메뉴 건너뛰기




Volumn 95, Issue 3-4, 2003, Pages 141-156

Conducting the initiation of protein synthesis: The role of eIF4G

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; INITIATION FACTOR; INITIATION FACTOR 4A; INITIATION FACTOR 4E; INITIATION FACTOR 4F; INITIATION FACTOR 4G; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 0037781584     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0248-4900(03)00031-5     Document Type: Review
Times cited : (190)

References (150)
  • 1
    • 0035421213 scopus 로고    scopus 로고
    • Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation
    • Ali, I.K., McKendrick, L., Morley, S.J., Jackson, R.J., 2001. Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation. EMBO J. 20, 4233-4242.
    • (2001) EMBO J. , vol.20 , pp. 4233-4242
    • Ali, I.K.1    McKendrick, L.2    Morley, S.J.3    Jackson, R.J.4
  • 2
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade, M.A., Bork, P., 1995. HEAT repeats in the Huntington's disease protein. Nat. Genet 11, 115-116.
    • (1995) Nat. Genet , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 3
    • 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., de la Luna, S., Novoa, I., Carrasco, L., Ortin, J., Nieto, A., 2000. Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol. Cell. Biol. 20, 6259-6268.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6259-6268
    • Aragon, T.1    de la Luna, S.2    Novoa, I.3    Carrasco, L.4    Ortin, J.5    Nieto, A.6
  • 4
    • 0023051331 scopus 로고
    • Structure of initiation factor eIF-3 from rat liver. Hydrodynamic and electron microscopic investigations
    • Behlke, J., Bommer, U.A., Lutsch, G., Henske, A., Bielka, H., 1986. Structure of initiation factor eIF-3 from rat liver. Hydrodynamic and electron microscopic investigations. Ent. J. Biochem. 157, 523-530.
    • (1986) Ent. J. Biochem. , vol.157 , pp. 523-530
    • Behlke, J.1    Bommer, U.A.2    Lutsch, G.3    Henske, A.4    Bielka, H.5
  • 5
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham, G.J., McInerney, G.M., Ross-Smith, N., 2000. Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74, 272-280.
    • (2000) J. Virol. , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 6
    • 0034543678 scopus 로고    scopus 로고
    • Picornavirus IRESes and the poly(A) tail jointly promote cap- independent translation in a mammalian cell-free system
    • Bergamini, G., Preiss, T., Hentze, M.W., 2000. Picornavirus IRESes and the poly(A) tail jointly promote cap- independent translation in a mammalian cell-free system. RNA 6, 1781-1790.
    • (2000) RNA , vol.6 , pp. 1781-1790
    • Bergamini, G.1    Preiss, T.2    Hentze, M.W.3
  • 7
    • 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., Sonenberg, N., 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
  • 8
    • 0030614716 scopus 로고    scopus 로고
    • elF4G and its proteolytic cleavage products: Effect on initiation of protein synthesis from capped, uncapped, and IRES-containing mRNAs
    • Borman, A.M., Kirchweger, R., Ziegler, E., Rhoads, R.E., Skern, T., Kean, K.M., 1997. elF4G and its proteolytic cleavage products: effect on initiation of protein synthesis from capped, uncapped, and IRES-containing mRNAs. RNA 3, 186-196.
    • (1997) RNA , vol.3 , pp. 186-196
    • Borman, A.M.1    Kirchweger, R.2    Ziegler, E.3    Rhoads, R.E.4    Skern, T.5    Kean, K.M.6
  • 9
    • 0037184089 scopus 로고    scopus 로고
    • Free poly(A) stimulates capped mRNA translation in vitro through the eIF4G-poly(A)-binding protein interaction
    • Borman, A.M., Michel, Y.M., Malnou, C.E., Kean, K.M., 2002. Free poly(A) stimulates capped mRNA translation in vitro through the eIF4G-poly(A)-binding protein interaction. J. Biol. Chem. 277, 36818-36824.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36818-36824
    • Borman, A.M.1    Michel, Y.M.2    Malnou, C.E.3    Kean, K.M.4
  • 10
    • 0032486249 scopus 로고    scopus 로고
    • Direct cleavage of elF4G by poliovirus 2A protease is inefficient in vitro
    • Bovee, M.L., Lamphear, B.J., Rhoads, R.E., Lloyd, R.E., 1998a. Direct cleavage of elF4G 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
  • 11
    • 0032486281 scopus 로고    scopus 로고
    • The predominant elF4G-specific cleavage activity in poliovirus-infected HeLa cells is distinct from 2A protease
    • Bovee, M.L., Marissen, W.E., Zamora, M., Lloyd, R.E., 1998b. 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
  • 12
    • 0037066737 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the N terminus of translational initiation factor eIF4G-1 reveals novel isoforms
    • Bradley, C.A., Padovan, J.C., Thompson, T.L., Benoit, C.A., Chait, B.T., Rhoads, R.E., 2002. Mass spectrometric analysis of the N terminus of translational initiation factor eIF4G-1 reveals novel isoforms. J. Biol. Chem. 277, 12559-12571.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12559-12571
    • Bradley, C.A.1    Padovan, J.C.2    Thompson, T.L.3    Benoit, C.A.4    Chait, B.T.5    Rhoads, R.E.6
  • 13
    • 0030266994 scopus 로고    scopus 로고
    • The plant translational apparatus
    • Browning, K.S., 1996. The plant translational apparatus. Plant Mol. Biol. 32, 107-144.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 107-144
    • Browning, K.S.1
  • 14
    • 0023264868 scopus 로고
    • The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells
    • Buckley, B., Ehrenfeld, E., 1987. The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 262, 13599-13606.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13599-13606
    • Buckley, B.1    Ehrenfeld, E.2
  • 15
    • 0033016770 scopus 로고    scopus 로고
    • Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis
    • Bushell, M., McKendrick, L., Janicke, R.U., Clemens, M.J., Morley, S.J., 1999. Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis. FEBS Lett. 451, 332-336.
