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Volumn 14, Issue 4, 2010, Pages 241-253

The role of internal ribosome entry site (IRES) in the initiation of translation;Le rôle des IRES dans l'initiation de la traduction

Author keywords

Cap; Cellular IRES; mRNA; Ribosome; Translation initiation; Viral IRES

Indexed keywords

CELL PROTEIN; MESSENGER RNA;

EID: 77955617241     PISSN: 12678694     EISSN: 19506961     Source Type: Journal    
DOI: 10.1684/vir.2010.0312     Document Type: Review
Times cited : (2)

References (59)
  • 1
    • 0034731347 scopus 로고    scopus 로고
    • Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1
    • Korneeva NL, Lamphear BJ, Hennigan FL, Rhoads RE. Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J Biol Chem 2000; 275: 41369-76.
    • (2000) J Biol Chem , vol.275 , pp. 41369-41376
    • Korneeva, N.L.1    Lamphear, B.J.2    Hennigan, F.L.3    Rhoads, R.E.4
  • 2
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova TV, Hellen CU, Shatsky IN. Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol Cell Biol 1996; 16: 6859-69.
    • (1996) Mol Cell Biol , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 3
    • 0023660877 scopus 로고
    • At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells
    • Kozak M. At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J Mol Biol 1987; 196: 947-50.
    • (1987) J Mol Biol , vol.196 , pp. 947-950
    • Kozak, M.1
  • 4
    • 33644779804 scopus 로고    scopus 로고
    • Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • Pisarev AV, Kolupaeva VG, Pisareva VP, Merrick WC, Hellen CU, Pestova TV. Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev 2006; 20: 624-36.
    • (2006) Genes Dev , vol.20 , pp. 624-636
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Pisareva, V.P.3    Merrick, W.C.4    Hellen, C.U.5    Pestova, T.V.6
  • 5
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • Kapp LD, Lorsch JR. The molecular mechanics of eukaryotic translation. Annu Rev Biochem 2004; 73: 657-704.
    • (2004) Annu Rev Biochem , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 6
    • 0035816596 scopus 로고    scopus 로고
    • Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein
    • Williams DD, Price NT, Loughlin AJ, Proud CG. Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein. J Biol Chem 2001; 276: 24697-703.
    • (2001) J Biol Chem , vol.276 , pp. 24697-24703
    • Williams, D.D.1    Price, N.T.2    Loughlin, A.J.3    Proud, C.G.4
  • 7
    • 35348815020 scopus 로고    scopus 로고
    • Recycling of eukaryotic postter-mination ribosomal complexes
    • Pisarev AV, Hellen CU, Pestova TV. Recycling of eukaryotic postter-mination ribosomal complexes. Cell 2007; 131: 286-99.
    • (2007) Cell , vol.131 , pp. 286-299
    • Pisarev, A.V.1    Hellen, C.U.2    Pestova, T.V.3
  • 8
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat A, Mader S, Pause A, Sonenberg N. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J 1995; 14: 5701-9.
    • (1995) EMBO J , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 9
    • 0037101945 scopus 로고    scopus 로고
    • Stressful initiations
    • Anderson P, Kedersha N. Stressful initiations. J Cell Sci 2002; 115: 3227-34.
    • (2002) J Cell Sci , vol.115 , pp. 3227-3234
    • Anderson, P.1    Kedersha, N.2
  • 10
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • Pavitt GD, Ramaiah KV, Kimball SR, Hinnebusch AG. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev 1998; 12: 514-26.
    • (1998) Genes Dev , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 11
    • 0031755021 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells
    • Marissen WE, Lloyd RE. Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells. Mol Cell Biol 1998; 18: 7565-74.
    • (1998) Mol Cell Biol , vol.18 , pp. 7565-7574
    • Marissen, W.E.1    Lloyd, R.E.2
  • 12
    • 0033948682 scopus 로고    scopus 로고
    • Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: Characterisation of an internal fragment generated by caspase-3-mediated cleavage
    • Bushell M, Poncet D, Marissen WE, et al. Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: characterisation of an internal fragment generated by caspase-3-mediated cleavage. Cell Death Differ 2000; 7: 628-36.
