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Volumn 64, Issue 4, 2000, Pages 709-724

Cytopathogenesis and inhibition of host gene expression by RNA viruses

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR; M PROTEIN; TRANSCRIPTION FACTOR; VIRUS PROTEIN; VIRUS RNA;

EID: 0034440598     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.64.4.709-724.2000     Document Type: Review
Times cited : (150)

References (148)
  • 2
    • 0031662097 scopus 로고    scopus 로고
    • Effect of vesicular stomatitis virus matrix protein on transcription directed by host RNA polymerases I. II, and III
    • Ahmed, M., and D. S. Lyles. 1998. Effect of vesicular stomatitis virus matrix protein on transcription directed by host RNA polymerases I. II, and III. J. Virol. 72:8413-8419.
    • (1998) J. Virol. , vol.72 , pp. 8413-8419
    • Ahmed, M.1    Lyles, D.S.2
  • 3
    • 0030683577 scopus 로고    scopus 로고
    • Identification of a consensus mutation in M protein of vesicular stomatitis virus from persistently infected cells that affects inhibition of host-directed gene expression
    • Ahmed, M., and D. S. Lyles. 1997. Identification of a consensus mutation in M protein of vesicular stomatitis virus from persistently infected cells that affects inhibition of host-directed gene expression. Virology 237:378-388.
    • (1997) Virology , vol.237 , pp. 378-388
    • Ahmed, M.1    Lyles, D.S.2
  • 4
    • 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., M. E. Nemeroff, Y. Qiu, and R. M. Krug. 1992. Nucleocytoplasmic transport: the influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA. Genes Dev. 6:255-267.
    • (1992) Genes Dev. , vol.6 , pp. 255-267
    • Alonso-Caplen, F.V.1    Nemeroff, M.E.2    Qiu, Y.3    Krug, R.M.4
  • 5
    • 0033970831 scopus 로고    scopus 로고
    • Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/Caspase-8 death signaling pathway
    • Balachandran, S., P. C. Roberts, T. Kipperman, K. N. Bhalla, R. W. Compans, D. R. Archer, and G. N. Barber. 2000. Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/Caspase-8 death signaling pathway. J. Virol. 74:1513-1523.
    • (2000) J. Virol. , vol.74 , pp. 1513-1523
    • Balachandran, S.1    Roberts, P.C.2    Kipperman, T.3    Bhalla, K.N.4    Compans, R.W.5    Archer, D.R.6    Barber, G.N.7
  • 6
    • 0142137398 scopus 로고
    • The effect of mengovirus infection on the activity of DNA dependent RNA polymerase activity of L cells
    • USA
    • Baltimore, D., and R. M. Franklin. 1962. The effect of mengovirus infection on the activity of DNA dependent RNA polymerase activity of L cells. Proc. Natl. Acad. Sci. USA 48:1383-1390.
    • (1962) Proc. Natl. Acad. Sci. , vol.48 , pp. 1383-1390
    • Baltimore, D.1    Franklin, R.M.2
  • 7
    • 0027051117 scopus 로고
    • 5′ sequence of vesicular stomatitis virus N-gene confers selective translation of mRNA
    • Berg, D. T., and B. W. Grinnell. 1992. 5′ sequence of vesicular stomatitis virus N-gene confers selective translation of mRNA. Biochem. Biophys. Res. Commun. 189:1585-1590.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1585-1590
    • Berg, D.T.1    Grinnell, B.W.2
  • 8
    • 0028140267 scopus 로고
    • Effect of vesicular stomatitis virus matrix protein on host-directed translation in vivo
    • Black, B. L., G. Brewer, and D. S. Lyles. 1994. Effect of vesicular stomatitis virus matrix protein on host-directed translation in vivo. J. Virol. 68:555-560.
    • (1994) J. Virol. , vol.68 , pp. 555-560
    • Black, B.L.1    Brewer, G.2    Lyles, D.S.3
  • 9
    • 0026664168 scopus 로고
    • Vesicular stomatitis virus matrix protein inhibits host cell-directed transcription of target genes in vivo
    • Black, B. L., and D. S. Lyles. 1992. Vesicular stomatitis virus matrix protein inhibits host cell-directed transcription of target genes in vivo. J. Virol. 66:4058-4064.
    • (1992) J. Virol. , vol.66 , pp. 4058-4064
    • Black, B.L.1    Lyles, D.S.2
  • 10
    • 0027321038 scopus 로고
    • The role of vesicular stomatitis virus matrix protein in inhibition of host-directed gene expression is genetically separable from its function in virus assembly
    • Black, B. L., R. B. Rhodes, M. McKenzie, and D. S. Lyles. 1993. The role of vesicular stomatitis virus matrix protein in inhibition of host-directed gene expression is genetically separable from its function in virus assembly. J. Virol. 67:4814-4821.
    • (1993) J. Virol. , vol.67 , pp. 4814-4821
    • Black, B.L.1    Rhodes, R.B.2    McKenzie, M.3    Lyles, D.S.4
  • 11
    • 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. 63:2244-2251.
    • (1989) J. Virol. , vol.63 , pp. 2244-2251
    • Black, T.L.1    Safer, B.2    Hovanessian, A.3    Katze, M.G.4
  • 12
    • 0025238554 scopus 로고
    • Role of matrix protein in cytopathogenesis of vesicular stomatitis virus
    • Blondel, D., G. G. Harmison, and M. Schubert. 1990. Role of matrix protein in cytopathogenesis of vesicular stomatitis virus. J. Virol. 64:1716-1725.
    • (1990) J. Virol. , vol.64 , pp. 1716-1725
    • Blondel, D.1    Harmison, G.G.2    Schubert, M.3
  • 13
    • 0030847041 scopus 로고    scopus 로고
    • Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA
    • Blyn, L. B., J. S. Towner, B. L. Semler, and E. Ehrenfeld. 1997. Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA. J. Virol. 71:6243-6246.
    • (1997) J. Virol. , vol.71 , pp. 6243-6246
    • Blyn, L.B.1    Towner, J.S.2    Semler, B.L.3    Ehrenfeld, E.4
  • 14
    • 0023134622 scopus 로고
    • Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection
    • Bonneau, A. M., and N. Sonenberg. 1987. Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection. J. Virol. 61:986-991.
    • (1987) J. Virol. , vol.61 , pp. 986-991
    • Bonneau, A.M.1    Sonenberg, N.2
  • 15
    • 0030131138 scopus 로고    scopus 로고
    • NF-kappaB activation Is delayed in mouse L929 cells infected with interferon suppressing, but not inducing, vesicular stomatitis virus strains
    • Boulares, A. H., M. C. Ferran, and J. Lucas-Lenard. 1996. NF-kappaB activation Is delayed in mouse L929 cells infected with interferon suppressing, but not inducing, vesicular stomatitis virus strains. Virology 218:71-80.
    • (1996) Virology , vol.218 , pp. 71-80
    • Boulares, A.H.1    Ferran, M.C.2    Lucas-Lenard, J.3
  • 16
    • 0032486249 scopus 로고    scopus 로고
    • Direct cleavage of eIF4G by poliovirus 2A protease is inefficient in vitro
    • Bovee, M. L., B. J. Lamphear, R. E. Rhoads, and R. E. Lloyd. 1998. Direct cleavage of eIF4G by poliovirus 2A protease is inefficient in vitro. Virology 245:241-249.
    • (1998) Virology , vol.245 , pp. 241-249
    • Bovee, M.L.1    Lamphear, B.J.2    Rhoads, R.E.3    Lloyd, R.E.4
  • 17
    • 0032486281 scopus 로고    scopus 로고
    • The predominant elF4G-specific cleavage activity in poliovirus-infected HeLa cells is distinct from 2A protease
    • Bovee, M. L., W. E. Marissen, M. Zamora, and R. E. Lloyd. 1998. The predominant elF4G-specific cleavage activity in poliovirus-infected HeLa cells is distinct from 2A protease. Virology 245:229-240.