    • (1999) FEBS Lett. , vol.451 , pp. 332-336
    • Bushell, M.1    McKendrick, L.2    Janicke, R.U.3    Clemens, M.J.4    Morley, S.J.5
  • 16
    • 0033948682 scopus 로고    scopus 로고
    • Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: Characterisation of an internal fragment generated by caspase-3-mediated cleavage
    • Bushell, M., Poncet, D., Marissen, W.E., Flotow, H., Lloyd, R.E., Clemens, M.J., Morley, S.J., 2000. Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: characterisation of an internal fragment generated by caspase-3-mediated cleavage. Cell Death Differ. 7, 628-636.
    • (2000) Cell Death Differ. , vol.7 , pp. 628-636
    • Bushell, M.1    Poncet, D.2    Marissen, W.E.3    Flotow, H.4    Lloyd, R.E.5    Clemens, M.J.6    Morley, S.J.7
  • 17
    • 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., Lloyd, R.E., 2002. Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons. Mol. Cell. Biol. 22, 4499-4511.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4499-4511
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 18
    • 0032481114 scopus 로고    scopus 로고
    • Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines
    • Clemens, M.J., Bushell, M., Morley, S.J., 1998. Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines. Oncogene 17, 2921-2931.
    • (1998) Oncogene , vol.17 , pp. 2921-2931
    • Clemens, M.J.1    Bushell, M.2    Morley, S.J.3
  • 19
    • 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., Sonenberg, N., 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392, 520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 20
    • 0034659505 scopus 로고    scopus 로고
    • Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes
    • Cuesta, R., Laroia, G., Schneider, R.J., 2000a. Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14, 1460-1470.
    • (2000) Genes Dev. , vol.14 , pp. 1460-1470
    • Cuesta, R.1    Laroia, G.2    Schneider, R.J.3
  • 21
    • 0034600839 scopus 로고    scopus 로고
    • Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F
    • Cuesta, R., Xi, Q., Schneider, R.J., 2000b. Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F. EMBO J. 19, 3465-3474.
    • (2000) EMBO J. , vol.19 , pp. 3465-3474
    • Cuesta, R.1    Xi, Q.2    Schneider, R.J.3
  • 22
    • 0033200316 scopus 로고    scopus 로고
    • Translation driven by an eIF4G core domain in vivo
    • De Gregorio, E., Preiss, T., Hentze, M.W., 1999. Translation driven by an eIF4G core domain in vivo. EMBO J. 18, 4865-4874.
    • (1999) EMBO J. , vol.18 , pp. 4865-4874
    • De Gregorio, E.1    Preiss, T.2    Hentze, M.W.3
  • 23
    • 0031869508 scopus 로고    scopus 로고
    • Translational activation of uncapped mRNAs by the central part of human eIF4G is 5′ end-dependent
    • De Gregorio, E., Preiss, T., Hentze, M.W., 1998. Translational activation of uncapped mRNAs by the central part of human eIF4G is 5′ end-dependent. RNA 4, 828-836.
    • (1998) RNA , vol.4 , pp. 828-836
    • De Gregorio, E.1    Preiss, T.2    Hentze, M.W.3
  • 24
    • 0024110509 scopus 로고
    • Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex
    • Devaney, M.A., Vakharia, V.N., Lloyd, R.E., Ehrenfeld, E., Grubman, M.J., 1988. Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex. J. Virol. 62, 4407-4409.
    • (1988) J. Virol. , vol.62 , pp. 4407-4409
    • Devaney, M.A.1    Vakharia, V.N.2    Lloyd, R.E.3    Ehrenfeld, E.4    Grubman, M.J.5
  • 25
    • 0035310917 scopus 로고    scopus 로고
    • Structural and functional similarities between the central eukaryotic initiation factor (eIF)4A-binding domain of mammalian eIF4G and the eIF4A-binding domain of yeast eIF4G
    • Dominguez, D., Kislig, E., Altmann, M., Trachsel, H., 2001. Structural and functional similarities between the central eukaryotic initiation factor (eIF)4A-binding domain of mammalian eIF4G and the eIF4A-binding domain of yeast eIF4G. Biochem. J. 355, 223-230.
    • (2001) Biochem. J. , vol.355 , pp. 223-230
    • Dominguez, D.1    Kislig, E.2    Altmann, M.3    Trachsel, H.4
  • 26
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison, D., Milburn, S.C., Edery, I., Sonenberg, N., Hershey, J.W., 1982. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J. Biol. Chem. 257, 14806-14810.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 27
    • 0017157438 scopus 로고
    • Structural difference between the 5′ termini of viral and cellular mRNA in poliovirus-infected cells: Possible basis for the inhibition of host protein synthesis
    • Fernandez-Munoz, R., Darnell, J.E., 1976. Structural difference between the 5′ termini of viral and cellular mRNA in poliovirus-infected cells: possible basis for the inhibition of host protein synthesis. J. Virol. 18, 719-726.
    • (1976) J. Virol. , vol.18 , pp. 719-726
    • Fernandez-Munoz, R.1    Darnell, J.E.2
  • 28
    • 0037113946 scopus 로고    scopus 로고
    • Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases
    • Foeger, N., Glaser, W., Skern, T., 2002. Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases. J. Biol. Chem. 277, 44300-44309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44300-44309
    • Foeger, N.1    Glaser, W.2    Skern, T.3
  • 29
    • 0033636895 scopus 로고    scopus 로고
    • The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation
    • Fortes, P., Inada, T., Preiss, T., Hentze, M.W., Mattaj, I.W., Sachs, A.B., 2000. The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation. Mol. Cell 6, 191-196.
    • (2000) Mol. Cell , vol.6 , pp. 191-196
    • Fortes, P.1    Inada, T.2    Preiss, T.3    Hentze, M.W.4    Mattaj, I.W.5    Sachs, A.B.6
  • 30
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed, E.O., 1998. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 251, 1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 31
    • 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., Hunter, T., 1997. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16, 1921-1933.
