, B.2
  • 21
    • 0024593159 scopus 로고
    • r protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: Implications for translational regulation
    • r protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection. implications for translational regulation J. Virol. 63:1989;2244-2252.
    • (1989) J. Virol. , vol.63 , pp. 2244-2252
    • Black, T.1    Safer, B.2    Hovanessian, A.G.3    Katze, M.G.4
  • 23
    • 0030928832 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR
    • Brand S. R., Kobayashi R., Mathews M. B. The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. J. Biol. Chem. 272:1997;8388-8395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8388-8395
    • Brand, S.R.1    Kobayashi, R.2    Mathews, M.B.3
  • 24
    • 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., Graziano V., Schneider D., Maitra R. K., Lee X., Williams B. R. G. Characterization of the solution structure between the interferon-induced double-stranded RNA-activated protein kinase and HIV-1 transactivating region RNA. J. Biol. Chem. 272:1997;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
  • 25
    • 0027163011 scopus 로고
    • Recombinant vaccinia virus K3L gene product prevents activation of dsRNA dependent eIF 2 kinase
    • Carroll K., Elroy-Stein O., Moss R., Jagus R. Recombinant vaccinia virus K3L gene product prevents activation of dsRNA dependent eIF 2 kinase. J. Biol. Chem. 268:1993;12837-12842.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12837-12842
    • Carroll, K.1    Elroy-Stein, O.2    Moss, R.3    Jagus, R.4
  • 26
    • 0027163047 scopus 로고
    • Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA
    • Chang H.-W., Jacobs B. L. Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA. Virology. 194:1993;537-547.
    • (1993) Virology , vol.194 , pp. 537-547
    • Chang, H.-W.1    Jacobs, B.L.2
  • 27
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon induced, dsRNA dependent protein kinase
    • Chang H.-W., Watson J. C., Jacobs B. L. The E3L gene of vaccinia virus encodes an inhibitor of the interferon induced, dsRNA dependent protein kinase. Proc. Natl. Acad. Sci. USA. 89:1992;4825-4829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4825-4829
    • Chang, H.-W.1    Watson, J.C.2    Jacobs, B.L.3
  • 29
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2α kinase
    • Chen J.-J., London I. M. Regulation of protein synthesis by heme-regulated eIF-2α kinase. Trends Biochem. Sci. 20:1995;105-108.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.-J.1    London, I.M.2
  • 30
    • 0025779365 scopus 로고
    • Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2α kinase
    • Chen J., Pal J., Throop M. S., Gehrke L., Kuo I., Pal J. K., Brodsky M., London I. M. Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase of rabbit reticulocytes. homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2α kinase Proc. Natl. Acad. Sci. USA. 88:1991;7729-7733.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7729-7733
    • Chen, J.1    Pal, J.2    Throop, M.S.3    Gehrke, L.4    Kuo, I.5    Pal, J.K.6    Brodsky, M.7    London, I.M.8
  • 32
    • 0026539149 scopus 로고
    • The γ34.5 gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programmed cell death in neuronal cells
    • Chou J., Roizman B. The γ34.5 gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programmed cell death in neuronal cells. Proc. Natl. Acad. Sci. USA. 89:1992;3266-3270.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3266-3270
    • Chou, J.1    Roizman, B.2
  • 33
    • 0025175643 scopus 로고
    • Translation control by the Epstein-Barr virus small RNA EBER-1: Reversal of the double-stranded RNA-induced inhibition of protein synthesis in reticulocyte lysates
    • Clarke P. A., Sharp N. A., Clemens M. J. Translation control by the Epstein-Barr virus small RNA EBER-1. reversal of the double-stranded RNA-induced inhibition of protein synthesis in reticulocyte lysates Eur. J. Biochem. 193:1990;635-641.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 635-641
    • Clarke, P.A.1    Sharp, N.A.2    Clemens, M.J.3
  • 34
    • 0025971705 scopus 로고
    • Binding of Epstein-Barr virus small RNA EBER-1 to the double-stranded RNA-induced inhibitor of protein synthesis in reticulocyte lysates
    • Clarke P. A., Schwemmle M., Schickinger J., Hilse K., Clemens M. J. Binding of Epstein-Barr virus small RNA EBER-1 to the double-stranded RNA-induced inhibitor of protein synthesis in reticulocyte lysates. Nucl. Acids Res. 19:1991;243-248.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 243-248
    • Clarke, P.A.1    Schwemmle, M.2    Schickinger, J.3    Hilse, K.4    Clemens, M.J.5
  • 35
    • 0027551185 scopus 로고
    • The small RNAs of Epstein-Barr virus
    • Clemens M. J. The small RNAs of Epstein-Barr virus. Mol. Biol. Rep. 17:1993;81-92.
    • (1993) Mol. Biol. Rep. , vol.17 , pp. 81-92
    • Clemens, M.J.1
  • 36
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinases that phosphorylate eIF-2 and eIF-2B, and their role in eukaryotic cell translational control
    • Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Press, Cold Spring Harbor
    • Clemens, M. J. (1996) Protein kinases that phosphorylate eIF-2 and eIF-2B, and their role in eukaryotic cell translational control. In: Translational Control, pp. 139-172. Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Press, Cold Spring Harbor.
    • (1996) In: Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 37
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR - Structure and function
    • in press
    • Clemens, M. J. and Elia, A. (1997) The double-stranded RNA-dependent protein kinase PKR - structure and function. J. Interferon Cytokine Res., in press.
    • (1997) J. Interferon Cytokine Res.
    • Clemens, M.J.1    Elia, A.2
  • 40
    • 0028141913 scopus 로고
    • Specific inhibition of viral protein synthesis in HIV-infected cells in response to interferon treatment
    • Coccia E. M., Krust B., Hovanessian A. G. Specific inhibition of viral protein synthesis in HIV-infected cells in response to interferon treatment. J. Biol. Chem. 269:1994;23087-23094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23087-23094
    • Coccia, E.M.1    Krust, B.2    Hovanessian, A.G.3
  • 41
    • 0014666797 scopus 로고
    • Double-stranded RNA in vaccinia virus infected cells
    • Colby C., Duesberg P. H. Double-stranded RNA in vaccinia virus infected cells. Nature. 222:1969;940-944.
    • (1969) Nature , vol.222 , pp. 940-944
    • Colby, C.1    Duesberg, P.H.2
  • 43
    • 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., Cosentino G. P., Donze O., Sonenberg N. 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. 271:1996;24526-24533.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24526-24533
    • Craig, A.W.1    Cosentino, G.P.2    Donze, O.3    Sonenberg, N.4
  • 44
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig E. A., Gambill B. D., Nelson R. J. Heat shock proteins. molecular chaperones of protein biogenesis Microbiol. Rev. 57:1993;402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 45
    • 0027347338 scopus 로고
    • Protein synthesis in different cell lines infected with orthoreovirus serotype 3: Inhibition of host-cell protein synthesis correlates with accelerated viral multiplication and cell killing
    • Danis C., Lemay G. Protein synthesis in different cell lines infected with orthoreovirus serotype 3. inhibition of host-cell protein synthesis correlates with accelerated viral multiplication and cell killing Biochem. Cell Biol. 71:1993;81-85.
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 81-85
    • Danis, C.1    Lemay, G.2
  • 46
    • 0026537228 scopus 로고
    • The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the alpha subunit of eukaryotic initiation factor 2
    • Davies M. V., Elroy-Stein O., Jagus R., Moss B., Kaufman R. J. The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the alpha subunit of eukaryotic initiation factor 2. J. Virol. 66:1992;1943-1950.