    • (1998) Virology , vol.245 , pp. 229-240
    • Bovee, M.L.1    Marissen, W.E.2    Zamora, M.3    Lloyd, R.E.4
  • 18
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • Burley, S. K., and R. G. Roeder. 1996. Biochemistry and structural biology of transcription factor IID (TFIID). Annu. Rev. Biochem. 65:769-799.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 20
    • 0020067379 scopus 로고
    • Regulation of protein synthesis in vesicular stomatitis virus-infected mouse L-929 cells by decreased protein synthesis initiation factor 2 activity
    • Centrella, M., and J. Lucas-Lenard. 1982. Regulation of protein synthesis in vesicular stomatitis virus-infected mouse L-929 cells by decreased protein synthesis initiation factor 2 activity. J. Virol. 41:781-791.
    • (1982) J. Virol. , vol.41 , pp. 781-791
    • Centrella, M.1    Lucas-Lenard, J.2
  • 21
    • 0033560753 scopus 로고    scopus 로고
    • Influenza a virus NS1 protein targets poly(A)-binding protein II of the cellular 3′-end processing machinery
    • Chen, Z., Y. Li, and R. M. Krug. 1999. Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3′-end processing machinery. EMBO J. 18:2273-2283.
    • (1999) EMBO J. , vol.18 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 22
    • 0028926274 scopus 로고
    • Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport
    • Cheng, Y., J. E. Dahlberg, and E. Lund. 1995. Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport. Science 267:1807-1810.
    • (1995) Science , vol.267 , pp. 1807-1810
    • Cheng, Y.1    Dahlberg, J.E.2    Lund, E.3
  • 23
    • 0342602773 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 24
    • 0025130462 scopus 로고
    • A transcriptionally active form of TFIIIC is modified in poliovirus-infected HeLa cells
    • Clark, M. E., and A. Dasgupta. 1990. A transcriptionally active form of TFIIIC is modified in poliovirus-infected HeLa cells. Mol. Cell. Biol. 10: 5106-5113.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5106-5113
    • Clark, M.E.1    Dasgupta, A.2
  • 25
    • 0025885346 scopus 로고
    • Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: A mechanism for inhibition of host cell polymerase III transcription by poliovirus
    • Clark, M. E., T. Hammerle, E. Wimmer, and A. Dasgupta. 1991. Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J. 10:2941-2947.
    • (1991) EMBO J. , vol.10 , pp. 2941-2947
    • Clark, M.E.1    Hammerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 26
    • 0027535652 scopus 로고
    • Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
    • Clark, M. E., P. M. Lieberman, A. J. Berk, and A. Dasgupta. 1993. Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro. Mol. Cell. Biol. 13:1232-1237.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1232-1237
    • Clark, M.E.1    Lieberman, P.M.2    Berk, A.J.3    Dasgupta, A.4
  • 27
    • 0030784958 scopus 로고    scopus 로고
    • Mechanism and regulation of mRNA polyadenylation
    • Colgan, D. F., and J. L. Manley. 1997. Mechanism and regulation of mRNA polyadenylation. Genes Dev. 11:2755-2766.
    • (1997) Genes Dev. , vol.11 , pp. 2755-2766
    • Colgan, D.F.1    Manley, J.L.2
  • 29
    • 0019811525 scopus 로고
    • Inhibition of transcription factor activity by poliovirus
    • Crawford, N., A. Fire, M. Samuels, P. A. Sharp, and D. Baltimore. 1981. Inhibition of transcription factor activity by poliovirus. Cell 27:555-561.
    • (1981) Cell , vol.27 , pp. 555-561
    • Crawford, N.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4    Baltimore, D.5
  • 30
    • 0027154003 scopus 로고
    • Identification of the cleavage site and determinants required for poliovirus 3CPro-catalyzed cleavage of human TATA-binding transcription factor TBP
    • Das, S., and A. Dasgupta. 1993. Identification of the cleavage site and determinants required for poliovirus 3CPro-catalyzed cleavage of human TATA-binding transcription factor TBP. J. Virol. 67:3326-3331.
    • (1993) J. Virol. , vol.67 , pp. 3326-3331
    • Das, S.1    Dasgupta, A.2
  • 31
    • 0026315441 scopus 로고
    • The effect of poliovirus proteinase 2Apro expression on cellular metabolism. Inhibition of DNA replication, RNA polymerase II transcription, and translation
    • Davies, M. V., J. Pelletier, K. Meerovitch, N. Sonenberg, and R. J. Kaufman. 1991. The effect of poliovirus proteinase 2Apro expression on cellular metabolism. Inhibition of DNA replication, RNA polymerase II transcription, and translation. J. Biol. Chem. 266:14714-14720.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14714-14720
    • Davies, M.V.1    Pelletier, J.2    Meerovitch, K.3    Sonenberg, N.4    Kaufman, R.J.5
  • 32
    • 0032975750 scopus 로고    scopus 로고
    • Sendai virus and simian virus 5 block activation of interferon- Responsive genes: Importance for virus pathogenesis
    • Didcock, L., D. F. Young, S. Goodbourn, and R. E. Randall. 1999. Sendai virus and simian virus 5 block activation of interferon- responsive genes: importance for virus pathogenesis. J. Virol. 73:3125-3133.
    • (1999) J. Virol. , vol.73 , pp. 3125-3133
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 33
    • 0032731094 scopus 로고    scopus 로고
    • The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation
    • Didcock, L., D. F. Young, S. Goodbourn, and R. E. Randall. 1999. The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation. J. Virol. 73:9928-9933.
    • (1999) J. Virol. , vol.73 , pp. 9928-9933
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 34
    • 0021755214 scopus 로고
    • Catalytic utilization of eIF-2 and mRNA binding proteins are limiting in lysates from vesicular stomatitis virus infected L cells
    • Dratewka-Kos, E., I. Kiss, J. Lucas-Lenard, H. B. Mehta, C. L. Woodley, and A. J. Wahba. 1984. Catalytic utilization of eIF-2 and mRNA binding proteins are limiting in lysates from vesicular stomatitis virus infected L cells. Biochemistry 23:6184-6190.
    • (1984) Biochemistry , vol.23 , pp. 6184-6190
    • Dratewka-Kos, E.1    Kiss, I.2    Lucas-Lenard, J.3    Mehta, H.B.4    Woodley, C.L.5    Wahba, A.J.6
  • 35
    • 0022634412 scopus 로고
    • Lack of correlation between the accumulation of plus-strand leader RNA and the inhibition of protein and RNA synthesis in vesicular stomatitis virus infected mouse L cells
    • Dunigan, D. D., S. Baird, and J. Lucas-Lenard. 1986. Lack of correlation between the accumulation of plus-strand leader RNA and the inhibition of protein and RNA synthesis in vesicular stomatitis virus infected mouse L cells. Virology 150:231-246.
    • (1986) Virology , vol.150 , pp. 231-246
    • Dunigan, D.D.1    Baird, S.2    Lucas-Lenard, J.3
  • 37
    • 0027252545 scopus 로고
    • Modification of eukaryotic initiation factor 4F during infection by influenza virus
    • Feigenblum, D., and R. J. Schneider. 1993. Modification of eukaryotic initiation factor 4F during infection by influenza virus. J. Virol 67:3027-3035.
    • (1993) J. Virol , vol.67 , pp. 3027-3035
    • Feigenblum, D.1    Schneider, R.J.2
  • 38
    • 0020037359 scopus 로고
    • The presence of viral-induced proteins in nuclei from poliovirus-infected HeLa cells
    • Fernandez-Tomas, C. 1982. The presence of viral-induced proteins in nuclei from poliovirus-infected HeLa cells. Virology 116:629-634.