    • (1997) EMBO J. , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 32
    • 0343431521 scopus 로고    scopus 로고
    • Translational control of viral gene expression in eukaryotes
    • Gale Jr., M., Tan, S.L., Katze, M.G., 2000. Translational control of viral gene expression in eukaryotes. Microbiol. Mol. Biol. Rev. 64, 239-280.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 239-280
    • Gale M., Jr.1    Tan, S.L.2    Katze, M.G.3
  • 33
    • 0026038913 scopus 로고
    • The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie, D.R., 1991. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5, 2108-2116.
    • (1991) Genes Dev. , vol.5 , pp. 2108-2116
    • Gallie, D.R.1
  • 34
    • 0032541485 scopus 로고    scopus 로고
    • A tale of two termini: A functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation
    • Gallie, D.R., 1998. A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene 216, 1-11.
    • (1998) Gene , vol.216 , pp. 1-11
    • Gallie, D.R.1
  • 35
    • 0035813149 scopus 로고    scopus 로고
    • eIF4G functionally differs from eIFiso4G in promoting internal initiation, cap-independent translation, and translation of structured mRNAs
    • Gallie, D.R., Browning, K.S., 2001. eIF4G functionally differs from eIFiso4G in promoting internal initiation, cap-independent translation, and translation of structured mRNAs. J. Biol. Chem. 276, 36951-36960.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36951-36960
    • Gallie, D.R.1    Browning, K.S.2
  • 36
    • 0032570708 scopus 로고    scopus 로고
    • Functional characterization of the internal ribosome entry site of eIF4G mRNA
    • Gan, W., Celle, M.L., Rhoads, R.E., 1998. Functional characterization of the internal ribosome entry site of eIF4G mRNA. J. Biol. Chem. 273, 5006-5012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5006-5012
    • Gan, W.1    Celle, M.L.2    Rhoads, R.E.3
  • 37
    • 0030021166 scopus 로고    scopus 로고
    • Internal initiation of translation directed by the 5′-untranslated region of the mRNA for eIF4G, a factor involved in the picornavirus-induced switch from cap-dependent to internal initiation
    • Gan, W., Rhoads, R.E., 1996. Internal initiation of translation directed by the 5′-untranslated region of the mRNA for eIF4G, a factor involved in the picornavirus-induced switch from cap-dependent to internal initiation. J. Biol. Chem. 271, 623-626.
    • (1996) J. Biol. Chem. , vol.271 , pp. 623-626
    • Gan, W.1    Rhoads, R.E.2
  • 38
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A.C., Raught, B., Sonenberg, N., 1999. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68, 913-963.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 39
    • 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., Sonenberg, N., 1996. Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus. Proc. Natl. Acad. Sci. USA 93, 5578-5583.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5578-5583
    • Gingras, A.C.1    Svitkin, Y.2    Belsham, G.J.3    Pause, A.4    Sonenberg, N.5
  • 41
    • 0027219266 scopus 로고
    • TIF4631 and TIF4632: Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function
    • Goyer, C., Altmann, M., Lee, H.S., Blanc, A., Deshmukh, M., Woolford Jr., J.L., Trachsel, H., Sonenberg, N., 1993. TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell. Biol. 13, 4860-4874.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4860-4874
    • Goyer, C.1    Altmann, M.2    Lee, H.S.3    Blanc, A.4    Deshmukh, M.5    Woolford J.L., Jr.6    Trachsel, H.7    Sonenberg, N.8
  • 43
    • 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
    • Gradi, A., Svitkin, Y.V., Imataka, H., Sonenberg, N., 1998b. 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. USA , vol.95 , pp. 11089-11094
    • Gradi, A.1    Svitkin, Y.V.2    Imataka, H.3    Sonenberg, N.4
  • 45
    • 0029861190 scopus 로고    scopus 로고
    • The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase
    • Haghighat, A., Svitkin, Y., Novoa, I., Kuechler, E., Skern, T., Sonenberg, N., 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
  • 46
    • 0026443004 scopus 로고
    • Translational enhancement of the polio-virus 5′ noncoding region mediated by virus-encoded polypeptide 2A
    • Hambidge, S.J., Sarnow, P., 1992. Translational enhancement of the polio-virus 5′ noncoding region mediated by virus-encoded polypeptide 2A. Proc. Natl. Acad. Sci. USA 89, 10272-10276.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10272-10276
    • Hambidge, S.J.1    Sarnow, P.2
  • 47
    • 0036838078 scopus 로고    scopus 로고
    • Regulation of gene expression by internal ribosome entry sites or cryptic promoters: The eIF4G story
    • Han, B., Zhang, J.T., 2002. Regulation of gene expression by internal ribosome entry sites or cryptic promoters: the eIF4G story. Mol. Cell. Biol. 22, 7372-7384.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7372-7384
    • Han, B.1    Zhang, J.T.2
  • 48
    • 0029394949 scopus 로고
    • Protein synthesis in eukaryotic organisms: New insights into the function of translation initiation factor eIF-3
    • Hannig, E.M., 1995. Protein synthesis in eukaryotic organisms: new insights into the function of translation initiation factor eIF-3. Bioessays 17, 915-919.
    • (1995) Bioessays , vol.17 , pp. 915-919
    • Hannig, E.M.1
  • 49
    • 0018184292 scopus 로고
    • Control of protein synthesis in extracts from poliovirus-infected cells. I. mRNA discrimination by crude initiation factors
    • Helentjaris, T., Ehrenfeld, E., 1978. Control of protein synthesis in extracts from poliovirus-infected cells. I. mRNA discrimination by crude initiation factors. J. Virol. 26, 510-521.
