메뉴 건너뛰기




Volumn 11, Issue 10, 2004, Pages 992-1000

eIF4G is required for the pioneer round of translation in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

CAP BINDING PROTEIN; INITIATION FACTOR 4G; MESSENGER RNA; PROTEIN CBP20; PROTEIN CBP80; PROTEINASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 4744347153     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb824     Document Type: Article
Times cited : (80)

References (48)
  • 1
    • 0742323558 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Splicing, translation and mRNP dynamics
    • Maquat, L.E. Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics. Nat. Rev. Mol. Cell Biol. 5, 89-99 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 89-99
    • Maquat, L.E.1
  • 2
    • 1842689543 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: A comparative analysis of different species
    • Maquat, L.E. Nonsense-mediated mRNA decay: a comparative analysis of different species. Curr. Genomics 5, 175-190 (2004).
    • (2004) Curr. Genomics , vol.5 , pp. 175-190
    • Maquat, L.E.1
  • 3
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: When nonsense affects RNA abundance
    • Nagy, E. & Maquat, L.E. A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem. Sci. 23, 198-199 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 4
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H., Izaurralde, E., Maquat, L.E. & Moore, M.J. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19, 6860-6869 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 5
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • Le Hir, H., Moore, M.J. & Maquat, L.E. Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev. 14, 1098-1108 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 6
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • Le Hir, H., Gatfield, D., Izaurralde, E. & Moore, M.J. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J. 20, 4987-4997 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 7
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V.N., Kataoka, N. & Dreyfuss, G. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293, 1832-1836 (2001).
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 8
    • 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. 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).
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 9
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • Lejeune, F., Ishigaki, Y., Li, X. & Maquat, L.E. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling. EMBO J. 21, 3536-3545 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 10
    • 0028125262 scopus 로고
    • Mammalian nonsense codons can be cis effectors of nuclear mRNA half-life
    • Belgrader, P., Cheng, J., Zhou, X., Stephenson, L.S. & Maquat, L.E. Mammalian nonsense codons can be cis effectors of nuclear mRNA half-life. Mol. Cell. Biol. 14, 8219-8228 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8219-8228
    • Belgrader, P.1    Cheng, J.2    Zhou, X.3    Stephenson, L.S.4    Maquat, L.E.5
  • 11
    • 0027536976 scopus 로고
    • Nonsense codons can reduce the abundance of nuclear mRNA without affecting the abundance of pre-mRNA or the half-life of cytoplasmic mRNA
    • Cheng, J. & Maquat, L.E. Nonsense codons can reduce the abundance of nuclear mRNA without affecting the abundance of pre-mRNA or the half-life of cytoplasmic mRNA. Mol. Cell. Biol. 13, 1892-1902 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1892-1902
    • Cheng, J.1    Maquat, L.E.2
  • 12
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune, F., Li, X. & Maquat, L.E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12, 675-687 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 13
    • 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., Rerreira, J., Morley, S.J. & Lewis, J.D. 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).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3632-3641
    • McKendrick, L.1    Thompson, E.2    Rerreira, J.3    Morley, S.J.4    Lewis, J.D.5
  • 14
    • 1842682946 scopus 로고    scopus 로고
    • The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
    • Chiu, S.Y., Lejeune, F., Ranganathan, A.C. & Maquat, L.E. The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex. Genes Dev. 18, 745-754 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 745-754
    • Chiu, S.Y.1    Lejeune, F.2    Ranganathan, A.C.3    Maquat, L.E.4
  • 15
    • 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. Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons. Mol. Cell. Biol. 22, 4499-4511 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4499-4511
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 16
    • 1842794166 scopus 로고    scopus 로고
    • Expression of fragments of translation initiation factor eIF4GI reveals a nuclear localisation signal within the N-terminal apoptotic cleavage fragment N-FAG
    • Coldwell, M.J., Hashemzadeh-Bonehi, L., Hinton, T.M., Morley, S.J. & Pain, V.M. Expression of fragments of translation initiation factor eIF4GI reveals a nuclear localisation signal within the N-terminal apoptotic cleavage fragment N-FAG. J. Cell Sci. 117, 2545-2555 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 2545-2555
    • Coldwell, M.J.1    Hashemzadeh-Bonehi, L.2    Hinton, T.M.3    Morley, S.J.4    Pain, V.M.5
  • 17
    • 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. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68, 913-963 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 18
    • 0030610901 scopus 로고    scopus 로고
    • eIF4G: Translation's mystery factor begins to yield its secrets
    • Morley, S.J., Curtis, P.S. & Pain, V.M. eIF4G: translation's mystery factor begins to yield its secrets. RNA 3, 1085-1104 (1997).