    • (1982) Virology , vol.116 , pp. 629-634
    • Fernandez-Tomas, C.1
  • 39
    • 0031060138 scopus 로고    scopus 로고
    • The vesicular stomatitis virus matrix protein inhibits transcription from the human beta interferon promoter
    • Ferran, M. C., and J. M. Lucas-Lenard. 1997. The vesicular stomatitis virus matrix protein inhibits transcription from the human beta interferon promoter. J. Virol. 71:371-377.
    • (1997) J. Virol. , vol.71 , pp. 371-377
    • Ferran, M.C.1    Lucas-Lenard, J.M.2
  • 40
    • 17544391108 scopus 로고
    • Etude genetique du virus de la stomatite vesiculaire: Classement de mutants thermosensibles spontanes en groupes de complementation
    • Flamand, A. 1970. Etude genetique du virus de la stomatite vesiculaire: classement de mutants thermosensibles spontanes en groupes de complementation. J. Gen. Virol. 8:187-195.
    • (1970) J. Gen. Virol. , vol.8 , pp. 187-195
    • Flamand, A.1
  • 41
    • 0028008470 scopus 로고
    • Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport
    • Fortes, P., A. Beloso, and J. Ortin. 1994. Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport. EMBO J. 13:704-712.
    • (1994) EMBO J. , vol.13 , pp. 704-712
    • Fortes, P.1    Beloso, A.2    Ortin, J.3
  • 42
    • 0023442679 scopus 로고
    • Inhibition of host cell RNA polymerase III-mediated transcription by poliovirus: Inactivation of specific transcription factors
    • Fradkin, L. G., S. K. Yoshinaga, A. J. Berk, and A. Dasgupta. 1987. Inhibition of host cell RNA polymerase III-mediated transcription by poliovirus: inactivation of specific transcription factors. Mol. Cell. Biol. 7:3880-3887.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3880-3887
    • Fradkin, L.G.1    Yoshinaga, S.K.2    Berk, A.J.3    Dasgupta, A.4
  • 43
    • 0023143345 scopus 로고
    • Rapid inhibition of processing and assembly of small nuclear ribonucleoproteins after infection with vesicular stomatitis virus
    • Fresco, L. D., M. G. Kurilla, and J. D. Keene. 1987. Rapid inhibition of processing and assembly of small nuclear ribonucleoproteins after infection with vesicular stomatitis virus. Mol. Cell. Biol. 7:1148-1155.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1148-1155
    • Fresco, L.D.1    Kurilla, M.G.2    Keene, J.D.3
  • 44
    • 0032924734 scopus 로고    scopus 로고
    • Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells
    • Frolov, I., E. Agapov, T. A. Hoffman, Jr., B. M. Pragai, M. Lippa, S. Schlesinger, and C. M. Rice. 1999. Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells. J. Virol. 73:3854-3865.
    • (1999) J. Virol. , vol.73 , pp. 3854-3865
    • Frolov, I.1    Agapov, E.2    Hoffman T.A., Jr.3    Pragai, B.M.4    Lippa, M.5    Schlesinger, S.6    Rice, C.M.7
  • 45
    • 0031872125 scopus 로고    scopus 로고
    • Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells
    • Fujimoto, I., T. Takizawa, Y. Ohba, and Y. Nakanishi. 1998. Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells. Cell Death Differ. 5:426-431.
    • (1998) Cell Death Differ. , vol.5 , pp. 426-431
    • Fujimoto, I.1    Takizawa, T.2    Ohba, Y.3    Nakanishi, Y.4
  • 46
    • 0030861261 scopus 로고    scopus 로고
    • Two functional complexes formed by KH domain containing proteins with the 5′ noncoding region of poliovirus RNA
    • Gamarnik, A. V., and R. Andino. 1997. Two functional complexes formed by KH domain containing proteins with the 5′ noncoding region of poliovirus RNA. RNA 3:882-892.
    • (1997) RNA , vol.3 , pp. 882-892
    • Gamarnik, A.V.1    Andino, R.2
  • 49
    • 0032775438 scopus 로고    scopus 로고
    • Sendai virus C proteins counteract the interferon-mediated induction of an antiviral state
    • Garcin, D., P. Latorre, and D. Kolakofsky. 1999. Sendai virus C proteins counteract the interferon-mediated induction of an antiviral state. J. Virol. 73:6559-6565.
    • (1999) J. Virol. , vol.73 , pp. 6559-6565
    • Garcin, D.1    Latorre, P.2    Kolakofsky, D.3
  • 50
    • 0032827262 scopus 로고    scopus 로고
    • Knockout of the Sendai virus C gene eliminates the viral ability to prevent the interferon-alpha/beta-mediated responses
    • Gotoh, B., K. Takeuchi, T. Komatsu, J. Yokoo, Y. Kimura, A. Kurotani, A. Kato, and Y. Nagai. 1999. Knockout of the Sendai virus C gene eliminates the viral ability to prevent the interferon-alpha/beta-mediated responses. FEBS Lett. 459:205-210.
    • (1999) FEBS Lett. , vol.459 , pp. 205-210
    • Gotoh, B.1    Takeuchi, K.2    Komatsu, T.3    Yokoo, J.4    Kimura, Y.5    Kurotani, A.6    Kato, A.7    Nagai, Y.8
  • 52
    • 0032530480 scopus 로고    scopus 로고
    • Proteolysis of human eukaryotic translation initiation factor eIF4GII. but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection
    • USA
    • Gradi, A., Y. V. Svitkin, H. Imataka, and N. Sonenberg. 1998. Proteolysis of human eukaryotic translation initiation factor eIF4GII. but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection. Proc. Natl. Acad. Sci. USA 95:11089-11094.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 11089-11094
    • Gradi, A.1    Svitkin, Y.V.2    Imataka, H.3    Sonenberg, N.4
  • 53
    • 0030984433 scopus 로고    scopus 로고
    • Selection and nuclear immobilization of exportable RNAs
    • USA
    • Grimm, C., E. Lund, and J. E. Dahlberg. 1997. Selection and nuclear immobilization of exportable RNAs. Proc. Natl. Acad. Sci USA 94:10122-10127.
    • (1997) Proc. Natl. Acad. Sci , vol.94 , pp. 10122-10127
    • Grimm, C.1    Lund, E.2    Dahlberg, J.E.3
  • 54
    • 0022256646 scopus 로고
    • Inhibition of DNA-dependent transcription by the leader RNA of vesicular stomatitis virus: Role of specific nucleotide sequences and cell protein binding
    • Grinnell, B. W., and R. R. Wagner. 1985. Inhibition of DNA-dependent transcription by the leader RNA of vesicular stomatitis virus: role of specific nucleotide sequences and cell protein binding. Mol. Cell. Biol. 5:2502-2513.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2502-2513
    • Grinnell, B.W.1    Wagner, R.R.2
  • 55
    • 0021382584 scopus 로고
    • Nucleotide sequence and secondary structure of VSV leader RNA and homologous DNA involved in inhibition of DNA-dependent transcription
    • Grinnell, B. W., and R. R. Wagner. 1984. Nucleotide sequence and secondary structure of VSV leader RNA and homologous DNA involved in inhibition of DNA-dependent transcription. Cell 36:533-543.
    • (1984) Cell , vol.36 , pp. 533-543
    • Grinnell, B.W.1    Wagner, R.R.2
  • 56
    • 0029861190 scopus 로고    scopus 로고
    • The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase
    • Haghighat, A., Y. Svitkin, I. Novoa, E. Kuechler, T. Skern, and N. Sonenberg. 1996. The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase. J. Virol. 70:8444-8450.