    • (1978) J. Virol. , vol.26 , pp. 510-521
    • Helentjaris, T.1    Ehrenfeld, E.2
  • 50
    • 0037117540 scopus 로고    scopus 로고
    • The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins
    • Henis-Korenblit, S., Shani, G., Sines, T., Marash, L., Shohat, G., Kimchi, A., 2002. The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins. Proc. Natl. Acad. Sci. USA 99, 5400-5405.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5400-5405
    • Henis-Korenblit, S.1    Shani, G.2    Sines, T.3    Marash, L.4    Shohat, G.5    Kimchi, A.6
  • 51
    • 0033980394 scopus 로고    scopus 로고
    • A novel form of DAP5 protein accumulates in apoptotic cells as a result of caspase cleavage and internal ribosome entry site-mediated translation
    • Henis-Korenblit, S., Strumpf, N.L., Goldstaub, D., Kimchi, A., 2000. A novel form of DAP5 protein accumulates in apoptotic cells as a result of caspase cleavage and internal ribosome entry site-mediated translation. Mol. Cell. Biol. 20, 496-506.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 496-506
    • Henis-Korenblit, S.1    Strumpf, N.L.2    Goldstaub, D.3    Kimchi, A.4
  • 52
    • 0031024024 scopus 로고    scopus 로고
    • eIF4G: A multipurpose ribosome adapter?
    • Hentze, M.W., 1997. eIF4G: a multipurpose ribosome adapter? Science 275, 500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 53
    • 0033597729 scopus 로고    scopus 로고
    • The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4Gl
    • Hershey, P.E., McWhirter, S.M., Gross, J.D., Wagner, G., Alber, T., Sachs, A.B., 1999. The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4Gl. J. Biol. Chem. 274, 21297-21304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21297-21304
    • Hershey, P.E.1    McWhirter, S.M.2    Gross, J.D.3    Wagner, G.4    Alber, T.5    Sachs, A.B.6
  • 54
    • 0036463655 scopus 로고    scopus 로고
    • Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress
    • Hinnebusch, A.G., Natarajan, K., 2002. Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress. Eukaryot. Cell 1, 22-32.
    • (2002) Eukaryot. Cell , vol.1 , pp. 22-32
    • Hinnebusch, A.G.1    Natarajan, K.2
  • 55
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein
    • Hoshino, S., Imai, M., Kobayashi, T., Uchida, N., Katada, T, 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein. J. Biol. Chem. 274, 16677-16680.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 56
    • 0025857246 scopus 로고
    • Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein
    • Huang, J.T., Schneider, R.J., 1991. Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein. Cell 65, 271-280.
    • (1991) Cell , vol.65 , pp. 271-280
    • Huang, J.T.1    Schneider, R.J.2
  • 57
    • 0028034493 scopus 로고
    • Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae
    • Iizuka, N., Najita, L., Franzusoff, A., Sarnow, P., 1994. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell. Biol. 14, 7322-7330.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7322-7330
    • Iizuka, N.1    Najita, L.2    Franzusoff, A.3    Sarnow, P.4
  • 58
    • 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., Gradi, A., Sonenberg, N., 1998. 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, 7480-7489.
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 59
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • Imataka, H., Olsen, H.S., Sonenberg, N., 1997. A new translational regulator with homology to eukaryotic translation initiation factor 4G. EMBO J. 16, 817-825.
    • (1997) EMBO J. , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, H.S.2    Sonenberg, N.3
  • 60
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka, H., Sonenberg, N., 1997. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol. 17, 6940-6947.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 61
    • 0028874823 scopus 로고
    • Monensin and nigericin prevent the inhibition of host translation by poliovirus, without affecting p220 cleavage
    • Irurzun, A., Sanchez-Palomino, S., Novoa, I., Carrasco, L., 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
  • 62
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
    • Ishigaki, Y., Li, X., Serin, G., Maquat, L.E., 2001. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617.
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 63
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims, M., Van Breugel, P.C., Lloyd, R.E., 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
  • 64
    • 0031790633 scopus 로고    scopus 로고
    • Cap-independent polysomal association of natural mRNAs encoding c-myc, BiP, and eIF4G conferred by internal ribosome entry sites
    • Johannes, G., Sarnow, P., 1998. Cap-independent polysomal association of natural mRNAs encoding c-myc, BiP, and eIF4G conferred by internal ribosome entry sites. RNA 4, 1500-1513.
    • (1998) RNA , vol.4 , pp. 1500-1513
    • Johannes, G.1    Sarnow, P.2
  • 65
    • 0030787486 scopus 로고    scopus 로고
    • Cap-independent translation initiation in Xenopus oocytes
    • Keiper, B.D., Rhoads, R.E., 1997. Cap-independent translation initiation in Xenopus oocytes. Nucleic Acids Res. 25, 395-402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 395-402
    • Keiper, B.D.1    Rhoads, R.E.2
  • 66
    • 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., Keiper, B.D., Badorff, C., Cai, A., Knowlton K.U., Rhoads, R.E., 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
  • 67
    • 0031972645 scopus 로고    scopus 로고
    • RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G
    • Kessler, S.H., Sachs, A.B., 1998. RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 18, 51-57.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 51-57
    • Kessler, S.H.1    Sachs, A.B.2
  • 69
    • 0037219005 scopus 로고    scopus 로고
    • Eukaryotic initiation factors 4G and 4A mediate conformational changes downstream of the initiation codon of the encephalomyocarditis virus internal ribosomal entry site
    • Kolupaeva, V.G., Lomakin, I.B., Pestova, T.V., Hellen, C.U., 2003. Eukaryotic initiation factors 4G and 4A mediate conformational changes downstream of the initiation codon of the encephalomyocarditis virus internal ribosomal entry site. Mol. Cell. Biol. 23, 687-698.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 687-698
    • Kolupaeva, V.G.1    Lomakin, I.B.2    Pestova, T.V.3    Hellen, C.U.4
  • 71
    • 0034731347 scopus 로고    scopus 로고
    • Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1
    • Korneeva, N.L., Lamphear, B.J., Hennigan, F.L., Rhoads, R.E., 2000. Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J. Biol. Chem. 275, 41369-41376.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41369-41376
    • Korneeva, N.L.1    Lamphear, B.J.2    Hennigan, F.L.3    Rhoads, R.E.4
  • 72
    • 0023201040 scopus 로고
    • Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p220
    • Krausslich, H.G., Nicklin, M.J., Toyoda, H., Etchison, D., Wimmer, E., 1987. Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p220. J. Virol. 61, 2711-2718.
