메뉴 건너뛰기




Volumn 49, Issue 2, 2014, Pages 164-177

Transcriptome-wide studies uncover the diversity of modes of mRNA recruitment to eukaryotic ribosomes

Author keywords

5 UTR secondary structure; Cap independent translation enhancer; Cellular IRESs; DAP5; EIF4F; EIF4G; Ribosome profiling; Translation initiation factor eIF4E

Indexed keywords

INITIATION FACTOR 4F; INITIATION FACTOR 4G; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; TRANSCRIPTOME;

EID: 84896368727     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2014.887051     Document Type: Review
Times cited : (50)

References (127)
  • 1
    • 84871233832 scopus 로고    scopus 로고
    • EIF4E/4E-BP ratio predicts the efficacy of mTOR targeted therapies
    • Alain T, Morita M, Fonseca BD, et al. (2012). eIF4E/4E-BP ratio predicts the efficacy of mTOR targeted therapies. Cancer Res 72: 6468-76.
    • (2012) Cancer Res , vol.72 , pp. 6468-6476
    • Alain, T.1    Morita, M.2    Fonseca, B.D.3
  • 2
    • 84879992021 scopus 로고    scopus 로고
    • Translation initiation in eukary-otes: Versatility of the scanning model
    • Alekhina OM, Vassilenko KS. (2012). Translation initiation in eukary-otes: versatility of the scanning model. Biochemistry (Mosc) 77: 1465-77.
    • (2012) Biochemistry (Mosc) , vol.77 , pp. 1465-1477
    • Alekhina, O.M.1    Vassilenko, K.S.2
  • 3
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • Amrani N, Ghosh S, Mangus DA, Jacobson A. (2008). Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453:1276-80.
    • (2008) Nature , vol.453 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 4
    • 70350696063 scopus 로고    scopus 로고
    • Differential contribution of the m7G-cap to the 5 end-dependent translation initiation of mammalian mRNAs
    • Andreev DE, Dmitriev SE, Terenin IM, et al. (2009). Differential contribution of the m7G-cap to the 5 end-dependent translation initiation of mammalian mRNAs. Nucleic Acids Res 37:6135-47.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6135-6147
    • Andreev, D.E.1    Dmitriev, S.E.2    Terenin, I.M.3
  • 5
    • 84869497130 scopus 로고    scopus 로고
    • The 5 untranslated region of Apaf-1 mRNA directs translation under apoptosis conditions via a 5 end-dependent scanning mechanism
    • Andreev DE, Dmitriev SE, Zinovkin R, et al. (2012). The 5 untranslated region of Apaf-1 mRNA directs translation under apoptosis conditions via a 5 end-dependent scanning mechanism. FEBS Lett 586:4139-43.
    • (2012) FEBS Lett , vol.586 , pp. 4139-4143
    • Andreev, D.E.1    Dmitriev, S.E.2    Zinovkin, R.3
  • 6
    • 84869216705 scopus 로고    scopus 로고
    • DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs
    • Badura M, Braunstein S, Zavadil J, Schneider RJ. (2012). DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs. Proc Natl Acad Sci USA 109:18767-72.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 18767-18772
    • Badura, M.1    Braunstein, S.2    Zavadil, J.3    Schneider, R.J.4
  • 7
    • 34548186156 scopus 로고    scopus 로고
    • Translational control of meiotic cell cycle progression and spermatid differentiation in male germ cells by a novel eIF4G homolog
    • Baker CC, Fuller MT. (2007). Translational control of meiotic cell cycle progression and spermatid differentiation in male germ cells by a novel eIF4G homolog. Development 134: 2863-9.
    • (2007) Development , vol.134 , pp. 2863-2869
    • Baker, C.C.1    Fuller, M.T.2
  • 8
    • 0038719941 scopus 로고    scopus 로고
    • RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae
    • Berset C, Zurbriggen A, Djafarzadeh S, et al. (2003). RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae. RNA 9:871-80.
    • (2003) RNA , vol.9 , pp. 871-880
    • Berset, C.1    Zurbriggen, A.2    Djafarzadeh, S.3
  • 9
    • 81155154337 scopus 로고    scopus 로고
    • Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation
    • Bolger TA, Wente SR. (2011). Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation. J Biol Chem 286:39750-9.