    • (1996) J. Virol. , vol.70 , pp. 8444-8450
    • Haghighat, A.1    Svitkin, Y.2    Novoa, I.3    Kuechler, E.4    Skern, T.5    Sonenberg, N.6
  • 57
    • 0009227133 scopus 로고    scopus 로고
    • Viral effects on cellular functions
    • In N. Nathanson (ed.), Lippincott-Raven Publishers, Philadelphia, Pa
    • Hardwick, J. M., and D. E. Griffin. 1997. Viral effects on cellular functions, p. 55-83. In N. Nathanson (ed.), Viral pathogenesis. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1997) Viral Pathogenesis , pp. 55-83
    • Hardwick, J.M.1    Griffin, D.E.2
  • 58
    • 0027102716 scopus 로고
    • Binding of influenza a virus NS1 protein to dsRNA in vitro
    • Hatada, E., and R. Fukuda. 1992. Binding of influenza A virus NS1 protein to dsRNA in vitro. J. Gen. Virol. 73:3325-3329.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3325-3329
    • Hatada, E.1    Fukuda, R.2
  • 59
    • 0027172207 scopus 로고
    • A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein
    • USA
    • Hellen, C. U., G. W. Witherell, M. Schmid, S. H. Shin, T. V. Pestova, A. Gil, and E. Wimmer. 1993. A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein. Proc. Natl. Acad Sci USA 90:7642-7646.
    • (1993) Proc. Natl. Acad Sci , vol.90 , pp. 7642-7646
    • Hellen, C.U.1    Witherell, G.W.2    Schmid, M.3    Shin, S.H.4    Pestova, T.V.5    Gil, A.6    Wimmer, E.7
  • 60
    • 0030810744 scopus 로고    scopus 로고
    • Inhibition of Ran guanosine triphosphatase-dependent nuclear transport by the matrix protein of vesicular stomatitis virus
    • Her, L. S., E. Lund, and J. E. Dahlherg. 1997. Inhibition of Ran guanosine triphosphatase-dependent nuclear transport by the matrix protein of vesicular stomatitis virus. Science 276:1845-1848.
    • (1997) Science , vol.276 , pp. 1845-1848
    • Her, L.S.1    Lund, E.2    Dahlherg, J.E.3
  • 61
    • 0009841072 scopus 로고
    • Nucleic acid and protein synthesis during poliovirus infection of human cells
    • Holland, J. J., and J. A. Peterson. 1964. Nucleic acid and protein synthesis during poliovirus infection of human cells. J. Mol. Biol. 8:556-573.
    • (1964) J. Mol. Biol. , vol.8 , pp. 556-573
    • Holland, J.J.1    Peterson, J.A.2
  • 62
    • 0040724074 scopus 로고    scopus 로고
    • Localization of viral infections
    • N. Nathanson (ed.), Lippincott-Raven Publishers, Philadelphia, Pa
    • Holmes, K. V. 1997. Localization of viral infections, p. 35-53. In N. Nathanson (ed.), Viral pathogenesis. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1997) Viral Pathogenesis , pp. 35-53
    • Holmes, K.V.1
  • 63
    • 0033557935 scopus 로고    scopus 로고
    • unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA
    • Hunt, S. L., J. J. Hsuan, N. Totty, and R. J. Jackson. 1999. unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes Dev 13:437-448.
    • (1999) Genes Dev , vol.13 , pp. 437-448
    • Hunt, S.L.1    Hsuan, J.J.2    Totty, N.3    Jackson, R.J.4
  • 64
    • 0028874823 scopus 로고
    • Monensin and nigericin prevent the inhibition of host translation by poliovirus, without affecting p220 cleavage
    • Irurzun, A., S. Sanchez-Palomino, I. Novoa, and L. Carrasco. 1995. Monensin and nigericin prevent the inhibition of host translation by poliovirus, without affecting p220 cleavage. J. Virol. 69:7453-7460.
    • (1995) J. Virol. , vol.69 , pp. 7453-7460
    • Irurzun, A.1    Sanchez-Palomino, S.2    Novoa, I.3    Carrasco, L.4
  • 65
    • 0031954020 scopus 로고    scopus 로고
    • Transport of macromolecules between the nucleus and the cytoplasm
    • Izaurralde, E., and S. Adam. 1998. Transport of macromolecules between the nucleus and the cytoplasm. RNA 4:351-364.
    • (1998) RNA , vol.4 , pp. 351-364
    • Izaurralde, E.1    Adam, S.2
  • 66
    • 0032710836 scopus 로고    scopus 로고
    • Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication
    • Jan, J. T., and D. E. Griffin. 1999. Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication. J. Virol 73: 10296-10302.
    • (1999) J. Virol , vol.73 , pp. 10296-10302
    • Jan, J.T.1    Griffin, D.E.2
  • 67
    • 0029126160 scopus 로고
    • Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4
    • Joachims, M., K. S. Harris, and D. Etchison. 1995. Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4. Virology 211:451-461.
    • (1995) Virology , vol.211 , pp. 451-461
    • Joachims, M.1    Harris, K.S.2    Etchison, D.3
  • 68
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims, M., P. C. Van Breugel, and R. E. Lloyd. 1999. Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J. Virol. 73:718-727.
    • (1999) J. Virol. , vol.73 , pp. 718-727
    • Joachims, M.1    Van Breugel, P.C.2    Lloyd, R.E.3
  • 69
    • 0025978451 scopus 로고
    • Sequences of the vesicular stomatitis virus matrix protein involved in binding to nucleocapsids
    • Kaptur, P. E., R. B. Rhodes, and D. S. Lyles. 1991. Sequences of the vesicular stomatitis virus matrix protein involved in binding to nucleocapsids. J. Virol. 65:1057-1065.
    • (1991) J. Virol. , vol.65 , pp. 1057-1065
    • Kaptur, P.E.1    Rhodes, R.B.2    Lyles, D.S.3
  • 70
    • 0021678670 scopus 로고
    • Metabolism and expression of RNA polymerase II transcripts in influenza virus-infected cells
    • Katze, M. G., and R. M. Krug. 1984. Metabolism and expression of RNA polymerase II transcripts in influenza virus-infected cells. Mol. Cell. Biol 4:2198-2206.
    • (1984) Mol. Cell. Biol , vol.4 , pp. 2198-2206
    • Katze, M.G.1    Krug, R.M.2
  • 71
    • 0032889326 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: Another mechanism for host protein synthesis shutoff?
    • Kerekatte, V., B. D. Keiper, C. Badorff, A. Cai, K. U. Knowlton, and R. E. Rhoads. 1999. Cleavage of poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff? J. Virol. 73:709-717.
    • (1999) J. Virol. , vol.73 , pp. 709-717
    • Kerekatte, V.1    Keiper, B.D.2    Badorff, C.3    Cai, A.4    Knowlton, K.U.5    Rhoads, R.E.6
  • 72
    • 0023774851 scopus 로고
    • An RNA polymerase II transcription factor inactivated in poliovirus-infected cells copurifies with transcription factor TFIID
    • Kliewer, S., and A. Dasgupta. 1988. An RNA polymerase II transcription factor inactivated in poliovirus-infected cells copurifies with transcription factor TFIID. Mol. Cell. Biol. 8:3175-3182.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3175-3182
    • Kliewer, S.1    Dasgupta, A.2
  • 73
    • 0003054014 scopus 로고    scopus 로고
    • Virus-host cell interactions
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa
    • Knipe, D. M. 1996. Virus-host cell interactions, p. 239-265. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Fundamental virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fundamental Virology, 3rd Ed. , pp. 239-265
    • Knipe, D.M.1
  • 74
    • 0029144682 scopus 로고
    • Induction of apoptotic DNA fragmentation by the infection of vesicular stomatitis virus
    • Koyama, A. H. 1995. Induction of apoptotic DNA fragmentation by the infection of vesicular stomatitis virus. Virus Res. 37:285-290.
    • (1995) Virus Res. , vol.37 , pp. 285-290
    • Koyama, A.H.1
  • 76
    • 0025180598 scopus 로고
    • Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells
    • USA
    • Lee, T. G., J. Tomita, A. G. Hovanessian, and M. G. Katze. 1990. Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells. Proc. Natl. Acad. Sci. USA 87:6208-6212.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 6208-6212
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 77
    • 0029961533 scopus 로고    scopus 로고
    • Negative-strand virus M and retrovirus MA proteins: All in a family?
