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Volumn 119, Issue 1, 2006, Pages 89-99

Phosphorylation and dephosphorylation events that regulate viral mRNA translation

Author keywords

Phosphorylation; Translational control; Viruses

Indexed keywords

INITIATION FACTOR 4E; INITIATION FACTOR 4F; MAMMALIAN TARGET OF RAPAMYCIN; POLYADENYLIC ACID BINDING PROTEIN; VIRUS MESSENGER RNA;

EID: 32644446560     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2005.10.009     Document Type: Article
Times cited : (36)

References (128)
  • 1
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E., Denzler K.L., Tartaglia J., Perkus M.E., Paoletti E., and 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
    • (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
  • 3
    • 0038668784 scopus 로고    scopus 로고
    • P58(IPK), a plant ortholog of double-stranded RNA-dependent protein kinase PKR inhibitor, functions in viral pathogenesis
    • Bilgin D.D., Liu Y., Schiff M., and Dinesh-Kumar S.P. P58(IPK), a plant ortholog of double-stranded RNA-dependent protein kinase PKR inhibitor, functions in viral pathogenesis. Dev. Cell 4 (2003) 651-661
    • (2003) Dev. Cell , vol.4 , pp. 651-661
    • Bilgin, D.D.1    Liu, Y.2    Schiff, M.3    Dinesh-Kumar, S.P.4
  • 4
    • 0028147382 scopus 로고
    • ICP34.5 mutants of herpes simplex virus type 1 strain 17syn+ are attenuated for neurovirulence in mice and for replication in confluent primary mouse embryo cell cultures
    • Bolovan C.A., Sawtell N.M., and Thompson R.L. ICP34.5 mutants of herpes simplex virus type 1 strain 17syn+ are attenuated for neurovirulence in mice and for replication in confluent primary mouse embryo cell cultures. J. Virol. 68 (1994) 48-55
    • (1994) J. Virol. , vol.68 , pp. 48-55
    • Bolovan, C.A.1    Sawtell, N.M.2    Thompson, R.L.3
  • 5
    • 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., and 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
  • 6
    • 0035158662 scopus 로고    scopus 로고
    • Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model
    • Brandt T.A., and Jacobs B.L. Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model. J. Virol. 75 (2001) 850-856
    • (2001) J. Virol. , vol.75 , pp. 850-856
    • Brandt, T.A.1    Jacobs, B.L.2
  • 7
    • 0035125267 scopus 로고    scopus 로고
    • Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase
    • Burysek L., and Pitha P.M. Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase. J. Virol. 75 (2001) 2345-2352
    • (2001) J. Virol. , vol.75 , pp. 2345-2352
    • Burysek, L.1    Pitha, P.M.2
  • 8
    • 0036272304 scopus 로고    scopus 로고
    • Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons
    • Byrd M.P., Zamora M., and Lloyd R.E. Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons. Mol. Cell. Biol. 22 (2002) 4499-4511
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4499-4511
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 9
    • 0027361738 scopus 로고
    • The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency
    • Cai W., Astor T.L., Liptak L.M., Cho C., Coen D.M., and Schaffer P.A. The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency. J. Virol. 67 (1993) 7501-7512
    • (1993) J. Virol. , vol.67 , pp. 7501-7512
    • Cai, W.1    Astor, T.L.2    Liptak, L.M.3    Cho, C.4    Coen, D.M.5    Schaffer, P.A.6
  • 10
    • 2442679170 scopus 로고    scopus 로고
    • Selective modification of eukaryotic initiation factor 4F (eIF4F) at the onset of cell differentiation: recruitment of eIF4GII and long lasting phosphorylation of eIF4E
    • Caron S., Charon M., Cramer E., Sonenberg N., and Dusanter-Fourt I. Selective modification of eukaryotic initiation factor 4F (eIF4F) at the onset of cell differentiation: recruitment of eIF4GII and long lasting phosphorylation of eIF4E. Mol. Cell. Biol. 24 (2004) 4920-4928
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4920-4928
    • Caron, S.1    Charon, M.2    Cramer, E.3    Sonenberg, N.4    Dusanter-Fourt, I.5
  • 11
    • 0344405787 scopus 로고    scopus 로고
    • 134.5 protein of herpes simplex virus 1 have differential effects on viral response to interferon-α
    • 134.5 protein of herpes simplex virus 1 have differential effects on viral response to interferon-α. Virology 307 (2003) 290-300
    • (2003) Virology , vol.307 , pp. 290-300
    • Cerveny, M.1    Hessefort, S.2    Yang, K.3    Cheng, G.4    Gross, M.5    He, B.6
  • 12
    • 11144247914 scopus 로고    scopus 로고
    • Factor-independent assembly of elongation-competent ribosomes by an internal ribosome entry site located in an RNA virus that infects penaeid shrimp
    • Cevallos R.C., and Sarnow P. Factor-independent assembly of elongation-competent ribosomes by an internal ribosome entry site located in an RNA virus that infects penaeid shrimp. J. Virol. 79 (2005) 677-683
    • (2005) J. Virol. , vol.79 , pp. 677-683
    • Cevallos, R.C.1    Sarnow, P.2
  • 13
    • 0030725392 scopus 로고    scopus 로고
    • Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation
    • Chang Y.W., and Traugh J.A. Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation. J. Biol. Chem. 272 (1997) 28252-28257
    • (1997) J. Biol. Chem. , vol.272 , pp. 28252-28257
    • Chang, Y.W.1    Traugh, J.A.2
  • 14
    • 0035841360 scopus 로고    scopus 로고
    • 134.5 protein of herpes simplex virus 1 are required for viral resistance to interferon α/β
    • 134.5 protein of herpes simplex virus 1 are required for viral resistance to interferon α/β. Virology 290 (2001) 115-120