    • (1992) J. Virol. , vol.66 , pp. 1943-1950
    • Davies, M.V.1    Elroy-Stein, O.2    Jagus, R.3    Moss, B.4    Kaufman, R.J.5
  • 47
    • 0027407080 scopus 로고
    • The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA dependent protein kinase by different mechanisms
    • Davies M. V., Chang H.-W., Jacobs B. L., Kaufman R. J. The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA dependent protein kinase by different mechanisms. J. Virol. 67:1993;1688-1692.
    • (1993) J. Virol. , vol.67 , pp. 1688-1692
    • Davies, M.V.1    Chang, H.-W.2    Jacobs, B.L.3    Kaufman, R.J.4
  • 48
    • 0030033398 scopus 로고    scopus 로고
    • In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA from the 3' untranslated regions of human alpha-tropomyosin
    • Davis S., Watson J. C. In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA from the 3' untranslated regions of human alpha-tropomyosin. Proc. Natl. Acad. Sci. USA. 93:1996;508-513.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 508-513
    • Davis, S.1    Watson, J.C.2
  • 49
    • 0028106465 scopus 로고
    • Site-directed mutagenic analysis of reovirus σ3 protein binding to dsRNA
    • Denzler K. L., Jacobs B. L. Site-directed mutagenic analysis of reovirus σ3 protein binding to dsRNA. Virology. 204:1994;190-199.
    • (1994) Virology , vol.204 , pp. 190-199
    • Denzler, K.L.1    Jacobs, B.L.2
  • 50
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der S. D., Yang Y. L., Weissman C., Williams B. R. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA. 94:1997;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.4
  • 51
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene specific translational control of GCN4 in yeast
    • Dever T. E., Feng L., Wek R. C., Cigan A. M., Donahue T. F., Hinnebusch A. G. Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene specific translational control of GCN4 in yeast. Cell. 68:1992;585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.F.5    Hinnebusch, A.G.6
  • 52
    • 0027324505 scopus 로고
    • Mammalian eukaryotic initiation factor elF2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism in yeast
    • Dever T. E., Chen J.-J., Barber G. N., Cigan A. M., Feng L., Donahue T. F., London I., Katze M. G., Hinnebusch A. G. Mammalian eukaryotic initiation factor elF2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism in yeast. Proc. Natl. Acad. Sci. USA. 90:1994;4616-4620.
    • (1994) 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.7    Katze, M.G.8    Hinnebusch, A.G.9
  • 54
    • 0024576640 scopus 로고
    • Activation of double-stranded RNA-dependent kinase (dsI) by the TAR region of HIV-1 mRNA: A novel translation control mechanism
    • Edery I., Petryshyn R., Sonenberg N. Activation of double-stranded RNA-dependent kinase (dsI) by the TAR region of HIV-1 mRNA. a novel translation control mechanism Cell. 56:1989;303-312.
    • (1989) Cell , vol.56 , pp. 303-312
    • Edery, I.1    Petryshyn, R.2    Sonenberg, N.3
  • 55
    • 0029910938 scopus 로고    scopus 로고
    • Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome
    • Elia A., Laing K. G., Schofield A., Tilleray V. J., Clemens M. J. Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome. Nucl. Acids Res. 24:1996;4471-4478.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4471-4478
    • Elia, A.1    Laing, K.G.2    Schofield, A.3    Tilleray, V.J.4    Clemens, M.J.5
  • 56
    • 0030971781 scopus 로고    scopus 로고
    • High level of transgene expression in cell cultures and in the mouse by replication-incompetent adenoviruses harboring VAI genes
    • Eloit M., Adam M., Fournier A. High level of transgene expression in cell cultures and in the mouse by replication-incompetent adenoviruses harboring VAI genes. J. Virol. 71:1997;5375-5381.
    • (1997) J. Virol. , vol.71 , pp. 5375-5381
    • Eloit, M.1    Adam, M.2    Fournier, A.3
  • 57
    • 0029161576 scopus 로고
    • Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b: Sensitivity to interferon is conferred by amino acid substitutions in the NS5A region
    • Enomoto N., Sakuma I., Asahina Y., Kurosaki M., Murakami T., Yamamoto C., Izumi N., Marumo F., Sato C. Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b. sensitivity to interferon is conferred by amino acid substitutions in the NS5A region J. Clin. Invest. 96:1995;224-230.
    • (1995) J. Clin. Invest. , vol.96 , pp. 224-230
    • Enomoto, N.1    Sakuma, I.2    Asahina, Y.3    Kurosaki, M.4    Murakami, T.5    Yamamoto, C.6    Izumi, N.7    Marumo, F.8    Sato, C.9
  • 59
    • 0026653870 scopus 로고
    • Identification of dsRNA binding domains in the interferon-induced dsRNA-activated P68 kinase
    • Feng G. S., Chong K. L., Kumara A., Williams B. R. G. Identification of dsRNA binding domains in the interferon-induced dsRNA-activated P68 kinase. Proc. Natl. Acad. Sci. USA. 89:1992;5447-5451.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5447-5451
    • Feng, G.S.1    Chong, K.L.2    Kumara, A.3    Williams, B.R.G.4
  • 60
    • 0026534643 scopus 로고
    • Interferons in the persistence, pathogenesis, and treatment of HIV infection
    • Francis M. L., Meltzer M. S., Gendelman H. E. Interferons in the persistence, pathogenesis, and treatment of HIV infection. AIDS Res. Hum. Retroviruses. 8:1992;199-207.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 199-207
    • Francis, M.L.1    Meltzer, M.S.2    Gendelman, H.E.3
  • 62
    • 0024543242 scopus 로고
    • The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase
    • Galabru J., Katze M. G., Robert N., Hovanessian A. G. The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase. Eur. J. Biochem. 178:1989;581-589.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 581-589
    • Galabru, J.1    Katze, M.G.2    Robert, N.3    Hovanessian, A.G.4
  • 63
    • 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. 16:1996;4172-4181.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4172-4181
    • Gale M., Jr.1    Tan, S.-L.2    Wambach, M.3    Katze, M.G.4
  • 64
    • 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., Korth M. J., Tang N. M., Tan S. L., Hopkins D. A., Dever T. E., Polyak S. J., Gretch D. R., Katze M. G. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology. 230:1997;217-227.
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale M., Jr.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
  • 66
    • 0025876881 scopus 로고
    • Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR
    • Gatignol A., Buckler-White A., Berkhout B., Jeang K. T. Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR. Science. 251:1991;1597-1600.
    • (1991) Science , vol.251 , pp. 1597-1600
    • Gatignol, A.1    Buckler-White, A.2    Berkhout, B.3    Jeang, K.T.4
  • 67
    • 0027478445 scopus 로고
    • Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen
    • Gatignol A., Buckler C., Jeang K.-T. Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen. Mol. Cell. Biol. 13:1993;2193-2202.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2193-2202
    • Gatignol, A.1    Buckler, C.2    Jeang, K.-T.3
  • 68
    • 0025800227 scopus 로고
    • Binding of the adenovirus VAI RNA to the interferon-induced 68-kDa protein kinase correlates with function
    • Ghadge G., Swaminathan S., Katze M. G., Thimmappaya B. Binding of the adenovirus VAI RNA to the interferon-induced 68-kDa protein kinase correlates with function. Proc. Natl. Acad. Sci. USA. 88:1991;7140-7144.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7140-7144
    • Ghadge, G.1    Swaminathan, S.2    Katze, M.G.3    Thimmappaya, B.4
  • 69
    • 0024318804 scopus 로고
    • Stimulation of chloramphenicol acetyl transferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected Cos cells
    • Giantini M., Shatkin A. Stimulation of chloramphenicol acetyl transferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected Cos cells. J. Virol. 63:1989;2415-2421.