    • (2000) Cell Death Differ , vol.7 , pp. 628-636
    • Bushell, M.1    Poncet, D.2    Marissen, W.E.3
  • 13
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear BJ, Kirchweger R, Skern T, Rhoads RE. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J Biol Chem 1995; 270: 21975-83.
    • (1995) J Biol Chem , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 14
    • 0029976319 scopus 로고    scopus 로고
    • The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E
    • Ohlmann T, Rau M, Pain VM, Morley SJ. The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E. EMBO J 1996; 15: 1371-82.
    • (1996) EMBO J , vol.15 , pp. 1371-1382
    • Ohlmann, T.1    Rau, M.2    Pain, V.M.3    Morley, S.J.4
  • 15
    • 63049133085 scopus 로고    scopus 로고
    • Mechanisms employed by retroviruses to exploit host factors for translational control of a complicated proteome
    • Bolinger C, Boris-Lawrie K. Mechanisms employed by retroviruses to exploit host factors for translational control of a complicated proteome. Retrovirology 2009; 6: 8.
    • (2009) Retrovirology , vol.6 , pp. 8
    • Bolinger, C.1    Boris-Lawrie, K.2
  • 16
    • 0031037987 scopus 로고    scopus 로고
    • Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins
    • Spotts GD, Patel SV, Xiao Q, Hann SR. Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins. Mol Cell Biol 1997; 17: 1459-68.
    • (1997) Mol Cell Biol , vol.17 , pp. 1459-1468
    • Spotts, G.D.1    Patel, S.V.2    Xiao, Q.3    Hann, S.R.4
  • 17
    • 77949505053 scopus 로고    scopus 로고
    • Expression of the VP2 protein of murine norovirus by a translation termination-reinitiation strategy
    • Napthine S, Lever RA, Powell ML, Jackson RJ, Brown TD, Brierley I. Expression of the VP2 protein of murine norovirus by a translation termination-reinitiation strategy. PLoS One 2009; 4: e8390.
    • (2009) PLoS One , vol.4
    • Napthine, S.1    Lever, R.A.2    Powell, M.L.3    Jackson, R.J.4    Brown, T.D.5    Brierley, I.6
  • 18
    • 0027318243 scopus 로고
    • Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA
    • DOI 10.1016/0092-8674(93)90257-Q
    • Futterer J, Kiss-Laszlo Z, Hohn T. Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA. Cell 1993; 73: 789-802. (Pubitemid 23159016)
    • (1993) Cell , vol.73 , Issue.4 , pp. 789-802
    • Futterer, J.1    Kiss-Laszio, Z.2    Hohn, T.3
  • 19
    • 17444389700 scopus 로고    scopus 로고
    • Regulation of translation by ribosome shunting through phosphotyrosine-dependent coupling of adenovirus protein 100k to viral mRNAs
    • Xi Q, Cuesta R, Schneider RJ. Regulation of translation by ribosome shunting through phosphotyrosine-dependent coupling of adenovirus protein 100k to viral mRNAs. J Virol 2005; 79: 5676-83.
    • (2005) J Virol , vol.79 , pp. 5676-5683
    • Xi, Q.1    Cuesta, R.2    Schneider, R.J.3
  • 20
    • 0034090845 scopus 로고    scopus 로고
    • Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA
    • Yueh A, Schneider RJ. Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA. Genes Dev 2000; 14: 414-21.
    • (2000) Genes Dev , vol.14 , pp. 414-421
    • Yueh, A.1    Schneider, R.J.2
  • 21
    • 0023758546 scopus 로고
    • A segment of the 5? Nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang SK, Krausslich HG, Nicklin MJ, Duke GM, Palmenberg AC, Wimmer E. A segment of the 5? nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J Virol 1988; 62: 2636-43.
    • (1988) J Virol , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 22
    • 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: 320-5.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 23
    • 33644874187 scopus 로고    scopus 로고
    • IRESite: The database of experimentally verified IRES structures
    • Mokrejs M, Vopalensky V, Kolenaty O, et al. IRESite: the database of experimentally verified IRES structures (www.iresite.org). Nucleic Acids Res 2006; 34 (Database issue): D125-D130.