    • (2001) Virology , vol.290 , pp. 115-120
    • Cheng, G.1    Brett, M.E.2    He, B.3
  • 15
    • 13744253138 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein
    • Cheng G., Feng Z., and He B. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein. J. Virol. 79 (2005) 1379-1388
    • (2005) J. Virol. , vol.79 , pp. 1379-1388
    • Cheng, G.1    Feng, Z.2    He, B.3
  • 16
    • 0346995213 scopus 로고    scopus 로고
    • Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1
    • Child S.J., Hakki M., De Niro K.L., and Geballe A.P. Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1. J. Virol. 78 (2004) 197-205
    • (2004) J. Virol. , vol.78 , pp. 197-205
    • Child, S.J.1    Hakki, M.2    De Niro, K.L.3    Geballe, A.P.4
  • 17
    • 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., and 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. U.S.A. 89 (1992) 3266-3270
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3266-3270
    • Chou, J.1    Roizman, B.2
  • 18
    • 0028277376 scopus 로고
    • Herpes simplex virus 1 gamma(1)34.5 gene function, which blocks the host response to infection, maps in the homologous domain of the genes expressed during growth arrest and DNA damage
    • Chou J., and Roizman B. Herpes simplex virus 1 gamma(1)34.5 gene function, which blocks the host response to infection, maps in the homologous domain of the genes expressed during growth arrest and DNA damage. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5247-55251
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5247-55251
    • Chou, J.1    Roizman, B.2
  • 19
    • 0025688373 scopus 로고
    • Mapping of herpes simplex virus-1 neurovirulence to gamma (1) 34.5, a gene nonessential for growth in culture
    • Chou J., Kern E.R., Whitley R.J., and Roizman B. Mapping of herpes simplex virus-1 neurovirulence to gamma (1) 34.5, a gene nonessential for growth in culture. Science 250 (1990) 1262-1266
    • (1990) Science , vol.250 , pp. 1262-1266
    • Chou, J.1    Kern, E.R.2    Whitley, R.J.3    Roizman, B.4
  • 20
    • 0030965882 scopus 로고    scopus 로고
    • Surprising specificity of PKR binding to delta agent genomic RNA
    • Circle D.A., Neel O.D., Robertson H.D., Clarke P.A., and Mathews M.B. Surprising specificity of PKR binding to delta agent genomic RNA. RNA 3 (1997) 438-448
    • (1997) RNA , vol.3 , pp. 438-448
    • Circle, D.A.1    Neel, O.D.2    Robertson, H.D.3    Clarke, P.A.4    Mathews, M.B.5
  • 21
    • 0036785522 scopus 로고    scopus 로고
    • Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1
    • Connor J.H., and Lyles D.S. Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1. J. Virol. 76 (2002) 10177-19187
    • (2002) J. Virol. , vol.76 , pp. 10177-19187
    • Connor, J.H.1    Lyles, D.S.2
  • 22
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate binding protein with the eIF4G homologue PAIP enhances translation
    • Craig A.W., Haghighat A., Yu A.T., and Sonenberg N. Interaction of polyadenylate binding protein with the eIF4G homologue PAIP enhances translation. Nature 392 (1998) 520-523
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 23
    • 0034600839 scopus 로고    scopus 로고
    • Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F
    • Cuesta R., Xi Q., and Schneider R.J. Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F. EMBO J. 19 (2000) 3465-3474
    • (2000) EMBO J. , vol.19 , pp. 3465-3474
    • Cuesta, R.1    Xi, Q.2    Schneider, R.J.3
  • 24
    • 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., and 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
  • 25
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever T.E. Gene-specific regulation by general translation factors. Cell 108 (2002) 545-556
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 26
    • 0025747520 scopus 로고
    • Differential dependence of herpes simplex virus immediate-early gene expression on de novo-infected cell protein synthesis
    • Elshiekh N.A., Harris-Hamilton E., and Bachenheimer S.L. Differential dependence of herpes simplex virus immediate-early gene expression on de novo-infected cell protein synthesis. J. Virol. 65 (1991) 6430-6437
    • (1991) J. Virol. , vol.65 , pp. 6430-6437
    • Elshiekh, N.A.1    Harris-Hamilton, E.2    Bachenheimer, S.L.3
  • 27
    • 0033624137 scopus 로고    scopus 로고
    • ICP0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett R.D. ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioassays 22 (2000) 761-770
    • (2000) Bioassays , vol.22 , pp. 761-770
    • Everett, R.D.1
  • 28
    • 0027252545 scopus 로고
    • Modification of eukaryotic initiation factor 4F during infection by influenza virus
    • Feigenblum D., and Schneider R.J. Modification of eukaryotic initiation factor 4F during infection by influenza virus. J. Virol. 67 (1993) 3027-3035
    • (1993) J. Virol. , vol.67 , pp. 3027-3035
    • Feigenblum, D.1    Schneider, R.J.2
  • 29
    • 0029791354 scopus 로고    scopus 로고
    • Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation
    • Feigenblum D., and Schneider R.J. Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation. Mol. Cell. Biol. 16 (1996) 5450-5457
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5450-5457
    • Feigenblum, D.1    Schneider, R.J.2
  • 30
    • 0037166289 scopus 로고    scopus 로고
    • Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2 alpha
    • Fernandez J., Yaman I., Sarnow P., Snider M.D., and Hatzoglou M. Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2 alpha. J. Biol. Chem. 277 (2002) 19198-19205