    • (1987) J. Virol. , vol.61 , pp. 2711-2718
    • Krausslich, H.G.1    Nicklin, M.J.2    Toyoda, H.3    Etchison, D.4    Wimmer, E.5
  • 73
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear, B.J., Kirchweger, R., Skern, T., Rhoads, R.E., 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J. Biol. Chem. 270, 21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 74
    • 0027182923 scopus 로고
    • Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus
    • Lamphear, B.J., Yan, R., Yang, F., Waters, D., Liebig, H.D., Klump, H., Kuechler, E., Skern, T., Rhoads, R.E., 1993. Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus. J. Biol. Chem. 268, 19200-19203.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19200-19203
    • Lamphear, B.J.1    Yan, R.2    Yang, F.3    Waters, D.4    Liebig, H.D.5    Klump, H.6    Kuechler, E.7    Skern, T.8    Rhoads, R.E.9
  • 75
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • Le, H., Tanguay, R.L., Balasta, M.L., Wei, C.C., Browning, K.S., Metz, A.M., Goss, D.J., Gallie, D.R., 1997. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J. Biol. Chem. 272, 16247-16255.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 76
    • 0015152589 scopus 로고
    • Regulation of protein synthesis in HeLa cells. 3. Inhibition during poliovirus infection
    • Leibowitz, R., Penman, S., 1971. Regulation of protein synthesis in HeLa cells. 3. Inhibition during poliovirus infection. J. Virol. 8, 661-668.
    • (1971) J. Virol. , vol.8 , pp. 661-668
    • Leibowitz, R.1    Penman, S.2
  • 77
    • 0031017473 scopus 로고    scopus 로고
    • DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death
    • Levy-Strumpf, N., Deiss, L.P., Berissi, H., Kimchi, A., 1997. DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death. Mol. Cell. Biol. 17, 1615-1625.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1615-1625
    • Levy-Strumpf, N.1    Deiss, L.P.2    Berissi, H.3    Kimchi, A.4
  • 78
    • 0035800819 scopus 로고    scopus 로고
    • Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo
    • Li, W., Belsham, G.J., Proud, C.G., 2001. Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo. J. Biol. Chem. 276, 29111-29115.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29111-29115
    • Li, W.1    Belsham, G.J.2    Proud, C.G.3
  • 79
    • 0037125190 scopus 로고    scopus 로고
    • A thermosensitive mutant of HRV2 2A proteinase: Evidence for direct cleavage of eIF4GI and eIF4GII
    • Liebig, H.D., Seipelt, J., Vassilieva, E., Gradi, A., Kuechler, E., 2002. A thermosensitive mutant of HRV2 2A proteinase: evidence for direct cleavage of eIF4GI and eIF4GII. FEBS Lett. 523, 53-57.
    • (2002) FEBS Lett. , vol.523 , pp. 53-57
    • Liebig, H.D.1    Seipelt, J.2    Vassilieva, E.3    Gradi, A.4    Kuechler, E.5
  • 82
    • 0027185479 scopus 로고
    • Persistent infection of human erythroblastoid cells by poliovirus
    • Lloyd, R.E., Bovee, M., 1993. Persistent infection of human erythroblastoid cells by poliovirus. Virology 194, 200-209.
    • (1993) Virology , vol.194 , pp. 200-209
    • Lloyd, R.E.1    Bovee, M.2
  • 83
    • 0023774517 scopus 로고
    • Relationship of p220 cleavage during picornavirus infection to 2A proteinase sequencing
    • Lloyd, R.E., Grubman, M.J., Ehrenfeld, E., 1988. Relationship of p220 cleavage during picornavirus infection to 2A proteinase sequencing. J. Virol. 62, 4216-4223.
    • (1988) J. Virol. , vol.62 , pp. 4216-4223
    • Lloyd, R.E.1    Grubman, M.J.2    Ehrenfeld, E.3
  • 84
    • 0022647104 scopus 로고
    • Cleavage of the cap binding protein complex polypeptide p220 is not effected by the second poliovirus protease 2A
    • Lloyd, R.E., Toyoda, H., Etchison, D., Wimmer, E., Ehrenfeld, E., 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
  • 85
    • 0033852315 scopus 로고    scopus 로고
    • Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation
    • Lomakin, I.B., Hellen, C.U., Pestova, T.V., 2000. Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation. Mol. Cell. Biol. 20, 6019-6029.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6019-6029
    • Lomakin, I.B.1    Hellen, C.U.2    Pestova, T.V.3
  • 86
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader, S., Lee, H., Pause, A., Sonenberg, N., 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15, 4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 87
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., Gingras, A.C., Sonenberg, N., Burley, S.K., 1997. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89, 951-961.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 88
  • 89
    • 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., Lloyd, R.E., 2000. Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis. Cell Death Differ. 7, 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
  • 90
    • 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., Lloyd, R.E., 1998. Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells. Mol. Cell. Biol. 18, 7565-7574.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7565-7574
    • Marissen, W.E.1    Lloyd, R.E.2
  • 92
    • 0035008608 scopus 로고    scopus 로고
    • Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap
    • McKendrick, L., Thompson, E., Ferreira, J., Morley, S.J., Lewis, J.D., 2001. Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap. Mol. Cell. Biol. 21, 3632-3641.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3632-3641
    • McKendrick, L.1    Thompson, E.2    Ferreira, J.3    Morley, S.J.4    Lewis, J.D.5
  • 93
    • 0034977831 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation
    • Michel, Y.M., Borman, A.M., Paulous, S., Kean, K.M., 2001. Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation. Mol. Cell. Biol. 21, 4097-4109.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4097-4109
    • Michel, Y.M.1    Borman, A.M.2    Paulous, S.3    Kean, K.M.4
  • 94
    • 0034644749 scopus 로고    scopus 로고
    • Cap-Poly(A) synergy in mammalian cell-free extracts. Investigation of the requirements for poly(A)-mediated stimulation of translation initiation
    • Michel, Y.M., Poncet, D., Piron, M., Kean, K.M., Borman, A.M., 2000. Cap-Poly(A) synergy in mammalian cell-free extracts. Investigation of the requirements for poly(A)-mediated stimulation of translation initiation. J. Biol. Chem. 275, 32268-32276.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32268-32276
    • Michel, Y.M.1    Poncet, D.2    Piron, M.3    Kean, K.M.4    Borman, A.M.5
  • 95
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • Morino, S., Imataka, H., Svitkin, Y.V., Pestova, T.V., Sonenberg, N., 2000. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol. Cell. Biol. 20, 468-477.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 96
    • 0030610901 scopus 로고    scopus 로고
    • eIF4G: Translation's mystery factor begins to yield its secrets
    • Morley, S.J., Curtis, P.S., Pain, V.M., 1997. eIF4G: translation's mystery factor begins to yield its secrets. RNA 3, 1085-1104.
