메뉴 건너뛰기




Volumn 502, Issue 2, 2012, Pages 75-86

A new framework for understanding IRES-mediated translation

Author keywords

Cap dependent translation; Eukaryotic protein synthesis; IRES mediated translation; MRNAs

Indexed keywords

ELONGATION FACTOR 1ALPHA; GUANOSINE TRIPHOSPHATE; INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 3; INITIATION FACTOR 4A; INITIATION FACTOR 4B; INITIATION FACTOR 4E; INITIATION FACTOR 4F; INITIATION FACTOR 4G; INITIATION FACTOR 5B; MESSENGER RNA; RNA HELICASE; TRANSFER RNA; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 84861342693     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.04.039     Document Type: Review
Times cited : (69)

References (122)
  • 1
    • 78650907809 scopus 로고    scopus 로고
    • Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning
    • Abaeva I.S., Marintchev A., Pisareva V.P., Hellen C.U., Pestova T.V. Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning. EMBO J. 2011, 30:115-129.
    • (2011) EMBO J. , vol.30 , pp. 115-129
    • Abaeva, I.S.1    Marintchev, A.2    Pisareva, V.P.3    Hellen, C.U.4    Pestova, T.V.5
  • 2
    • 0016774054 scopus 로고
    • Eukaryotic initiation complex formation: evidence for two distinct pathways
    • Adams S.L., Safer B., Anderson W.F., Merrick W.C. Eukaryotic initiation complex formation: evidence for two distinct pathways. J. Biol. Chem. 1975, 250:9083-9089.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9083-9089
    • Adams, S.L.1    Safer, B.2    Anderson, W.F.3    Merrick, W.C.4
  • 3
    • 0035385075 scopus 로고    scopus 로고
    • Translational control of the picornavirus phenotype
    • Agol V.I. Translational control of the picornavirus phenotype. Mol. Biol. 2001, 35:691-701.
    • (2001) Mol. Biol. , vol.35 , pp. 691-701
    • Agol, V.I.1
  • 4
    • 0027186325 scopus 로고
    • A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity
    • Altman M., Muller P.P., Wittmer B., Ruchti F., Lanker S., Trachsel H. A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity. EMBO J. 1993, 12:3997-4003.
    • (1993) EMBO J. , vol.12 , pp. 3997-4003
    • Altman, M.1    Muller, P.P.2    Wittmer, B.3    Ruchti, F.4    Lanker, S.5    Trachsel, H.6
  • 5
    • 34447530523 scopus 로고    scopus 로고
    • Differential factor requirement to assemble translation initiation complexes at the alternative start codons of foot-and-mouth disease virus RNA
    • Andreev D.E., et al. Differential factor requirement to assemble translation initiation complexes at the alternative start codons of foot-and-mouth disease virus RNA. RNA 2007, 13:1366-1374.
    • (2007) RNA , vol.13 , pp. 1366-1374
    • Andreev, D.E.1
  • 7
    • 0025743912 scopus 로고
    • Eukaryotic initiation factor (eIF)-4F: implications for a role in internal initiation of translation
    • Anthony D.D., Merrick W.C. Eukaryotic initiation factor (eIF)-4F: implications for a role in internal initiation of translation. J. Biol. Chem. 1991, 266:10218-10226.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10218-10226
    • Anthony, D.D.1    Merrick, W.C.2
  • 8
    • 34547907409 scopus 로고    scopus 로고
    • A search for structurally similar cellular internal ribosome entry sites
    • Baird S.D., Lewis S.M., Turcotte M., Holcik M. A search for structurally similar cellular internal ribosome entry sites. Nucleic Acids Res. 2007, 35:4664-4677.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4664-4677
    • Baird, S.D.1    Lewis, S.M.2    Turcotte, M.3    Holcik, M.4
  • 9
    • 83255187900 scopus 로고    scopus 로고
    • Requirement of rRNA methylation for 80S ribosome assembly on a cohort of cellular internal ribosome entry sites
    • Basu A., et al. Requirement of rRNA methylation for 80S ribosome assembly on a cohort of cellular internal ribosome entry sites. Mol. Cell. Biol. 2011, 31:4482-4499.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4482-4499
    • Basu, A.1
  • 11
    • 80054080846 scopus 로고    scopus 로고
    • Crystal structure of the HCV IRES central domain reveals strategy for start-codon positioning
    • Berry K.E., Waghray S., Mortimer S.A., Bai Y., Doudna J.A. Crystal structure of the HCV IRES central domain reveals strategy for start-codon positioning. Structure 2011, 19:1456-1466.
    • (2011) Structure , vol.19 , pp. 1456-1466
    • Berry, K.E.1    Waghray, S.2    Mortimer, S.A.3    Bai, Y.4    Doudna, J.A.5
  • 13
    • 27644484907 scopus 로고    scopus 로고
    • Structure of the hepatitis C virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES
    • Boehringer D., Thermann R., Ostareck-Lederer A., Lewis J.D., Stark H. Structure of the hepatitis C virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES. Structure 2005, 13:1695-1706.