    • (2006) Nucleic Acids Res , vol.34 , Issue.DATABASE ISSUE
    • Mokrejs, M.1    Vopalensky, V.2    Kolenaty, O.3
  • 24
    • 0029437960 scopus 로고
    • Internal initiation of translation in eukaryotes: The picornavirus paradigm and beyond
    • Jackson RJ, Kaminski A. Internal initiation of translation in eukaryotes: the picornavirus paradigm and beyond. RNA 1995; 1: 985-1000.
    • (1995) RNA , vol.1 , pp. 985-1000
    • Jackson, R.J.1    Kaminski, A.2
  • 25
    • 59749095351 scopus 로고    scopus 로고
    • Divergent picornavirus IRES elements
    • Belsham GJ. Divergent picornavirus IRES elements. Virus Res 2009; 139: 183-92.
    • (2009) Virus Res , vol.139 , pp. 183-192
    • Belsham, G.J.1
  • 26
    • 0036237981 scopus 로고    scopus 로고
    • Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation
    • Kieft JS, Zhou K, Grech A, Jubin R, Doudna JA. Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation. Nat Struct Biol 2002; 9: 370-4.
    • (2002) Nat Struct Biol , vol.9 , pp. 370-374
    • Kieft, J.S.1    Zhou, K.2    Grech, A.3    Jubin, R.4    Doudna, J.A.5
  • 27
    • 46549086974 scopus 로고    scopus 로고
    • Viral IRES RNA structures and ribosome interactions
    • Kieft JS. Viral IRES RNA structures and ribosome interactions. Trends Biochem Sci 2008; 33: 274-83.
    • (2008) Trends Biochem Sci , vol.33 , pp. 274-283
    • Kieft, J.S.1
  • 28
    • 0030766564 scopus 로고    scopus 로고
    • Functional involvement of polypyrimidine tract-binding protein in translation initiation complexes with the internal ribosome entry site of foot-and-mouth disease virus
    • Niepmann M, Petersen A, Meyer K, Beck E. Functional involvement of polypyrimidine tract-binding protein in translation initiation complexes with the internal ribosome entry site of foot-and-mouth disease virus. J Virol 1997; 71: 8330-9.
    • (1997) J Virol , vol.71 , pp. 8330-8339
    • Niepmann, M.1    Petersen, A.2    Meyer, K.3    Beck, E.4
  • 29
    • 0034670124 scopus 로고    scopus 로고
    • Translation from the internal ribosome entry site of bovine viral diarrhea virus is independent of the interaction with polypyrimidine tract-binding protein
    • Sanderbrand SA, Tautz N, Thiel HJ, Ochs K, Beck E, Niepmann M. Translation from the internal ribosome entry site of bovine viral diarrhea virus is independent of the interaction with polypyrimidine tract-binding protein. Vet Microbiol 2000; 77: 215-27.
    • (2000) Vet Microbiol , vol.77 , pp. 215-227
    • Sanderbrand, S.A.1    Tautz, N.2    Thiel, H.J.3    Ochs, K.4    Beck, E.5    Niepmann, M.6
  • 30
    • 0024694124 scopus 로고
    • A cellular protein that binds to the 5′-noncoding region of poliovirus RNA: Implications for internal translation initiation
    • Meerovitch K, Pelletier J, Sonenberg N. A cellular protein that binds to the 5′-noncoding region of poliovirus RNA: implications for internal translation initiation. Genes Dev 1989; 3: 1026-34.
    • (1989) Genes Dev , vol.3 , pp. 1026-1034
    • Meerovitch, K.1    Pelletier, J.2    Sonenberg, N.3
  • 31
    • 0033557935 scopus 로고    scopus 로고
    • unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA
    • Hunt SL, Hsuan JJ, Totty N, Jackson RJ. unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes Dev 1999; 13: 437-48.