    • (2002) J. Biol. Chem. , vol.277 , pp. 19198-19205
    • Fernandez, J.1    Yaman, I.2    Sarnow, P.3    Snider, M.D.4    Hatzoglou, M.5
  • 31
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplex RNA: one motif, multiple functions
    • Fierro-Monti I., and Mathews M.B. Proteins binding to duplex RNA: one motif, multiple functions. Trends Biochem. Sci. 25 (2000) 241-246
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 241-246
    • Fierro-Monti, I.1    Mathews, M.B.2
  • 32
    • 9644289432 scopus 로고    scopus 로고
    • Proteomics of herpes simplex virus infected cell protein 27: association with translation initiation factors
    • Fontaine-Rodriguez E.C., Taylor T.J., Olesky M., and Knipe D.M. Proteomics of herpes simplex virus infected cell protein 27: association with translation initiation factors. Virology 330 (2004) 487-492
    • (2004) Virology , vol.330 , pp. 487-492
    • Fontaine-Rodriguez, E.C.1    Taylor, T.J.2    Olesky, M.3    Knipe, D.M.4
  • 33
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • Fukunaga R., and Hunter T. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16 (1997) 1921-1933
    • (1997) EMBO J. , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 35
    • 0030694555 scopus 로고    scopus 로고
    • Adenovirus infection inactivates the translational inhibitors 4E-BP1 and 4E-BP2
    • Gingras A.C., and Sonenberg N. Adenovirus infection inactivates the translational inhibitors 4E-BP1 and 4E-BP2. Virology 237 (1997) 182-186
    • (1997) Virology , vol.237 , pp. 182-186
    • Gingras, A.C.1    Sonenberg, N.2
  • 36
    • 0029890687 scopus 로고    scopus 로고
    • Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus
    • Gingras A.C., Svitkin Y., Belsham G.J., Pause A., and Sonenberg N. Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 5578-5583
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5578-5583
    • Gingras, A.C.1    Svitkin, Y.2    Belsham, G.J.3    Pause, A.4    Sonenberg, N.5
  • 37
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras A.-C., Raught B., and Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68 (1999) 913-963
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 38
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras A.-C., Raught B., and Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15 (2001) 807-826
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 40
    • 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., Rice A.P., Robertson H.D., and 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. U.S.A. 87 (1990) 8687-8691
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8687-8691
    • Gunnery, S.1    Rice, A.P.2    Robertson, H.D.3    Mathews, M.B.4
  • 41
    • 1242342140 scopus 로고    scopus 로고
    • Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1
    • Hagglund R., and Roizman B. Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J. Virol. 78 (2004) 2169-2178
    • (2004) J. Virol. , vol.78 , pp. 2169-2178
    • Hagglund, R.1    Roizman, B.2
  • 42
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat A., Mader S., Pause A., and Sonenberg N. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J. 14 (1995) 5701-5709
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 43
    • 0035100854 scopus 로고    scopus 로고
    • ICP0 is required for efficient reactivation of herpes simplex virus type 1 from neuronal latency
    • Halford W.P., and Schaffer P.A. ICP0 is required for efficient reactivation of herpes simplex virus type 1 from neuronal latency. J. Virol. 75 (2001) 3240-3249
    • (2001) J. Virol. , vol.75 , pp. 3240-3249
    • Halford, W.P.1    Schaffer, P.A.2
  • 44
    • 0032980412 scopus 로고    scopus 로고
    • Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells
    • Hatada E., Saito S., and Fukuda R. Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J. Virol. 73 (1999) 2425-2433
    • (1999) J. Virol. , vol.73 , pp. 2425-2433
    • Hatada, E.1    Saito, S.2    Fukuda, R.3
  • 45
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1 alpha to dephosphorylate the alpha subunit of eukaryotic initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • He B., Gross M., and Roizman B. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1 alpha to dephosphorylate the alpha subunit of eukaryotic initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 843-848
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 46
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen C.U., and Sarnow P. Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev. 15 (2001) 1593-1612
    • (2001) Genes Dev. , vol.15 , pp. 1593-1612
    • Hellen, C.U.1    Sarnow, P.2
  • 47
    • 0025857246 scopus 로고
    • Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein
    • Huang J.T., and Schneider R.J. Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein. Cell 65 (1991) 271-280
    • (1991) Cell , vol.65 , pp. 271-280
    • Huang, J.T.1    Schneider, R.J.2
  • 48
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataja H., Gradi A., and Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17 (1998) 7480-7489
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataja, H.1    Gradi, A.2    Sonenberg, N.3
  • 49
    • 0016795964 scopus 로고
    • RNA synthesis in cells infected with herpes simplex virus. Part X: properties of viral symmetric transcripts and of double-stranded RNA prepared from them