    • (2011) J Biol Chem , vol.286 , pp. 39750-39759
    • Bolger, T.A.1    Wente, S.R.2
  • 10
    • 0034327417 scopus 로고    scopus 로고
    • Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: The eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5-end
    • Borman AM, Michel YM, Kean KM. (2000). Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5-end. Nucleic Acids Res 28:4068-75.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4068-4075
    • Borman, A.M.1    Michel, Y.M.2    Kean, K.M.3
  • 11
    • 67651207956 scopus 로고    scopus 로고
    • Selective recruitment of proteins to 5 cap complexes during the growth cycle in Arabidopsis
    • Bush MS, Hutchins AP, Jones AM, et al. (2009). Selective recruitment of proteins to 5 cap complexes during the growth cycle in Arabidopsis. Plant J 59:400-12.
    • (2009) Plant J , vol.59 , pp. 400-412
    • Bush, M.S.1    Hutchins, A.P.2    Jones, A.M.3
  • 12
    • 21444446061 scopus 로고    scopus 로고
    • Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection
    • Byrd MP, Zamora M, Lloyd RE. (2005). Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection. J Biol Chem 280: 18610-22.
    • (2005) J Biol Chem , vol.280 , pp. 18610-18622
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 13
    • 38549117402 scopus 로고    scopus 로고
    • SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein
    • Cakmakci NG, Lerner RS, Wagner EJ, et al. (2008). SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein. Mol Cell Biol 28:1182-94.
    • (2008) Mol Cell Biol , vol.28 , pp. 1182-1194
    • Cakmakci, N.G.1    Lerner, R.S.2    Wagner, E.J.3
  • 14
    • 80052865292 scopus 로고    scopus 로고
    • Glucose depletion inhibits translation initiation via eIF4A loss and subsequent 48S preinitiation complex accumulation, while the pentose phosphate pathway is coordinately up-regulated
    • Castelli LM, Lui J, Campbell SG, et al. (2011). Glucose depletion inhibits translation initiation via eIF4A loss and subsequent 48S preinitiation complex accumulation, while the pentose phosphate pathway is coordinately up-regulated. Mol Biol Cell 22:3379-93.
    • (2011) Mol Biol Cell , vol.22 , pp. 3379-3393
    • Castelli, L.M.1    Lui, J.2    Campbell, S.G.3
  • 15
    • 79954750336 scopus 로고    scopus 로고
    • Genetic alterations in oral squamous cell carcinoma progression detected by combining array-based comparative genomic hybridization and multiplex ligation-dependent probe amplification
    • Cha JD, Kim HJ, Cha IH. (2011). Genetic alterations in oral squamous cell carcinoma progression detected by combining array-based comparative genomic hybridization and multiplex ligation-dependent probe amplification. Oral Surg Oral Med Oral Pathol Oral Radiol Endod 111:594-607.
    • (2011) Oral Surg Oral Med Oral Pathol Oral Radiol Endod , vol.111 , pp. 594-607
    • Cha, J.D.1    Kim, H.J.2    Cha, I.H.3
  • 16
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: Inhibition via 5-3 mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho PF, Poulin F, Cho-Park YA, et al. (2005). A new paradigm for translational control: inhibition via 5-3 mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell 121:411-23.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3
  • 17
    • 84861534940 scopus 로고    scopus 로고
    • Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g
    • Choe J, Oh N, Park S, et al. (2012). Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g. J Biol Chem 287: 18500-9.
    • (2012) J Biol Chem , vol.287 , pp. 18500-18509
    • Choe, J.1    Oh, N.2    Park, S.3
  • 18
    • 77949353765 scopus 로고    scopus 로고
    • Functional overlap between eIF4G isoforms in Saccharomyces cerevisiae
    • Clarkson BK, Gilbert WV, Doudna JA. (2010). Functional overlap between eIF4G isoforms in Saccharomyces cerevisiae. PLoS One 5: e9114.
    • (2010) PLoS One , vol.5
    • Clarkson, B.K.1    Gilbert, W.V.2    Doudna, J.A.3
  • 19
    • 33750997021 scopus 로고    scopus 로고
    • Specific isoforms of translation initiation factor 4GI show differences in translational activity
    • Coldwell MJ, Morley SJ. (2006). Specific isoforms of translation initiation factor 4GI show differences in translational activity. Mol Cell Biol 26:8448-60.