    • (2005) Structure , vol.13 , pp. 1695-1706
    • Boehringer, D.1    Thermann, R.2    Ostareck-Lederer, A.3    Lewis, J.D.4    Stark, H.5
  • 14
    • 66149118241 scopus 로고    scopus 로고
    • Upstream open reading frames cause wide spread reduction of protein expression and are polymorphic among humans
    • Calvo S.E., Pagliarini D.J., Mootha V.K. Upstream open reading frames cause wide spread reduction of protein expression and are polymorphic among humans. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:7507-7512.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 7507-7512
    • Calvo, S.E.1    Pagliarini, D.J.2    Mootha, V.K.3
  • 15
    • 0032582798 scopus 로고    scopus 로고
    • Site-directed mutagenesis of yeast eEF1A
    • Cavallius J., Merrick W.C. Site-directed mutagenesis of yeast eEF1A. J. Biol. Chem. 1998, 273:28752-28758.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28752-28758
    • Cavallius, J.1    Merrick, W.C.2
  • 16
    • 3042718952 scopus 로고    scopus 로고
    • Biochemical and functional analysis of a 9-nt RNA sequence that affects translation efficiency in eukaryotic cells
    • Chappell S.A., Edelman G.M., Mauro V.P. Biochemical and functional analysis of a 9-nt RNA sequence that affects translation efficiency in eukaryotic cells. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:9590-9594.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9590-9594
    • Chappell, S.A.1    Edelman, G.M.2    Mauro, V.P.3
  • 17
    • 33745453438 scopus 로고    scopus 로고
    • Ribosomal shunting mediated by a translational enhancer element that base pairs to 18S rRNA
    • Chappell S.A., Dresios J., Edelman G.M., Mauro V.P. Ribosomal shunting mediated by a translational enhancer element that base pairs to 18S rRNA. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:9488-9493.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9488-9493
    • Chappell, S.A.1    Dresios, J.2    Edelman, G.M.3    Mauro, V.P.4
  • 18
    • 34347348110 scopus 로고    scopus 로고
    • Cytoplasmic and mitochondrial protein translation in axonal and dendritic terminal arboization
    • Chihara T., Luginbuhl D., Luo L. Cytoplasmic and mitochondrial protein translation in axonal and dendritic terminal arboization. Nat. Neurosci. 2007, 10:828-837.
    • (2007) Nat. Neurosci. , vol.10 , pp. 828-837
    • Chihara, T.1    Luginbuhl, D.2    Luo, L.3
  • 19
    • 0032510912 scopus 로고    scopus 로고
    • Promotion of met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast
    • Choi S.K., Lee J.H., Zoll W.L., Merrick W.C., Dever T.E. Promotion of met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast. Science 1998, 280:1757-1760.
    • (1998) Science , vol.280 , pp. 1757-1760
    • Choi, S.K.1    Lee, J.H.2    Zoll, W.L.3    Merrick, W.C.4    Dever, T.E.5
  • 20
    • 79953688726 scopus 로고    scopus 로고
    • The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1
    • Daugeron M.C., Prouteau M., Lacroute F., Seraphin B. The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1. Nucleic Acids Res. 2011, 39:2221-2233.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2221-2233
    • Daugeron, M.C.1    Prouteau, M.2    Lacroute, F.3    Seraphin, B.4
  • 21
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever T.E., Feng L., Wek R.C., Cigan A.M., Donahue T.F., Hinnebusch A.G. Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 1992, 68:585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.F.5    Hinnebusch, A.G.6
  • 22
    • 34347326163 scopus 로고    scopus 로고
    • Efficient translation initiation directed by the 900-nucleotide and GC-rich 5' untranslated region of the human retroposon LINE-1 mRNA is strictly cap-dependent rather than internal ribosome entry site mediated
    • Dmitriev S.E., et al. Efficient translation initiation directed by the 900-nucleotide and GC-rich 5' untranslated region of the human retroposon LINE-1 mRNA is strictly cap-dependent rather than internal ribosome entry site mediated. Mol. Cell. Biol. 2007, 27:4685-4697.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4685-4697
    • Dmitriev, S.E.1
  • 23
    • 77956245342 scopus 로고    scopus 로고
    • GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor
    • Dmitriev S.E., et al. GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor. J. Biol. Chem. 2010, 285:26779-26787.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26779-26787
    • Dmitriev, S.E.1
  • 25
    • 36749042932 scopus 로고    scopus 로고
    • Translation initiation by cellular internal ribosome entry sites
    • Cold Spring Harbor Press, Cold Spring Harbor, New York, N. Sonenberg, J.W.H. Hershey, M. Matthews (Eds.)
    • Elroy-Stein O., Merrick W.C. Translation initiation by cellular internal ribosome entry sites. Translational Control in Biology and Medicine 2007, 155-172. Cold Spring Harbor Press, Cold Spring Harbor, New York. N. Sonenberg, J.W.H. Hershey, M. Matthews (Eds.).
    • (2007) Translational Control in Biology and Medicine , pp. 155-172
    • Elroy-Stein, O.1    Merrick, W.C.2
  • 26
    • 1642570293 scopus 로고    scopus 로고
    • A nascent polypeptide domain that can regulate translation elongation
    • Fang P., Spevak C.C., Wu C., Sachs M.S. A nascent polypeptide domain that can regulate translation elongation. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:4059-4064.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4059-4064
    • Fang, P.1    Spevak, C.C.2    Wu, C.3    Sachs, M.S.4
  • 27
    • 66849089596 scopus 로고    scopus 로고
    • Toward a structural understanding of IRES RNA function
    • Filbin M.E., Kieft J.S. Toward a structural understanding of IRES RNA function. Curr. Opin. Struct. Biol. 2009, 19:267-276.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 267-276
    • Filbin, M.E.1    Kieft, J.S.2
  • 28
    • 0027318243 scopus 로고
    • Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA
    • Futterer J., Kiss-Laszlo Z., Hohn T. Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA. Cell 1993, 73:789-802.
