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Volumn 28, Issue 3, 2003, Pages 130-136

Translation initiation and viral tricks

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; GENE PRODUCT; INITIATION FACTOR; INITIATION FACTOR 4F; MESSENGER RNA; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 0037333760     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00029-X     Document Type: Review
Times cited : (170)

References (65)
  • 1
    • 0343431521 scopus 로고    scopus 로고
    • Translational control of viral gene expression in eukaryotes
    • Gale M. Jr, et al. Translational control of viral gene expression in eukaryotes. Microbiol. Mol. Biol. Rev. 64:2000;239-280.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 239-280
    • Gale M., Jr.1
  • 2
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • J.W.B. et al. Hershey. Cold Spring Harbor Laboratory Press
    • Hershey J.W.B., Merrick W.C. Pathway and mechanism of initiation of protein synthesis. Hershey J.W.B., et al. Translational Regulation of Gene Expression. 2000;33-88 Cold Spring Harbor Laboratory Press.
    • (2000) Translational Regulation of Gene Expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 3
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras A.-C., et al. 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
  • 4
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF-4G mediates in vitro polyA tail dependent translation
    • Tarun S.Z., et al. Translation initiation factor eIF-4G mediates in vitro polyA tail dependent translation. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9046-9051.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1
  • 5
    • 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
    • Imataka H., et al. 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
    • Imataka, H.1
  • 6
    • 0031982683 scopus 로고    scopus 로고
    • A novel functional human eukaryotic translation initiation factor 4G
    • Gradi A., et al. A novel functional human eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 18:1998;334-342.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 334-342
    • Gradi, A.1
  • 7
    • 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., et al. 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
  • 8
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
    • Pyronnet S., et al. 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
  • 9
    • 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., et al. Phosphorylation of the cap-binding protein eukaryotic translation initiation 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
  • 10
    • 0035912725 scopus 로고    scopus 로고
    • Molecular mechanisms of translation initiation in eukaryotes
    • Pestova T.V., et al. Molecular mechanisms of translation initiation in eukaryotes. Proc. Natl. Acad. Sci. U. S. A. 98:2001;7029-7036.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7029-7036
    • Pestova, T.V.1
  • 11
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak M. The scanning model for translation: an update. J. Cell Biol. 108:1989;229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 12
    • 0002570015 scopus 로고    scopus 로고
    • Viral translational strategies and host defense mechanisms
    • Hershey, J.W.B. et al., eds), Cold Spring Harbor Laboratory Press
    • Pe'ery, T. and Mathews, M.B. (2000) Viral translational strategies and host defense mechanisms. In Translational Control of Gene expression (Vol. Monograph 39) (Hershey, J.W.B. et al., eds), pp. 371-424, Cold Spring Harbor Laboratory Press.
    • (2000) Translational Control of Gene expression (Vol. Monograph 39) , pp. 371-424
    • Pe'ery, T.1    Mathews, M.B.2
  • 13
    • 0002813638 scopus 로고    scopus 로고
    • Adenovirus inhibition of cellular protein synthesis and preferential translation of viral mRNAs
    • J.W.B. et al. Hershey. Cold Spring Harbor Laboratory Press
    • Schneider R.J. Adenovirus inhibition of cellular protein synthesis and preferential translation of viral mRNAs. Hershey J.W.B., et al. Translational Regulation. 2000;901-914 Cold Spring Harbor Laboratory Press.
    • (2000) Translational Regulation , pp. 901-914
    • Schneider, R.J.1
  • 14
    • 0027551185 scopus 로고
    • The small RNAs of Epstein-Barr virus
    • Clemens M.J. The small RNAs of Epstein-Barr virus. Mol. Biol. Rep. 17:1993;81-92.
    • (1993) Mol. Biol. Rep. , vol.17 , pp. 81-92
    • Clemens, M.J.1
  • 15
    • 0036500131 scopus 로고    scopus 로고
    • Epstein-Barr virus RNA confers resistance to interferon-alpha-induced apoptosis in Burkitt's lymphoma
    • Nanbo A., et al. Epstein-Barr virus RNA confers resistance to interferon-alpha-induced apoptosis in Burkitt's lymphoma. EMBO J. 21:2002;954-965.
