메뉴 건너뛰기




Volumn 7, Issue 5, 2000, Pages 356-361

Eukaryotic translation initiation: There are (at least) two sides to every story

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4E;

EID: 0034100762     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/75120     Document Type: Review
Times cited : (110)

References (50)
  • 1
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • (eds. Hershey, J.W.B., Matthews, M. & Sonenberg, N.) Cold Spring Harbor Press, Cold Spring Harbor
    • Merrick, W.C. & Hershey, J.W.B. The pathway and mechanism of eukaryotic protein synthesis. In Translational Control (eds. Hershey, J.W.B., Matthews, M. & Sonenberg, N.) 31-69 (Cold Spring Harbor Press, Cold Spring Harbor; 1996).
    • (1996) Translational Control , pp. 31-69
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 2
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: Translation initiation in eucaryotes
    • Sachs, A.B., Sarnow, P. & Hentze, M.W. Starting at the beginning, middle, and end: translation initiation in eucaryotes. Cell 89, 831-838 (1997).
    • (1997) Cell , vol.89 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 3
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells, S.E., Hillner, P., Vale, R. & Sachs, A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2, 135-140 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.2    Vale, R.3    Sachs, A.B.4
  • 4
    • 0024356102 scopus 로고
    • Altered mRNA cap recognition activity of initiation factor 4E in the yeast cell cycle division mutant cdc33
    • Altmann, M. & Trachsel, H. Altered mRNA cap recognition activity of initiation factor 4E in the yeast cell cycle division mutant cdc33. Nuc. Acids Res. 17, 5923-5931 (1989).
    • (1989) Nuc. Acids Res. , vol.17 , pp. 5923-5931
    • Altmann, M.1    Trachsel, H.2
  • 5
    • 1842403614 scopus 로고    scopus 로고
    • Binding of elF4E to elF4G represses translation of uncapped mRNA
    • Tarun, S.Z. & Sachs, A.B. Binding of elF4E to elF4G represses translation of uncapped mRNA. Mol. Cell. Biol. 17, 6876-6886 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6876-6886
    • Tarun, S.Z.1    Sachs, A.B.2
  • 6
    • 0029949032 scopus 로고    scopus 로고
    • Analysis of the mRNA cap-binding ability of human eukaryotic initiation factor-4E by use of recombinant wild-type and mutant forms
    • Morino, S., et al. Analysis of the mRNA cap-binding ability of human eukaryotic initiation factor-4E by use of recombinant wild-type and mutant forms. Eur J. Biochem. 239, 597-601 (1996).
    • (1996) Eur J. Biochem. , vol.239 , pp. 597-601
    • Morino, S.1
  • 7
    • 0030832026 scopus 로고    scopus 로고
    • elF4G dramatically enhances the binding of elF4E to the mRNA 5′-cap structure
    • Haghighat, A. & Sonenberg, N. elF4G dramatically enhances the binding of elF4E to the mRNA 5′-cap structure. J. Biol. Chem. 272, 21677-21680 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 8
    • 0032541425 scopus 로고    scopus 로고
    • Cooperative modulation by elF4G of elF4E-binding to the mRNA 5′ cap in yeast involves a site partially shared by p20
    • Ptushkina, M., et al. Cooperative modulation by elF4G of elF4E-binding to the mRNA 5′ cap in yeast involves a site partially shared by p20. EMBO J. 17, 4798-808 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4798-4808
    • Ptushkina, M.1
  • 9
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (elF4G) recruits Mnk1 to phosphorylate elF4E
    • Pyronnet, S., et al. Human eukaryotic translation initiation factor 4G (elF4G) recruits Mnk1 to phosphorylate elF4E. EMBO J. 18, 270-279 (1999).
    • (1999) EMBO J. , vol.18 , pp. 270-279
    • Pyronnet, S.1
  • 10
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor elF-4E: Increased cap affinity of the phosphorylated form
    • Minich, W.B., Balasta, M.L., Goss, D.J. & Rhoads, R.E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor elF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91, 7668-7672 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 11
    • 0029791354 scopus 로고    scopus 로고
    • Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation
    • Feigenblum, D. & Schneider, R.J. Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation. Mol. Cell. Biol. 16, 5450-5457 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5450-5457
    • Feigenblum, D.1    Schneider, R.J.2
  • 12
    • 0030826444 scopus 로고    scopus 로고
    • Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein
    • Matsuo, H., et al. Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein. Nature Struct. Biol. 4, 717-724 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 717-724
    • Matsuo, H.1
  • 13
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of elF4G
    • Marcotrigiano, J., Gingras, A.C., Sonenberg, N. & Burley, S.K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of elF4G. Mol. Cell 3, 707-716 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 14
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (elF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., Gingras, A.C., Sonenberg, N. & Burley, S.K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (elF4E) bound to 7-methyl-GDP. Cell 89, 951-961 (1997).
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 15
    • 0029166687 scopus 로고
    • The translation initiation factor elF-4E binds to a common motif shared by the translation factor elF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., Lee, H., Pause, A. & Sonenberg, N. The translation initiation factor elF-4E binds to a common motif shared by the translation factor elF-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
  • 16
