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Volumn 290, Issue 40, 2015, Pages 24091-24099

eIF4F: A retrospective

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BINS; MAMMALS; PROTEINS;

EID: 84943338797     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R115.675280     Document Type: Review
Times cited : (114)

References (90)
  • 1
    • 0021099436 scopus 로고
    • New initiation factor activity required for globin mRNA translation
    • Grifo, J. A., and Tahara., S. M., Morgan, M. A., Shatkin, A.J., and Merrick, W. C. (1983) New initiation factor activity required for globin mRNA translation. J. Biol. Chem. 258, 5804-5810
    • (1983) J. Biol. Chem. , vol.258 , pp. 5804-5810
    • Grifo, J.A.1    Tahara, S.M.2    Morgan, M.A.3    Shatkin, A.J.4    Merrick, W.C.5
  • 2
    • 0016751816 scopus 로고
    • Ribosome binding to reovirus mRNA in protein synthesis requires 5' terminal 7-methylguanosine
    • Both, G. W., Furuichi, Y., Muthukrishnan, S., and Shatkin, A. J. (1975) Ribosome binding to reovirus mRNA in protein synthesis requires 5' terminal 7-methylguanosine. Cell 6, 185-195
    • (1975) Cell , vol.6 , pp. 185-195
    • Both, G.W.1    Furuichi, Y.2    Muthukrishnan, S.3    Shatkin, A.J.4
  • 5
    • 0021765648 scopus 로고
    • Purification of the messenger RNA cap-binding protein using a new affinity medium
    • Webb, N. R., and Chari., R. V., DePillis, G., Kozarich, J. W., and Rhoads, R. E. (1984) Purification of the messenger RNA cap-binding protein using a new affinity medium. Biochemistry 23, 177-181
    • (1984) Biochemistry , vol.23 , pp. 177-181
    • Webb, N.R.1    Chari, R.V.2    DePillis, G.3    Kozarich, J.W.4    Rhoads, R.E.5
  • 6
    • 0017696975 scopus 로고
    • Reovirus mRNA can be covalently crosslinked via the 5' cap to proteins in initiation complexes
    • Sonenberg, N, and Shatkin, A. J. (1977) Reovirus mRNA can be covalently crosslinked via the 5' cap to proteins in initiation complexes. Proc. Natl. Acad. Sci. U.S.A. 74, 4288-4292
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 4288-4292
    • Sonenberg, N.1    Shatkin, A.J.2
  • 7
    • 0019877161 scopus 로고
    • 7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells
    • 7G-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
  • 8
    • 0018220249 scopus 로고
    • Initiation factor eIF-4B (IF-M3)-de-pendent recognition and translation of capped versus uncapped eukaryotic mRNAs
    • Padilla, M., Canaani, D., Groner, Y., Weinstein, J. A., Bar-Joseph, M., Merrick, W., and Shafritz, D. A. (1978) Initiation factor eIF-4B (IF-M3)-de-pendent recognition and translation of capped versus uncapped eukaryotic mRNAs. J. Biol. Chem. 253, 5939-5945
    • (1978) J. Biol. Chem. , vol.253 , pp. 5939-5945
    • Padilla, M.1    Canaani, D.2    Groner, Y.3    Weinstein, J.A.4    Bar-Joseph, M.5    Merrick, W.6    Shafritz, D.A.7
  • 9
    • 0020045412 scopus 로고
    • Association of cap-binding protein with eukaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected HeLa cells
    • Hansen, J., Etchison, D., Hershey, J. W., and Ehrenfeld, E. (1982) Association of cap-binding protein with eukaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected HeLa cells. J. Virol. 42, 200-207
    • (1982) J. Virol. , vol.42 , pp. 200-207
    • Hansen, J.1    Etchison, D.2    Hershey, J.W.3    Ehrenfeld, E.4
  • 10
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eukaryotic initiation factor 3 and a cap-binding protein complex
    • Etchison, D., and Milburn., S. C., Edery, I., Sonenberg, N., and 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 eukaryotic 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
  • 13
    • 0023894279 scopus 로고
    • Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA
    • Abramson, R. D., and Dever., T. E., and Merrick, W. C. (1988) Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA. J. Biol. Chem. 263, 6016-6019