    • Jacquemont B., and Roizman B. RNA synthesis in cells infected with herpes simplex virus. Part X: properties of viral symmetric transcripts and of double-stranded RNA prepared from them. J. Virol. 15 (1975) 707-713
    • (1975) J. Virol. , vol.15 , pp. 707-713
    • Jacquemont, B.1    Roizman, B.2
  • 50
    • 0036776317 scopus 로고    scopus 로고
    • Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells
    • Jordan R., Wang L., Graczyk T.M., Block T.M., and Romano P.R. Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells. J. Virol. 76 (2002) 9588-9599
    • (2002) J. Virol. , vol.76 , pp. 9588-9599
    • Jordan, R.1    Wang, L.2    Graczyk, T.M.3    Block, T.M.4    Romano, P.R.5
  • 51
    • 0035787721 scopus 로고    scopus 로고
    • The mRNA closed-loop model: the function of PABP and PABP-interacting proteins in mRNA translation
    • Kahvejian A., Roy G., and Sonenberg N. The mRNA closed-loop model: the function of PABP and PABP-interacting proteins in mRNA translation. Cold Spring Harb. Symp. Q. Biol. 66 (2001) 293-300
    • (2001) Cold Spring Harb. Symp. Q. Biol. , vol.66 , pp. 293-300
    • Kahvejian, A.1    Roy, G.2    Sonenberg, N.3
  • 52
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • Kahvejian A., Svitkin Y.V., Sukarieh R., M'Boutchou M.N., and Sonenberg N. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 19 (2005) 104-113
    • (2005) Genes Dev. , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.N.4    Sonenberg, N.5
  • 53
    • 0001815885 scopus 로고    scopus 로고
    • Double-stranded RNA-activated protein kinase PKR
    • Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Kaufman R.J. Double-stranded RNA-activated protein kinase PKR. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). Translational Control (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 503-528
    • (2000) Translational Control , pp. 503-528
    • Kaufman, R.J.1
  • 54
    • 0031911640 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1 delta is hyperphosphorylated by the UI13 gene of herpes simplex virus 1
    • Kawaguchi Y., Van Sant C., and Roizman B. Eukaryotic elongation factor 1 delta is hyperphosphorylated by the UI13 gene of herpes simplex virus 1. J. Virol. 72 (1998) 1731-1736
    • (1998) J. Virol. , vol.72 , pp. 1731-1736
    • Kawaguchi, Y.1    Van Sant, C.2    Roizman, B.3
  • 55
    • 0032954616 scopus 로고    scopus 로고
    • Cellular elongation factor 1 delta is modified in cells infected with representative alpha, beta, or gammaherpes viruses
    • Kawaguchi Y., Matsumara T., Roizman B., and Hirai K. Cellular elongation factor 1 delta is modified in cells infected with representative alpha, beta, or gammaherpes viruses. J. Virol. 73 (1999) 4456-4460
    • (1999) J. Virol. , vol.73 , pp. 4456-4460
    • Kawaguchi, Y.1    Matsumara, T.2    Roizman, B.3    Hirai, K.4
  • 56
    • 0037319965 scopus 로고    scopus 로고
    • Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1 delta
    • Kawaguchi Y., Kato K., Tanaka M., Kanamori M., Nishiyama Y., and Yamanashi Y. Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1 delta. J. Virol. 77 (2003) 2359-2368
    • (2003) J. Virol. , vol.77 , pp. 2359-2368
    • Kawaguchi, Y.1    Kato, K.2    Tanaka, M.3    Kanamori, M.4    Nishiyama, Y.5    Yamanashi, Y.6
  • 58
    • 0036888921 scopus 로고    scopus 로고
    • Characterization of RNA determinants recognized by the arginine- and proline-rich region of Us11, a herpes simplex virus type 1-encoded double-stranded RNA binding protein that prevents PKR activation
    • Khoo D., Perez C., and Mohr I. Characterization of RNA determinants recognized by the arginine- and proline-rich region of Us11, a herpes simplex virus type 1-encoded double-stranded RNA binding protein that prevents PKR activation. J. Virol. 76 (2002) 11971-11981
    • (2002) J. Virol. , vol.76 , pp. 11971-11981
    • Khoo, D.1    Perez, C.2    Mohr, I.3
  • 59
    • 0000942112 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott/The Williams & Wilkins Co., Philadelphia
    • Kieff E., and Rickinson A.B. Epstein-Barr virus and its replication. In: Knipe D.M., and Howley P.M. (Eds). Fields' Virology. fourth ed. (2001), Lippincott/The Williams & Wilkins Co., Philadelphia 2511-2574
    • (2001) Fields' Virology. fourth ed. , pp. 2511-2574
    • Kieff, E.1    Rickinson, A.B.2
  • 60
    • 4644252994 scopus 로고    scopus 로고
    • Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase
    • Kudchodkar S.B., Yu Y., Maguire T.G., and Alwine J.C. Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase. J. Virol. 78 (2004) 11030-11039
    • (2004) J. Virol. , vol.78 , pp. 11030-11039
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 61
  • 63
    • 0030863401 scopus 로고    scopus 로고
    • 4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential α27 gene
    • 4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential α27 gene. J. Virol. 71 (1997) 8602-8614
    • (1997) J. Virol. , vol.71 , pp. 8602-8614
    • Lium, E.K.1    Silverstein, S.J.2
  • 64
    • 0026465267 scopus 로고
    • Translational stimulation by reovirus polypeptide sigma 3: substitution for VAI RNA and inhibition of phosphorylation of the alpha subunit of eukaryotic initiation factor 2
    • Lloyd R.M., and Shatkin A.J. Translational stimulation by reovirus polypeptide sigma 3: substitution for VAI RNA and inhibition of phosphorylation of the alpha 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
  • 65
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor
    • Lu Y., Wambach M., Katze M.G., and Krug R.M. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-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