    • (1989) J. Virol. , vol.63 , pp. 2415-2421
    • Giantini, M.1    Shatkin, A.2
  • 71
    • 0025922586 scopus 로고
    • The TPR snap helix: A novel protein repeat motif from mitosis to transcription
    • Goebl M., Yanagida M. The TPR snap helix. a novel protein repeat motif from mitosis to transcription Trends Biochem. Sci. 16:1991;173-177.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 173-177
    • Goebl, M.1    Yanagida, M.2
  • 72
    • 0027105279 scopus 로고
    • Two RNA binding motifs in the double-stranded RNA activated protein kinase, DAI
    • Green S. R., Mathews M. B. Two RNA binding motifs in the double-stranded RNA activated protein kinase, DAI. Genes Dev. 6:1992;2478-2490.
    • (1992) Genes Dev. , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 73
    • 0025228070 scopus 로고
    • Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded RNA-activated protein kinase
    • Gunnery S. A., Rice P., Robertson H. D., Mathews M. B. Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA. 87:1990;8687-8691.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8687-8691
    • Gunnery, S.A.1    Rice, P.2    Robertson, H.D.3    Mathews, M.B.4
  • 74
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks S. K., Quinn A. M., Hunter T. The protein kinase family. conserved features and deduced phylogeny of the catalytic domains Science. 241:1988;42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 75
    • 0027102716 scopus 로고
    • Binding of influenza A virus NS1 protein to dsRNA in vitro
    • Hatada E., Fukuda R. Binding of influenza A virus NS1 protein to dsRNA in vitro. J. Gen. Virol. 73:1992;3325-3329.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3325-3329
    • Hatada, E.1    Fukuda, R.2
  • 76
    • 0030793170 scopus 로고    scopus 로고
    • - herpes simplex virus 1: Failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the a47 gene
    • a
    • - herpes simplex virus 1. failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the a47 gene J. Virol. 71:1997;6049-6054. a.
    • (1997) J. Virol. , vol.71 , pp. 6049-6054
    • He, B.1    Chou, J.2    Brandimarti, R.3    Mohr, I.4    Gluzman, Y.5    Roizman, B.6
  • 77
    • 0031017382 scopus 로고    scopus 로고
    • The γ4.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • b
    • He B., Gross M., Roizman B. The γ4.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA. 94:1997;843-848. b.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 78
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89 kilodalton heat shock protein
    • Hickey E., Brandon S. E., Smale G., Lloyd D., Weber L. A. Sequence and regulation of a gene encoding a human 89 kilodalton heat shock protein. Mol. Cell. Biol. 9:1989;2615-2626.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3    Lloyd, D.4    Weber, L.A.5
  • 79
    • 0028695223 scopus 로고
    • The eIF-2α kinases: Regulators of protein synthesis in starvation and stress
    • Hinnebusch A. G. The eIF-2α kinases. regulators of protein synthesis in starvation and stress Semin. Cell Biol. 5:1994;417-426.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 417-426
    • Hinnebusch, A.G.1
  • 80
    • 0030009311 scopus 로고    scopus 로고
    • Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA
    • a
    • Ho C.-K., Shuman S. Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA. J. Virol. 70:1996;2611-2614. a.
    • (1996) J. Virol. , vol.70 , pp. 2611-2614
    • Ho, C.-K.1    Shuman, S.2
  • 81
    • 0029963273 scopus 로고    scopus 로고
    • Physical and functional characterization of the double-stranded RNA binding protein encoded by the vaccinia virus E3 gene
    • b
    • Ho C.-K., Shuman S. Physical and functional characterization of the double-stranded RNA binding protein encoded by the vaccinia virus E3 gene. Virology. 217:1996;272-284. b.
    • (1996) Virology , vol.217 , pp. 272-284
    • Ho, C.-K.1    Shuman, S.2
  • 82
    • 0028311492 scopus 로고
    • Therapy of acute and chronic viral hepatitis
    • Hoofnagle J. H. Therapy of acute and chronic viral hepatitis. Adv. Intern. Med. 39:1994;241-275.
    • (1994) Adv. Intern. Med. , vol.39 , pp. 241-275
    • Hoofnagle, J.H.1
  • 83
    • 0017253105 scopus 로고
    • Reovirus-coded polypeptides in infected cells: Isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively
    • Huismans H., Joklik W. K. Reovirus-coded polypeptides in infected cells. isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively Virology. 70:1976;411-424.
    • (1976) Virology , vol.70 , pp. 411-424
    • Huismans, H.1    Joklik, W.K.2
  • 84
    • 0025999848 scopus 로고
    • TIK, a novel serine/threonine kinase, is recognized by antibodies directed against phosphotyrosine
    • Icely P. L., Gros P., Bergeron J. J. M., Devault A., Afar D. E. H., Bell J. C. TIK, a novel serine/threonine kinase, is recognized by antibodies directed against phosphotyrosine. J. Biol. Chem. 266:1991;16073-16077.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16073-16077
    • Icely, P.L.1    Gros, P.2    Bergeron, J.J.M.3    Devault, A.4    Afar, D.E.H.5    Bell, J.C.6
  • 85
    • 0028025682 scopus 로고
    • Current state of interferon therapy for chronic hepatitis C
    • Iino S., Hino K., Yasuda K. Current state of interferon therapy for chronic hepatitis C. Intervirology. 37:1994;87-100.
    • (1994) Intervirology , vol.37 , pp. 87-100
    • Iino, S.1    Hino, K.2    Yasuda, K.3
  • 86
    • 0000588762 scopus 로고
    • Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein
    • Imani F., Jacobs B. L. Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein. Proc. Natl. Acad. Sci. USA. 85:1988;7887-7891.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7887-7891
    • Imani, F.1    Jacobs, B.L.2
  • 87
    • 0026002147 scopus 로고
    • The Lang strain of reovirus serotype 1 and the Dearing strain of reovirus serotype 3 differ in their sensitivities to beta interferon
    • Jacobs B. L., Ferguson R. E. The Lang strain of reovirus serotype 1 and the Dearing strain of reovirus serotype 3 differ in their sensitivities to beta interferon. J. Virol. 65:1991;5102-5104.
    • (1991) J. Virol. , vol.65 , pp. 5102-5104
    • Jacobs, B.L.1    Ferguson, R.E.2
  • 88
    • 0029046288 scopus 로고
    • The interferon system: A review with emphasis on the role of PKR in growth control
    • Jaramillo M. L., Abraham N., Bell J. C. The interferon system. a review with emphasis on the role of PKR in growth control Cancer Invest. 13:1995;327-338.
    • (1995) Cancer Invest. , vol.13 , pp. 327-338
    • Jaramillo, M.L.1    Abraham, N.2    Bell, J.C.3
  • 91
    • 0000335423 scopus 로고
    • r protein kinase
    • r protein kinase Semin. Virol. 4:1993;259-268.