    • (1988) J. Biol. Chem. , vol.263 , pp. 6016-6019
    • Abramson, R.D.1    Dever, T.E.2    Merrick, W.C.3
  • 14
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • Rogers, G. W., Jr., Richter, N. J., Lima, W. F., and Merrick, W. C. (2001) Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J. Biol. Chem. 276, 30914-30922
    • (2001) J. Biol. Chem. , vol.276 , pp. 30914-30922
    • Rogers Jr, . G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 16
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky, E., and Gross., C. H., Shuman, S., and Pyle, A. M. (2001) Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291, 121-125
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 17
    • 0028222129 scopus 로고
    • Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors
    • Hu, C., Pang, S., Kong, X., Velleca, M., and Lawrence, J. C. Jr (1994) Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors. Proc. Natl. Acad. Sci. U.S.A. 91, 3730-3734
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 3730-3734
    • Hu, C.1    Pang, S.2    Kong, X.3    Velleca, M.4    Lawrence Jr, . J.C.5
  • 18
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    • Pause, A., and Belsham., G. J., Gingras, A. C., Donzé, O., Lin, T. A., Lawrence, J. C., Jr., and Sonenberg, N. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature 371, 762-767
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donzé, O.4    Lin, T.A.5    Lawrence Jr, . J.C.6    Sonenberg, N.7
  • 19
    • 84889564693 scopus 로고    scopus 로고
    • Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface
    • Lukhele, S., Bah, A., Lin, H., Sonenberg, N., and Forman-Kay, J. D. (2013) Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface. Structure 21, 2186-2196
    • (2013) Structure , vol.21 , pp. 2186-2196
    • Lukhele, S.1    Bah, A.2    Lin, H.3    Sonenberg, N.4    Forman-Kay, J.D.5
  • 21
    • 0016722009 scopus 로고
    • Competition between α and β globin messenger RNA
    • Temple, G., and Lodish, H.F. (1975) Competition between α and β globin messenger RNA. Biochem. Biophys. Res. Comm. 63, 971-979
    • (1975) Biochem. Biophys. Res. Comm. , vol.63 , pp. 971-979
    • Temple, G.1    Lodish, H.F.2
  • 22
    • 0018613233 scopus 로고
    • A kinetic model of protein synthesis: Application to hemoglobin synthesis and translational control
    • Bergmann, J. E., and Lodish, H. F. (1979) A kinetic model of protein synthesis: application to hemoglobin synthesis and translational control. J. Biol. Chem. 254, 11927-11937
    • (1979) J. Biol. Chem. , vol.254 , pp. 11927-11937
    • Bergmann, J.E.1    Lodish, H.F.2
  • 23
    • 0019888598 scopus 로고
    • The role of mRNA competition in regulating translation. IV kinetic model
    • Godefroy-Colburn, T., and Thach, R. E. (1981) The role of mRNA competition in regulating translation. IV Kinetic model. J. Biol. Chem. 256, 11762-11773
    • (1981) J. Biol. Chem. , vol.256 , pp. 11762-11773
    • Godefroy-Colburn, T.1    Thach, R.E.2
  • 24
    • 0022425746 scopus 로고
    • Cap accessibility correlates with the initiation efficiency of alfalfa mosaic virus RNAs
    • Godefroy-Colburn, T., Ravelonandro, M., and Pinck, L. (1985) Cap accessibility correlates with the initiation efficiency of alfalfa mosaic virus RNAs. Eur. J. Biochem. 147, 549-552
    • (1985) Eur. J. Biochem. , vol.147 , pp. 549-552
    • Godefroy-Colburn, T.1    Ravelonandro, M.2    Pinck, L.3
  • 25
    • 0037216626 scopus 로고    scopus 로고
    • The transformation suppressor pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation
    • Yang, H. S., and Jansen., A. P., Komar, A. A., Zheng, X., Merrick, W. C, Costes, S., and Lockett., S. J., Sonenberg, N., and Colburn, N. H. (2003) The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Mol. Cell. Biol. 23, 26-37
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 26-37