    • (1997) RNA , vol.3 , pp. 1085-1104
    • Morley, S.J.1    Curtis, P.S.2    Pain, V.M.3
  • 19
    • 0032858414 scopus 로고    scopus 로고
    • From factors to mechanisms: Translation and translational control in eukaryotes
    • Preiss, T. & Hentze, M.W. From factors to mechanisms: translation and translational control in eukaryotes. Curr. Opin. Genet. Dev. 9, 515-521 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 515-521
    • Preiss, T.1    Hentze, M.W.2
  • 20
    • 2442679170 scopus 로고    scopus 로고
    • Selective modification of eukaryotic initiation factor 4R (eIF4F) at the onset of cell differentiation: Recruitment of eIF4GII and long-lasting phosphorylation of eIF4E
    • Caron, S., Charon, M., Cramer, E., Sonenberg, N. & Dusanter-Rourt, I. Selective modification of eukaryotic initiation factor 4R (eIF4F) at the onset of cell differentiation: recruitment of eIF4GII and long-lasting phosphorylation of eIF4E. Mol. Cell. Biol. 24, 4920-4928 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4920-4928
    • Caron, S.1    Charon, M.2    Cramer, E.3    Sonenberg, N.4    Dusanter-Rourt, I.5
  • 21
    • 0032696240 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4AIII (eIF4AIII) is functionally distinct from eIF4AI and eIF4AII
    • Li, Q. et al. Eukaryotic translation initiation factor 4AIII (eIF4AIII) is functionally distinct from eIF4AI and eIF4AII. Mol. Cell. Biol. 19, 7336-7346 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7336-7346
    • Li, Q.1
  • 22
    • 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. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol. 17, 6940-6947 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 23
    • 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, G.G. Eukaryotic initiation factors 4A(eIF4A) and 4G(eIF4G) mutually interact in a 1:1 ratio in vivo. J. Biol. Chem. 276, 29111-29115 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29111-29115
    • Li, W.1    Belsham, G.J.2    Proud, G.G.3
  • 24
    • 1542361776 scopus 로고    scopus 로고
    • eIF4A3 is a novel component of the exon junction complex
    • Chan, C.C. et al. eIF4A3 is a novel component of the exon junction complex. RNA 10, 200-209 (2004).
    • (2004) RNA , vol.10 , pp. 200-209
    • Chan, C.C.1
  • 25
    • 1642570265 scopus 로고    scopus 로고
    • A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay
    • Ferraiuolo, M.A. et al. A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay. Proc. Natl. Acad. Sci. USA 101, 4118-4123 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4118-4123
    • Ferraiuolo, M.A.1
  • 26
    • 1442354190 scopus 로고    scopus 로고
    • An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay
    • Palacios, I.M., Gatfield, D., St Johnston, D. & Izaurralde, E. An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay. Nature 427, 753-757 (2004).
    • (2004) Nature , vol.427 , pp. 753-757
    • Palacios, I.M.1    Gatfield, D.2    St. Johnston, D.3    Izaurralde, E.4
  • 27
    • 1842577707 scopus 로고    scopus 로고
    • eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay
    • Shibuya, T., Tange, T.O., Sonenberg, N. & Moore, MJ. eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay. Nat. Struct. Mol. Biol. 11, 346-351 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 346-351
    • Shibuya, T.1    Tange, T.O.2    Sonenberg, N.3    Moore, M.J.4
  • 28
    • 0033828440 scopus 로고    scopus 로고
    • Eukaryote-specific domains in translation initiation factors: Implications for translation regulation and evolution of the translation system
    • Aravind, L. & Koonin, E.V. Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system. Genome Res. 10, 1172-1184 (2000).
    • (2000) Genome Res. , vol.10 , pp. 1172-1184
    • Aravind, L.1    Koonin, E.V.2
  • 29
    • 0034284394 scopus 로고    scopus 로고
    • Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay
    • Ponting, C.P. Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay. Trends Biochem. Sci. 25, 423-426 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 423-426
    • Ponting, C.P.1
  • 31
    • 0242661870 scopus 로고    scopus 로고
    • The eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases
    • Alvarez, E., Menendez-Arias, L. & Carrasco, L. The eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases. J. Virol. 77, 12392-12400 (2003).
    • (2003) J. Virol. , vol.77 , pp. 12392-12400
    • Alvarez, E.1    Menendez-Arias, L.2    Carrasco, L.3
  • 32
    • 0027969151 scopus 로고
    • A nuclear cap binding protein complex involved in pre-mRNA splicing
    • Izaurralde, E. et al. A nuclear cap binding protein complex involved in pre-mRNA splicing. Cell 78, 657-668 (1994).