    • (1999) Genes Dev , vol.13 , pp. 437-448
    • Hunt, S.L.1    Hsuan, J.J.2    Totty, N.3    Jackson, R.J.4
  • 32
    • 3543095590 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein L interacts with the 3′ border of the internal ribosomal entry site of hepatitis C virus
    • Hahm B, Kim YK, Kim JH, Kim TY, Jang SK. Heterogeneous nuclear ribonucleoprotein L interacts with the 3′ border of the internal ribosomal entry site of hepatitis C virus. J Virol 1998; 72: 8782-8.
    • (1998) J Virol , vol.72 , pp. 8782-8788
    • Hahm, B.1    Kim, Y.K.2    Kim, J.H.3    Kim, T.Y.4    Jang, S.K.5
  • 33
    • 0034663980 scopus 로고    scopus 로고
    • A cell cycle-dependent protein serves as a template-specific translation initiation factor
    • Pilipenko EV, Pestova TV, Kolupaeva VG, et al. A cell cycle-dependent protein serves as a template-specific translation initiation factor. Genes Dev 2000; 14: 2028-45.
    • (2000) Genes Dev , vol.14 , pp. 2028-2045
    • Pilipenko, E.V.1    Pestova, T.V.2    Kolupaeva, V.G.3
  • 34
    • 0035877795 scopus 로고    scopus 로고
    • Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus
    • Fukushi S, Okada M, Stahl J, Kageyama T, Hoshino FB, Katayama K. Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus. J Biol Chem 2001; 276: 20824-6.
    • (2001) J Biol Chem , vol.276 , pp. 20824-20826
    • Fukushi, S.1    Okada, M.2    Stahl, J.3    Kageyama, T.4    Hoshino, F.B.5    Katayama, K.6
  • 35
    • 57749173840 scopus 로고    scopus 로고
    • Human initiation factor eIF3 subunit b interacts with HCV IRES RNA through its N-terminal RNA recognition motif
    • Perard J, Rasia R, Medenbach J, et al. Human initiation factor eIF3 subunit b interacts with HCV IRES RNA through its N-terminal RNA recognition motif. FEBS Lett 2009; 583: 70-4.
    • (2009) FEBS Lett , vol.583 , pp. 70-74
    • Perard, J.1    Rasia, R.2    Medenbach, J.3
  • 36
    • 38849172516 scopus 로고    scopus 로고
    • Re-programming of translation following cell stress allows IRES-mediated translation to predominate
    • DOI 10.1042/BC20070098
    • Spriggs KA, Stoneley M, Bushell M, Willis AE. Re-programming of translation following cell stress allows IRES-mediated translation to predominate. Biol Cell 2008; 100: 27-38. (Pubitemid 351201431)
    • (2008) Biology of the Cell , vol.100 , Issue.1 , pp. 27-38
    • Spriggs, K.A.1    Stoneley, M.2    Bushell, M.3    Willis, A.E.4
  • 37
    • 34548535363 scopus 로고    scopus 로고
    • Cap-independent translation is required for starvation-induced differentiation in yeast
    • Gilbert WV, Zhou K, Butler TK, Doudna JA. Cap-independent translation is required for starvation-induced differentiation in yeast. Science 2007; 317: 1224-7.
    • (2007) Science , vol.317 , pp. 1224-1227
    • Gilbert, W.V.1    Zhou, K.2    Butler, T.K.3    Doudna, J.A.4
  • 38
    • 0025883162 scopus 로고
    • Internal initiation of translation mediated by the 5′ leader of a cellular mRNA
    • Macejak DG, Sarnow P. Internal initiation of translation mediated by the 5′ leader of a cellular mRNA. Nature 1991; 353: 90-4.
    • (1991) Nature , vol.353 , pp. 90-94
    • Macejak, D.G.1    Sarnow, P.2
  • 39
    • 1842791485 scopus 로고    scopus 로고
    • Preferential translation of internal ribosome entry site-containing mRNAs during the mitotic cycle in mammalian cells
    • Qin X, Sarnow P. Preferential translation of internal ribosome entry site-containing mRNAs during the mitotic cycle in mammalian cells. J Biol Chem 2004; 279: 13721-8.