    • Yang, H.S.1    Jansen, A.P.2    Komar, A.A.3    Zheng, X.4    Merrick, W.C.5    Costes, S.6    Lockett, S.J.7    Sonenberg, N.8    Colburn, N.H.9
  • 28
    • 84871178729 scopus 로고    scopus 로고
    • Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis
    • Dennis, M. D., and Jefferson., L. S., and Kimball, S. R. (2012) Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis. J. Biol. Chem. 287, 42890-42899
    • (2012) J. Biol. Chem. , vol.287 , pp. 42890-42899
    • Dennis, M.D.1    Jefferson, L.S.2    Kimball, S.R.3
  • 29
    • 0033544894 scopus 로고    scopus 로고
    • Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H
    • Richter, N.J., Rogers, G. W., Jr., Hensold, J. O., and Merrick, W. C. (1999) Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H. J. Biol. Chem. 274, 35415-35424
    • (1999) J. Biol. Chem. , vol.274 , pp. 35415-35424
    • Richter, N.J.1    Rogers Jr, . G.W.2    Hensold, J.O.3    Merrick, W.C.4
  • 30
    • 0018371457 scopus 로고
    • Purification of protein synthesis initiation factors from rabbit reticulocytes
    • Merrick, W. C (1979) Purification of protein synthesis initiation factors from rabbit reticulocytes. Methods Enzymol. 60, 101-108
    • (1979) Methods Enzymol. , vol.60 , pp. 101-108
    • Merrick, W.C.1
  • 32
    • 0029086291 scopus 로고
    • The saccharomyces cerevisiae translation initiation factor tif3 and its Mammalian homologue, eIF4B, have RNA annealing activity
    • Altmann, M., Wittmer, B., Méthot, N., Sonenberg, N., and Trachsel, H. (1995) The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF4B, have RNA annealing activity. EMBOJ. 14, 3820-3827
    • (1995) EMBOJ , vol.14 , pp. 3820-3827
    • Altmann, M.1    Wittmer, B.2    Méthot, N.3    Sonenberg, N.4    Trachsel, H.5
  • 34
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • Méthot, N., and Song., M. S., and Sonenberg, N. (1996) A region rich in aspartic acid, arginine, tyrosine and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol. Cell. Biol. 16, 5328-5334
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Méthot, N.1    Song, M.S.2    Sonenberg, N.3
  • 35
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers, J. M., and Johnson., E. R., and McKay, D. B. (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc. Natl. Acad. Sci. U.S.A. 97, 13080-13085
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 36
    • 84899801759 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the allosteric regulation of eIF4A protein from the open to closed state, induced by ATP and RNA substrates
    • Meng, H., Li, C, Wang, Y., and Chen, G. (2014) Molecular dynamics simulation of the allosteric regulation of eIF4A protein from the open to closed state, induced by ATP and RNA substrates. PLoS One 9, e86104
    • (2014) PLoS One , vol.9
    • Meng, H.1    Li, C.2    Wang, Y.3    Chen, G.4
  • 37
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain with eIF4G directs assembly of the translation initiation machinery
    • Marcotrigiano, J., and Lomakin., I. B., Sonenberg, N, and Pestova., T. V., Hellen, C. U. T., and Burley, S. K. (2001) A conserved HEAT domain with eIF4G directs assembly of the translation initiation machinery. Mol. Cell 7, 193-203
    • (2001) Mol. Cell , vol.7 , pp. 193-203
    • Marcotrigiano, J.1    Lomakin, I.B.2    Sonenberg, N.3    Pestova, T.V.4    Hellen, C.U.T.5    Burley, S.K.6
  • 38
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of the eIF4A helicase activity by eIF4G
    • Oberer, M., Marintchev, A., and Wagner, G. (2005) Structural basis for the enhancement of the eIF4A helicase activity by eIF4G. Genes Dev. 19, 2212-2223
    • (2005) Genes Dev. , vol.19 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 39
    • 33646341222 scopus 로고    scopus 로고
    • Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and mnk1
    • Bellsolell, L., Cho-Park, P. F., Poulin, F., Sonenberg, N, and Burley, S. K. (2006) Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Structure 14, 913-923