    • (1993) Cell , vol.73 , pp. 789-802
    • Futterer, J.1    Kiss-Laszlo, Z.2    Hohn, T.3
  • 29
    • 77956548291 scopus 로고    scopus 로고
    • Alternate ways to think about cellular internal ribosome entry
    • Gilbert W.V. Alternate ways to think about cellular internal ribosome entry. J. Biol. Chem. 2010, 285:29033-29038.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29033-29038
    • Gilbert, W.V.1
  • 30
    • 79952453456 scopus 로고    scopus 로고
    • Functional specialization of ribosomes?
    • Gilbert W.V. Functional specialization of ribosomes?. Trends Biochem. Sci. 2011, 36:127-132.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 127-132
    • Gilbert, W.V.1
  • 31
    • 34548535363 scopus 로고    scopus 로고
    • Cap-independent translation is required for starvation-induced differentiation in yeast
    • Gilbert W.V., Zhou K., Butler T.K., Doudna J.A. Cap-independent translation is required for starvation-induced differentiation in yeast. Science 2007, 317:1224-1227.
    • (2007) Science , vol.317 , pp. 1224-1227
    • Gilbert, W.V.1    Zhou, K.2    Butler, T.K.3    Doudna, J.A.4
  • 32
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • Glisovic T., Bachorik J.L., Yong J., Dreyfuss G. RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett. 2008, 582:1977-1986.
    • (2008) FEBS Lett. , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 33
    • 0021270173 scopus 로고
    • RNA-stimulated ATPase activity of eukaryotic initiation factors
    • Grifo J.A., Abramson R.D., Satler C.A., Merrick W.C. RNA-stimulated ATPase activity of eukaryotic initiation factors. J. Biol. Chem. 1984, 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
  • 34
    • 1842335136 scopus 로고    scopus 로고
    • Translation of an uncapped mRNA involves scanning
    • Gunnery S., Maivali U., Mathews M.B. Translation of an uncapped mRNA involves scanning. J. Biol. Chem. 1997, 272:21642-21646.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21642-21646
    • Gunnery, S.1    Maivali, U.2    Mathews, M.B.3
  • 35
    • 79960236176 scopus 로고    scopus 로고
    • The putative RNA helicase HELZ promotes cell proliferation, translation initiation and ribosomal protein S6 phosphorylation
    • Hasgall P.A., Hoogewijs D., Faza M.B., Panse V.G., Wenger R.H., Camenisch G. The putative RNA helicase HELZ promotes cell proliferation, translation initiation and ribosomal protein S6 phosphorylation. PLoS One 2011, 6(7):e22107.
    • (2011) PLoS One , vol.6 , Issue.7
    • Hasgall, P.A.1    Hoogewijs, D.2    Faza, M.B.3    Panse, V.G.4    Wenger, R.H.5    Camenisch, G.6
  • 36
    • 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., Parker R. The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol. Cell 2011, 43:962-972.
    • (2011) Mol. Cell , vol.43 , pp. 962-972
    • Hilliker, A.1    Gao, Z.2    Jankowsky, E.3    Parker, R.4
  • 37
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • Hinnebusch A.G. Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol. Mol. Biol. Rev. 2011, 75:434-467.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 38
    • 0032903304 scopus 로고    scopus 로고
    • A phylogenetically conserved stem-loop structure at the 5' border of the internal ribosome entry site of hepatitis C virus is required for cap-independent viral translation
    • Honda M., Beard M.R., Ping L.H., Lemon S.M. A phylogenetically conserved stem-loop structure at the 5' border of the internal ribosome entry site of hepatitis C virus is required for cap-independent viral translation. J. Virol. 1999, 73:1165-1174.
    • (1999) J. Virol. , vol.73 , pp. 1165-1174
    • Honda, M.1    Beard, M.R.2    Ping, L.H.3    Lemon, S.M.4
  • 39
    • 17044409660 scopus 로고    scopus 로고
    • UAUG and uORFs in human and rodent 5' untranslated mRNAs
    • Iacono M., Mignone F., Pesole G. uAUG and uORFs in human and rodent 5' untranslated mRNAs. Gene 2005, 349:97-105.
    • (2005) Gene , vol.349 , pp. 97-105
    • Iacono, M.1    Mignone, F.2    Pesole, G.3
  • 40
    • 81355153985 scopus 로고    scopus 로고
    • RRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells
    • Jack K., et al. rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells. Mol. Cell 2011, 44:660-666.
    • (2011) Mol. Cell , vol.44 , pp. 660-666
    • Jack, K.1
  • 41
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen C.U., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 2010, 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
  • 42
    • 0035788058 scopus 로고    scopus 로고
    • Initiator Met-tRNA-independent translation mediated by an internal ribosome entry site element in cricket paralysis virus-like insect viruses
    • Jan E., Thompson S.R., Wilson J.E., Pestova T.V., Hellen C.U., Sarnow P. Initiator Met-tRNA-independent translation mediated by an internal ribosome entry site element in cricket paralysis virus-like insect viruses. Cold Spring Harb. Symp. Quant. Biol. 2001, 66:285-292.
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 285-292
    • Jan, E.1    Thompson, S.R.2    Wilson, J.E.3    Pestova, T.V.4    Hellen, C.U.5    Sarnow, P.6
  • 43
    • 0025146035 scopus 로고
    • Cap-independent translation of encephalomyocarditis virus RNA: structural elements of the internal ribosomal entry site and involvement of a cellular 57-kD RNA-binding protein
    • Jang S.K., Wimmer E. Cap-independent translation of encephalomyocarditis virus RNA: structural elements of the internal ribosomal entry site and involvement of a cellular 57-kD RNA-binding protein. Genes Dev. 1990, 9:1560-1572.