    • (2004) J Biol Chem , vol.279 , pp. 13721-13728
    • Qin, X.1    Sarnow, P.2
  • 40
    • 0034307483 scopus 로고    scopus 로고
    • Internal ribosome initiation of translation and the control of cell death
    • Holcik M, Sonenberg N, Korneluk RG. Internal ribosome initiation of translation and the control of cell death. Trends Genet 2000; 16: 469-73.
    • (2000) Trends Genet , vol.16 , pp. 469-473
    • Holcik, M.1    Sonenberg, N.2    Korneluk, R.G.3
  • 41
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M, Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 2005; 6: 318-27.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 42
    • 2342421272 scopus 로고    scopus 로고
    • Targeting translation for treatment of cancer - A novel role for IRES?
    • Holcik M. Targeting translation for treatment of cancer - a novel role for IRES? Curr Cancer Drug Targets 2004; 4: 299-311.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 299-311
    • Holcik, M.1
  • 44
    • 0031452563 scopus 로고    scopus 로고
    • Alternative translation of the proto-oncogene c-myc by an internal ribosome entry site
    • Nanbru C, Lafon I, Audigier S, et al. Alternative translation of the proto-oncogene c-myc by an internal ribosome entry site. J Biol Chem 1997; 272: 32061-6.
    • (1997) J Biol Chem , vol.272 , pp. 32061-32066
    • Nanbru, C.1    Lafon, I.2    Audigier, S.3
  • 45
    • 0030903767 scopus 로고    scopus 로고
    • PDGF2/c-sis mRNA leader contains a differentiation-linked internal ribosomal entry site (DIRES)
    • Bernstein J, Sella O, Le SY, Elroy-Stein O. PDGF2/c-sis mRNA leader contains a differentiation-linked internal ribosomal entry site (DIRES). J Biol Chem 1997; 272: 9356-62.
    • (1997) J Biol Chem , vol.272 , pp. 9356-9362
    • Bernstein, J.1    Sella, O.2    Le, S.Y.3    Elroy-Stein, O.4
  • 46
    • 0032537757 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor (VEGF) expression is mediated by internal initiation of translation and alternative initiation of transcription
    • Akiri G, Nahari D, Finkelstein Y, Le SY, Elroy-Stein O, Levi BZ. Regulation of vascular endothelial growth factor (VEGF) expression is mediated by internal initiation of translation and alternative initiation of transcription. Oncogene 1998; 17: 227-36.
    • (1998) Oncogene , vol.17 , pp. 227-236
    • Akiri, G.1    Nahari, D.2    Finkelstein, Y.3    Le, S.Y.4    Elroy-Stein, O.5    Levi, B.Z.6
  • 47
    • 24044502285 scopus 로고    scopus 로고
    • An internal ribosome entry site mediates translation of lymphoid enhancer factor-1
    • Jimenez J, Jang GM, Semler BL, Waterman ML. An internal ribosome entry site mediates translation of lymphoid enhancer factor-1. RNA 2005; 11: 1385-99.
    • (2005) RNA , vol.11 , pp. 1385-1399
    • Jimenez, J.1    Jang, G.M.2    Semler, B.L.3    Waterman, M.L.4
  • 48
    • 75549090211 scopus 로고    scopus 로고
    • IRESite - A tool for the examination of viral and cellular internal ribosome entry sites
    • Mokrejs M, Masek T, Vopalensky V, Hlubucek P, Delbos P, Pospisek M. IRESite - a tool for the examination of viral and cellular internal ribosome entry sites. Nucleic Acids Res 2009; 38 (Database issue): D131-D136.
    • (2009) Nucleic Acids Res , vol.38 , Issue.DATABASE ISSUE
    • Mokrejs, M.1    Masek, T.2    Vopalensky, V.3    Hlubucek, P.4    Delbos, P.5    Pospisek, M.6
  • 50
    • 0345549480 scopus 로고    scopus 로고
    • Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo
    • Evans JR, Mitchell SA, Spriggs KA, et al. Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo. Oncogene 2003; 22: 8012-20.