    • (2006) Structure , vol.14 , pp. 913-923
    • Bellsolell, L.1    Cho-Park, P.F.2    Poulin, F.3    Sonenberg, N.4    Burley, S.K.5
  • 41
    • 0030728936 scopus 로고    scopus 로고
    • Co-crystal structure of the messenger RNA 5' cap-binding protein (eIF4E) boundto7-methyl-GDP
    • Marcotrigiano, J., Gingras, A. C, Sonenberg, N, and Burley, S. K. (1997) Co-crystal structure of the messenger RNA 5' cap-binding protein (eIF4E) boundto7-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
  • 43
    • 67649302863 scopus 로고    scopus 로고
    • Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site
    • Brown, C. J., and Verma., C. S., Walkinshaw, M. D., and Lane, D. P. (2009) Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site. Cell Cycle 8, 1905-1911
    • (2009) Cell Cycle , vol.8 , pp. 1905-1911
    • Brown, C.J.1    Verma, C.S.2    Walkinshaw, M.D.3    Lane, D.P.4
  • 45
    • 84882291342 scopus 로고    scopus 로고
    • Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity
    • Feoktistova, K., Tuvshintogs, E., Do, A., and Fraser, C. S. (2013) Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity. Proc. Natl. Acad. Sci. U.S.A. 110, 13339-13344
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 13339-13344
    • Feoktistova, K.1    Tuvshintogs, E.2    Do, A.3    Fraser, C.S.4
  • 46
    • 84881226665 scopus 로고    scopus 로고
    • Translation initiation requires cell division cycle 123 (Cdc123) to facilitate biogenesis of the eukaryotic initiation factor 2 (eIF2)
    • Perzlmaier, A. F., Richter, F., and Seufert, W. (2013) Translation initiation requires cell division cycle 123 (Cdc123) to facilitate biogenesis of the eukaryotic initiation factor 2 (eIF2). J. Biol. Chem. 288, 21537-21546
    • (2013) J. Biol. Chem. , vol.288 , pp. 21537-21546
    • Perzlmaier, A.F.1    Richter, F.2    Seufert, W.3
  • 47
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B
    • Özeş, A. R., Feoktistova, K., Avanzino, B. C, and Fraser, C. S. (2011) Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. J. Mol. Biol. 412, 674-687
    • (2011) J. Mol. Biol. , vol.412 , pp. 674-687
    • Özeş, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 50
    • 0018143765 scopus 로고
    • A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA
    • Sonenberg, N., and Morgan., M. A., Merrick, W. C, and Shatkin, A. J. (1978) A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA. Proc. Natl. Acad. Sci. U.S.A. 75, 4843-4847
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4843-4847
    • Sonenberg, N.1    Morgan, M.A.2    Merrick, W.C.3    Shatkin, A.J.4
  • 51
    • 0020490589 scopus 로고
    • A polypeptide which reverses cap analog inhibition of cell-free protein synthesis: Purification and binding to capped oligonucleotides
    • Hellmann, G. M., Chu, L.-Y., and Rhoads, R. E. (1982) A polypeptide which reverses cap analog inhibition of cell-free protein synthesis: Purification and binding to capped oligonucleotides. J. Biol. Chem. 257, 4056-4062
    • (1982) J. Biol. Chem. , vol.257 , pp. 4056-4062
    • Hellmann, G.M.1    Chu, L.-Y.2    Rhoads, R.E.3
  • 53
    • 0027418308 scopus 로고
    • The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF4A
    • Yoder-Hill, J., Pause, A., Sonenberg, N., and Merrick, W. C. (1993) The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF4A. J. Biol. Chem. 268, 5566-5573
    • (1993) J. Biol. Chem. , vol.268 , pp. 5566-5573
    • Yoder-Hill, J.1    Pause, A.2    Sonenberg, N.3    Merrick, W.C.4
  • 54
    • 0028197298 scopus 로고
    • Dominant negative mutants of Mammalian translation initiation factor eIF4A define a critical role for eIF4F in cap-dependent and cap-independent initiation of translation
    • Pause, A., Méthot, N., Svitkin, Y., Merrick, W. C, and Sonenberg, N. (1994) Dominant negative mutants of mammalian translation initiation factor eIF4A define a critical role for eIF4F in cap-dependent and cap-independent initiation of translation. EMBOJ. 13, 1205-1215