    • (2006) Mol Cell Biol , vol.26 , pp. 8448-8460
    • Coldwell, M.J.1    Morley, S.J.2
  • 20
    • 84867806665 scopus 로고    scopus 로고
    • Multiple isoforms of the translation initiation factor eIF4GII are generated via use of alternative promoters, splice sites and a non-canonical initiation codon
    • Coldwell MJ, Sack U, Cowan JL, et al. (2012). Multiple isoforms of the translation initiation factor eIF4GII are generated via use of alternative promoters, splice sites and a non-canonical initiation codon. Biochem J 448:1-11.
    • (2012) Biochem J , vol.448 , pp. 1-11
    • Coldwell, M.J.1    Sack, U.2    Cowan, J.L.3
  • 21
    • 41149133368 scopus 로고    scopus 로고
    • Translational control of the innate immune response through IRF-7
    • Colina R, Costa-Mattioli M, Dowling RJ, et al. (2008). Translational control of the innate immune response through IRF-7. Nature 452: 323-8.
    • (2008) Nature , vol.452 , pp. 323-328
    • Colina, R.1    Costa-Mattioli, M.2    Dowling, R.J.3
  • 22
    • 47249161257 scopus 로고    scopus 로고
    • Depletion of the cap-associated isoform of translation factor eIF4G induces germline apoptosis in C. Elegans
    • Contreras V, Richardson MA, Hao E, Keiper BD. (2008). Depletion of the cap-associated isoform of translation factor eIF4G induces germline apoptosis in C. elegans. Cell Death Differ 15: 1232-42.
    • (2008) Cell Death Differ , vol.15 , pp. 1232-1242
    • Contreras, V.1    Richardson, M.A.2    Hao, E.3    Keiper, B.D.4
  • 23
    • 78650424915 scopus 로고    scopus 로고
    • Identifying eIF4E-binding protein translationally-controlled transcripts reveals links to mRNAs bound by specific PUF proteins
    • Cridge AG, Castelli LM, Smirnova JB, et al. (2010). Identifying eIF4E-binding protein translationally-controlled transcripts reveals links to mRNAs bound by specific PUF proteins. Nucleic Acids Res 38: 8039-50.
    • (2010) Nucleic Acids Res , vol.38 , pp. 8039-8050
    • Cridge, A.G.1    Castelli, L.M.2    Smirnova, J.B.3
  • 24
    • 80053625750 scopus 로고    scopus 로고
    • Translational coregulation of 5TOP mRNAs by TIA-1 and TIAR
    • Damgaard CK, Lykke-Andersen J. (2011). Translational coregulation of 5TOP mRNAs by TIA-1 and TIAR. Genes Dev 25:2057-68.
    • (2011) Genes Dev , vol.25 , pp. 2057-2068
    • Damgaard, C.K.1    Lykke-Andersen, J.2
  • 25
    • 84865645908 scopus 로고    scopus 로고
    • Cytoplasmic RNA-binding proteins and the control of complex brain function
    • Darnell JC, Richter JD. (2012). Cytoplasmic RNA-binding proteins and the control of complex brain function. Cold Spring Harb Perspect Biol 4:a012344.
    • (2012) Cold Spring Harb Perspect Biol , vol.4
    • Darnell, J.C.1    Richter, J.D.2
  • 26
    • 84871178729 scopus 로고    scopus 로고
    • Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis
    • Dennis MD, Jefferson LS, Kimball SR. (2012). Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis. J Biol Chem 287: 42890-9.
    • (2012) J Biol Chem , vol.287 , pp. 42890-42899
    • Dennis, M.D.1    Jefferson, L.S.2    Kimball, S.R.3
  • 27
    • 61349086812 scopus 로고    scopus 로고
    • Efficient cap-dependent translation of mammalian mRNAs with long and highly structured 5-untranslated regions in vitro and in vivo
    • Dmitriev SE, Andreev DE, Adyanova ZV, et al. (2009). Efficient cap-dependent translation of mammalian mRNAs with long and highly structured 5-untranslated regions in vitro and in vivo. Mol Biol (Mosk) 43:108-13.
    • (2009) Mol Biol (Mosk) , vol.43 , pp. 108-113
    • Dmitriev, S.E.1    Andreev, D.E.2    Adyanova, Z.V.3
  • 28
    • 34347326163 scopus 로고    scopus 로고
    • Efficient translation initiation directed by the 900-nucleotide-long and GC-rich 5 untranslated region of the human retrotransposon LINE-1 mRNA is strictly cap dependent rather than internal ribosome entry site mediated
    • Dmitriev SE, Andreev DE, Terenin IM, et al. (2007). Efficient translation initiation directed by the 900-nucleotide-long and GC-rich 5 untranslated region of the human retrotransposon LINE-1 mRNA is strictly cap dependent rather than internal ribosome entry site mediated. Mol Cell Biol 27:4685-97.