  • 66
    • 0025975357 scopus 로고
    • Herpes simplex virus type 1 deletion variants 1714 and 1716 pinpoint neurovirulence-related sequences in Glasgow strain 17+ between immediate early gene 1 and the 'a' sequence
    • Maclean A.R., Ul-Fareed M., Robertson L., Harland J., and Brown S.M. Herpes simplex virus type 1 deletion variants 1714 and 1716 pinpoint neurovirulence-related sequences in Glasgow strain 17+ between immediate early gene 1 and the 'a' sequence. J. Gen. Virol. 72 (1991) 631-639
    • (1991) J. Gen. Virol. , vol.72 , pp. 631-639
    • Maclean, A.R.1    Ul-Fareed, M.2    Robertson, L.3    Harland, J.4    Brown, S.M.5
  • 67
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4G and the translational repressors 4E-binding proteins
    • Mader S., Lee H., Pause A., and Sonenberg N. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4G and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15 (1995) 4990-4997
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 69
    • 0023948036 scopus 로고
    • Characterization of the double-stranded RNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNA
    • Maran A., and Mathews M.B. Characterization of the double-stranded RNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNA. Virology 164 (1988) 106-113
    • (1988) Virology , vol.164 , pp. 106-113
    • Maran, A.1    Mathews, M.B.2
  • 70
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J., Gingras A.C., Sonenberg N., and Burley S.K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 3 (1999) 707-716
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 71
    • 0031755021 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells
    • Marissen W.E., and Lloyd R.E. Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells. Mol. Cell. Biol. 18 (1998) 7565-7574
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7565-7574
    • Marissen, W.E.1    Lloyd, R.E.2
  • 72
    • 0034517764 scopus 로고    scopus 로고
    • Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis
    • Marissen W.E., Gradi A., Sonenberg N., and Lloyd R.E. Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis. Cell Death Differ. 7 (2000) 1234-1243
    • (2000) Cell Death Differ. , vol.7 , pp. 1234-1243
    • Marissen, W.E.1    Gradi, A.2    Sonenberg, N.3    Lloyd, R.E.4
  • 74
    • 0001593941 scopus 로고    scopus 로고
    • Cytomegaloviruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott/The Williams & Wilkins Co., Philadelphia
    • Mocarski Jr. E.S., and Courcelle C.T. Cytomegaloviruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields' Virology. fourth ed. (2001), Lippincott/The Williams & Wilkins Co., Philadelphia 2629-2673
    • (2001) Fields' Virology. fourth ed. , pp. 2629-2673
    • Mocarski Jr., E.S.1    Courcelle, C.T.2
  • 75
    • 0037319231 scopus 로고    scopus 로고
    • Genetic metamorphosis of herpes simplex virus-1 into a biological therapeutic for human cancer
    • Mohr I. Genetic metamorphosis of herpes simplex virus-1 into a biological therapeutic for human cancer. Expert Opin. Biol. Ther. 3 (2003) 113-125
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 113-125
    • Mohr, I.1
  • 76
    • 33646891506 scopus 로고    scopus 로고
    • Mohr, I. Hailing the arrival of the messenger: strategies for translational control in herpes simplex virus-infected cells. In: Sandri-Goldin, R. (Ed.), New Developments in Alphaherpesvirus Research. Horizon Scientific Press, Norwich, UK, in press.
  • 77
    • 0029841340 scopus 로고    scopus 로고
    • A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function
    • Mohr I., and Gluzman Y. A herpesvirus 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
  • 79
    • 0033013721 scopus 로고    scopus 로고
    • A herpesvirus ribosome associated. RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function
    • Mulvey M., Poppers J., Ladd A., and Mohr I. A herpesvirus ribosome associated. RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function. J. Virol. 73 (1999) 3375-3385
    • (1999) J. Virol. , vol.73 , pp. 3375-3385
    • Mulvey, M.1    Poppers, J.2    Ladd, A.3    Mohr, I.4
  • 80
    • 0141566327 scopus 로고    scopus 로고
    • Regulation of eIF2 alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle
    • Mulvey M., Poppers J., Sternberg D., and Mohr I. Regulation of eIF2 alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle. J. Virol. 77 (2003) 10917-10928
    • (2003) J. Virol. , vol.77 , pp. 10917-10928
    • Mulvey, M.1    Poppers, J.2    Sternberg, D.3    Mohr, I.4
  • 82
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA binding protein sigma 3 at 1.8A resolution
    • Olland A.M., Jane-Valbuena J., Schiff L.A., Nibert M.L., and Harrison S.C. Structure of the reovirus outer capsid and dsRNA binding protein sigma 3 at 1.8A resolution. EMBO J. 20 (2001) 979-989
    • (2001) EMBO J. , vol.20 , pp. 979-989
    • Olland, A.M.1    Jane-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 83
    • 17144403770 scopus 로고    scopus 로고
    • Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication
    • O'Shea C., Klupsch K., Choi S., Bagus B., Soria C., Shen J., McCormick F., and Stokoe D. Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication. EMBO J. 24 (2005) 1211-1221
    • (2005) EMBO J. , vol.24 , pp. 1211-1221
    • O'Shea, C.1    Klupsch, K.2    Choi, S.3    Bagus, B.4    Soria, C.5    Shen, J.6    McCormick, F.7    Stokoe, D.8
  • 84
    • 0032480017 scopus 로고    scopus 로고