    • (2002) EMBO J. , vol.21 , pp. 954-965
    • Nanbo, A.1
  • 16
    • 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., et al. 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
  • 17
    • 0028042337 scopus 로고
    • HIV-1 TAR RNA has an intrinsic ability to activate interferon-inducible enzymes
    • Maitra R.K., et al. HIV-1 TAR RNA has an intrinsic ability to activate interferon-inducible enzymes. Virology. 204:1994;823-827.
    • (1994) Virology , vol.204 , pp. 823-827
    • Maitra, R.K.1
  • 18
    • 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., et al. 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
  • 19
    • 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., et al. 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
  • 20
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E., et al. 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
  • 21
    • 0026465267 scopus 로고
    • Translational stimulation by reovirus polypeptide 3: Substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2
    • Lloyd R.M., Shatkin A.J. Translational stimulation by reovirus polypeptide 3: substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2. J. Virol. 66:1992;6878-6884.
    • (1992) J. Virol. , vol.66 , pp. 6878-6884
    • Lloyd, R.M.1    Shatkin, A.J.2
  • 22
    • 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., et al. 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
  • 23
    • 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., et al. 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
  • 24
    • 0036839211 scopus 로고    scopus 로고
    • Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein
    • Peters G.A., et al. 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
  • 25
    • 0036168638 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 US11 protein interacts with protein kinase R in infected cells and requires a 30 amino acid sequence adjacent to a kinase substrate domain
    • Cassady K.A., Gross M. The herpes simplex virus type 1 US11 protein interacts with protein kinase R in infected cells and requires a 30 amino acid sequence adjacent to a kinase substrate domain. J. Virol. 76:2002;2029-2035.
    • (2002) J. Virol. , vol.76 , pp. 2029-2035
    • Cassady, K.A.1    Gross, M.2
  • 26
    • 0037213277 scopus 로고    scopus 로고
    • Identification of a lytic Epstein-Barr virus gene product that can regulate PKR activation
    • Poppers J., et al. Identification of a lytic 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
  • 27
    • 0035125267 scopus 로고    scopus 로고
    • Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-standed RNA-activated protein kinase
    • Burysek L., Pitha P.M. Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-standed 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
  • 28
    • 0031017382 scopus 로고    scopus 로고
    • The γ(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • He B., et al. The γ(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. U. S. A. 94:1997;843-848.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 843-848
    • He, B.1
  • 29
    • 0027163011 scopus 로고
    • Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 α-specific protein kinase
    • Carroll K., et al. Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 α-specific protein kinase. J. Biol. Chem. 268:1993;12837-12842.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12837-12842
    • Carroll, K.1
  • 30
    • 0036239936 scopus 로고    scopus 로고
    • Complementation of Vaccinia virus lacking the double-stranded RNA-binding protein gene E3L by human Cytomegalovirus
    • Child S.J., et al. Complementation of Vaccinia virus lacking the double-stranded RNA-binding protein gene E3L by human Cytomegalovirus. J. Virol. 76:2002;4912-4918.
    • (2002) J. Virol. , vol.76 , pp. 4912-4918
    • Child, S.J.1
  • 31
    • 17144463221 scopus 로고    scopus 로고
    • Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: Molecular mechanisms of kinase regulation
    • Gale M. Jr, et al. Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation. Mol. Cell. Biol. 18:1998;5208-5218.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5208-5218
    • Gale M., Jr.1
  • 32
    • 0035661068 scopus 로고    scopus 로고
    • Effects of mutation in hepatitis C virus nonstructural protein 5A on interferon resistance mediated by inhibition of PKR kinase activity in mammalian cells
    • Noguchi T., et al. Effects of mutation in hepatitis C virus nonstructural protein 5A on interferon resistance mediated by inhibition of PKR kinase activity in mammalian cells. Microbiol. Immunol. 45:2001;829-840.
    • (2001) Microbiol. Immunol. , vol.45 , pp. 829-840
    • Noguchi, T.1
  • 33
    • 0035041305 scopus 로고    scopus 로고
    • Regulation of mRNA translation and cellular signaling by hepatitis C virus NS5A nonstructural protein
    • He Y., et al. Regulation of mRNA translation and cellular signaling by hepatitis C virus NS5A nonstructural protein. J. Virol. 75:2001;5090-5098.