    • (1993) Semin. Virol. , vol.4 , pp. 259-268
    • Katze, M.G.1
  • 92
    • 0028815704 scopus 로고
    • Regulation of the interferon-induced PKR: Can viruses cope?
    • Katze M. G. Regulation of the interferon-induced PKR. can viruses cope? Trends Microbiol. 3:1995;75-78.
    • (1995) Trends Microbiol. , vol.3 , pp. 75-78
    • Katze, M.G.1
  • 93
    • 0002833852 scopus 로고    scopus 로고
    • Translational control in cells infected with influenza virus and reovirus
    • Hershey, J. W. B., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Katze, M. G. (1996) Translational control in cells infected with influenza virus and reovirus. In: Translational Control, pp. 607-630, Hershey, J. W. B., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1996) In: Translational Control , pp. 607-630
    • Katze, M.G.1
  • 94
    • 0025679966 scopus 로고
    • The regulation of viral and cellular RNA turnover in cells infected by eukaryotic viruses including human immunodeficiency virus, HIV-1
    • Katze M. G., Agy M. B. The regulation of viral and cellular RNA turnover in cells infected by eukaryotic viruses including human immunodeficiency virus, HIV-1. Enzyme. 44:1990;332-346.
    • (1990) Enzyme , vol.44 , pp. 332-346
    • Katze, M.G.1    Agy, M.B.2
  • 96
    • 0023708282 scopus 로고
    • Influenza virus regulates protein synthesis during infection by repressing the autophosphorylation and activity of the cellular 68,000 Mr protein kinase
    • Katze M. G., Tomita J., Black T., Krug R. M., Safer B., Hovanessian A. G. Influenza virus regulates protein synthesis during infection by repressing the autophosphorylation and activity of the cellular 68,000 Mr protein kinase. J. Virol. 62:1988;3710-3717.
    • (1988) J. Virol. , vol.62 , pp. 3710-3717
    • Katze, M.G.1    Tomita, J.2    Black, T.3    Krug, R.M.4    Safer, B.5    Hovanessian, A.G.6
  • 98
    • 0024582782 scopus 로고
    • The phosphorylation state of eukaryotic initiation factor 2 alters translational efficiency of specific mRNAs
    • Kaufman R. J., Davies M. V., Pathak V. K., Hershey J. W. B. The phosphorylation state of eukaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell. Biol. 9:1989;946-958.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 946-958
    • Kaufman, R.J.1    Davies, M.V.2    Pathak, V.K.3    Hershey, J.W.B.4
  • 100
    • 0029148470 scopus 로고
    • IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR
    • Kirchhoff S., Koromilas A. E., Schaper F., Grashof M., Sonenberg N., Hauser H. IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR. Oncogene. 11:1995;439-445.
    • (1995) Oncogene , vol.11 , pp. 439-445
    • Kirchhoff, S.1    Koromilas, A.E.2    Schaper, F.3    Grashof, M.4    Sonenberg, N.5    Hauser, H.6
  • 102
    • 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
    • Kobayashi M., Locke E., Silverman J., Ung T., Dever T. E. 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. 17:1997;4146-4158.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4146-4158
    • Kobayashi, M.1    Locke, E.2    Silverman, J.3    Ung, T.4    Dever, T.E.5
  • 104
    • 0028820772 scopus 로고
    • The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene
    • Koromilas A. E., Cantin C., Craig A. W. B., Jagus R., Hiscott J., Sonenberg N. The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene. J. Biol. Chem. 270:1995;25426-25434.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25426-25434
    • Koromilas, A.E.1    Cantin, C.2    Craig, A.W.B.3    Jagus, R.4    Hiscott, J.5    Sonenberg, N.6
  • 105
    • 0029996422 scopus 로고    scopus 로고
    • Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase
    • Korth M. J., Lyons C. N., Wambach M., Katze M. G. Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase. Gene. 170:1996;181-188.
    • (1996) Gene , vol.170 , pp. 181-188
    • Korth, M.J.1    Lyons, C.N.2    Wambach, M.3    Katze, M.G.4
  • 106
    • 0022374451 scopus 로고
    • Inhibition of influenza viral messenger RNA synthesis in cells expressing the interferon-induced Mx gene product
    • Krug R. M., Shaw M., Broni B., Shapiro G., Haller O. Inhibition of influenza viral messenger RNA synthesis in cells expressing the interferon-induced Mx gene product. J. Virol. 56:1985;201-206.
    • (1985) J. Virol. , vol.56 , pp. 201-206
    • Krug, R.M.1    Shaw, M.2    Broni, B.3    Shapiro, G.4    Haller, O.5
  • 107
    • 0002210298 scopus 로고
    • Expression and replication of the influenza virus genome
    • Krug, R. M. (ed.) Plenum Publishing Co., New York
    • Krug, R. M., Alonso-Caplen, F., Julkunen, I. and Katze, M. G. (1989) Expression and replication of the influenza virus genome. In: Influenza Viruses, 77th edn., pp. 89-152, Krug, R. M. (ed.) Plenum Publishing Co., New York.
    • (1989) In: Influenza Viruses, 77th Edn. , pp. 89-152
    • Krug, R.M.1    Alonso-Caplen, F.2    Julkunen, I.3    Katze, M.G.4
  • 108
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB
    • Kumar A., Haque J., Lacoste J., Hiscott J., Williams B. R. G. Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB. Proc. Natl. Acad. Sci. USA. 91:1994;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
  • 109
    • 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., Yang Y., Flati V., Der S., Kadereit S., Deb A., Haque J., Reis L., Weissmann C., Williams B. R. G. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene. role of IRF-1 and NF-κB EMBO J. 16:1997;406-413.
    • (1997) EMBO J. , vol.16 , pp. 406-413
    • Kumar, A.1    Yang, Y.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
  • 110
    • 0028998441 scopus 로고
    • Tetratricopeptide repeat interactions: To TPR or not to TPR?
    • Lamb J. R., Tugendreich S., Hieter P. Tetratricopeptide repeat interactions. to TPR or not to TPR? Trends Biochem. Sci. 20:1995;257-259.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 111
    • 0025788445 scopus 로고
    • Diversity of coding strategies in influenza viruses
    • Lamb R. A., Horvath C. M. Diversity of coding strategies in influenza viruses. Trends Genet. 7:1991;261-266.
    • (1991) Trends Genet. , vol.7 , pp. 261-266
    • Lamb, R.A.1    Horvath, C.M.2
  • 113
    • 0025029239 scopus 로고
    • Immunology of HIV infection, I: Biology of interferons
    • Laurence J. Immunology of HIV infection, I. biology of interferons AIDS Res. Hum. Retroviruses. 6:1990;1149-1156.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 1149-1156
    • Laurence, J.1
  • 114
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee S. B., Esteban M. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology. 199:1994;491-496.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 115
    • 0343812093 scopus 로고    scopus 로고
    • The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream from Bcl-2, and involves ICE-like proteases
    • Lee S. B., Rodriguez D., Rodriguez J. R., Esteban M. The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream from Bcl-2, and involves ICE-like proteases. Virology. 231:1997;81-88.
    • (1997) Virology , vol.231 , pp. 81-88
    • Lee, S.B.1    Rodriguez, D.2    Rodriguez, J.R.3    Esteban, M.4
  • 116
    • 0028247651 scopus 로고
    • Cellular inhibitors of the interferon-induced, dsRNA-activated protein kinase
    • Lee T.-G., Katze M. G. Cellular inhibitors of the interferon-induced, dsRNA-activated protein kinase. Prog. Mol. Subcell. Biol. 14:1993;48-65.