    • (1990) Genes Dev. , vol.9 , pp. 1560-1572
    • Jang, S.K.1    Wimmer, E.2
  • 44
    • 10344243545 scopus 로고    scopus 로고
    • Coordinated assembly of human translation initiation complexes by the hepatitis C virus internal ribosome entry site RNA
    • Ji H., Fraser C.S., Yu Y., Leary J., Doudna J.A. Coordinated assembly of human translation initiation complexes by the hepatitis C virus internal ribosome entry site RNA. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:16990-16995.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16990-16995
    • Ji, H.1    Fraser, C.S.2    Yu, Y.3    Leary, J.4    Doudna, J.A.5
  • 45
    • 0033539681 scopus 로고    scopus 로고
    • Identification of eukaryotic mRNAs that are translated at reduced cap binding complex eIF4F concentrations using a cDNA microarray
    • Johannes G., Carter M.S., Eisen M.B., Brown P.O., Sarnow P. Identification of eukaryotic mRNAs that are translated at reduced cap binding complex eIF4F concentrations using a cDNA microarray. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:13118-13123.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13118-13123
    • Johannes, G.1    Carter, M.S.2    Eisen, M.B.3    Brown, P.O.4    Sarnow, P.5
  • 46
    • 79958804665 scopus 로고    scopus 로고
    • EIF2A mediates translation of hepatitis C viral mRNA under stress conditions
    • Kim J.H., Park S.M., Park J.H., Keum S.J., Jang S.K. eIF2A mediates translation of hepatitis C viral mRNA under stress conditions. EMBO J. 2011, 30:2454-2464.
    • (2011) EMBO J. , vol.30 , pp. 2454-2464
    • Kim, J.H.1    Park, S.M.2    Park, J.H.3    Keum, S.J.4    Jang, S.K.5
  • 47
    • 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. 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. 2003, 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
  • 48
    • 21244431682 scopus 로고    scopus 로고
    • Internal ribosome entry sites in cellular mRNAs: mystery of their existence
    • Komar A.A., Hatzoglou M. Internal ribosome entry sites in cellular mRNAs: mystery of their existence. J. Biol. Chem. 2005, 280(25):23425-23428.
    • (2005) J. Biol. Chem. , vol.280 , Issue.25 , pp. 23425-23428
    • Komar, A.A.1    Hatzoglou, M.2
  • 49
    • 79551554217 scopus 로고    scopus 로고
    • Cellular IRES-mediated translation: the war of ITAFs in pathophysiological states
    • Komar A.A., Hatzoglou M. Cellular IRES-mediated translation: the war of ITAFs in pathophysiological states. Cell Cycle 2011, 10:229-240.
    • (2011) Cell Cycle , vol.10 , pp. 229-240
    • Komar, A.A.1    Hatzoglou, M.2
  • 50
    • 0037416198 scopus 로고    scopus 로고
    • Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells
    • Komar A.A., Lesnik T., Cullin C., Merrick W.C., Trachsel H., Altmann M. Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells. EMBO J. 2003, 22:1199-1209.
    • (2003) EMBO J. , vol.22 , pp. 1199-1209
    • Komar, A.A.1    Lesnik, T.2    Cullin, C.3    Merrick, W.C.4    Trachsel, H.5    Altmann, M.6
  • 51
    • 18144363165 scopus 로고    scopus 로고
    • Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae initiation factor eIF2A
    • Komar A.A., et al. Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae initiation factor eIF2A. J. Biol. Chem. 2005, 280:15601-15611.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15601-15611
    • Komar, A.A.1
  • 52
    • 0028914004 scopus 로고
    • Adherence to the first-AUG rule when a second AUG codon follows closely upon the first
    • Kozak M. Adherence to the first-AUG rule when a second AUG codon follows closely upon the first. Proc. Natl. Acad. Sci. U. S. A. 1984, 92:2662-2666.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2662-2666
    • Kozak, M.1
  • 53
    • 0021760394 scopus 로고
    • Selection of initiation sites by eukaryotic ribosomes: effect of inserting AUG triplets upstream from the coding sequence for preproinsulin
    • Kozak M. Selection of initiation sites by eukaryotic ribosomes: effect of inserting AUG triplets upstream from the coding sequence for preproinsulin. Nucleic Acids Res. 1984, 12:3873-3893.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3873-3893
    • Kozak, M.1
  • 54
    • 0021239085 scopus 로고
    • Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo
    • Kozak M. Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo. Nature 1984, 308:241-246.
    • (1984) Nature , vol.308 , pp. 241-246
    • Kozak, M.1
  • 55
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translatin by eukaryotic ribosomes
    • Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translatin by eukaryotic ribosomes. Cell 1986, 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 56
    • 0024414469 scopus 로고
    • Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs
    • Kozak M. Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs. Mol. Cell. Biol. 1989, 11:5134-5142.
    • (1989) Mol. Cell. Biol. , vol.11 , pp. 5134-5142
    • Kozak, M.1
  • 57
    • 0025107694 scopus 로고
    • Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes
    • Kozak M. Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:8301-8305.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 8301-8305
    • Kozak, M.1
  • 58
    • 0242285647 scopus 로고    scopus 로고
    • Alternative ways to think about mRNA sequences and proteins that appear to promote internal initiation of translation
    • Kozak M. Alternative ways to think about mRNA sequences and proteins that appear to promote internal initiation of translation. Gene 2003, 318:1-23.