    • (1997) RNA , vol.3 , pp. 1085-1104
    • Morley, S.J.1    Curtis, P.S.2    Pain, V.M.3
  • 97
    • 0032582744 scopus 로고    scopus 로고
    • Cleavage of translation initiation factor 4G (eIF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase
    • Morley, S.J., McKendrick, L., Bushell, M., 1998. Cleavage of translation initiation factor 4G (eIF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase. FEBS Lett. 438, 41-48.
    • (1998) FEBS Lett. , vol.438 , pp. 41-48
    • Morley, S.J.1    McKendrick, L.2    Bushell, M.3
  • 98
    • 0032777549 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally
    • Neff, C.L., Sachs, A.B., 1999. Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally. Mol. Cell. Biol. 19, 5557-5564.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5557-5564
    • Neff, C.L.1    Sachs, A.B.2
  • 99
    • 0037423208 scopus 로고    scopus 로고
    • Distinct regulation of internal ribosome entry site-mediated translation following cellular stress is mediated by apoptotic fragments of eIF4G translation initiation factor family members eIF4GI and p97/DAP5/NAT1
    • Nevins, T.A., Harder, Z.M., Korneluk, R.G., Holcik, M., 2003. Distinct regulation of internal ribosome entry site-mediated translation following cellular stress is mediated by apoptotic fragments of eIF4G translation initiation factor family members eIF4GI and p97/DAP5/NAT1. J. Biol. Chem. 278, 3572-3579.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3572-3579
    • Nevins, T.A.1    Harder, Z.M.2    Korneluk, R.G.3    Holcik, M.4
  • 100
    • 0031054338 scopus 로고    scopus 로고
    • The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate
    • Ohlmann, T., Pain, V.M., Wood, W., Rau, M., Morley, S.J., 1997. The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E 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
  • 101
    • 0036308653 scopus 로고    scopus 로고
    • In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system
    • Ohlmann, T., Prevot, D., Decimo, D., Roux, F., Garin, J., Morley, S.J., Darlix, J.L., 2002. In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system. J. Mol. Biol. 318, 9-20.
    • (2002) J. Mol. Biol. , vol.318 , pp. 9-20
    • Ohlmann, T.1    Prevot, D.2    Decimo, D.3    Roux, F.4    Garin, J.5    Morley, S.J.6    Darlix, J.L.7
  • 102
    • 0029036269 scopus 로고
    • Effect of cleavage of the p220 subunit of eukaryotic translation initiation factor eIF-4F on protein synthesis in vitro
    • Ohlmann, T., Rau, M., Morley, S., Pain, V.M., 1995a. Effect of cleavage of the p220 subunit of eukaryotic translation initiation factor eIF-4F on protein synthesis in vitro. Biochem. Soc. Trans. 23, 315S.
    • (1995) Biochem. Soc. Trans. , vol.23
    • Ohlmann, T.1    Rau, M.2    Morley, S.3    Pain, V.M.4
  • 103
    • 0028901902 scopus 로고
    • Proteolytic cleavage of initiation factor eIF-4 gamma in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs
    • Ohlmann, T., Rau, M., Morley, S. J., Pain, V.M., 1995b. Proteolytic cleavage of initiation factor eIF-4 gamma in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs. Nucleic Acids Res. 23, 334-340.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 334-340
    • Ohlmann, T.1    Rau, M.2    Morley, S.J.3    Pain, V.M.4
  • 104
    • 0029976319 scopus 로고    scopus 로고
    • The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E
    • Ohlmann, T., Rau, M., Pain, V.M., Morley, S.J., 1996. The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E. EMBO J. 15, 1371-1382.
    • (1996) EMBO J. , vol.15 , pp. 1371-1382
    • Ohlmann, T.1    Rau, M.2    Pain, V.M.3    Morley, S.J.4
  • 105
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause, A., Methot, N., Sonenberg, N., 1993. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol. Cell. Biol. 13, 6789-6798.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 106
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation
    • Pause, A., Methot, N., Svitkin, Y., Merrick, W.C., Sonenberg, N., 1994. Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation. EMBO J. 13, 1205-1215.
    • (1994) EMBO J. , vol.13 , pp. 1205-1215
    • Pause, A.1    Methot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 107
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A., Sonenberg, N., 1992. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11, 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 108
    • 0026750639 scopus 로고
    • Lack of direct correlation between p220 cleavage and the shut-off of host translation after poliovirus infection
    • Perez, L., Carrasco, L., 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
  • 109
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova, T.V., Hellen, C.U., Shatsky, I.N., 1996a. Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol. Cell. Biol. 16, 6859-6869.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 111
    • 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., Shatsky, I.N., Fletcher, S.P., Jackson, R.J., Hellen, C.U., 1998. 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, 67-83.