    • (1993) Prog. Mol. Subcell. Biol. , vol.14 , pp. 48-65
    • Lee, T.-G.1    Katze, M.G.2
  • 118
    • 0026628369 scopus 로고
    • Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase
    • Lee T. G., Tomita J., Hovanessian A. G., Katze M. G. Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase. J. Biol. Chem. 267:1992;14238-14243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14238-14243
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 119
    • 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., Tang N., Thompson S., Miller J., Katze M. G. 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. 14:1994;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
  • 120
    • 0023020029 scopus 로고
    • Expression of the cloned S4 gene of reovirus serotype 3 in transformed eucaryotic cells: Enrichment of the viral protein in the crude initiation factor fraction
    • Lemay G., Millward S. Expression of the cloned S4 gene of reovirus serotype 3 in transformed eucaryotic cells. enrichment of the viral protein in the crude initiation factor fraction Virus Res. 6:1986;133-140.
    • (1986) Virus Res. , vol.6 , pp. 133-140
    • Lemay, G.1    Millward, S.2
  • 121
    • 0023280220 scopus 로고
    • The viral protein sigma 3 participates in translation of late viral mRNA in reovirus-infected L cells
    • Lemieux R., Lemay G., Millward S. The viral protein sigma 3 participates in translation of late viral mRNA in reovirus-infected L cells. J. Virol. 61:1987;2472-2479.
    • (1987) J. Virol. , vol.61 , pp. 2472-2479
    • Lemieux, R.1    Lemay, G.2    Millward, S.3
  • 122
    • 0024516201 scopus 로고
    • The involvement of NF-κB in β-interferon gene regulation reveals its role as a widely inducible mediator of signal transduction
    • Lenardo M. J., Fan C. M., Maniatis T., Baltimore D. The involvement of NF-κB in β-interferon gene regulation reveals its role as a widely inducible mediator of signal transduction. Cell. 57:1989;287-294.
    • (1989) Cell , vol.57 , pp. 287-294
    • Lenardo, M.J.1    Fan, C.M.2    Maniatis, T.3    Baltimore, D.4
  • 123
    • 0026010912 scopus 로고
    • Activation of the double-stranded RNA-dependent eIF-2α kinase by cellular RNA from 3T3-F442A cells
    • Li J., Petryshyn R. A. Activation of the double-stranded RNA-dependent eIF-2α kinase by cellular RNA from 3T3-F442A cells. Eur. J. Biochem. 195:1991;41-48.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 41-48
    • Li, J.1    Petryshyn, R.A.2
  • 124
    • 0026465267 scopus 로고
    • Translational stimulation by reovirus polypeptide 3: Substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2
    • Lloyd R. M., Shatkin A. J. Translational stimulation by reovirus polypeptide 3. substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2 J. Virol. 66:1992;6878-6884.
    • (1992) J. Virol. , vol.66 , pp. 6878-6884
    • Lloyd, R.M.1    Shatkin, A.J.2
  • 126
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the eIF-2 translation initiation factor
    • Lu Y., Wambach M., Katze M. G., Krug R. M. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the eIF-2 translation initiation factor. Virology. 214:1995;222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 127
    • 0029903806 scopus 로고    scopus 로고
    • Secondary and tertiary structure in the central domain of adenovirus type 2 VAI RNA
    • Ma Y., Mathews M. B. Secondary and tertiary structure in the central domain of adenovirus type 2 VAI RNA. RNA. 2:1996;937-955.
    • (1996) RNA , vol.2 , pp. 937-955
    • Ma, Y.1    Mathews, M.B.2
  • 129
    • 0026713151 scopus 로고
    • Interactions between dsRNA regulators and the protein kinase, DAI
    • Manche L., Green S. R., Schmedt C., Mathews M. B. Interactions between dsRNA regulators and the protein kinase, DAI. Mol. Cell. Biol. 12:1992;5238-5248.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5238-5248
    • Manche, L.1    Green, S.R.2    Schmedt, C.3    Mathews, M.B.4
  • 130
    • 0023948036 scopus 로고
    • Characterization of the dsRNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNA 1
    • Maran A., Mathews M. B. Characterization of the dsRNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNA 1. Virology. 164:1988;106-113.
    • (1988) Virology , vol.164 , pp. 106-113
    • Maran, A.1    Mathews, M.B.2
  • 132
    • 0000519248 scopus 로고
    • Viral evasion of cellular defense mechanisms: Regulation of the protein kinase DAI by RNA effectors
    • Mathews M. B. Viral evasion of cellular defense mechanisms. regulation of the protein kinase DAI by RNA effectors Semin. Virol. 4:1993;507.1-507.12.
    • (1993) Semin. Virol. , vol.4 , pp. 5071-50712
    • Mathews, M.B.1
  • 133
    • 0000519248 scopus 로고
    • Viral evasion of cellular defense mechanisms: Regulation of the protein kinase DAI by RNA effectors
    • Mathews M. B. Viral evasion of cellular defense mechanisms. regulation of the protein kinase DAI by RNA effectors Semin. Virol. 4:1995;247-257.
    • (1995) Semin. Virol. , vol.4 , pp. 247-257
    • Mathews, M.B.1
  • 134
    • 0001016282 scopus 로고    scopus 로고
    • Interactions between viruses and the cellular machinery for protein synthesis
    • Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Mathews, M. B. (1996) Interactions between viruses and the cellular machinery for protein synthesis. In: Translational Control, pp. 505-548, Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1996) In: Translational Control , pp. 505-548
    • Mathews, M.B.1
  • 135
    • 0025656869 scopus 로고
    • Control of translation in adenovirus-infected cells
    • Mathews M. B., Shenk T. Control of translation in adenovirus-infected cells. Enzyme. 44:1990;250-264.
    • (1990) Enzyme , vol.44 , pp. 250-264
    • Mathews, M.B.1    Shenk, T.2
  • 136
    • 0025931571 scopus 로고
    • Adenovirus virus-associated RNA and translation control
    • Mathews M. B., Shenk T. Adenovirus virus-associated RNA and translation control. J. Virol. 65:1991;5657-5662.
    • (1991) J. Virol. , vol.65 , pp. 5657-5662
    • Mathews, M.B.1    Shenk, T.2
  • 138
    • 0018083729 scopus 로고
    • The nature of the polypeptide encoded by each of the 10 double-stranded RNA segments of reovirus type 3
    • McCrae M. A., Joklik W. K. The nature of the polypeptide encoded by each of the 10 double-stranded RNA segments of reovirus type 3. Virology. 89:1978;578-593.
    • (1978) Virology , vol.89 , pp. 578-593
    • McCrae, M.A.1    Joklik, W.K.2
  • 140
    • 0025361887 scopus 로고
    • 1 with the protein kinase DAI: Nonequivalence of binding and function
    • 1 with the protein kinase DAI. nonequivalence of binding and function Cell. 61:1990;843-852.