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor elF-4G
    • Tarun, S.Z. & Sachs, A.B. Association of the yeast poly(A) tail binding protein with translation initiation factor elF-4G. EMBO J. 15, 7168-7177 (1996).
    • (1996) EMBO J. , vol.15 , pp. 7168-7177
    • Tarun, S.Z.1    Sachs, A.B.2
  • 17
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (elF4E) binding site and the middle one-third of elF4GI 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. Eukaryotic translation initiation factor 4E (elF4E) binding site and the middle one-third of elF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol. Cell. Biol. 20, 468-77 (2000).
    • (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
  • 18
    • 0033578620 scopus 로고    scopus 로고
    • Interaction of translation initiation factor elF4G with elF4A in the yeast Saccharomyces cerevisiae
    • Dominguez, D., Altmann, M., Benz, J., Baumann, U. & Trachsel, H. Interaction of translation initiation factor elF4G with elF4A in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 274, 26720-6 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26720-26726
    • Dominguez, D.1    Altmann, M.2    Benz, J.3    Baumann, U.4    Trachsel, H.5
  • 19
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human elF4G 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 elF4G 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
  • 20
    • 0032777549 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally
    • Neff, C. & Sachs, A.B. Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally. Mol. Cell. Biol. 19, 5557-5564 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5557-5564
    • Neff, C.1    Sachs, A.B.2
  • 21
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with elF-4E
    • Stebbins-Boaz, B., Cao, Q., de Moor, C.H., Mendez, R. & Richter, J.D. Maskin is a CPEB-associated factor that transiently interacts with elF-4E. Mol. Cell 4, 1017-27 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 22
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor elF-4G mediates in vitro poly(A) tail-dependent translation
    • Tarun, S.Z., Wells, S.E., Deardorff, J.A. & Sachs, A.B. Translation initiation factor elF-4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94, 9046-9051 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1    Wells, S.E.2    Deardorff, J.A.3    Sachs, A.B.4
  • 23
    • 0026038913 scopus 로고
    • The cap and the poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie, D.R. The cap and the poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5, 2108-2116 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 2108-2116
    • Gallie, D.R.1
  • 24
    • 0023405161 scopus 로고
    • A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability
    • Sachs, A.B., Davis, R.W. & Kornberg, R.D. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol. Cell. Biol. 7, 3268-3276 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3268-3276
    • Sachs, A.B.1    Davis, R.W.2    Kornberg, R.D.3
  • 25
    • 0023053585 scopus 로고
    • A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: Domain structure and expression
    • Sachs, A.B., Bond, M.W. & Kornberg, R.D. A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell 45, 827-35 (1986).
    • (1986) Cell , vol.45 , pp. 827-835
    • Sachs, A.B.1    Bond, M.W.2    Kornberg, R.D.3
  • 26
    • 0022766180 scopus 로고
    • mRNA polyadenylate-binding protein: Gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence
    • Adam, S.A., Nakagawa, T., Swanson, M.S., Woodruff, T.K. & Dreyfuss, G. mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol. Cell. Biol. 6, 2932-2943 (1986).
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2932-2943
    • Adam, S.A.1    Nakagawa, T.2    Swanson, M.S.3    Woodruff, T.K.4    Dreyfuss, G.5
  • 27
    • 0031860374 scopus 로고    scopus 로고
    • RNA recognition by RNP proteins during RNA processing
    • Varani, G. & Nagai, K. RNA recognition by RNP proteins during RNA processing. Annu. Rev. Biophys. Biomol. Struct. 27, 407-445 (1998).
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 407-445
    • Varani, G.1    Nagai, K.2
  • 28
    • 0025762042 scopus 로고
    • The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities
    • Burd, C.G., Matunis, E.L. & Dreyfuss, G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11, 3419-3424 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3419-3424
    • Burd, C.G.1    Matunis, E.L.2    Dreyfuss, G.3
  • 29
    • 0031591391 scopus 로고    scopus 로고
    • Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein
    • Deardorff, J.A. & Sachs, A.B. Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein. J. Mol. Biol. 269, 67-81 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 67-81
    • Deardorff, J.A.1    Sachs, A.B.2
  • 30
    • 0038063499 scopus 로고    scopus 로고
    • Xenopus poly(A) binding protein:Functional domains in RNA binding and protein-protein interactions
    • Kuhn, U. & Pieler, T. Xenopus poly(A) binding protein:functional domains in RNA binding and protein-protein interactions. J. Mol. Biol. 256, 20-30 (1996).
    • (1996) J. Mol. Biol. , vol.256 , pp. 20-30
    • Kuhn, U.1    Pieler, T.2
  • 31
    • 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. 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).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 51-57
    • Kessler, S.H.1    Sachs, A.B.2
  • 32
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo, R.C., Bonanno, J.B., Sonenberg, N. & Burley, S.K. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 98, 835-45 (1999).
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 33
    • 0032834055 scopus 로고    scopus 로고