    • PACT: a protein activator of the interferon-induced protein kinase, PKR
    • Patel R.C., and Sen G.C. PACT: a protein activator of the interferon-induced protein kinase, PKR. EMBO J. 17 (1998) 4379-4390
    • (1998) EMBO J. , vol.17 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 85
    • 0036145483 scopus 로고    scopus 로고
    • Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKR
    • Pavio N., Taylor D.R., and Lai M.M. Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKR. J. Virol. 76 (2002) 1265-1272
    • (2002) J. Virol. , vol.76 , pp. 1265-1272
    • Pavio, N.1    Taylor, D.R.2    Lai, M.M.3
  • 86
    • 0037333913 scopus 로고    scopus 로고
    • Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2 alpha kinase PERK
    • Pavio N., Romano P.R., Graczyk T.M., Feinstone S.M., and Taylor D.R. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2 alpha kinase PERK. J. Virol. 77 (2003) 3578-3585
    • (2003) J. Virol. , vol.77 , pp. 3578-3585
    • Pavio, N.1    Romano, P.R.2    Graczyk, T.M.3    Feinstone, S.M.4    Taylor, D.R.5
  • 87
    • 0002570015 scopus 로고    scopus 로고
    • Viral translational strategies and host defense mechanisms
    • Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Pe'ery T., and Mathews M.B. Viral translational strategies and host defense mechanisms. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). Translational Control (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 371-424
    • (2000) Translational Control , pp. 371-424
    • Pe'ery, T.1    Mathews, M.B.2
  • 88
    • 0036839211 scopus 로고    scopus 로고
    • Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein
    • Peters G.A., Khoo D., Mohr I., and Sen G.C. Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein. J. Virol. 76 (2002) 11054-11064
    • (2002) J. Virol. , vol.76 , pp. 11054-11064
    • Peters, G.A.1    Khoo, D.2    Mohr, I.3    Sen, G.C.4
  • 89
    • 33646866136 scopus 로고    scopus 로고
    • Inhibition of PKR activation by the proline rich RNA binding domain of the HSV-1 Us11 protein
    • Poppers J., Mulvey M., Khoo D., and Mohr I. Inhibition of PKR activation by the proline rich RNA binding domain of the HSV-1 Us11 protein. J. Virol. 74 (2000) 112315-112321
    • (2000) J. Virol. , vol.74 , pp. 112315-112321
    • Poppers, J.1    Mulvey, M.2    Khoo, D.3    Mohr, I.4
  • 90
    • 0037213277 scopus 로고    scopus 로고
    • Identification of a lytic-cycle Epstein-Barr virus gene product that can regulate PKR activation
    • Poppers J., Mulvey M., Perez C., Khoo D., and Mohr I. Identification of a lytic-cycle Epstein-Barr virus gene product that can regulate PKR activation. J. Virol. 77 (2003) 228-236
    • (2003) J. Virol. , vol.77 , pp. 228-236
    • Poppers, J.1    Mulvey, M.2    Perez, C.3    Khoo, D.4    Mohr, I.5
  • 91
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., and Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18 (1999) 270-279
    • (1999) EMBO J. , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.-C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 92
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught B., Gingras A.C., Gygy S.P., Imataka H., Morino S., Gradi A., Aebersold R., and Sonenberg N. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19 (2000) 434-444
    • (2000) EMBO J. , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygy, S.P.3    Imataka, H.4    Morino, S.5    Gradi, A.6    Aebersold, R.7    Sonenberg, N.8
  • 93
    • 0030013732 scopus 로고    scopus 로고
    • Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR
    • Robertson H.D., Manche L., and 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
  • 95
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott/The Williams & Wilkins Co., Philadelphia
    • Roizman B., and Knipe D. Herpes simplex viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields' Virology. fourth ed. (2001), Lippincott/The Williams & Wilkins Co., Philadelphia 2239-2459
    • (2001) Fields' Virology. fourth ed. , pp. 2239-2459
    • Roizman, B.1    Knipe, D.2
  • 96
    • 0031723958 scopus 로고    scopus 로고
    • Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain
    • Romano P.R., Zhang F., Tan S.L., Garcia-Barrio M.T., Katze M.G., Dever T.E., and Hinnebusch A.G. Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain. Mol. Cell. Biol. 18 (1998) 7304-7316
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7304-7316
    • Romano, P.R.1    Zhang, F.2    Tan, S.L.3    Garcia-Barrio, M.T.4    Katze, M.G.5    Dever, T.E.6    Hinnebusch, A.G.7
  • 97
    • 0023135555 scopus 로고
    • Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture
    • Sacks W.R., and Schaffer P.A. Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture. J. Virol. 61 (1987) 829-839
    • (1987) J. Virol. , vol.61 , pp. 829-839
    • Sacks, W.R.1    Schaffer, P.A.2
  • 98
    • 0036147256 scopus 로고    scopus 로고
    • Effects of influenza A virus NS1 protein on protein expression: the NS1 protein enhances translation and is not required for shutoff of host protein synthesis
    • Salvatore M., Basler C.F., Parisien J.P., Horvath C.M., Bourmakina S., Zheng H., Muster T., Palese P., and Garcia-Sastre A. Effects of influenza A virus NS1 protein on protein expression: the NS1 protein enhances translation and is not required for shutoff of host protein synthesis. J. Virol. 76 (2002) 1206-1212
    • (2002) J. Virol. , vol.76 , pp. 1206-1212
    • Salvatore, M.1    Basler, C.F.2    Parisien, J.P.3    Horvath, C.M.4    Bourmakina, S.5    Zheng, H.6    Muster, T.7    Palese, P.8    Garcia-Sastre, A.9