    • Lenard, J. 1996. Negative-strand virus M and retrovirus MA proteins: all in a family? Virology 216:289-298.
    • (1996) Virology , vol.216 , pp. 289-298
    • Lenard, J.1
  • 78
    • 0018409607 scopus 로고
    • The cytoskeletal framework and poliovuus metabolism
    • Lenk, R., and S. Penman. 1979. The cytoskeletal framework and poliovuus metabolism. Cell 16:289-301.
    • (1979) Cell , vol.16 , pp. 289-301
    • Lenk, R.1    Penman, S.2
  • 79
    • 0023836518 scopus 로고
    • Expression of the M gene of vesicular stomatitis virus cloned in various vaccinia virus vectors
    • Li, Y., L. Z. Luo, R. M. Snyder, and R. R. Wagner. 1988. Expression of the M gene of vesicular stomatitis virus cloned in various vaccinia virus vectors. J. Virol. 62:776-782.
    • (1988) J. Virol. , vol.62 , pp. 776-782
    • Li, Y.1    Luo, L.Z.2    Snyder, R.M.3    Wagner, R.R.4
  • 80
    • 0343908584 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 81
    • 0022647104 scopus 로고
    • Cleavage of the cap binding protein complex polypeptide p220 is not effected by the second poliovirus protease 2A
    • Lloyd, R. E., H. Toyoda, D. Etchison, E. Wimmer, and E. Ehrenfeld. 1986. Cleavage of the cap binding protein complex polypeptide p220 is not effected by the second poliovirus protease 2A. Virology 150:299-303.
    • (1986) Virology , vol.150 , pp. 299-303
    • Lloyd, R.E.1    Toyoda, H.2    Etchison, D.3    Wimmer, E.4    Ehrenfeld, E.5
  • 82
    • 0019209524 scopus 로고
    • Translational control of protein synthesis after infection by vesicular stomatitis virus
    • Lodish, H. F., and M. Porter. 1980. Translational control of protein synthesis after infection by vesicular stomatitis virus. J. Virol. 36:719-733.
    • (1980) J. Virol. , vol.36 , pp. 719-733
    • Lodish, H.F.1    Porter, M.2
  • 83
    • 0028040760 scopus 로고
    • The influenza virus NS1 protein: A novel inhibitor of pre-mRNA splicing
    • Lu, Y., X. Y. Qian, and R. M. Krug. 1994. The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing. Genes Dev. 8:1817-1828.
    • (1994) Genes Dev. , vol.8 , pp. 1817-1828
    • Lu, Y.1    Qian, X.Y.2    Krug, R.M.3
  • 84
    • 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., M. Wambach, M. G. Katze, and R. M. Krug. 1995. 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 214:222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 85
    • 0031550792 scopus 로고    scopus 로고
    • Activity of vesicular stomatitis virus M protein mutants in cell rounding is correlated with the ability to inhibit host gene expression and is not correlated with virus assembly function
    • Lyles, D. S., and M. O. McKenzie. 1997. Activity of vesicular stomatitis virus M protein mutants in cell rounding is correlated with the ability to inhibit host gene expression and is not correlated with virus assembly function. Virology 229:77-89.
    • (1997) Virology , vol.229 , pp. 77-89
    • Lyles, D.S.1    McKenzie, M.O.2
  • 86
    • 0030297141 scopus 로고    scopus 로고
    • Potency of wild-type and temperature-sensitive vesicular stomatitis virus matrix protein in the inhibition of host-directed gene expression
    • Lyles, D. S., M. O. McKenzie, M. Ahmed, and S. C. Woolwine. 1996. Potency of wild-type and temperature-sensitive vesicular stomatitis virus matrix protein in the inhibition of host-directed gene expression. Virology 225:172-180.
    • (1996) Virology , vol.225 , pp. 172-180
    • Lyles, D.S.1    McKenzie, M.O.2    Ahmed, M.3    Woolwine, S.C.4
  • 87
    • 0023787830 scopus 로고
    • Vesicular stomatitis virus M protein in the nuclei of infected cells
    • Lyles, D. S., L. Puddington, and B. J. McCreedy, Jr. 1988. Vesicular stomatitis virus M protein in the nuclei of infected cells. J. Virol. 62:4387-4392.
    • (1988) J. Virol. , vol.62 , pp. 4387-4392
    • Lyles, D.S.1    Puddington, L.2    McCreedy B.J., Jr.3
  • 88
    • 0031974477 scopus 로고    scopus 로고
    • Interferon induction as a quasispecies marker of vesicular stomatitis virus populations
    • Marcus, P. I., L. L. Rodriguez, and M. J. Sekellick. 1998. Interferon induction as a quasispecies marker of vesicular stomatitis virus populations. J. Virol. 72:542-549.
    • (1998) J. Virol. , vol.72 , pp. 542-549
    • Marcus, P.I.1    Rodriguez, L.L.2    Sekellick, M.J.3
  • 89
    • 0027723983 scopus 로고
    • Interferon induction by viruses. XXII. Vesicular stomatitis virus-Indiana: M-protein and leader RNA do not regulate interferon induction in chicken embryo cells
    • Marcus, P. L., M. J. Sekellick, C. F. Spiropoulou, and S. T. Nichol. 1993. Interferon induction by viruses. XXII. Vesicular stomatitis virus-Indiana: M-protein and leader RNA do not regulate interferon induction in chicken embryo cells. J. Interferon Res. 13:413-418.
    • (1993) J. Interferon Res. , vol.13 , pp. 413-418
    • Marcus, P.L.1    Sekellick, M.J.2    Spiropoulou, C.F.3    Nichol, S.T.4
  • 90
    • 0030694071 scopus 로고    scopus 로고
    • The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation
    • Marion, R. M., T. Aragon, A. Beloso, A. Nieto, and J. Ortin. 1997. The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation. Nucleic Acids Res. 25:4271-4277.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4271-4277
    • Marion, R.M.1    Aragon, T.2    Beloso, A.3    Nieto, A.4    Ortin, J.5
  • 91
    • 0020035760 scopus 로고
    • The plus-strand leader RNA of VSV inhibits DNA-dependent transcription of adenovirus and SV40 genes in a soluble whole-cell extract
    • McGowan, J. J., S. U. Emerson, and R. R. Wagner. 1982. The plus-strand leader RNA of VSV inhibits DNA-dependent transcription of adenovirus and SV40 genes in a soluble whole-cell extract. Cell 28:325-333.
    • (1982) Cell , vol.28 , pp. 325-333
    • McGowan, J.J.1    Emerson, S.U.2    Wagner, R.R.3
  • 93
    • 0028100460 scopus 로고
    • Interaction between tubulin and the viral matrix protein of vesicular stomatitis virus: Possible implications in the viral cytopathic effect
    • Melki, R., Y. Gaudin, and D. Blondel. 1994. Interaction between tubulin and the viral matrix protein of vesicular stomatitis virus: possible implications in the viral cytopathic effect. Virology 202:339-347.
    • (1994) Virology , vol.202 , pp. 339-347
    • Melki, R.1    Gaudin, Y.2    Blondel, D.3
  • 94
    • 0023098977 scopus 로고
    • Phenotypic revenants of temperature-sensitive M protein mutants of vesicular stomatitis virus: Sequence analysis and functional characterization
    • Morita, K., R. Vanderoef, and J. Lenard. 1987. Phenotypic revenants of temperature-sensitive M protein mutants of vesicular stomatitis virus: sequence analysis and functional characterization. J. Virol. 61:256-263.