    • (2003) Gene , vol.318 , pp. 1-23
    • Kozak, M.1
  • 59
    • 29144444289 scopus 로고    scopus 로고
    • A second look at cellular mRNA sequences said to function as internal ribosome entry sites
    • Kozak M. A second look at cellular mRNA sequences said to function as internal ribosome entry sites. Nucleic Acids Res. 2005, 33:6593-6602.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6593-6602
    • Kozak, M.1
  • 60
    • 72549101167 scopus 로고    scopus 로고
    • RPS25 is essential for translation initiation by the dicistroviridae and hepatitis C viral IRESs
    • Landry D.M., Hertz M.I., Thompson R.R. RPS25 is essential for translation initiation by the dicistroviridae and hepatitis C viral IRESs. Genes Dev. 2009, 23:2753-2764.
    • (2009) Genes Dev. , vol.23 , pp. 2753-2764
    • Landry, D.M.1    Hertz, M.I.2    Thompson, R.R.3
  • 61
    • 0035851192 scopus 로고    scopus 로고
    • Polyamine regulation of ribosome pausing at the upstream open reading frame of S-adenosylmethionine decarboxylase
    • Law G.L., Raney A., Heusner C., Morris D.R. Polyamine regulation of ribosome pausing at the upstream open reading frame of S-adenosylmethionine decarboxylase. J. Biol. Chem. 2001, 276:38036-38043.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38036-38043
    • Law, G.L.1    Raney, A.2    Heusner, C.3    Morris, D.R.4
  • 62
    • 0020265917 scopus 로고
    • Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus
    • Lee K.A., Sonenberg N. Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:3447-3451.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3447-3451
    • Lee, K.A.1    Sonenberg, N.2
  • 63
    • 39149111540 scopus 로고    scopus 로고
    • For IRES trans-acting factors, it is all about location
    • Lewis S.M., Holcik M. For IRES trans-acting factors, it is all about location. Oncogene 2008, 27:1033-1035.
    • (2008) Oncogene , vol.27 , pp. 1033-1035
    • Lewis, S.M.1    Holcik, M.2
  • 64
    • 2442591621 scopus 로고    scopus 로고
    • Capped mRNA with a single nucleotide leader is optimally translated in a primitive eukaryote, Giardia lamblia
    • Li L., Wang C.C. Capped mRNA with a single nucleotide leader is optimally translated in a primitive eukaryote, Giardia lamblia. J. Biol. Chem. 2004, 279:14656-14664.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14656-14664
    • Li, L.1    Wang, C.C.2
  • 65
    • 0023056875 scopus 로고
    • Secondary structure model for mouse beta Maj globin mRNA derived from enzymatic digestion data, comparative sequence and computer analysis
    • Lockard R.E., Currey K., Browner M., Lawrence C., Maizel J. Secondary structure model for mouse beta Maj globin mRNA derived from enzymatic digestion data, comparative sequence and computer analysis. Nucleic Acids Res. 1986, 14:5827-5841.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5827-5841
    • Lockard, R.E.1    Currey, K.2    Browner, M.3    Lawrence, C.4    Maizel, J.5
  • 66
    • 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. 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. 2000, 20:6019-6029.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6019-6029
    • Lomakin, I.B.1    Hellen, C.U.2    Pestova, T.V.3
  • 67
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu P.D., Harding H.P., Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J. Cell Biol. 2004, 167:27-33.
    • (2004) J. Cell Biol. , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 68
    • 59749085225 scopus 로고    scopus 로고
    • Structure and function of HCV IRES domains
    • Lukavsky P.J. Structure and function of HCV IRES domains. Virus Res. 2009, 139:166-171.
    • (2009) Virus Res. , vol.139 , pp. 166-171
    • Lukavsky, P.J.1
  • 72
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick W.C. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 1992, 56:291-315.
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 73
    • 0348134941 scopus 로고    scopus 로고
    • Initiation of protein biosynthesis in eukaryotes
    • Merrick W.C. Initiation of protein biosynthesis in eukaryotes. Biochem. Mol. Biol. Educ. 2003, 31:378-385.
    • (2003) Biochem. Mol. Biol. Educ. , vol.31 , pp. 378-385
    • Merrick, W.C.1
  • 74
    • 2442466927 scopus 로고    scopus 로고
    • Cap-dependent and cap-independent translation in eukaryotic systems
    • Merrick W.C. Cap-dependent and cap-independent translation in eukaryotic systems. Gene 2004, 332:1-11.
    • (2004) Gene , vol.332 , pp. 1-11
    • Merrick, W.C.1
  • 75
    • 77954356006 scopus 로고    scopus 로고
    • Eukaryotic protein synthesis: still a mystery
    • Merrick W.C. Eukaryotic protein synthesis: still a mystery. J. Biol. Chem. 2010, 285:21197-21201.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21197-21201
    • Merrick, W.C.1
  • 76
    • 0016658724 scopus 로고
    • Purification and characterization of homogeneous protein synthesis initiation factor M1 from rabbit reticulocytes
    • Merrick W.C., Anderson W.F. Purification and characterization of homogeneous protein synthesis initiation factor M1 from rabbit reticulocytes. J. Biol. Chem. 1975, 250:1197-1206.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1197-1206
    • Merrick, W.C.1    Anderson, W.F.2
  • 77
    • 0022512237 scopus 로고
    • Multiple upstream AUG codons mediate translational control of GCN4
    • Meuller P.P., Hinnebusch A.G. Multiple upstream AUG codons mediate translational control of GCN4. Cell 1986, 45:201-207.