    • (1990) Cell , vol.61 , pp. 843-852
    • Mellits, K.H.1    Kostura, M.2    Mathews, M.B.3
  • 142
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Merrick, W. C. and Hershey, J. W. B. (1996) The pathway and mechanism of eukaryotic protein synthesis. In: Translational Control, pp. 31-70, Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1996) In: Translational Control , pp. 31-70
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 143
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E., Chong K. L., Galabru J., Thomas N., Kerr I., Williams B. R. G., Hovanessian A. G. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell. 62:1990;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
  • 144
    • 0027396813 scopus 로고
    • Tumour suppressor function of the interferon-induced double-stranded RNA-activated 68,000-Mr protein kinase
    • Meurs E., Galabru J., Barber G. N., Katze M. G., Hovanessian A. G. Tumour suppressor function of the interferon-induced double-stranded RNA-activated 68,000-Mr protein kinase. Proc. Natl. Acad. Sci. USA. 90:1993;232-236.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 232-236
    • Meurs, E.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 145
    • 0027180921 scopus 로고
    • Mechanisms for the inhibition of HIV replication by interferons-alpha, -beta, and -gamma in primary human macrophages
    • Meylan P. R. A., Guatelli J. C., Munis J. R., Richman D. D., Kornbluth R. S. Mechanisms for the inhibition of HIV replication by interferons-alpha, -beta, and -gamma in primary human macrophages. Virology. 193:1993;138-148.
    • (1993) Virology , vol.193 , pp. 138-148
    • Meylan, P.R.A.1    Guatelli, J.C.2    Munis, J.R.3    Richman, D.D.4    Kornbluth, R.S.5
  • 146
    • 0026785224 scopus 로고
    • Proteolytic cleavage of the reovirus sigma 3 protein results in enhanced double-stranded RNA-binding activity: Identification of a repeated basic amino acid motif within the C-terminal binding region
    • Miller J. E., Samuel C. E. Proteolytic cleavage of the reovirus sigma 3 protein results in enhanced double-stranded RNA-binding activity. identification of a repeated basic amino acid motif within the C-terminal binding region J. Virol. 66:1992;5347-5356.
    • (1992) J. Virol. , vol.66 , pp. 5347-5356
    • Miller, J.E.1    Samuel, C.E.2
  • 147
    • 0029841340 scopus 로고    scopus 로고
    • A herpes virus genetic element which affects translation in the absence of the viral GADD34 function
    • Mohr I., Gluzman Y. A herpes virus genetic element which affects translation in the absence of the viral GADD34 function. EMBO J. 15:1996;4759-4766.
    • (1996) EMBO J. , vol.15 , pp. 4759-4766
    • Mohr, I.1    Gluzman, Y.2
  • 148
    • 0003720391 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • Morimoto, R. I., Tissieres, A. and Georgopoulos, C. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Morimoto, R. I., Tissieres, A. and Georgopoulos, C. (1994) Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In: The Biology of Heat Shock Proteins and Molecular Chaperones, pp. 1-30, Morimoto, R. I., Tissieres, A. and Georgopoulos, C. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1994) In: The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 1-30
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 150
    • 0028852619 scopus 로고
    • Platelet-derived growth factor signal transduction through the interferon-inducible kinase PKR
    • Mundschau L. J., Faller D. V. Platelet-derived growth factor signal transduction through the interferon-inducible kinase PKR. J. Biol. Chem. 270:1995;3100-3106.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3100-3106
    • Mundschau, L.J.1    Faller, D.V.2
  • 151
    • 0022547029 scopus 로고
    • A mechanism for the control of protein synthesis by adenovirus VA RNA
    • O'Malley R. P., Mariano T. M., Siekierka J., Mathews M. B. A mechanism for the control of protein synthesis by adenovirus VA RNA. Cell. 44:1994;391-400.
    • (1994) Cell , vol.44 , pp. 391-400
    • O'Malley, R.P.1    Mariano, T.M.2    Siekierka, J.3    Mathews, M.B.4
  • 152
    • 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., McCotter M. D., Henry G. L., McCormack S. J., Thomis D. C., Samuel C. E. Mechanism of interferon action. biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells Virology. 215:1996;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
  • 154
    • 0026686791 scopus 로고
    • Identification of the double stranded RNA-binding domain of the human interferon-inducible protein kinase
    • Patel R., Sen G. C. Identification of the double stranded RNA-binding domain of the human interferon-inducible protein kinase. J. Biol. Chem. 267:1992;7871-7876.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7871-7876
    • Patel, R.1    Sen, G.C.2
  • 155
    • 0029115903 scopus 로고
    • The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo
    • Patel R. C., Stanton P., McMillan N. M. J., Williams B. R. G., Sen G. C. The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo. Proc. Natl. Acad. Sci. USA. 92:1995;8283-8287.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8283-8287
    • Patel, R.C.1    Stanton, P.2    McMillan, N.M.J.3    Williams, B.R.G.4    Sen, G.C.5
  • 156
    • 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., Stanton P., Sen G. C. 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. 271:1996;25657-25663.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 157
    • 0026365944 scopus 로고
    • The antiviral potentials of Mx proteins
    • Pavlovic J., Staehli P. The antiviral potentials of Mx proteins. J. Interferon Res. 11:1991;215-219.
    • (1991) J. Interferon Res. , vol.11 , pp. 215-219
    • Pavlovic, J.1    Staehli, P.2
  • 159
    • 0030751945 scopus 로고    scopus 로고
    • Characterization and mapping of the double-stranded regions involved in activation of PKR within a cellular RNA from 3T3-F442A cells
    • Petryshyn R. A., Ferrenz A. G., Li J. Characterization and mapping of the double-stranded regions involved in activation of PKR within a cellular RNA from 3T3-F442A cells. Nucl. Acids Res. 25:1997;2672-2678.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2672-2678
    • Petryshyn, R.A.1    Ferrenz, A.G.2    Li, J.3
  • 160
    • 0026398174 scopus 로고
    • Multiple effects of interferon on HIV-1 replication
    • Pitha P. Multiple effects of interferon on HIV-1 replication. J. Interferon Res. 11:1991;313-318.
    • (1991) J. Interferon Res. , vol.11 , pp. 313-318
    • Pitha, P.1
  • 161
    • 0024364803 scopus 로고
    • Interferon-alpha but not AZT suppresses HIV expression in chronically
    • Poli G., Orenstein J. M., Kinter A., Folks T. M., Fauci A. S. Interferon-alpha but not AZT suppresses HIV expression in chronically infected cell lines. Science. 244:1989;575-577.
    • (1989) Science , vol.244 , pp. 575-577
    • Poli, G.1    Orenstein, J.M.2    Kinter, A.3    Folks, T.M.4    Fauci, A.S.5
  • 162
    • 0030026945 scopus 로고    scopus 로고
    • The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity
    • Polyak S. J., Tang N., Wambach M., Barber G. N., Katze M. G. The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity. J. Biol. Chem. 271:1996;1702-1707.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1702-1707
    • Polyak, S.J.1    Tang, N.2    Wambach, M.3    Barber, G.N.4    Katze, M.G.5
  • 163
    • 0031550784 scopus 로고    scopus 로고
    • 134.5 genes of herpes simplex virus
    • 134.5 genes of herpes simplex virus. Virology. 229:1997;98-105.
    • (1997) Virology , vol.229 , pp. 98-105
    • Poon, A.P.W.1    Roizman, B.2
  • 164
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • Proud C. G. PKR. a new name and new roles Trends Biochem. Sci. 20:1995;241-246.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 165
    • 0028274131 scopus 로고
    • The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A)
    • Qiu Y., Krug R. M. The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J. Virol. 68:1994;2425-2432.