    • (1998) Genes Dev. , vol.12 , pp. 67-83
    • Pestova, T.V.1    Shatsky, I.N.2    Fletcher, S.P.3    Jackson, R.J.4    Hellen, C.U.5
  • 112
    • 0029968997 scopus 로고    scopus 로고
    • Functional dissection of eukaryotic initiation factor 4F: The 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes
    • Pestova, T.V., Shatsky, I.N., Hellen, C.U., 1996b. Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes. Mol. Cell. Biol. 16, 6870-6878.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6870-6878
    • Pestova, T.V.1    Shatsky, I.N.2    Hellen, C.U.3
  • 113
    • 0032190508 scopus 로고    scopus 로고
    • Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
    • Piron, M., Vende, P., Cohen, J., Poncet, D., 1998. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. EMBO J. 17, 5811-5821.
    • (1998) EMBO J. , vol.17 , pp. 5811-5821
    • Piron, M.1    Vende, P.2    Cohen, J.3    Poncet, D.4
  • 114
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast
    • Preiss, T., Hentze, M.W., 1998. Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature 392, 516-520.
    • (1998) Nature , vol.392 , pp. 516-520
    • Preiss, T.1    Hentze, M.W.2
  • 115
    • 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., Sonenberg, N., 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. 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
  • 116
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • Rau, M., Ohlmann, T., Morley, S.J., Pain, V.M., 1996. A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate. J. Biol. Chem. 271, 8983-8990.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8983-8990
    • Rau, M.1    Ohlmann, T.2    Morley, S.J.3    Pain, V.M.4
  • 117
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught, B., Gingras, A.C., Gygi, S.P., Imataka, H., Morino, S., Gradi, A., Aebersold, R., Sonenberg, N., 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19, 434-444.
    • (2000) EMBO J. , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygi, S.P.3    Imataka, H.4    Morino, S.5    Gradi, A.6    Aebersold, R.7    Sonenberg, N.8
  • 120
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., Edery, I., Meerovitch, K., Dever, T.E., Merrick, W.C., Sonenberg, N., 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell. Biol. 10, 1134-1144.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 121
    • 0025177657 scopus 로고
    • The poly(A)-binding protein is required for translation initiation and poly(A) tail shortening
    • Sachs, A., Davis, R., 1990. The poly(A)-binding protein is required for translation initiation and poly(A) tail shortening. Mol. Biol. Rep. 14, 73.
    • (1990) Mol. Biol. Rep. , vol.14 , pp. 73
    • Sachs, A.1    Davis, R.2
  • 122
    • 0024416021 scopus 로고
    • The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation
    • Sachs, A.B., Davis, R.W., 1989. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell 58, 857-867.
    • (1989) Cell , vol.58 , pp. 857-867
    • Sachs, A.B.1    Davis, R.W.2
  • 123
    • 0034100762 scopus 로고    scopus 로고
    • Eukaryotic translation initiation: There are (at least) two sides to every story
    • Sachs, A.B., Varani, G., 2000. Eukaryotic translation initiation: there are (at least) two sides to every story. Nat. Struct. Biol. 7, 356-361.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 356-361
    • Sachs, A.B.1    Varani, G.2
  • 124
    • 0037048650 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4GI is a poor substrate for HIV-1 proteinase
    • Schlick, P., Skern, T., 2002. Eukaryotic initiation factor 4GI is a poor substrate for HIV-1 proteinase. FEBS Lett. 529, 337-340.
    • (2002) FEBS Lett. , vol.529 , pp. 337-340
    • Schlick, P.1    Skern, T.2
  • 125
    • 0018143765 scopus 로고
    • A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA
    • Sonenberg, N., Morgan, M.A., Merrick, W.C., Shatkin, A.J., 1978. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA. Proc. Natl. Acad. Sci. USA 75, 4843-4847.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4843-4847
    • Sonenberg, N.1    Morgan, M.A.2    Merrick, W.C.3    Shatkin, A.J.4
  • 126
  • 127
    • 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., Gradi, A., Imataka, H., Morino, S., Sonenberg, N., 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
  • 128
    • 0019877161 scopus 로고
    • Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells
    • Tahara, S.M., Morgan, M.A., Shatkin, A.J., 1981. Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 256, 7691-7694.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7691-7694
    • Tahara, S.M.1    Morgan, M.A.2    Shatkin, A.J.3
  • 129
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
    • Tarun Jr., S.Z., Sachs, A.B., 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15, 7168-7177.
    • (1996) EMBO J. , vol.15 , pp. 7168-7177
    • Tarun S.Z., Jr.1    Sachs, A.B.2
  • 130
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun Jr., S.Z., Sachs, A.B., 1995. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9, 2997-3007.
    • (1995) Genes Dev. , vol.9 , pp. 2997-3007
    • Tarun S.Z., Jr.1    Sachs, A.B.2
  • 131
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail- Dependent translation
    • Tarun Jr., S.Z., Wells, S.E., Deardorff, J.A., Sachs, A.B., 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail- dependent translation. Proc. Natl. Acad. Sci. USA 94, 9046-9051.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9046-9051
    • Tarun S.Z., Jr.1    Wells, S.E.2    Deardorff, J.A.3    Sachs, A.B.4
  • 133
    • 0033790503 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae
    • Tucker, M., Parker, R., 2000. Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae. Annu. Rev. Biochem. 69, 571-595.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 571-595
    • Tucker, M.1    Parker, R.2
  • 134
    • 0037184899 scopus 로고    scopus 로고
    • A Novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation
    • Uchida, N., Hoshino, S., Imataka, H., Sonenberg, N., Katada, T., 2002. A Novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation. J. Biol. Chem. 277, 50286-50292.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 135
    • 0035818541 scopus 로고    scopus 로고
    • HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation
    • Ventoso, I., Blanco, R., Perales, C., Carrasco, L., 2001. HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation. Proc. Natl. Acad. Sci. USA 23, 23.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.23 , pp. 23
    • Ventoso, I.1    Blanco, R.2    Perales, C.3    Carrasco, L.4
  • 136
    • 0034663782 scopus 로고    scopus 로고
    • The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex
    • Vilela, C., Velasco, C., Ptushkina, M., McCarthy, J.E., 2000. The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex. EMBO J. 19, 4372-4382.