    • (1994) EMBOJ , vol.13 , pp. 1205-1215
    • Pause, A.1    Méthot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 55
    • 0021099528 scopus 로고
    • Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis
    • Duncan, R., and Hershey, J. W. (1983) Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 258, 7228-7235
    • (1983) J. Biol. Chem. , vol.258 , pp. 7228-7235
    • Duncan, R.1    Hershey, J.W.2
  • 56
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in saccharomyces cerevisiae and their role in capcomplex function
    • von der Haar, T., and McCarthy, J. E. G. (2002) Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in capcomplex function. Mol. Microbiol. 46, 531-544
    • (2002) Mol. Microbiol. , vol.46 , pp. 531-544
    • Von Der Haar, T.1    McCarthy, J.E.G.2
  • 57
    • 84873866604 scopus 로고    scopus 로고
    • Yeast eukaryotic initiation factor 4B (eIF4B) enhances complex assembly between eIF4A and eIF4G
    • Park, E. H., and Walker., S. E., Zhou, F., Lee, J. M., Rajagopal, V., Lorsch, J. R., and Hinnebusch, A. G. (2013) Yeast eukaryotic initiation factor 4B (eIF4B) enhances complex assembly between eIF4A and eIF4G. J. Biol. Chem. 288, 2340-2354
    • (2013) J. Biol. Chem. , vol.288 , pp. 2340-2354
    • Park, E.H.1    Walker, S.E.2    Zhou, F.3    Lee, J.M.4    Rajagopal, V.5    Lorsch, J.R.6    Hinnebusch, A.G.7
  • 58
    • 77956940474 scopus 로고    scopus 로고
    • The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway
    • Mitchell, S. F., and Walker., S. E., Algire, M. A., Park, E.-H., and Hinnebusch., A. G., and Lorsch, J. R. (2010) The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway. Mol. Cell 39, 950-962
    • (2010) Mol. Cell , vol.39 , pp. 950-962
    • Mitchell, S.F.1    Walker, S.E.2    Algire, M.A.3    Park, E.-H.4    Hinnebusch, A.G.5    Lorsch, J.R.6
  • 59
    • 27944483724 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4E availability controls the switch between cap-dependent and internal ribosome entry site-mediated translation
    • Svitkin, Y. V., Herdy, B., Costa-Mattioli, M., Gingras, A. C, Raught, B., and Sonenberg, N. (2005) Eukaryotic initiation factor 4E availability controls the switch between cap-dependent and internal ribosome entry site-mediated translation. Mol. Cell. Biol. 25, 10556-10565
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10556-10565
    • Svitkin, Y.V.1    Herdy, B.2    Costa-Mattioli, M.3    Gingras, A.C.4    Raught, B.5    Sonenberg, N.6
  • 60
    • 0035032444 scopus 로고    scopus 로고
    • The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure
    • Svitkin, Y. V., Pause, A., Haghighat, A., Pyronnet, S., Witherell, G., Belsham, G. J., and Sonenberg, N. (2001) The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure. RNA 7, 382-394
    • (2001) RNA , vol.7 , pp. 382-394
    • Svitkin, Y.V.1    Pause, A.2    Haghighat, A.3    Pyronnet, S.4    Witherell, G.5    Belsham, G.J.6    Sonenberg, N.7
  • 61
    • 0030614360 scopus 로고    scopus 로고
    • Requirement of the DEAD-box protein ded1p for messenger RNA translation
    • Chuang, R. Y., and Weaver., P. L., Liu, Z., and Chang, T. H. (1997) Requirement of the DEAD-box protein Ded1p for messenger RNA translation. Science 275, 1468-1471
    • (1997) Science , vol.275 , pp. 1468-1471
    • Chuang, R.Y.1    Weaver, P.L.2    Liu, Z.3    Chang, T.H.4
  • 62
    • 80053022305 scopus 로고    scopus 로고
    • The DEAD-box protein ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex
    • Hilliker, A., Gao, Z., Jankowsky, E., and Parker, R. (2011) The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol. Cell 43, 962-972
    • (2011) Mol. Cell , vol.43 , pp. 962-972
    • Hilliker, A.1    Gao, Z.2    Jankowsky, E.3    Parker, R.4
  • 63
    • 84866361659 scopus 로고    scopus 로고
    • DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs
    • Soto-Rifo, R., Rubilar, P. S., Limousin, T., de Breyne, S., Décimo, D., and Ohlmann T. (2012) DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs. EMBOJ. 31, 3745-3756
    • (2012) EMBOJ , vol.31 , pp. 3745-3756
    • Soto-Rifo, R.1    Rubilar, P.S.2    Limousin, T.3    De Breyne, S.4    Décimo, D.5    Ohlmann, T.6
  • 64
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on Mammalian mRNAs with structured 5' UTRs requires DExH-box protein DHX29
    • Pisareva, V. P., and Pisarev., A. V., Komar, A. A., Hellen, C. U., and Pestova, T. V. (2008) Translation initiation on mammalian mRNAs with structured 5' UTRs requires DExH-box protein DHX29. Cell 135, 1237-1250
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3    Hellen, C.U.4    Pestova, T.V.5
  • 66
    • 21844442364 scopus 로고    scopus 로고
    • Functional diversity of the eukaryotic translation factors belong to eIF4 families
    • Hernández, G., and Vazquez-Pianzola, P. (2005) Functional diversity of the eukaryotic translation factors belong to eIF4 families. Mech. Dev. 122, 865-876
    • (2005) Mech. Dev. , vol.122 , pp. 865-876
    • Hernández, G.1    Vazquez-Pianzola, P.2
  • 67
    • 13544276792 scopus 로고    scopus 로고
    • Mouse p56 blocks a distinct function of eukaryotic initiation factor 3 in translation initiation
    • Hui, D. J., Terenzi, F., Merrick, W. C, and Sen, G. C. (2005) Mouse p56 blocks a distinct function of eukaryotic initiation factor 3 in translation initiation. J. Biol. Chem. 280, 3433-3440
    • (2005) J. Biol. Chem. , vol.280 , pp. 3433-3440
    • Hui, D.J.1    Terenzi, F.2    Merrick, W.C.3    Sen, G.C.4
  • 68
    • 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. J., and Ashe., M. P., and Sachs, A. B. (1999) The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBOJ. 18, 3153-3163
    • (1999) EMBOJ , vol.18 , pp. 3153-3163
    • Otero, L.J.1    Ashe, M.P.2    Sachs, A.B.3
  • 69
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells, S. E., and Hillner., P. E., Vale, R. D., and 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
  • 70
    • 84862000545 scopus 로고    scopus 로고
    • Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5'-overhangs
    • Rajagopal, V., Park, E.-H., and Hinnebusch., A. G., and Lorsch, J. R. (2012) Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5'-overhangs. J. Biol. Chem. 287, 20301-20312
    • (2012) J. Biol. Chem. , vol.287 , pp. 20301-20312
    • Rajagopal, V.1    Park, E.-H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 71
    • 0021270173 scopus 로고
    • RNA-stimulated ATPase activity of eukaryotic initiation factors
    • Grifo, J. A., and Abramson., R. D., Satler, C. A., and Merrick, W. C. (1984) RNA-stimulated ATPase activity of eukaryotic initiation factors. J. Biol. Chem. 259, 8648-8654
    • (1984) J. Biol. Chem. , vol.259 , pp. 8648-8654
    • Grifo, J.A.1    Abramson, R.D.2    Satler, C.A.3    Merrick, W.C.4
  • 72
    • 77954373163 scopus 로고    scopus 로고
    • Molecular view of 43S complex formation and start site selection in eukaryotic translation initiation
    • Lorsch, J. R., and Dever, T. E. (2010) Molecular view of 43S complex formation and start site selection in eukaryotic translation initiation. J. Biol. Chem. 285, 21203-21207
    • (2010) J. Biol. Chem. , vol.285 , pp. 21203-21207
    • Lorsch, J.R.1    Dever, T.E.2
  • 73
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R. J., and Hellen., C. U., and Pestova, T. V. (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11, 113-127
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 74
    • 78751662371 scopus 로고    scopus 로고
    • RNA helicases: Emerging roles in viral replication and the host innate response
    • Ranji, A., and Boris-Lawrie, K. (2010) RNA helicases: Emerging roles in viral replication and the host innate response. RNA Biol. 7, 775-787