    • (2003) Oncogene , vol.22 , pp. 8012-8020
    • Evans, J.R.1    Mitchell, S.A.2    Spriggs, K.A.3
  • 51
    • 0035033521 scopus 로고    scopus 로고
    • Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are selectively expressed in colon cancer
    • Hovanes K, Li TW, Munguia JE, et al. Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are selectively expressed in colon cancer. Nat Genet 2001; 28: 53-7.
    • (2001) Nat Genet , vol.28 , pp. 53-57
    • Hovanes, K.1    Li, T.W.2    Munguia, J.E.3
  • 52
    • 77449131843 scopus 로고    scopus 로고
    • MicroRNA assassins: Factors that regulate the disappearance of miRNAs
    • Kai ZS, Pasquinelli AE. MicroRNA assassins: factors that regulate the disappearance of miRNAs. Nat Struct Mol Biol 2010; 17: 5-10.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 5-10
    • Kai, Z.S.1    Pasquinelli, A.E.2
  • 53
    • 33847727035 scopus 로고    scopus 로고
    • How do microRNAs regulate gene expression?
    • Jackson RJ, Standart N. How do microRNAs regulate gene expression? Sci STKE 2007; 2007: re1.
    • (2007) Sci STKE , vol.2007
    • Jackson, R.J.1    Standart, N.2
  • 54
    • 34547944309 scopus 로고    scopus 로고
    • MicroRNA inhibition of translation initiation in vitro by targeting the cap-binding complex eIF4F
    • Mathonnet G, Fabian MR, Svitkin YV, et al. MicroRNA inhibition of translation initiation in vitro by targeting the cap-binding complex eIF4F. Science 2007; 317: 1764-7.
    • (2007) Science , vol.317 , pp. 1764-1767
    • Mathonnet, G.1    Fabian, M.R.2    Svitkin, Y.V.3
  • 55
    • 67651000077 scopus 로고    scopus 로고
    • The GW182 protein family in animal cells: New insights into domains required for miRNA-mediated gene silencing
    • Eulalio A, Tritschler F, Izaurralde E. The GW182 protein family in animal cells: new insights into domains required for miRNA-mediated gene silencing. RNA 2009; 15: 1433-42.
    • (2009) RNA , vol.15 , pp. 1433-1442
    • Eulalio, A.1    Tritschler, F.2    Izaurralde, E.3
  • 56
    • 32444436121 scopus 로고    scopus 로고
    • Short RNAs repress translation after initiation in mammalian cells
    • Petersen CP, Bordeleau ME, Pelletier J, Sharp PA. Short RNAs repress translation after initiation in mammalian cells. Mol Cell 2006; 21: 533-42.
    • (2006) Mol Cell , vol.21 , pp. 533-542
    • Petersen, C.P.1    Bordeleau, M.E.2    Pelletier, J.3    Sharp, P.A.4
  • 57
    • 24644483623 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus RNA abundance by a liver-specific MicroRNA
    • Jopling CL, Yi M, Lancaster AM, Lemon SM, Sarnow P. Modulation of hepatitis C virus RNA abundance by a liver-specific MicroRNA. Science 2005; 309: 1577-81.
    • (2005) Science , vol.309 , pp. 1577-1581
    • Jopling, C.L.1    Yi, M.2    Lancaster, A.M.3    Lemon, S.M.4    Sarnow, P.5
  • 58
    • 58249106363 scopus 로고    scopus 로고
    • The VEGF IRESes are differentially susceptible to translation inhibition by miR-16
    • Karaa ZS, Iacovoni JS, Bastide A, Lacazette E, Touriol C, Prats H. The VEGF IRESes are differentially susceptible to translation inhibition by miR-16. RNA 2009; 15: 249-54.
    • (2009) RNA , vol.15 , pp. 249-254
    • Karaa, Z.S.1    Iacovoni, J.S.2    Bastide, A.3    Lacazette, E.4    Touriol, C.5    Prats, H.6
  • 59
    • 38949196321 scopus 로고    scopus 로고
    • Was the initiation of translation in early eukaryotes IRES-driven?
    • Hernández G. Was the initiation of translation in early eukaryotes IRES-driven? Trends Biochem Sci 2008; 33: 58-64.
    • (2008) Trends Biochem Sci , vol.33 , pp. 58-64
    • Hernández, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.