    • (1994) J. Virol. , vol.68 , pp. 2425-2432
    • Qiu, Y.1    Krug, R.M.2
  • 166
    • 0026410646 scopus 로고
    • A human homologue of the Escherichia coli DnaJ heat-shock protein
    • Raabe T., Manley J. L. A human homologue of the Escherichia coli DnaJ heat-shock protein. Nucl. Acids Res. 19:1991;6445.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 6445
    • Raabe, T.1    Manley, J.L.2
  • 169
    • 0030013732 scopus 로고    scopus 로고
    • Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR
    • Robertson H. D., Manche L., Mathews M. B. Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR. J. Virol. 70:1996;5611-5617.
    • (1996) J. Virol. , vol.70 , pp. 5611-5617
    • Robertson, H.D.1    Manche, L.2    Mathews, M.B.3
  • 170
    • 0028924758 scopus 로고
    • Structural requirements for dsRNA-binding, dimerization and activation of the human eIF-2α kinase DAI in yeast
    • Romano P. R., Green S. R., Barber G. N., Mathews M. B., Hinnebusch A. G. Structural requirements for dsRNA-binding, dimerization and activation of the human eIF-2α kinase DAI in yeast. Mol. Cell. Biol. 15:1995;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
  • 171
    • 0025267438 scopus 로고
    • Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product
    • Roy S., Katze M. G., Parkin N. T., Edery I., Hovanessian A. G., Sonenberg N. Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product. Science. 247:1990;1216-1219.
    • (1990) Science , vol.247 , pp. 1216-1219
    • Roy, S.1    Katze, M.G.2    Parkin, N.T.3    Edery, I.4    Hovanessian, A.G.5    Sonenberg, N.6
  • 173
    • 0025739093 scopus 로고
    • Antiviral actions of interferon interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel C. E. Antiviral actions of interferon interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology. 183:1991;1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 174
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel C. E. The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268:1993;7603-7606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 175
    • 0023673325 scopus 로고
    • Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein σ3
    • Schiff L. A., Nibert M. L., Co M. S., Brown E. G., Fields B. N. Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein σ3. Mol. Cell. Biol. 8:1988;273-283.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 273-283
    • Schiff, L.A.1    Nibert, M.L.2    Co, M.S.3    Brown, E.G.4    Fields, B.N.5
  • 176
    • 0030921401 scopus 로고    scopus 로고
    • Preferential translation of reovirus mRNA by a σ3-dependent mechanism
    • Schmechel S., Chute M., Skinner P., Anderson R., Schiff L. Preferential translation of reovirus mRNA by a σ3-dependent mechanism. Virology. 232:1997;62-73.
    • (1997) Virology , vol.232 , pp. 62-73
    • Schmechel, S.1    Chute, M.2    Skinner, P.3    Anderson, R.4    Schiff, L.5
  • 177
    • 0001204048 scopus 로고    scopus 로고
    • Adenovirus and vaccinia virus translational control
    • Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Schneider, R. J. (1996) Adenovirus and vaccinia virus translational control. In: Translational Control, pp. 575-606, Hershey, J., Mathews, M. B. and Sonenberg, N. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1996) In: Translational Control , pp. 575-606
    • Schneider, R.J.1
  • 178
    • 0026603671 scopus 로고
    • Translational effects and sequence comparisons of the three serotypes of the reovirus S4 gene
    • Seliger L. S., Giantini M., Shatkin A. J. Translational effects and sequence comparisons of the three serotypes of the reovirus S4 gene. Virology. 187:1992;202-210.
    • (1992) Virology , vol.187 , pp. 202-210
    • Seliger, L.S.1    Giantini, M.2    Shatkin, A.J.3
  • 179
    • 0026739463 scopus 로고
    • The interferon system: A bird's eye view of its biochemistry
    • Sen G. C., Lengyel P. The interferon system. a bird's eye view of its biochemistry J. Biol. Chem. 267:1992;5017-5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 180
    • 0027352378 scopus 로고
    • Interferon-induced antiviral actions and their regulation
    • Sen G. C., Ransohoff R. M. Interferon-induced antiviral actions and their regulation. Adv. Virus Res. 42:1993;57.
    • (1993) Adv. Virus Res. , vol.42 , pp. 57
    • Sen, G.C.1    Ransohoff, R.M.2
  • 182
    • 0020378988 scopus 로고
    • Reovirus inhibition of cellular RNA and protein synthesis: Role of the S4 gene
    • Sharpe A. H., Fields B. N. Reovirus inhibition of cellular RNA and protein synthesis. role of the S4 gene Virology. 122:1982;381-391.
    • (1982) Virology , vol.122 , pp. 381-391
    • Sharpe, A.H.1    Fields, B.N.2
  • 183
    • 0021824082 scopus 로고
    • Translational control by adenovirus: Lack of virus-associated RNA1 during adenovirus infection results in phosphorylation of initiation factor elF-2 and inhibition of protein synthesis
    • Siekierka J., Mariano T. M., Reichel P. A., Mathews M. B. Translational control by adenovirus. lack of virus-associated RNA1 during adenovirus infection results in phosphorylation of initiation factor elF-2 and inhibition of protein synthesis Proc. Natl. Acad. Sci. USA. 82:1985;1959-1963.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1959-1963
    • Siekierka, J.1    Mariano, T.M.2    Reichel, P.A.3    Mathews, M.B.4
  • 184
    • 0027169533 scopus 로고
    • Eukaryotic DnaJ homologs and the specificity of Hsp70 activity
    • Silver P. A., Way J. C. Eukaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell. 74:1993;5-6.
    • (1993) Cell , vol.74 , pp. 5-6
    • Silver, P.A.1    Way, J.C.2
  • 185
    • 0027931663 scopus 로고
    • Fascination with 2-5A-dependent RNase: A unique enzyme that functions in interferon action
    • Silverman R. H. Fascination with 2-5A-dependent RNase. a unique enzyme that functions in interferon action J. Interferon Res. 14:1994;101-104.
    • (1994) J. Interferon Res. , vol.14 , pp. 101-104
    • Silverman, R.H.1
  • 187
    • 0027227497 scopus 로고
    • Cloning and characterization of a human protein phosphatase 1-encoding cDNA
    • Song Q., Khanna K. K., Lu H., Lavin M. F. Cloning and characterization of a human protein phosphatase 1-encoding cDNA. Gene. 129:1993;291-295.
    • (1993) Gene , vol.129 , pp. 291-295
    • Song, Q.1    Khanna, K.K.2    Lu, H.3    Lavin, M.F.4
  • 189
    • 0029067408 scopus 로고
    • Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis
    • Srivastava S. P., Davies M. V., Kaufman R. J. Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J. Biol. Chem. 270:1995;16619-16624.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16619-16624
    • Srivastava, S.P.1    Davies, M.V.2    Kaufman, R.J.3
  • 190
    • 0025138795 scopus 로고
    • Interferon induced proteins and the antiviral state
    • Staehli P. Interferon induced proteins and the antiviral state. Adv. Virus Res. 38:1990;147-200.
    • (1990) Adv. Virus Res. , vol.38 , pp. 147-200
    • Staehli, P.1
  • 191
    • 0026717106 scopus 로고
    • Epstein-Barr virus-encoded small RNAs (EBERs) do not modulate interferon effects in infected lymphocytes
    • Swaminathan S., Huneycutt B. S., Reiss C. S., Kieff E. Epstein-Barr virus-encoded small RNAs (EBERs) do not modulate interferon effects in infected lymphocytes. J. Virol. 66:1992;5133-5136.