    • (1987) J. Virol. , vol.61 , pp. 256-263
    • Morita, K.1    Vanderoef, R.2    Lenard, J.3
  • 97
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′ end formation of cellular pre-mRNAs
    • Nemeroff, M. E., S. M. Barabino, Y. Li, W. Keller, and R. M. Krug. 1998. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′ end formation of cellular pre-mRNAs. Mol. Cell 1:991-1000.
    • (1998) Mol. Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 98
    • 0032913223 scopus 로고    scopus 로고
    • Cleavage of eukaryotic translation initiation factor 4G by exogenously added hybrid proteins containing poliovirus 2Apro in HeLa cells: Effects on gene expression
    • Novoa, I., and L. Carrasco. 1999. Cleavage of eukaryotic translation initiation factor 4G by exogenously added hybrid proteins containing poliovirus 2Apro in HeLa cells: effects on gene expression. Mol. Cell. Biol. 19:2445-2454.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2445-2454
    • Novoa, I.1    Carrasco, L.2
  • 99
    • 0031054338 scopus 로고    scopus 로고
    • The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by cIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate
    • Ohlmann, T., V. M. Pain, W. Wood, M. Rau, and S. J. Morley. 1997. The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by cIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate. EMBO J. 16:844-855.
    • (1997) EMBO J. , vol.16 , pp. 844-855
    • Ohlmann, T.1    Pain, V.M.2    Wood, W.3    Rau, M.4    Morley, S.J.5
  • 100
    • 0029656251 scopus 로고    scopus 로고
    • bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation
    • Olsen, C. W., J. C. Kehren, N. R. Dybdahl-Sissoko, and V. S. Hinshaw. 1996. bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation. J. Virol. 70:663-666.
    • (1996) J. Virol. , vol.70 , pp. 663-666
    • Olsen, C.W.1    Kehren, J.C.2    Dybdahl-Sissoko, N.R.3    Hinshaw, V.S.4
  • 101
    • 0024427394 scopus 로고
    • Inhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylaton of the alpha subunit of eucaryotic initiation factor 2
    • O'Neill, R. E., and V. R. Racaniello. 1989. Inhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylaton of the alpha subunit of eucaryotic initiation factor 2. J. Virol. 63:5069-5075.
    • (1989) J. Virol. , vol.63 , pp. 5069-5075
    • O'Neill, R.E.1    Racaniello, V.R.2
  • 102
    • 0029011061 scopus 로고
    • Inducible and conditional inhibition of human immunodeficiency virus proviral expression by vesicular stomatitis virus matrix protein
    • Paik, S. Y., A. C. Banerjea, G. G. Harmison, C. J. Chen, and M. Schubert. 1995. Inducible and conditional inhibition of human immunodeficiency virus proviral expression by vesicular stomatitis virus matrix protein. J. Virol. 69:3529-3537.
    • (1995) J. Virol. , vol.69 , pp. 3529-3537
    • Paik, S.Y.1    Banerjea, A.C.2    Harmison, G.G.3    Chen, C.J.4    Schubert, M.5
  • 103
    • 0000075974 scopus 로고    scopus 로고
    • Regulation of eukaryotic protein synthesis: Selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1
    • USA
    • Park, Y. W., J. Wilusz, and M. G. Katze. 1999. Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1. Proc. Natl. Acad. Sci. USA 96:6694-6699.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 6694-6699
    • Park, Y.W.1    Wilusz, J.2    Katze, M.G.3
  • 104
    • 0026750639 scopus 로고
    • Lack of direct correlation between p220 cleavage and the shut-off of host translation after poliovirus infection
    • Perez, L., and L. Carrasco. 1992. Lack of direct correlation between p220 cleavage and the shut-off of host translation after poliovirus infection. Virology 189:178-186.
    • (1992) Virology , vol.189 , pp. 178-186
    • Perez, L.1    Carrasco, L.2
  • 105
    • 0025375345 scopus 로고
    • Functional domains and upstream activation properties of cloned human TATA binding protein
    • Peterson, M. G., N. Tanese, B. F. Pugh, and R. Tjian. 1990. Functional domains and upstream activation properties of cloned human TATA binding protein. Science 248:1625-1630.
    • (1990) Science , vol.248 , pp. 1625-1630
    • Peterson, M.G.1    Tanese, N.2    Pugh, B.F.3    Tjian, R.4
  • 106
    • 0022003904 scopus 로고
    • The requirement of protein synthesis for VSV inhibition of host cell RNA synthesis
    • Poirot, M. K., W. M. Schnitzlein, and M. E. Reichmann. 1985. The requirement of protein synthesis for VSV inhibition of host cell RNA synthesis. Virology 140:91-101.
    • (1985) Virology , vol.140 , pp. 91-101
    • Poirot, M.K.1    Schnitzlein, W.M.2    Reichmann, M.E.3
  • 107
    • 0027422866 scopus 로고
    • Picornavirus nonstructural proteins: Emerging roles in virus replication and inhibition of host cell functions
    • Porter, A. G. 1993. Picornavirus nonstructural proteins: emerging roles in virus replication and inhibition of host cell functions. J. Virol. 67:6917-6921.
    • (1993) J. Virol. , vol.67 , pp. 6917-6921
    • Porter, A.G.1
  • 108
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate cIF4E
    • Pyronnet, S., H. Imataka, A. C. Gingras, R. Fukunaga, T. Hunter, and N. Sonenberg. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate cIF4E. EMBO J. 18:270-279.
    • (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
  • 109
    • 0028209823 scopus 로고
    • Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA
    • Qian, X. Y., F. Alonso-Caplen, and R. M. Krug. 1994. Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA. J. Virol. 68:2433-2441.
    • (1994) J. Virol. , vol.68 , pp. 2433-2441
    • Qian, X.Y.1    Alonso-Caplen, F.2    Krug, R.M.3
  • 110
    • 0029400032 scopus 로고
    • An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure
    • Qian, X. Y., C. Y. Chien, Y. Lu, G. T. Montelione, and R. M. Krug. 1995. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. RNA 1:948-956.
    • (1995) RNA , vol.1 , pp. 948-956
    • Qian, X.Y.1    Chien, C.Y.2    Lu, Y.3    Montelione, G.T.4    Krug, R.M.5
  • 111
    • 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., and R. M. Krug. 1994. The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J. Virol. 68:2425-2432.
    • (1994) J. Virol. , vol.68 , pp. 2425-2432
    • Qiu, Y.1    Krug, R.M.2
  • 112
    • 0029295578 scopus 로고
    • The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 and U6-U4 snRNA interactions during splicing
    • Qiu, Y., M. Nemeroff, and R. M. Krug. 1995. The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 and U6-U4 snRNA interactions during splicing. RNA 1:304-316.
    • (1995) RNA , vol.1 , pp. 304-316
    • Qiu, Y.1    Nemeroff, M.2    Krug, R.M.3
  • 113
    • 0030249381 scopus 로고    scopus 로고
    • The role of general initiation factors in transcription by RNA polymerase II
    • Roeder, R. G. 1996. The role of general initiation factors in transcription by RNA polymerase II. Trends Biochem. Sci. 21:327-335.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 327-335
    • Roeder, R.G.1
  • 114
    • 0020463493 scopus 로고
    • Translational control of vesicular stomatitis virus protein synthesis: Isolation of an mRNA-sequestering particle
    • Rosen, C. A., H. L. Ennis, and P. S. Cohen. 1982. Translational control of vesicular stomatitis virus protein synthesis: isolation of an mRNA-sequestering particle. J. Virol. 44:932-938.
    • (1982) J. Virol. , vol.44 , pp. 932-938
    • Rosen, C.A.1    Ennis, H.L.2    Cohen, P.S.3
  • 116
    • 0026582457 scopus 로고
    • Infection of HeLa cells with poliovirus results in modification of a complex that binds to the rRNA promoter
    • Rubinstein, S. J., T. Hammerle, E. Wimmer, and A. Dasgupta. 1992. Infection of HeLa cells with poliovirus results in modification of a complex that binds to the rRNA promoter. J. Virol. 66:3062-3068.