    • (2007) Mol Cell Biol , vol.27 , pp. 4685-4697
    • Dmitriev, S.E.1    Andreev, D.E.2    Terenin, I.M.3
  • 29
    • 0345060297 scopus 로고    scopus 로고
    • Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5 untranslated regions
    • Dmitriev SE, Terenin IM, Dunaevsky YE, et al. (2003). Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5 untranslated regions. Mol Cell Biol 23:8925-33.
    • (2003) Mol Cell Biol , vol.23 , pp. 8925-8933
    • Dmitriev, S.E.1    Terenin, I.M.2    Dunaevsky, Y.E.3
  • 30
    • 84892463438 scopus 로고    scopus 로고
    • Mitotic Phosphorylation of eukaryotic initiation factor 4G1 (eIF4G1) at Ser1232 by Cdk1: Cyclin B inhibits eIF4A helicase complex binding with RNA
    • Dobrikov MI, Shveygert M, Brown MC, Gromeier M. (2014). Mitotic Phosphorylation of eukaryotic initiation factor 4G1 (eIF4G1) at Ser1232 by Cdk1: cyclin B inhibits eIF4A helicase complex binding with RNA. Mol Cell Biol 34:439-51.
    • (2014) Mol Cell Biol , vol.34 , pp. 439-451
    • Dobrikov, M.I.1    Shveygert, M.2    Brown, M.C.3    Gromeier, M.4
  • 31
    • 84882291342 scopus 로고    scopus 로고
    • Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity
    • Feoktistova K, Tuvshintogs E, Do A, Fraser CS. (2013). Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity. Proc Natl Acad Sci USA 110:13339-44.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13339-13344
    • Feoktistova, K.1    Tuvshintogs, E.2    Do, A.3    Fraser, C.S.4
  • 32
    • 79959320660 scopus 로고    scopus 로고
    • HCV IRES domain IIb affects the configuration of coding RNA in the 40S subunit's decoding groove
    • Filbin ME, Kieft JS. (2011). HCV IRES domain IIb affects the configuration of coding RNA in the 40S subunit's decoding groove. RNA 17:1258-73.
    • (2011) RNA , vol.17 , pp. 1258-1273
    • Filbin, M.E.1    Kieft, J.S.2
  • 33
    • 34548170688 scopus 로고    scopus 로고
    • A novel eIF4G homolog, Off-schedule, couples translational control to meiosis and differentiation in Drosophila spermatocytes
    • Franklin-Dumont TM, Chatterjee C, Wasserman SA, Dinardo S. (2007). A novel eIF4G homolog, Off-schedule, couples translational control to meiosis and differentiation in Drosophila spermatocytes. Development 134:2851-61.
    • (2007) Development , vol.134 , pp. 2851-2861
    • Franklin-Dumont, T.M.1    Chatterjee, C.2    Wasserman, S.A.3    Dinardo, S.4
  • 34
    • 84855379287 scopus 로고    scopus 로고
    • Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogram-ming of translation after hyperosmotic shock
    • Garre E, Romero-Santacreu L, De Clercq N, et al. (2012). Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogram-ming of translation after hyperosmotic shock. Mol Biol Cell 23: 137-50.
    • (2012) Mol Biol Cell , vol.23 , pp. 137-150
    • Garre, E.1    Romero-Santacreu, L.2    De Clercq, N.3
  • 35
    • 84878741907 scopus 로고    scopus 로고
    • Initial quantitative proteomic map of 28 mouse tissues using the SILAC mouse
    • Geiger T, Velic A, Macek B, et al. (2013). Initial quantitative proteomic map of 28 mouse tissues using the SILAC mouse. Mol Cell Proteomics 12:1709-22.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1709-1722
    • Geiger, T.1    Velic, A.2    Macek, B.3
  • 36
    • 34548535363 scopus 로고    scopus 로고
    • Cap-independent translation is required for starvation-induced differentiation in yeast
    • Gilbert WV, Zhou K, Butler TK, Doudna JA. (2007). Cap-independent translation is required for starvation-induced differentiation in yeast. Science 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
  • 37
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N. (1999). eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 68:913-63.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 38
    • 84872595085 scopus 로고    scopus 로고
    • Autism-related deficits via dysregulated eIF4E-dependent translational control
    • Gkogkas CG, Khoutorsky A, Ran I, et al. (2013). Autism-related deficits via dysregulated eIF4E-dependent translational control. Nature 493: 371-7.