    • (1986) Cell , vol.45 , pp. 201-207
    • Meuller, P.P.1    Hinnebusch, A.G.2
  • 78
    • 37749006919 scopus 로고    scopus 로고
    • The amazing diversity of cap-independent translation elements in the 3'-untranslated regions of plant viral RNAs
    • Miller W.A., Wang Z., Treder K. The amazing diversity of cap-independent translation elements in the 3'-untranslated regions of plant viral RNAs. Biochem. Soc. Trans. 2007, 35:1629-1633.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1629-1633
    • Miller, W.A.1    Wang, Z.2    Treder, K.3
  • 79
    • 0032536842 scopus 로고    scopus 로고
    • Complex organization of the 5'-end of the humane glycine tRNA synthetase gene
    • Mudge S., Williams J., Sutherland G., Cowan P., Power D. Complex organization of the 5'-end of the humane glycine tRNA synthetase gene. Gene 1998, 209:45-50.
    • (1998) Gene , vol.209 , pp. 45-50
    • Mudge, S.1    Williams, J.2    Sutherland, G.3    Cowan, P.4    Power, D.5
  • 80
    • 76049108205 scopus 로고    scopus 로고
    • The helicase protein DHX29 promotes translation initiation, cell proliferation and tumorigenesis
    • Parsyan A., et al. The helicase protein DHX29 promotes translation initiation, cell proliferation and tumorigenesis. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:22217-22222.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22217-22222
    • Parsyan, A.1
  • 81
    • 31144443606 scopus 로고    scopus 로고
    • The autoregulatory translation control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex
    • Patel G.P., Ma S., Bag J. The autoregulatory translation control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex. Nucleic Acids Res. 2005, 33:7074-7089.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 7074-7089
    • Patel, G.P.1    Ma, S.2    Bag, J.3
  • 82
    • 0021799353 scopus 로고
    • Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency
    • Pelletier J., Sonenberg N. Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell 1985, 40:515-526.
    • (1985) Cell , vol.40 , pp. 515-526
    • Pelletier, J.1    Sonenberg, N.2
  • 83
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J., Sonenberg N. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 1988, 334:320-325.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 84
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic intiation factors determine initiation of translation by internal ribosomal entry
    • Pestova T.V., Hellen C.U., Shatsky I.N. Canonical eukaryotic intiation factors determine initiation of translation by internal ribosomal entry. Mol. Cell. Biol. 1996, 16:6859-6869.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 85
    • 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. 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. 1998, 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
  • 86
    • 41949130892 scopus 로고    scopus 로고
    • EIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II
    • Pestova T.V., de Breyne S., Pisarev A.V., Abaeva I.S., Hellen C.U. eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II. EMBO J. 2008, 27:1060-1072.
    • (2008) EMBO J. , vol.27 , pp. 1060-1072
    • Pestova, T.V.1    de Breyne, S.2    Pisarev, A.V.3    Abaeva, I.S.4    Hellen, C.U.5
  • 87
    • 33845335508 scopus 로고    scopus 로고
    • Structural basis for ribosome recruitment and manipulation by a viral IRES RNA
    • Pfingsten J.S., Costantino D.A., Kieft J.S. Structural basis for ribosome recruitment and manipulation by a viral IRES RNA. Science 2006, 314:1450-1454.
    • (2006) Science , vol.314 , pp. 1450-1454
    • Pfingsten, J.S.1    Costantino, D.A.2    Kieft, J.S.3
  • 88
    • 38449123748 scopus 로고    scopus 로고
    • Assembly and analysis of eukaryotic translation initiation complexes
    • Pisarev A.V., Unbehaun A., Hellen C.U., Pestova T.V. Assembly and analysis of eukaryotic translation initiation complexes. Methods Enzymol. 2007, 430:147-177.
    • (2007) Methods Enzymol. , vol.430 , pp. 147-177
    • Pisarev, A.V.1    Unbehaun, A.2    Hellen, C.U.3    Pestova, T.V.4
  • 89
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 5' UTRs requires DExH-box protein DhX29
    • Pisareva V.P., Pisarev A.V., Komar A.A., Hellen C.U., Pestova T.V. Translation initiation on mammalian mRNAs with structured 5' UTRs requires DExH-box protein DhX29. Cell 2008, 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
  • 90
    • 79953035983 scopus 로고    scopus 로고
    • Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs
    • Ranji A., Shkriabai N., Kyaratskhelia M., Musier-Forsyth K., Boris-Lawrie K. Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs. J. Biol. Chem. 2011, 286:5328-5337.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5328-5337
    • Ranji, A.1    Shkriabai, N.2    Kyaratskhelia, M.3    Musier-Forsyth, K.4    Boris-Lawrie, K.5
  • 91
    • 36749050097 scopus 로고    scopus 로고
    • Singnaling to translation initiation
    • Cold Spring Harbor Press, Cold Spring Harbor, NY, M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.)
    • Raught B., Gingras A.-C. Singnaling to translation initiation. Translational Control in Biology and Medicine 2007, 369-400. Cold Spring Harbor Press, Cold Spring Harbor, NY. M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.).
    • (2007) Translational Control in Biology and Medicine , pp. 369-400
    • Raught, B.1    Gingras, A.-C.2
  • 92
    • 80053914855 scopus 로고    scopus 로고
    • Translation without eIF2 promoted by poliovirus 2A protease
    • Redondo N., Sanz M.A., Welnowska E., Carrasco L. Translation without eIF2 promoted by poliovirus 2A protease. PLoS One 2011, 6:e25699.
    • (2011) PLoS One , vol.6
    • Redondo, N.1    Sanz, M.A.2    Welnowska, E.3    Carrasco, L.4
  • 93
    • 73249129769 scopus 로고    scopus 로고
    • Characterization of the functional role of nucleotides within the URE2 IRES element and the requirements for eIF2A-mediated repression
    • Reineke L.C., Merrick W.C. Characterization of the functional role of nucleotides within the URE2 IRES element and the requirements for eIF2A-mediated repression. RNA 2009, 15:2264-2277.