    • (2001) J. Virol. , vol.75 , pp. 5090-5098
    • He, Y.1
  • 34
    • 0037007105 scopus 로고    scopus 로고
    • Regulation of PKR and IRF-1 during hepatitis C virus RNA replication
    • Pflugheber J., et al. Regulation of PKR and IRF-1 during hepatitis C virus RNA replication. Proc. Natl. Acad. Sci. U. S. A. 99:2002;4650-4655.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4650-4655
    • Pflugheber, J.1
  • 35
    • 0032899696 scopus 로고    scopus 로고
    • Characterization of the effects of hepatitis C virus nonstructural 5A protein expression in human cell lines and on interferon-sensitive virus replication
    • Polyak S.J., et al. Characterization of the effects of hepatitis C virus nonstructural 5A protein expression in human cell lines and on interferon-sensitive virus replication. Hepatology. 29:1999;1262-1271.
    • (1999) Hepatology , vol.29 , pp. 1262-1271
    • Polyak, S.J.1
  • 36
    • 0242422098 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesis
    • Francois C., et al. Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesis. J. Virol. 74:2000;5587-5596.
    • (2000) J. Virol. , vol.74 , pp. 5587-5596
    • Francois, C.1
  • 37
    • 0034623816 scopus 로고    scopus 로고
    • Efficient initiation of HCV RNA replication in cell culture
    • Blight K.J., et al. Efficient initiation of HCV RNA replication in cell culture. Science. 290:2000;1972-1975.
    • (2000) Science , vol.290 , pp. 1972-1975
    • Blight, K.J.1
  • 38
    • 0033516497 scopus 로고    scopus 로고
    • Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein
    • Taylor D.R., et al. 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
  • 39
    • 0035148472 scopus 로고    scopus 로고
    • Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain
    • Taylor D.R., et al. Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain. J. Virol. 75:2001;1265-1273.
    • (2001) J. Virol. , vol.75 , pp. 1265-1273
    • Taylor, D.R.1
  • 40
    • 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., et al. 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
  • 41
    • 0037166289 scopus 로고    scopus 로고
    • Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2α
    • Fernandez J., et al. Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2α J. Biol. Chem. 277:2002;19198-19205.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19198-19205
    • Fernandez, J.1
  • 42
    • 0035421213 scopus 로고    scopus 로고
    • Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation
    • Ali I.K., et al. Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation. EMBO J. 20:2001;4233-4242.
    • (2001) EMBO J. , vol.20 , pp. 4233-4242
    • Ali, I.K.1
  • 43
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims M., et al. Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J. Virol. 73:1999;718-727.
    • (1999) J. Virol. , vol.73 , pp. 718-727
    • Joachims, M.1
  • 44
    • 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., et al. Cleavage of Poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff? J. Virol. 73:1999;709-717.
    • (1999) J. Virol. , vol.73 , pp. 709-717
    • Kerekatte, V.1
  • 45
    • 0029890687 scopus 로고    scopus 로고
    • Activation of the translational suppressor 4E-BP-1 following infection with encephalomyocarditis virus and poliovirus
    • Gingras A.-C., et al. Activation of the translational suppressor 4E-BP-1 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
  • 46
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen C.U., 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
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J., Sonenberg N. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature. 334:1988;320-325.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 48
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang S.K., et al. A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62:1988;2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1
  • 49
    • 0029053190 scopus 로고
    • Initiation of protein synthesis by the eukaryotic translational apparatus on circular RNAs
    • Chen C.Y., Sarnow P. Initiation of protein synthesis by the eukaryotic translational apparatus on circular RNAs. Science. 268:1995;415-417.
    • (1995) Science , vol.268 , pp. 415-417
    • Chen, C.Y.1    Sarnow, P.2
  • 50
    • 0031905698 scopus 로고    scopus 로고
    • A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs
    • Pestova T.V., et al. A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs. Genes Dev. 12:1998;67-83.
    • (1998) Genes Dev. , vol.12 , pp. 67-83
    • Pestova, T.V.1
  • 51
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian intiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation
    • Pause A., et al. Dominant negative mutants of mammalian intiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation. EMBO J. 13:1994;1205-1215.
    • (1994) EMBO J. , vol.13 , pp. 1205-1215
    • Pause, A.1
  • 52
    • 0033059194 scopus 로고    scopus 로고
    • Identification of the RNA-binding, dimerization, and eIF4GI-binding domains of rotavirus nonstructural protein NSP3
    • Piron M., et al. Identification of the RNA-binding, dimerization, and eIF4GI-binding domains of rotavirus nonstructural protein NSP3. J. Virol. 73:1999;5411-5421.