  • 99
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov D.D., Ali S.M., Kim D.H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., and Sabatini D.M. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14 (2004) 1296-1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 100
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
    • Scheper G.C., and Proud C.G. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?. Eur. J. Biochem. 269 (2002) 5350-5359
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 101
    • 0035133659 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells
    • Scheper G.C., Morrice N.A., Kleijn M., and Proud C.G. The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells. Mol. Cell. Biol. 21 (2001) 743-754
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 743-754
    • Scheper, G.C.1    Morrice, N.A.2    Kleijn, M.3    Proud, C.G.4
  • 102
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA
    • Scheper G.C., van Kollenburg B., Hu J., Luo Y., Goss D.J., and Proud C.G. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277 (2002) 3303-3309
    • (2002) J. Biol. Chem. , vol.277 , pp. 3303-3309
    • Scheper, G.C.1    van Kollenburg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 103
    • 0002813638 scopus 로고    scopus 로고
    • Adenovirus inhibition of cellular protein synthesis and preferential translation of viral mRNAs
    • Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Schneider R.J. Adenovirus inhibition of cellular protein synthesis and preferential translation of viral mRNAs. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). Translational Control (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 901-914
    • (2000) Translational Control , pp. 901-914
    • Schneider, R.J.1
  • 104
    • 0037333760 scopus 로고    scopus 로고
    • Translation initiation and viral tricks
    • Schneider R.J., and Mohr I. Translation initiation and viral tricks. Trends Biochem. Sci. 28 (2003) 130-136
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 130-136
    • Schneider, R.J.1    Mohr, I.2
  • 105
    • 0027487288 scopus 로고
    • Comparative analysis of the regulation of the interferon-inducible protein kinase PKR by Epstein-Barr virus RNAs EBER-1 and EBER-2 and adenovirus VAI RNA
    • Sharp T.V., Schwemmle M., Jeffrey I., Laing K., Mellor H., Proud C.G., Hilse K., and Clemens M.J. Comparative analysis of the regulation of the interferon-inducible protein kinase PKR by Epstein-Barr virus RNAs EBER-1 and EBER-2 and adenovirus VAI RNA. Nucleic Acids Res. 21 (1993) 4483-4490
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4483-4490
    • Sharp, T.V.1    Schwemmle, M.2    Jeffrey, I.3    Laing, K.4    Mellor, H.5    Proud, C.G.6    Hilse, K.7    Clemens, M.J.8
  • 106
    • 0034163483 scopus 로고    scopus 로고
    • Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans: Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress
    • Sood R., Porter A.C., Ma K., Quilliam L.A., and Wek R.C. Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans: Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress. Biochem. J. 346 (2000) 281-293
    • (2000) Biochem. J. , vol.346 , pp. 281-293
    • Sood, R.1    Porter, A.C.2    Ma, K.3    Quilliam, L.A.4    Wek, R.C.5
  • 107
    • 0015009707 scopus 로고
    • Control of macromolecular synthesis in proliferating and resting Syrian hamster cells in monolayer culture. Part I: ribosome function
    • Stanners C.P., and Becker H. Control of macromolecular synthesis in proliferating and resting Syrian hamster cells in monolayer culture. Part I: ribosome function. J. Cell. Physiol. 77 (1971) 31-42
    • (1971) J. Cell. Physiol. , vol.77 , pp. 31-42
    • Stanners, C.P.1    Becker, H.2
  • 108
    • 0022978685 scopus 로고
    • Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110
    • Stow N.D., and Stow E.C. Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J. Gen. Virol. 67 (1986) 2571-2585
    • (1986) J. Gen. Virol. , vol.67 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 109
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • Su H., Liao C., and Li Y. Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J. Virol. 76 (2002) 4162-4171
    • (2002) J. Virol. , vol.76 , pp. 4162-4171
    • Su, H.1    Liao, C.2    Li, Y.3
  • 110
    • 0031670374 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase
    • Tan S.L., and Katze M.G. Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase. J. Interferon Cytokine Res. 18 (1998) 757-766
    • (1998) J. Interferon Cytokine Res. , vol.18 , pp. 757-766
    • Tan, S.L.1    Katze, M.G.2
  • 111
    • 0031897318 scopus 로고    scopus 로고
    • Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor
    • Tan S.L., Gale Jr. M.J., and Katze M.G. Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor. Mol. Cell. Biol. 18 (1998) 2431-2443
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2431-2443
    • Tan, S.L.1    Gale Jr., M.J.2    Katze, M.G.3
  • 112
    • 0033516497 scopus 로고    scopus 로고
    • Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein
    • Taylor D.R., Shi S.T., Romano P.R., Barber G.N., and Lai M.M. Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 (1999) 107-110
    • (1999) Science , vol.285 , pp. 107-110
    • Taylor, D.R.1    Shi, S.T.2    Romano, P.R.3    Barber, G.N.4    Lai, M.M.5
  • 113
    • 0018749512 scopus 로고
    • Regulation of protein synthesis during the shift of quiescent animal cells into the proliferative state