    • (1994) Cell , vol.78 , pp. 657-668
    • Izaurralde, E.1
  • 33
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., Lee, H., Pause, A. & Sonenberg, N. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15, 4990-4997 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 34
    • 0033636895 scopus 로고    scopus 로고
    • The yeast nuclear cap binding complex can interact with translation factor eIF 4G and mediate translation initiation
    • Fortes, P. et al. The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation. Mol. Cell 6, 191-196 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 191-196
    • Fortes, P.1
  • 35
    • 0036096544 scopus 로고    scopus 로고
    • Paip1 interacts with poly(A) binding protein through two independent binding motifs
    • Roy, G. et al. Paip1 interacts with poly(A) binding protein through two independent binding motifs. Mol. Cell. Biol. 22, 3769-3782 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3769-3782
    • Roy, G.1
  • 36
    • 0038813732 scopus 로고    scopus 로고
    • The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast
    • Baron-Benhamou, J., Fortes, P., Inada, T., Preiss, T. & Hentze, M.W. The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast. RNA 9, 654-662 (2003).
    • (2003) RNA , vol.9 , pp. 654-662
    • Baron-Benhamou, J.1    Fortes, P.2    Inada, T.3    Preiss, T.4    Hentze, M.W.5
  • 37
    • 0025823443 scopus 로고
    • Modulation of firefly luciferase stability and impact on studies of gene regulation
    • Thompson, J.F., Hayes, L.S. & Lloyd, D.B. Modulation of firefly luciferase stability and impact on studies of gene regulation. Gene 103, 171-177 (1991).
    • (1991) Gene , vol.103 , pp. 171-177
    • Thompson, J.F.1    Hayes, L.S.2    Lloyd, D.B.3
  • 38
    • 0031870169 scopus 로고    scopus 로고
    • Intron function in the nonsense-mediated decay of β-globin mRNA: Indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm
    • Zhang, J., Sun, X., Qian, Y. & Maquat, L.E. Intron function in the nonsense-mediated decay of β-globin mRNA: indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm. RNA 4, 801-815 (1998).
    • (1998) RNA , vol.4 , pp. 801-815
    • Zhang, J.1    Sun, X.2    Qian, Y.3    Maquat, L.E.4
  • 39
    • 0031896755 scopus 로고    scopus 로고
    • Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likely to be nonsense codon-mediated decay of cytoplasmic mRNA
    • Moriarty, P.M., Reddy, C.C. & Maquat, L.E. Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likely to be nonsense codon-mediated decay of cytoplasmic mRNA. Mol. Cell. Biol. 18, 2932-2939 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2932-2939
    • Moriarty, P.M.1    Reddy, C.C.2    Maquat, L.E.3
  • 40
    • 0034852936 scopus 로고    scopus 로고
    • Crystal structure of the human nuclear cap binding complex
    • Mazza, C., Ohno, M., Segref, A., Mattaj, I.W. & Cusack, S. Crystal structure of the human nuclear cap binding complex. Mol. Cell 8, 383-396 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 383-396
    • Mazza, C.1    Ohno, M.2    Segref, A.3    Mattaj, I.W.4    Cusack, S.5
  • 41
    • 0034068905 scopus 로고    scopus 로고
    • The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation
    • Das, B., Quo, Z., Russo, P., Chartrand, P. & Sherman, F. The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation. Mol. Cell. Biol. 20, 2827-2838 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2827-2838
    • Das, B.1    Quo, Z.2    Russo, P.3    Chartrand, P.4    Sherman, F.5
  • 42
    • 0037304372 scopus 로고    scopus 로고
    • Nonsense-containing mRNAs that accumulate in the absence of a functional nonsense-mediated mRNA decay pathway are destabilized rapidly upon its restitution
    • Maderazo, A.B., Belk, J.P., He, F. & Jacobson, A. Nonsense-containing mRNAs that accumulate in the absence of a functional nonsense-mediated mRNA decay pathway are destabilized rapidly upon its restitution. Mol. Cell. Biol. 23, 842-851 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 842-851
    • Maderazo, A.B.1    Belk, J.P.2    He, F.3    Jacobson, A.4
  • 43
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases
    • Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. & Tollervey, D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases. Cell 91, 457-466 (1997).
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 44
    • 0019792466 scopus 로고
    • Biosynthesis of the major urinary proteins in mouse liver: A biochemical genetic study
    • Berger, F.G. & Szoka, P. Biosynthesis of the major urinary proteins in mouse liver: a biochemical genetic study. Biochem. Genet. 19, 1261-1273 (1981).
    • (1981) Biochem. Genet. , vol.19 , pp. 1261-1273
    • Berger, F.G.1    Szoka, P.2
  • 45
    • 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. 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).
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 46
    • 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. 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).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 47
    • 1542305510 scopus 로고    scopus 로고
    • The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro
    • Fraser, C.S. et al. The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro. J. Biol. Chem. 279, 8946-8956 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 8946-8956
    • Fraser, C.S.1
  • 48
    • 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. Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis. Cell Death Differ. 7, 1234-1243 (2000).
    • (2000) Cell Death Differ. , vol.7 , pp. 1234-1243
    • Marissen, W.E.1    Gradi, A.2    Sonenberg, N.3    Lloyd, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.