    • (2009) RNA , vol.15 , pp. 2264-2277
    • Reineke, L.C.1    Merrick, W.C.2
  • 94
    • 49649116679 scopus 로고    scopus 로고
    • A small stem loop element directs internal initiation of the URE2 internal ribosome entry site in Saccharomyces cerevisiae
    • Reineke L.C., Komar A.A., Caprara M.G., Merrick W.C. A small stem loop element directs internal initiation of the URE2 internal ribosome entry site in Saccharomyces cerevisiae. J. Biol. Chem. 2008, 283:19011-19025.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19011-19025
    • Reineke, L.C.1    Komar, A.A.2    Caprara, M.G.3    Merrick, W.C.4
  • 96
    • 33750532939 scopus 로고    scopus 로고
    • i ternary complex availability
    • i ternary complex availability. Mol. Biol. Cell 2006, 17:4632-4644.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4632-4644
    • Robert, F.1
  • 97
    • 33845361023 scopus 로고    scopus 로고
    • Structure of the ribosome-bound cricket paralysis virus IRES RNA
    • Schüler M., et al. Structure of the ribosome-bound cricket paralysis virus IRES RNA. Nat. Struct. Mol. Biol. 2006, 13:1092-1096.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1092-1096
    • Schüler, M.1
  • 98
    • 78650427660 scopus 로고    scopus 로고
    • Cap- and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs
    • Shatsky I.N., Dmitriev S.E., Terenin I.M., Andreev D.E. Cap- and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs. Mol. Cell 2010, 30:285-293.
    • (2010) Mol. Cell , vol.30 , pp. 285-293
    • Shatsky, I.N.1    Dmitriev, S.E.2    Terenin, I.M.3    Andreev, D.E.4
  • 99
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 100
    • 0035831269 scopus 로고    scopus 로고
    • Hepatitis C virus IRES RNA-induced changes in the conformation of the 40S ribosomal subunit
    • Spahn C.M., et al. Hepatitis C virus IRES RNA-induced changes in the conformation of the 40S ribosomal subunit. Science 2001, 291:1959-1962.
    • (2001) Science , vol.291 , pp. 1959-1962
    • Spahn, C.M.1
  • 101
    • 4644247805 scopus 로고    scopus 로고
    • Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor
    • Spahn C.M., Jan E., Mulder A., Grassucci R.A., Sarnow P., Frank J. Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor. Cell 2004, 118:465-475.
    • (2004) Cell , vol.118 , pp. 465-475
    • Spahn, C.M.1    Jan, E.2    Mulder, A.3    Grassucci, R.A.4    Sarnow, P.5    Frank, J.6
  • 102
    • 20044389169 scopus 로고    scopus 로고
    • Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors
    • Spriggs K.A., Bushell M., Mitchell S.A., Willis A.E. Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors. Cell Death Differ. 2005, 12:585-591.
    • (2005) Cell Death Differ. , vol.12 , pp. 585-591
    • Spriggs, K.A.1    Bushell, M.2    Mitchell, S.A.3    Willis, A.E.4
  • 103
    • 79958769095 scopus 로고    scopus 로고
    • Non-conventional sources of peptides presented by MHC class 1
    • Starck S.R., Shastri N. Non-conventional sources of peptides presented by MHC class 1. Cell. Mol. Life Sci. 2011, 68:1471-1479.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1471-1479
    • Starck, S.R.1    Shastri, N.2
  • 104
    • 54949134074 scopus 로고    scopus 로고
    • A distinct translation initation mechanism generates cryptic peptides for immune surveillance
    • Starck S.R., et al. A distinct translation initation mechanism generates cryptic peptides for immune surveillance. PLoS One 2008, 3:e3460.
    • (2008) PLoS One , vol.3
    • Starck, S.R.1
  • 105
    • 78649747797 scopus 로고    scopus 로고
    • Elucidating mechanistic principles underpinning eukaryotic translation initiation using quantitative fluorescence methods
    • Stevenson A.L., Juanes P.P., McCarthy J.E. Elucidating mechanistic principles underpinning eukaryotic translation initiation using quantitative fluorescence methods. Biochem. Soc. Trans. 2010, 38:1587-1592.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1587-1592
    • Stevenson, A.L.1    Juanes, P.P.2    McCarthy, J.E.3
  • 106
    • 84855863141 scopus 로고    scopus 로고
    • IRES-mediated translation of cellular messenger RNA operates in eIF2{alpha}-independent manner during stress
    • Thakor N., Holcik M. IRES-mediated translation of cellular messenger RNA operates in eIF2{alpha}-independent manner during stress. Nucleic Acids Res. 2011, 40:541-552.
    • (2011) Nucleic Acids Res. , vol.40 , pp. 541-552
    • Thakor, N.1    Holcik, M.2
  • 107
    • 0035818467 scopus 로고    scopus 로고
    • Internal initiation in Saccharomyces cerevisiae mediated by an initiator tRNA/eIF-2 independent internal ribosome entry site element
    • Thompson S.R., Gulyas K.D., Sarnow P. Internal initiation in Saccharomyces cerevisiae mediated by an initiator tRNA/eIF-2 independent internal ribosome entry site element. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:12972-12977.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12972-12977
    • Thompson, S.R.1    Gulyas, K.D.2    Sarnow, P.3
  • 108
    • 1242303422 scopus 로고    scopus 로고
    • Demonstrating internal ribosome entry sites in eukaryotic mRNAs using stringent RNA test procedures
    • Van Eden M.E., Byrd M.P., Sherrill K.W., Lloyd R.E. Demonstrating internal ribosome entry sites in eukaryotic mRNAs using stringent RNA test procedures. RNA 2004, 10:720-730.