    • (1992) J. Virol. , vol.66 , pp. 3062-3068
    • Rubinstein, S.J.1    Hammerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 117
    • 0020702301 scopus 로고
    • Effect of intracellular vesicular stomatitis virus mRNA concentration on the inhibition of host cell protein synthesis
    • Schnitzlein, W. M., M. K. O'Banion, M. K. Poirot, and M. E. Reichmann. 1983. Effect of intracellular vesicular stomatitis virus mRNA concentration on the inhibition of host cell protein synthesis. J. Virol. 45:206-214.
    • (1983) J. Virol. , vol.45 , pp. 206-214
    • Schnitzlein, W.M.1    O'Banion, M.K.2    Poirot, M.K.3    Reichmann, M.E.4
  • 118
    • 0029861191 scopus 로고    scopus 로고
    • Influenza virus neuraminidase activates latent transforming growth factor beta
    • Schultz-Cherry, S., and V. S. Hinshaw. 1996. Influenza virus neuraminidase activates latent transforming growth factor beta. J. Virol. 70:8624-8629.
    • (1996) J. Virol. , vol.70 , pp. 8624-8629
    • Schultz-Cherry, S.1    Hinshaw, V.S.2
  • 120
    • 0029815612 scopus 로고    scopus 로고
    • Novel exploitation of a nuclear function by influenza virus: The cellular SF2/ASF splicing factor controls the amount of the essential viral M2 ion channel protein in infected cells
    • Shih, S. R., and R. M. Krug. 1996. Novel exploitation of a nuclear function by influenza virus: the cellular SF2/ASF splicing factor controls the amount of the essential viral M2 ion channel protein in infected cells. EMBO J. 15:5415-5427.
    • (1996) EMBO J. , vol.15 , pp. 5415-5427
    • Shih, S.R.1    Krug, R.M.2
  • 121
    • 0025334048 scopus 로고
    • Sequential disassembly of the cytoskeleton in BHK21 cells infected with vesicular stomatitis virus
    • Simon, K. O., P. A. Whitaker-Dowling, J. S. Youngner, and C. C. Widnell. 1990. Sequential disassembly of the cytoskeleton in BHK21 cells infected with vesicular stomatitis virus. Virology 177:289-297.
    • (1990) Virology , vol.177 , pp. 289-297
    • Simon, K.O.1    Whitaker-Dowling, P.A.2    Youngner, J.S.3    Widnell, C.C.4
  • 122
    • 0017736843 scopus 로고
    • Analysis of VSV mutant with attenuated cytopathogenicity: Mutation in viral function, P, for inhibition of protein synthesis
    • Stanners, C. P., A. M. Francoeur, and T. Lam. 1977. Analysis of VSV mutant with attenuated cytopathogenicity: mutation in viral function, P, for inhibition of protein synthesis. Cell 11:273-281.
    • (1977) Cell , vol.11 , pp. 273-281
    • Stanners, C.P.1    Francoeur, A.M.2    Lam, T.3
  • 123
    • 0033050679 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4GII (eIF4GII), but not eIF4GI, cleavage correlates with inhibition of host cell protein synthesis after human rhinovirus infection
    • Svitkin, Y. V., A. Gradi, H. Imataka, S. Morino, and N. Sonenberg. 1999. Eukaryotic initiation factor 4GII (eIF4GII), but not eIF4GI, cleavage correlates with inhibition of host cell protein synthesis after human rhinovirus infection. J. Virol. 73:3467-3472.
    • (1999) J. Virol. , vol.73 , pp. 3467-3472
    • Svitkin, Y.V.1    Gradi, A.2    Imataka, H.3    Morino, S.4    Sonenberg, N.5
  • 124
    • 0027979132 scopus 로고
    • Internal translation initiation on poliovirus RNA: Further characterization of La function in poliovirus translation in vitro
    • Svitkin, Y. V., K. Meerovitch, H. S. Lee, J. N. Dholakia, D. J. Kenan, V. I. Agol, and N. Sonenberg. 1994. Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro. J. Virol. 68:1544-1550.
    • (1994) J. Virol. , vol.68 , pp. 1544-1550
    • Svitkin, Y.V.1    Meerovitch, K.2    Lee, H.S.3    Dholakia, J.N.4    Kenan, D.J.5    Agol, V.I.6    Sonenberg, N.7
  • 125
    • 0029063283 scopus 로고
    • Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon
    • Takizawa, T., R. Fukuda, T. Miyawaki, K. Ohashi, and Y. Nakanishi. 1995. Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon. Virology 209: 288-296.
    • (1995) Virology , vol.209 , pp. 288-296
    • Takizawa, T.1    Fukuda, R.2    Miyawaki, T.3    Ohashi, K.4    Nakanishi, Y.5
  • 126
    • 0027382362 scopus 로고
    • Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells
    • Takizawa, T., S. Matsukawa, Y. Higuchi, S. Nakamura, Y. Nakanishi, and R. Fukuda. 1993. Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells. J. Gen. Virol. 74:2347-2355.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2347-2355
    • Takizawa, T.1    Matsukawa, S.2    Higuchi, Y.3    Nakamura, S.4    Nakanishi, Y.5    Fukuda, R.6
  • 127
    • 0032717166 scopus 로고    scopus 로고
    • Matrix protein of Chandipura virus inhibits transcription from an RNA polymerase II promoter
    • Taylor, A., A. J. Easton, and A. C. Marriott. 1999. Matrix protein of Chandipura virus inhibits transcription from an RNA polymerase II promoter. Virus Genes 19:223-228.
    • (1999) Virus Genes , vol.19 , pp. 223-228
    • Taylor, A.1    Easton, A.J.2    Marriott, A.C.3
  • 129
    • 0028234786 scopus 로고
    • Neurovirulent strains of Alphavirus induce apoptosis in bcl-2-expressing cells: Role of a single amino acid change in the E2 glycoprotein
    • USA
    • Ubol, S., P. C. Tucker, D. E. Griffin, and J. M. Hardwick. 1994. Neurovirulent strains of Alphavirus induce apoptosis in bcl-2-expressing cells: role of a single amino acid change in the E2 glycoprotein. Proc. Natl. Acad. Sci. USA 91:5202-5206.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5202-5206
    • Ubol, S.1    Tucker, P.C.2    Griffin, D.E.3    Hardwick, J.M.4
  • 130
    • 0024467328 scopus 로고
    • Degradation of cellular proteins during poliovirus infection: Studies by two-dimensional gel electrophoresis
    • Urzainqui, A., and L. Carrasco. 1989. Degradation of cellular proteins during poliovirus infection: studies by two-dimensional gel electrophoresis. J. Virol. 63:4729-4735.
    • (1989) J. Virol. , vol.63 , pp. 4729-4735
    • Urzainqui, A.1    Carrasco, L.2
  • 131
    • 0032508655 scopus 로고    scopus 로고
    • Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex
    • Ventoso, I., S. E. MacMillan, J. W. Hershey, and L. Carrasco. 1998. Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex. FEBS Lett. 435:79-83.
    • (1998) FEBS Lett. , vol.435 , pp. 79-83
    • Ventoso, I.1    MacMillan, S.E.2    Hershey, J.W.3    Carrasco, L.4
  • 132
    • 0013864795 scopus 로고
    • Inhibition of RNA and interferon synthesis in Krebs-2 cells infected with vesicular stomatitis virus
    • Wagner, R. R., and A. S. Huang. 1966. Inhibition of RNA and interferon synthesis in Krebs-2 cells infected with vesicular stomatitis virus. Virology 28:1-10.