    • (2000) EMBO J. , vol.19 , pp. 4372-4382
    • Vilela, C.1    Velasco, C.2    Ptushkina, M.3    McCarthy, J.E.4
  • 137
    • 0034730734 scopus 로고    scopus 로고
    • Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5′-Cap by domains of eIF4G
    • von Der Haar, T., Ball, P.D., McCarthy, J.E., 2000. Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5′-Cap by domains of eIF4G. J. Biol. Chem. 275, 30551-30555.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30551-30555
    • von Der Haar, T.1    Ball, P.D.2    McCarthy, J.E.3
  • 138
    • 0032539532 scopus 로고    scopus 로고
    • Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues
    • Wei, C.C., Balasta, M.L., Ren, J., Goss, D.J., 1998. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues. Biochemistry 37, 1910-1916.
    • (1998) Biochemistry , vol.37 , pp. 1910-1916
    • Wei, C.C.1    Balasta, M.L.2    Ren, J.3    Goss, D.J.4
  • 139
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells, S.E., Hillner, P.E., Vale, R.D., Sachs, A.B., 1998. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2, 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
  • 140
    • 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., Sarnow, P., 2000. Initiation of protein synthesis from the A site of the ribosome. Cell 102, 511-520.
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.3    Sarnow, P.4
  • 142
    • 0025630440 scopus 로고
    • Eukaryotic initiation factor 3 is required for poliovirus 2A protease-induced cleavage of the p220 component of eukaryotic initiation factor 4F
    • Wyckoff, E.E., Hershey, J.W., Ehrenfeld, E., 1990. Eukaryotic initiation factor 3 is required for poliovirus 2A protease-induced cleavage of the p220 component of eukaryotic initiation factor 4F. Proc. Natl. Acad. Sci. USA 87, 9529-9533.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9529-9533
    • Wyckoff, E.E.1    Hershey, J.W.2    Ehrenfeld, E.3
  • 143
    • 0026549161 scopus 로고
    • Relationship of eukaryotic initiation factor 3 to poliovirus-induced p220 cleavage activity
    • Wyckoff, E.E., Lloyd, R.E., Ehrenfeld, E., 1992. Relationship of eukaryotic initiation factor 3 to poliovirus-induced p220 cleavage activity. J. Virol. 66, 2943-2951.
    • (1992) J. Virol. , vol.66 , pp. 2943-2951
    • Wyckoff, E.E.1    Lloyd, R.E.2    Ehrenfeld, E.3
  • 144
    • 0031048641 scopus 로고    scopus 로고
    • A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme
    • Yamanaka, S., Poksay, K.S., Arnold, K.S., Innerarity, T.L., 1997. A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme. Genes Dev. 11, 321-333.
    • (1997) Genes Dev. , vol.11 , pp. 321-333
    • Yamanaka, S.1    Poksay, K.S.2    Arnold, K.S.3    Innerarity, T.L.4
  • 145
    • 0028916284 scopus 로고
    • Human protein synthesis initiation factor eIF-4 gamma is encoded by a single gene (EIF4G) that maps to chromosome 3q27-qter
    • Yan, R., Rhoads, R.E., 1995. Human protein synthesis initiation factor eIF-4 gamma is encoded by a single gene (EIF4G) that maps to chromosome 3q27-qter. Genomics 26, 394-398.
    • (1995) Genomics , vol.26 , pp. 394-398
    • Yan, R.1    Rhoads, R.E.2
  • 146
    • 0026463868 scopus 로고
    • Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma
    • Yan, R., Rychlik, W., Etchison, D., Rhoads, R.E., 1992. Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma. J. Biol. Chem. 267, 23226-23231.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23226-23231
    • Yan, R.1    Rychlik, W.2    Etchison, D.3    Rhoads, R.E.4
  • 147
    • 0028284411 scopus 로고
    • Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos
    • Zapata, J.M., Martinez, M.A., Sierra, J.M., 1994. Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos. J. Biol. Chem. 269, 18047-18052.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18047-18052
    • Zapata, J.M.1    Martinez, M.A.2    Sierra, J.M.3
  • 148
    • 0028099721 scopus 로고
    • A late adenovirus factor induces eIF-4E dephosphorylation and inhibition of cell protein synthesis
    • Zhang, Y., Feigenblum, D., Schneider, R.J., 1994. A late adenovirus factor induces eIF-4E dephosphorylation and inhibition of cell protein synthesis. J. Virol. 68, 7040-7050.
    • (1994) J. Virol. , vol.68 , pp. 7040-7050
    • Zhang, Y.1    Feigenblum, D.2    Schneider, R.J.3
  • 149
    • 0028786192 scopus 로고
    • Picornavirus 2A proteinase-mediated stimulation of internal initiation of translation is dependent on enzymatic activity and the cleavage products of cellular proteins
    • Ziegler, E., Borman, A.M., Deliat, F.G., Liebig, H.D., Jugovic, D., Kean, K.M., Skern, T., Kuechler, E., 1995a. Picornavirus 2A proteinase-mediated stimulation of internal initiation of translation is dependent on enzymatic activity and the cleavage products of cellular proteins. Virology 213, 549-557.
    • (1995) Virology , vol.213 , pp. 549-557
    • Ziegler, E.1    Borman, A.M.2    Deliat, F.G.3    Liebig, H.D.4    Jugovic, D.5    Kean, K.M.6    Skern, T.7    Kuechler, E.8
  • 150
    • 0029008576 scopus 로고
    • Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin
    • Ziegler, E., Borman, A.M., Kirchweger, R., Skern, T., Kean, K.M., 1995b. Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin. J. Virol. 69, 3465-3474.
    • (1995) J. Virol. , vol.69 , pp. 3465-3474
    • Ziegler, E.1    Borman, A.M.2    Kirchweger, R.3    Skern, T.4    Kean, K.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.