    • Thomas G., and Gordon J. Regulation of protein synthesis during the shift of quiescent animal cells into the proliferative state. Cell Biol. Int. Rep. 3 (1979) 307-320
    • (1979) Cell Biol. Int. Rep. , vol.3 , pp. 307-320
    • Thomas, G.1    Gordon, J.2
  • 114
    • 0022981962 scopus 로고
    • Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: identification of specific proteins
    • Thomas G., and Thomas G. Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: identification of specific proteins. J. Cell. Biol. 103 (1986) 2137-2144
    • (1986) J. Cell. Biol. , vol.103 , pp. 2137-2144
    • Thomas, G.1    Thomas, G.2
  • 115
    • 0019817630 scopus 로고
    • Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells
    • Thomas G., Thomas G., and Luther H. Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells. Proc. Natl. Acad. Sci. U.S.A. 78 (1981) 5712-5716
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 5712-5716
    • Thomas, G.1    Thomas, G.2    Luther, H.3
  • 116
    • 1842831274 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by mnk-1 enhances HSV-1 translation and replication in quiescent cells
    • Walsh D., and Mohr I. Phosphorylation of eIF4E by mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev. 18 (2004) 660-672
    • (2004) Genes Dev. , vol.18 , pp. 660-672
    • Walsh, D.1    Mohr, I.2
  • 117
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • Walsh D., Perez C., Notary J., and Mohr I. Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J. Virol. 79 (2005) 8057-8064
    • (2005) J. Virol. , vol.79 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 118
    • 0032995665 scopus 로고    scopus 로고
    • RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of basic amino acids
    • Wang W., Riedel K., Lynch P., Chien C.Y., Montelione G.T., and Krug R.M. RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of basic amino acids. RNA 5 (1999) 195-205
    • (1999) RNA , vol.5 , pp. 195-205
    • Wang, W.1    Riedel, K.2    Lynch, P.3    Chien, C.Y.4    Montelione, G.T.5    Krug, R.M.6
  • 119
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases mnk1 and mnk2
    • Waskiewicz A.J., Flynn A., Proud C.G., and Cooper J.A. Mitogen-activated protein kinases activate the serine/threonine kinases mnk1 and mnk2. EMBO J. 16 (1997) 1909-1920
    • (1997) EMBO J. , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 120
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation factor 4E by protein kinase mnk1 in vivo
    • Waskiewicz A.J., Johnson J.C., Penn B., Mahalingam M., Kimball S.R., and Cooper J.A. Phosphorylation of the cap-binding protein eukaryotic translation factor 4E by protein kinase mnk1 in vivo. Mol. Cell. Biol. 19 (1999) 1871-1880
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 121
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells S.E., Hillner P.E., Vale R.D., and Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2 (1998) 135-140
    • (1998) Mol. Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 122
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the a site of the ribosome
    • Wilson J.E., Pestova T.V., Hellen C.U., and Sarnow P. Initiation of protein synthesis from the a site of the ribosome. Cell 102 (2000) 511-520
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.3    Sarnow, P.4
  • 123
    • 4043099204 scopus 로고    scopus 로고
    • Tethering of eIF4G to adenoviral mRNAs by viral 100K protein drives ribosome shunting
    • Xi Q., Cuesta R., and Schneider R.J. Tethering of eIF4G to adenoviral mRNAs by viral 100K protein drives ribosome shunting. Genes Dev. 18 (2004) 1997-2009
    • (2004) Genes Dev. , vol.18 , pp. 1997-2009
    • Xi, Q.1    Cuesta, R.2    Schneider, R.J.3
  • 124
    • 17444389700 scopus 로고    scopus 로고
    • Regulation of translation by ribosome shunting through phosphotyrosine-dependent coupling of adenovirus protein 100K to viral mRNAs
    • Xi Q., Cuesta R., and Schneider R.J. Regulation of translation by ribosome shunting through phosphotyrosine-dependent coupling of adenovirus protein 100K to viral mRNAs. J. Virol. 79 (2005) 5676-5683
    • (2005) J. Virol. , vol.79 , pp. 5676-5683
    • Xi, Q.1    Cuesta, R.2    Schneider, R.J.3
  • 125
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W., Frank C.L., Korth M.J., Sopher B.L., Novoa I., Ron D., and Katze M.G. Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 15920-15925
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6    Katze, M.G.7
  • 126
    • 0030836687 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins
    • Yue Z., and Shatkin A.J. Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins. Virology 234 (1997) 364-371
    • (1997) Virology , vol.234 , pp. 364-371
    • Yue, Z.1    Shatkin, A.J.2
  • 127
    • 0029785142 scopus 로고    scopus 로고
    • Selective translation initiation by ribosome jumping in adenovirus-infected and heat-shocked cells
    • Yueh A., and Schneider R.J. Selective translation initiation by ribosome jumping in adenovirus-infected and heat-shocked cells. Genes Dev. 10 (1996) 1557-1567
    • (1996) Genes Dev. , vol.10 , pp. 1557-1567
    • Yueh, A.1    Schneider, R.J.2
  • 128
    • 0034090845 scopus 로고    scopus 로고
    • Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA
    • Yueh A., and Schneider R.J. Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA. Genes Dev. 14 (2000) 414-421
    • (2000) Genes Dev. , vol.14 , pp. 414-421
    • Yueh, A.1    Schneider, R.J.2


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