    • (1999) J. Virol. , vol.73 , pp. 5411-5421
    • Piron, M.1
  • 53
    • 0033838456 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus
    • Aragon T., et al. Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol. Cell. Biol. 20:2000;6259-6268.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6259-6268
    • Aragon, T.1
  • 54
    • 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
    • Park Y.W., et al. Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1. Proc. Natl. Acad. Sci. U. S. A. 96:1999;6694-6699.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6694-6699
    • Park, Y.W.1
  • 55
    • 0027252545 scopus 로고
    • Modification of eukaryotic initiation factor 4F during infection by influenza virus
    • Feigenblum D., 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
  • 56
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • D.M. Knipe, Howley P. 4th edn Lippincott
    • Roizman B., Knipe D.M. Herpes simplex viruses and their replication. Knipe D.M., Howley P. 4th edn Field's Virology. Vol. 2:2001;2399-2460 Lippincott.
    • (2001) Field's Virology , vol.2 , pp. 2399-2460
    • Roizman, B.1    Knipe, D.M.2
  • 57
    • 0001798701 scopus 로고    scopus 로고
    • Control of mRNA stability during herpes simplex virus infections
    • J.B. Harford, & D.R. Morris. Wiley-Liss
    • Read G.S. Control of mRNA stability during herpes simplex virus infections. Harford J.B., Morris D.R. mRNA metabolism and Post-Transcriptional Gene Regulation. 1997;311-321 Wiley-Liss.
    • (1997) MRNA metabolism and Post-Transcriptional Gene Regulation , pp. 311-321
    • Read, G.S.1
  • 58
    • 0036333951 scopus 로고    scopus 로고
    • MRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: Genetic and biochemical evidence that Vhs is a nuclease
    • Everly D.N. Jr, et al. mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease. J. Virol. 76:2002;8560-8571.
    • (2002) J. Virol. , vol.76 , pp. 8560-8571
    • Everly D.N., Jr.1
  • 59
    • 0034796322 scopus 로고    scopus 로고
    • MRNA decay during herpesvirus infections: Interaction between a putative viral nuclease and a cellular translation factor
    • Feng P., et al. mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor. J. Virol. 75:2001;10272-10280.
    • (2001) J. Virol. , vol.75 , pp. 10272-10280
    • Feng, P.1
  • 60
    • 0034600839 scopus 로고    scopus 로고
    • Adenovirus specific translation by selective disassembly of cap-initiation complex
    • Cuesta R., et al. Adenovirus specific translation by selective disassembly of cap-initiation complex. EMBO J. 19:2000;3465-3474.
    • (2000) EMBO J. , vol.19 , pp. 3465-3474
    • Cuesta, R.1
  • 61
    • 0029785142 scopus 로고    scopus 로고
    • Selective translation by ribosome jumping in adenovirus infected and heat shocked cells
    • Yueh A., Schneider R.J. Selective translation 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
  • 62
    • 0034090845 scopus 로고    scopus 로고
    • Translation by ribosome shunting on adenovirus and Hsp70 mRNAs facilitated by complementarity to 18S rRNA
    • Yueh A., 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
  • 63
    • 0002261752 scopus 로고    scopus 로고
    • Ribosome shunting in eukaryotes: What the viruses tell me
    • J. Bailley-Serres, & D.R. et al. Gallie. American Soc. Plant Physiol
    • Hohn T., et al. Ribosome shunting in eukaryotes: what the viruses tell me. Bailley-Serres J., Gallie D.R., et al. A Look Beyond Transcription: Mechanisms Determining mRNA Stability and Translation in Plants. 1998;84-95 American Soc. Plant Physiol.
    • (1998) A Look Beyond Transcription: Mechanisms Determining mRNA Stability and Translation in Plants , pp. 84-95
    • Hohn, T.1
  • 64
    • 0031865049 scopus 로고    scopus 로고
    • Sendai virus Y proteins are initiated by a ribosomal shunt
    • Latorre P., et al. Sendai virus Y proteins are initiated by a ribosomal shunt. Mol. Cell. Biol. 18:1998;5021-5031.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5021-5031
    • Latorre, P.1
  • 65
    • 0032975255 scopus 로고    scopus 로고
    • Human papillomavirus type 18 E1 protein is translated from polycistronic mRNA by a discontinuous scanning mechanism
    • Remm M., et al. Human papillomavirus type 18 E1 protein is translated from polycistronic mRNA by a discontinuous scanning mechanism. J. Virol. 73:1999;3062-3070.
    • (1999) J. Virol. , vol.73 , pp. 3062-3070
    • Remm, M.1


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