    • (2004) RNA , vol.10 , pp. 720-730
    • Van Eden, M.E.1    Byrd, M.P.2    Sherrill, K.W.3    Lloyd, R.E.4
  • 109
    • 29944433224 scopus 로고    scopus 로고
    • Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR
    • Ventoso I., Sanz M.A., Molina S., Berlanga J.J., Carrasco L., Esteban M. Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR. Genes Dev. 2006, 20:87-100.
    • (2006) Genes Dev. , vol.20 , pp. 87-100
    • Ventoso, I.1    Sanz, M.A.2    Molina, S.3    Berlanga, J.J.4    Carrasco, L.5    Esteban, M.6
  • 110
    • 80052931005 scopus 로고    scopus 로고
    • Cryptic AUG is important for 48S ribosomal assembly during internal initiation of translation of coxsackievirus B3 RNA
    • Verma B., Ponnuswamy A., Gnanasundram S.V., Das S. Cryptic AUG is important for 48S ribosomal assembly during internal initiation of translation of coxsackievirus B3 RNA. J. Gen. Virol. 2011, 92:2310-2319.
    • (2011) J. Gen. Virol. , vol.92 , pp. 2310-2319
    • Verma, B.1    Ponnuswamy, A.2    Gnanasundram, S.V.3    Das, S.4
  • 111
    • 80052287098 scopus 로고    scopus 로고
    • Poliovirus switches to an eIF2-independent mode of translation during infection
    • White J.P., Reineke L.C., Lloyd R.E. Poliovirus switches to an eIF2-independent mode of translation during infection. J. Virol. 2011, 85:8884-8893.
    • (2011) J. Virol. , vol.85 , pp. 8884-8893
    • White, J.P.1    Reineke, L.C.2    Lloyd, R.E.3
  • 112
    • 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. Initiation of protein synthesis from the A site of the ribosome. Cell 2000, 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
  • 113
    • 76549116230 scopus 로고    scopus 로고
    • Strong eukaryotic IRESs have weak secondary structure
    • Xia X., Holcik M. Strong eukaryotic IRESs have weak secondary structure. PLoS One 2009, 4:e4136.
    • (2009) PLoS One , vol.4
    • Xia, X.1    Holcik, M.2
  • 114
    • 80054004461 scopus 로고    scopus 로고
    • Translation initiation: a regulatory role for poly(A) tracts in front of the AUG codon in Saccharomycves cerevisiae
    • Xia X., et al. Translation initiation: a regulatory role for poly(A) tracts in front of the AUG codon in Saccharomycves cerevisiae. Genetics 2011, 189:469-478.
    • (2011) Genetics , vol.189 , pp. 469-478
    • Xia, X.1
  • 115
    • 0037229799 scopus 로고    scopus 로고
    • A Shine-Delgarno-like sequence mediates in vitro ribosomal internal entry and subsequent scanning for translation initiation of coxsackievirus B3 RNA
    • Yang D., et al. A Shine-Delgarno-like sequence mediates in vitro ribosomal internal entry and subsequent scanning for translation initiation of coxsackievirus B3 RNA. Virology 2003, 305:31-43.
    • (2003) Virology , vol.305 , pp. 31-43
    • Yang, D.1
  • 116
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita
    • Yoon A., et al. Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita. Science 2006, 312:902-906.
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1
  • 117
    • 79959452628 scopus 로고    scopus 로고
    • Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors
    • Yu Y., Abaeva I.S., Marintchev A., Pestova T.V., Hellen C.U. Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors. Nucleic Acids Res. 2011, 39:4851-4865.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4851-4865
    • Yu, Y.1    Abaeva, I.S.2    Marintchev, A.3    Pestova, T.V.4    Hellen, C.U.5
  • 118
    • 0029785142 scopus 로고    scopus 로고
    • Selective translation initiation by ribosome jumping in adenovirus-infected and heat shocked cells
    • Yueh A., Schneider R.J. Selective translation initiation by ribosome jumping in adenovirus-infected and heat shocked cells. Genes Dev. 1996, 10:1557-1567.
    • (1996) Genes Dev. , vol.10 , pp. 1557-1567
    • Yueh, A.1    Schneider, R.J.2
  • 119
    • 0034090845 scopus 로고    scopus 로고
    • Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA
    • Yueh A., Schneider R.J. Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA. Genes Dev. 2000, 14:414-421.
    • (2000) Genes Dev. , vol.14 , pp. 414-421
    • Yueh, A.1    Schneider, R.J.2
  • 121
    • 0037020244 scopus 로고    scopus 로고
    • Characterization of mammalian eIF2A and identification of the yeast homolog
    • Zoll W.L., Horton L.E., Komar A.A., Hensold J.O., Merrick W.C. Characterization of mammalian eIF2A and identification of the yeast homolog. J. Biol. Chem. 2002, 277:37079-37087.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37079-37087
    • Zoll, W.L.1    Horton, L.E.2    Komar, A.A.3    Hensold, J.O.4    Merrick, W.C.5
  • 122
    • 78651105614 scopus 로고    scopus 로고
    • Non-ATG-initiated translation directed by microsatellite expansions
    • Zu T., et al. Non-ATG-initiated translation directed by microsatellite expansions. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:260-265.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 260-265
    • Zu, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.