    • (1992) J. Virol. , vol.66 , pp. 5133-5136
    • Swaminathan, S.1    Huneycutt, B.S.2    Reiss, C.S.3    Kieff, E.4
  • 192
    • 0029996794 scopus 로고    scopus 로고
    • Simian virus 40 bypasses the translational block imposed by the phosphorylation of eIF-2α
    • Swaminathan S., Rajan P., Savinova O., Jagus R., Thimmapaya B. Simian virus 40 bypasses the translational block imposed by the phosphorylation of eIF-2α Virology. 219:1996;321-323.
    • (1996) Virology , vol.219 , pp. 321-323
    • Swaminathan, S.1    Rajan, P.2    Savinova, O.3    Jagus, R.4    Thimmapaya, B.5
  • 193
    • 85083613644 scopus 로고    scopus 로고
    • IPK prevents dimerization of the interferon-induced, dsRNA-activated protein kinase: Implications for kinase modulation and Dna J domain function
    • in press
    • IPK prevents dimerization of the interferon-induced, dsRNA-activated protein kinase: implications for kinase modulation and Dna J domain function. Mol. Cell. Biol., in press.
    • (1998) Mol. Cell. Biol.
    • Tan, S.-L.1    Gale, M.J.2    Jr. Katze, M.G.3
  • 194
    • 0027999025 scopus 로고
    • Mechanism of interferon action: Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase
    • Tanaka H., Samuel C. E. Mechanism of interferon action. structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase Proc. Natl. Acad. Sci. USA. 91:1994;7995-7999.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7995-7999
    • Tanaka, H.1    Samuel, C.E.2
  • 195
    • 10244257563 scopus 로고    scopus 로고
    • Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR
    • Taylor D. R., Lee S. B., Romano P. R., Marshak D. R., Hinnebusch A. G., Esteban M., Mathews M. B. Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR. Mol. Cell. Biol. 16:1996;6295-6302.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6295-6302
    • Taylor, D.R.1    Lee, S.B.2    Romano, P.R.3    Marshak, D.R.4    Hinnebusch, A.G.5    Esteban, M.6    Mathews, M.B.7
  • 197
    • 0020425067 scopus 로고
    • Adenovirus VA1 RNA is required for efficient translation of viral mRNAs at late times after infection
    • Thimmappaya B., Weinberger C., Schneider R. J., Shenk T. Adenovirus VA1 RNA is required for efficient translation of viral mRNAs at late times after infection. Cell. 31:1982;543-551.
    • (1982) Cell , vol.31 , pp. 543-551
    • Thimmappaya, B.1    Weinberger, C.2    Schneider, R.J.3    Shenk, T.4
  • 198
    • 0029039746 scopus 로고
    • Mechanism of interferon action: Characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase
    • Thomis D. C., Samuel C. E. Mechanism of interferon action. characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase J. Virol. 69:1995;5195-5198.
    • (1995) J. Virol. , vol.69 , pp. 5195-5198
    • Thomis, D.C.1    Samuel, C.E.2
  • 199
    • 0026716253 scopus 로고
    • Mechanism of interferon action: CDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2α protein kinase from human cells
    • Thomis D. C., Doohan J. P., Samuel C. E. Mechanism of interferon action. cDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2α protein kinase from human cells Virology. 188:1992;33-46.
    • (1992) Virology , vol.188 , pp. 33-46
    • Thomis, D.C.1    Doohan, J.P.2    Samuel, C.E.3
  • 200
    • 0026608639 scopus 로고
    • Reovirus polypeptide σ3 and N-terminal myristoylation of polypeptide μ1are required for site-specific cleavage to μ1C in transfected cells
    • Tillotson L., Shatkin A. J. Reovirus polypeptide σ3 and N-terminal myristoylation of polypeptide μ1are required for site-specific cleavage to μ1C in transfected cells. J. Virol. 66:1992;2180-2186.
    • (1992) J. Virol. , vol.66 , pp. 2180-2186
    • Tillotson, L.1    Shatkin, A.J.2
  • 201
    • 0025947970 scopus 로고
    • Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase
    • Watson J. C., Chang H.-W., Jacobs B. L. Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase. Virology. 185:1991;206-216.
    • (1991) Virology , vol.185 , pp. 206-216
    • Watson, J.C.1    Chang, H.-W.2    Jacobs, B.L.3
  • 202
    • 0021140522 scopus 로고
    • Characterization of a specific kinase inhibitory factor produced by vaccinia virus which inhibits the interferon-induced protein kinase activity
    • Whitaker-Dowling P. A., Younger J. S. Characterization of a specific kinase inhibitory factor produced by vaccinia virus which inhibits the interferon-induced protein kinase activity. Virology. 137:1984;171-181.
    • (1984) Virology , vol.137 , pp. 171-181
    • Whitaker-Dowling, P.A.1    Younger, J.S.2
  • 203
    • 0028797781 scopus 로고
    • The role of the dsRNA-activated kinase, PKR, in signal transduction
    • Williams B. R. G. The role of the dsRNA-activated kinase, PKR, in signal transduction. Semin. Virol. 6:1995;191-202.
    • (1995) Semin. Virol. , vol.6 , pp. 191-202
    • Williams, B.R.G.1
  • 205
    • 0029981093 scopus 로고    scopus 로고
    • An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells
    • Yeung M. C., Liu J., Lau A. S. An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells. Proc. Natl. Acad. Sci. USA. 93:1996;12451-12455.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12451-12455
    • Yeung, M.C.1    Liu, J.2    Lau, A.S.3
  • 206
    • 0030836687 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins
    • a
    • Yue Z., Shatkin A. J. Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins. Virology. 234:1997;364-371. a.
    • (1997) Virology , vol.234 , pp. 364-371
    • Yue, Z.1    Shatkin, A.J.2
  • 207
    • 0030047418 scopus 로고    scopus 로고
    • Regulated, stable expression and nuclear presence of reovirus double-stranded RNA-binding protein σ3 in hela cells
    • b
    • Yue Z., Shatkin A. J. Regulated, stable expression and nuclear presence of reovirus double-stranded RNA-binding protein σ3 in hela cells. J. Virol. 70:1997;3497-3501. b.
    • (1997) J. Virol. , vol.70 , pp. 3497-3501
    • Yue, Z.1    Shatkin, A.J.2
  • 209
    • 0027510449 scopus 로고
    • Expression cloning of 2′-5′ A-dependent RNAase: A uniquely regulated mediator of interferon action
    • Zhou A., Hassel B. A., Silverman R. H. Expression cloning of 2′-5′ A-dependent RNAase. a uniquely regulated mediator of interferon action Cell. 72:1993;753-765.
    • (1993) Cell , vol.72 , pp. 753-765
    • Zhou, A.1    Hassel, B.A.2    Silverman, R.H.3
  • 210
    • 0030908706 scopus 로고    scopus 로고
    • Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2
    • Zhu S., Romano P. R., Wek R. C. Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2. J. Biol. Chem. 272:1997;14434-14441.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14434-14441
    • Zhu, S.1    Romano, P.R.2    Wek, R.C.3
  • 211
    • 0014819628 scopus 로고
    • Studies on the intercellular synthesis of reovirus-specified proteins
    • Zweerink H. J., Joklik W. K. Studies on the intercellular synthesis of reovirus-specified proteins. Virology. 44:1970;501-518.
    • (1970) Virology , vol.44 , pp. 501-518
    • Zweerink, H.J.1    Joklik, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.