    • elF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A.C., Raught, B. & Sonenberg, N. elF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Ann. Rev. Biochem. 68, 913-963 (1999).
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 34
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras, A.C., et al. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 13, 1422-37 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1422-1437
    • Gingras, A.C.1
  • 35
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping
    • Hakansson, K. & Wigley, D.B. Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping. Proc. Natl. Acad. Sci. USA 95, 1505-1510 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1505-1510
    • Hakansson, K.1    Wigley, D.B.2
  • 37
    • 0031993338 scopus 로고    scopus 로고
    • Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme
    • Hodel, A.E., Gershon, P.D. & Quiocho, F.A. Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme. Mol Cell 1, 443-7 (1998).
    • (1998) Mol Cell , vol.1 , pp. 443-447
    • Hodel, A.E.1    Gershon, P.D.2    Quiocho, F.A.3
  • 38
    • 0033594890 scopus 로고    scopus 로고
    • mRNA cap recognition: Dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains
    • Hu, G., Gershon, P.D., Hodel, A.E. & Quiocho, F.A. mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains. Proc. Natl. Acad. Sci. USA 96, 7149-54 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7149-7154
    • Hu, G.1    Gershon, P.D.2    Hodel, A.E.3    Quiocho, F.A.4
  • 39
    • 0029913438 scopus 로고    scopus 로고
    • RNA-protein complexes
    • Nagai, K. RNA-protein complexes. Curr Opin Struct Biol 6, 53-61 (1996).
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 53-61
    • Nagai, K.1
  • 40
    • 0028983915 scopus 로고
    • A cap-binding protein complex mediating U snRNA export
    • Izaurralde, E., et al. A cap-binding protein complex mediating U snRNA export. Nature 376, 709-712 (1995).
    • (1995) Nature , vol.376 , pp. 709-712
    • Izaurralde, E.1
  • 41
    • 0023929705 scopus 로고
    • Specific ring stacking interaction on the tryptophan-7-methylguanine system: Comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside, nucleotide complexes
    • Ishida, T., Doi, M., Ueda, H., Inoue, M. & Sheldrick, G.M. Specific ring stacking interaction on the tryptophan-7-methylguanine system: comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside, nucleotide complexes. J. Amer. Chem. Soc. 110, 2286-2294 (1988).
    • (1988) J. Amer. Chem. Soc. , vol.110 , pp. 2286-2294
    • Ishida, T.1    Doi, M.2    Ueda, H.3    Inoue, M.4    Sheldrick, G.M.5
  • 42
    • 0033565233 scopus 로고    scopus 로고
    • Repressor binding to a dorsal regulatory site traps human elF4E in a high cap-affinity state
    • Ptushkina, M., von der Haar, T., Karim, M.M., Hughes, J.M. & McCarthy, J.E. Repressor binding to a dorsal regulatory site traps human elF4E in a high cap-affinity state. EMBO J. 18, 4068-75 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4068-4075
    • Ptushkina, M.1    Von Der Haar, T.2    Karim, M.M.3    Hughes, J.M.4    McCarthy, J.E.5
  • 43
    • 0033597729 scopus 로고    scopus 로고
    • The cap-binding protein elF4E promotes folding of a functional domain of yeast translation initiation factor elF4G1
    • Hershey, P.E., et al. The Cap-binding protein elF4E promotes folding of a functional domain of yeast translation initiation factor elF4G1. J. Biol. Chem. 274, 21297-304 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21297-21304
    • Hershey, P.E.1
  • 44
    • 0032488627 scopus 로고    scopus 로고
    • 4E binding proteins inhibit the translation factor elF4E without folded structure
    • Fletcher, CM, et al. 4E binding proteins inhibit the translation factor elF4E without folded structure. Biochemistry 37, 9-15 (1998).
    • (1998) Biochemistry , vol.37 , pp. 9-15
    • Fletcher, C.M.1
  • 45
    • 0031821410 scopus 로고    scopus 로고
    • The interaction of elF4E with 4E-BP1 is an induced fit to a completely disordered protein
    • Fletcher, C.M. & Wagner, G. The interaction of elF4E with 4E-BP1 is an induced fit to a completely disordered protein. Protein Sci. 7, 1639-42 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 1639-1642
    • Fletcher, C.M.1    Wagner, G.2
  • 46
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation
    • Allain, F.H., et al. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation. Nature 380, 646-50 (1996).
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.1
  • 47
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 a resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.H. & Nagai, K. Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372, 432-438 (1994).
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 48
    • 0033560881 scopus 로고    scopus 로고
    • Structural basis for recognition of the tra mRNA precursor by the sex-lethal protein
    • Handa, N., et al. Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein. Nature 398, 579-585 (1999).
    • (1999) Nature , vol.398 , pp. 579-585
    • Handa, N.1
  • 49
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J., et al. Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 13, 1102-1115 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1
  • 50
    • 0033153302 scopus 로고    scopus 로고
    • The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms
    • Otero, L., Ashe, M. & Sachs, A. The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBO J. 18, 3153-3163 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3153-3163
    • Otero, L.1    Ashe, M.2    Sachs, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.