    • (1966) Virology , vol.28 , pp. 1-10
    • Wagner, R.R.1    Huang, A.S.2
  • 133
    • 0032806372 scopus 로고    scopus 로고
    • Differential utilization of poly(rC) binding protein 2 in translation directed by picornavirus IRES elements
    • Walter, B. L., J. H. Nguyen, E. Ehrenfeid, and B. L. Semler. 1999. Differential utilization of poly(rC) binding protein 2 in translation directed by picornavirus IRES elements. RNA 5:1570-1585.
    • (1999) RNA , vol.5 , pp. 1570-1585
    • Walter, B.L.1    Nguyen, J.H.2    Ehrenfeid, E.3    Semler, B.L.4
  • 134
    • 0031985445 scopus 로고    scopus 로고
    • U6atac snRNA, the highly divergent counterpart of U6 snRNA, is the specific target that mediates inhibition of AT-AC splicing by the influenza virus NS1 protein
    • Wang, W., and R. M. Krug. 1998. U6atac snRNA, the highly divergent counterpart of U6 snRNA, is the specific target that mediates inhibition of AT-AC splicing by the influenza virus NS1 protein. RNA 4:55-64.
    • (1998) RNA , vol.4 , pp. 55-64
    • Wang, W.1    Krug, R.M.2
  • 135
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz, A. J., J. C. Johnson, B. Penn, M. Mahalingam, S. R. Kimball, and J. A. Cooper. 1999. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol. 19:1871-1880.
    • (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
  • 136
    • 0018414725 scopus 로고
    • Transcription of vesicular stomatitis virus is required to shut off cellular RNA synthesis
    • Weck, P. K., and R. R. Wagner. 1979. Transcription of vesicular stomatitis virus is required to shut off cellular RNA synthesis. J. Virol. 30:410-413.
    • (1979) J. Virol. , vol.30 , pp. 410-413
    • Weck, P.K.1    Wagner, R.R.2
  • 137
    • 0018747744 scopus 로고
    • Vesicular stomatitis virus infection reduces the number of active DNA-dependent RNA polymerases in myeloma cells
    • Week, P. K., and R. R. Wagner. 1979. Vesicular stomatitis virus infection reduces the number of active DNA-dependent RNA polymerases in myeloma cells. J. Biol. Chem. 254:5430-5434.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5430-5434
    • Week, P.K.1    Wagner, R.R.2
  • 138
    • 0003000152 scopus 로고    scopus 로고
    • Nonspecific host responses to viral infections
    • N. Nathanson (ed.), Lippincott-Raven Publishers, Philadelphia, Pa
    • Welsh, R. M., and G. C. Sen. 1997. Nonspecific host responses to viral infections, p. 109-141. In N. Nathanson (ed.), Viral pathogenesis. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1997) Viral Pathogenesis , pp. 109-141
    • Welsh, R.M.1    Sen, G.C.2
  • 139
    • 0014861840 scopus 로고
    • Interferon production and inhibition of host synthesis in cells infected with vesicular stomatitis virus
    • Wertz, G. W., and J. S. Youngner. 1970. Interferon production and inhibition of host synthesis in cells infected with vesicular stomatitis virus. J Virol. 6:476-484.
    • (1970) J Virol. , vol.6 , pp. 476-484
    • Wertz, G.W.1    Youngner, J.S.2
  • 140
    • 0021052924 scopus 로고
    • Vaccinia rescue of VSV from interferon-induced resistance: Reversal of translation block and inhibition of protein kinase activity
    • Whitaker-Dowling, P., and J. S. Youngner. 1983. Vaccinia rescue of VSV from interferon-induced resistance: reversal of translation block and inhibition of protein kinase activity. Virology 131:128-136.
    • (1983) Virology , vol.131 , pp. 128-136
    • Whitaker-Dowling, P.1    Youngner, J.S.2
  • 141
    • 0018883391 scopus 로고
    • Inhibition of ribonucleic acid accumulation in mouse L cells infected with vesicular stomatitis virus requires viral ribonucleic acid transcription
    • Wu, F. S., and J. M. Lucas-Lenard. 1980. Inhibition of ribonucleic acid accumulation in mouse L cells infected with vesicular stomatitis virus requires viral ribonucleic acid transcription. Biochemistry 19:804-810.
    • (1980) Biochemistry , vol.19 , pp. 804-810
    • Wu, F.S.1    Lucas-Lenard, J.M.2
  • 142
    • 0030753160 scopus 로고    scopus 로고
    • Poliovirus-encoded protease 2APro cleaves the TATA-binding protein but does not inhibit host cell RNA polymerase II transcription in vitro
    • Yalamanchili, P., R. Banerjee, and A. Dasgupta. 1997. Poliovirus-encoded protease 2APro cleaves the TATA-binding protein but does not inhibit host cell RNA polymerase II transcription in vitro. J. Virol. 71:6881-6886.
    • (1997) J. Virol. , vol.71 , pp. 6881-6886
    • Yalamanchili, P.1    Banerjee, R.2    Dasgupta, A.3
  • 143
    • 0031016644 scopus 로고    scopus 로고
    • Inhibition of host cell transcription by poliovirus: Cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro
    • Yalamanchili, P., U. Datta, and A. Dasgupta. 1997. Inhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro. J. Virol. 71:1220-1226.
    • (1997) J. Virol. , vol.71 , pp. 1220-1226
    • Yalamanchili, P.1    Datta, U.2    Dasgupta, A.3
  • 144
    • 0029925258 scopus 로고    scopus 로고
    • Inhibition of basal transcription by poliovirus: A virus-encoded protease (3Cpro) inhibits formation of TBP-TATA box complex in vitro
    • Yalamanchili, P., K. Harris, E. Wimmer, and A. Dasgupta. 1996. Inhibition of basal transcription by poliovirus: a virus-encoded protease (3Cpro) inhibits formation of TBP-TATA box complex in vitro. J Virol 70:2922-2929.
    • (1996) J Virol , vol.70 , pp. 2922-2929
    • Yalamanchili, P.1    Harris, K.2    Wimmer, E.3    Dasgupta, A.4
  • 145
    • 0031458316 scopus 로고    scopus 로고
    • Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro
    • Yalamanchili, P., K. Weidman, and A. Dasgupta. 1997. Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro. Virology 239:176-185.
    • (1997) Virology , vol.239 , pp. 176-185
    • Yalamanchili, P.1    Weidman, K.2    Dasgupta, A.3
  • 146
    • 0028110071 scopus 로고
    • Membrane-binding domains and cytopathogenesis of the matrix protein of vesicular stomatitis virus
    • Ye, Z., W. Sun, K. Suryanarayana, P. Justice, D. Robinson, and R. R. Wagner. 1994. Membrane-binding domains and cytopathogenesis of the matrix protein of vesicular stomatitis virus. J. Virol. 68:7386-7396.
    • (1994) J. Virol. , vol.68 , pp. 7386-7396
    • Ye, Z.1    Sun, W.2    Suryanarayana, K.3    Justice, P.4    Robinson, D.5    Wagner, R.R.6
  • 147
    • 0032567085 scopus 로고    scopus 로고
    • Inhibition of host RNA polymerase II-dependent transcription by vesicular stomatitis virus results from inactivation of TFIID
    • Yuan, H., B. K. Yoza, and D. S. Lyles. 1998. Inhibition of host RNA polymerase II-dependent transcription by vesicular stomatitis virus results from inactivation of TFIID. Virology 251:383-392.
    • (1998) Virology , vol.251 , pp. 383-392
    • Yuan, H.1    Yoza, B.K.2    Lyles, D.S.3
  • 148
    • 0343037010 scopus 로고
    • RNA synthesis in poliovirus-infected cells
    • Zimmerman, E. F., M. Hecter, and J. E. Darnell. 1963. RNA synthesis in poliovirus-infected cells. Virology 19:400-408.
    • (1963) Virology , vol.19 , pp. 400-408
    • Zimmerman, E.F.1    Hecter, M.2    Darnell, J.E.3


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