    • (2010) RNA Biol. , vol.7 , pp. 775-787
    • Ranji, A.1    Boris-Lawrie, K.2
  • 75
    • 84882773211 scopus 로고    scopus 로고
    • The Royal Society of Chemistry, Cambridge, UK
    • Jankowsky, E. (2010) RNA Helicases, The Royal Society of Chemistry, Cambridge, UK
    • (2010) RNA Helicases
    • Jankowsky, E.1
  • 76
    • 79551554217 scopus 로고    scopus 로고
    • Cellular IRES-mediated translation: The warof ITAFs in pathophysiological states
    • Komar, A. A., and Hatzoglou, M. (2011) Cellular IRES-mediated translation: the warof ITAFs in pathophysiological states. Cell Cycle 10, 229-240
    • (2011) Cell Cycle , vol.10 , pp. 229-240
    • Komar, A.A.1    Hatzoglou, M.2
  • 77
    • 79953721157 scopus 로고    scopus 로고
    • Translation initiation: Variations in the mechanism can be anticipated
    • Malys, N., and McCarthy, J. E. (2011) Translation initiation: variations in the mechanism can be anticipated. Cell. Mol. Life Sci. 68, 991-1003
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 991-1003
    • Malys, N.1    McCarthy, J.E.2
  • 79
    • 84861342693 scopus 로고    scopus 로고
    • A new framework for understanding IRES-mediated translation
    • Komar, A. A., Mazumder, B., and Merrick, W. C. (2012) A new framework for understanding IRES-mediated translation. Gene 502, 75-86
    • (2012) Gene , vol.502 , pp. 75-86
    • Komar, A.A.1    Mazumder, B.2    Merrick, W.C.3
  • 80
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: New insights and challenges
    • Hinnebusch, A. G., and Lorsch, J. R. (2012) The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol. 4, a011544
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 82
    • 84902193122 scopus 로고    scopus 로고
    • The scanning mechanism of eukaryotic translation initiation
    • Hinnebusch, A. G. (2014) The scanning mechanism of eukaryotic translation initiation. Annu. Rev. Biochem. 83, 779-812
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 779-812
    • Hinnebusch, A.G.1
  • 84
    • 84920987074 scopus 로고    scopus 로고
    • Targeting the eIF4F translation initiation complex: A critical nexus for cancer development
    • Pelletier, J., Graff, J., Ruggero, D., and Sonenberg, N. (2015) Targeting the eIF4F translation initiation complex: a critical nexus for cancer development. Cancer Res. 75, 250-263
    • (2015) Cancer Res. , vol.75 , pp. 250-263
    • Pelletier, J.1    Graff, J.2    Ruggero, D.3    Sonenberg, N.4
  • 87
    • 84869085954 scopus 로고    scopus 로고
    • Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G
    • Safaee, N., Kozlov, G., Noronha, A. M., Xie, J., Wilds, C. J., and Gehring, K. (2012) Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. Mol. Cell 48, 375-386
    • (2012) Mol. Cell , vol.48 , pp. 375-386
    • Safaee, N.1    Kozlov, G.2    Noronha, A.M.3    Xie, J.4    Wilds, C.J.5    Gehring, K.6
  • 88
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
    • Gross, J. D., and Moerke., N. J., von der Haar, T., Lugovskoy, A. A., Sachs, A. B., McCarthy, J.E., and Wagner, G. (2003) Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell 115, 739-750
    • (2003) Cell , vol.115 , pp. 739-750
    • Gross, J.D.1    Moerke, N.J.2    Von Der Haar, T.3    Lugovskoy, A.A.4    Sachs, A.B.5    McCarthy, J.E.6    Wagner, G.7
  • 89
    • 84930383499 scopus 로고    scopus 로고
    • Quantitative studies of mRNA recruitment to the eukaryotic ribosome
    • Fraser, C. S. (2015) Quantitative studies of mRNA recruitment to the eukaryotic ribosome. Biochimie 114, 58-71
    • (2015) Biochimie , vol.114 , pp. 58-71
    • Fraser, C.S.1
  • 90
    • 77954356006 scopus 로고    scopus 로고
    • Eukaryotic protein synthesis: Still a mystery
    • Merrick, W. C. (2010) Eukaryotic protein synthesis: still a mystery. J. Biol. Chem. 285, 21197-21201
    • (2010) J. Biol. Chem. , vol.285 , pp. 21197-21201
    • Merrick, W.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.