    • (2013) Nature , vol.493 , pp. 371-377
    • Gkogkas, C.G.1    Khoutorsky, A.2    Ran, I.3
  • 39
    • 0034542075 scopus 로고    scopus 로고
    • Structure and function of a cap-independent translation element that functions in either the 3 or the 5 untranslated region
    • Guo L, Allen E, Miller WA. (2000). Structure and function of a cap-independent translation element that functions in either the 3 or the 5 untranslated region. RNA 6:1808-20.
    • (2000) RNA , vol.6 , pp. 1808-1820
    • Guo, L.1    Allen, E.2    Miller, W.A.3
  • 40
    • 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. (1995). Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J 14: 5701-9.
    • (1995) EMBO J , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 41
    • 0030832026 scopus 로고    scopus 로고
    • EIF4G dramatically enhances the binding of eIF4E to the mRNA 5-cap structure
    • Haghighat A, Sonenberg N. (1997). eIF4G dramatically enhances the binding of eIF4E to the mRNA 5-cap structure. J Biol Chem 272: 21677-80.
    • (1997) J Biol Chem , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 42
    • 33646124490 scopus 로고    scopus 로고
    • MTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin
    • Harris TE, Chi A, Shabanowitz J, et al. (2006). mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin. EMBO J 25:1659-68.
    • (2006) EMBO J , vol.25 , pp. 1659-1668
    • Harris, T.E.1    Chi, A.2    Shabanowitz, J.3
  • 43
    • 67650944993 scopus 로고    scopus 로고
    • Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
    • Harrison DE, Strong R, Sharp ZD, et al. (2009). Rapamycin fed late in life extends lifespan in genetically heterogeneous mice. Nature 460: 392-5.
    • (2009) Nature , vol.460 , pp. 392-395
    • Harrison, D.E.1    Strong, R.2    Sharp, Z.D.3
  • 44
    • 84864807356 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4E-3 is essential for meiotic chromosome segregation, cytokinesis and male fertility in Drosophila
    • Hernandez G, Han H, Gandin V, et al. (2012). Eukaryotic initiation factor 4E-3 is essential for meiotic chromosome segregation, cytokinesis and male fertility in Drosophila. Development 139: 3211-20.
    • (2012) Development , vol.139 , pp. 3211-3220
    • Hernandez, G.1    Han, H.2    Gandin, V.3
  • 45
    • 84880683340 scopus 로고    scopus 로고
    • Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster
    • Hernandez G, Miron M, Han H, et al. (2013). Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster. Mol Cell Biol 33: 2854-64.
    • (2013) Mol Cell Biol , vol.33 , pp. 2854-2864
    • Hernandez, G.1    Miron, M.2    Han, H.3
  • 46
    • 21844442364 scopus 로고    scopus 로고
    • Functional diversity of the eukaryotic translation initiation factors belonging to eIF4 families
    • Hernandez G, Vazquez-Pianzola P. (2005). Functional diversity of the eukaryotic translation initiation factors belonging to eIF4 families. Mech Dev 122:865-76.
    • (2005) Mech Dev , vol.122 , pp. 865-876
    • Hernandez, G.1    Vazquez-Pianzola, P.2
  • 47
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: New insights and challenges
    • Hinnebusch AG, Lorsch JR. (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
  • 48
    • 84862777192 scopus 로고    scopus 로고
    • The translational landscape of mTOR signalling steers cancer initiation and metastasis
    • Hsieh AC, Liu Y, Edlind MP, et al. (2012). The translational landscape of mTOR signalling steers cancer initiation and metastasis. Nature 485:55-61.
    • (2012) Nature , vol.485 , pp. 55-61
    • Hsieh, A.C.1    Liu, Y.2    Edlind, M.P.3
  • 49
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • Imataka H, Olsen HS, Sonenberg N. (1997). A new translational regulator with homology to eukaryotic translation initiation factor 4G. EMBO J 16:817-25.
    • (1997) EMBO J , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, H.S.2    Sonenberg, N.3
  • 50
    • 84864453787 scopus 로고    scopus 로고
    • The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments
    • Ingolia NT, Brar GA, Rouskin S, et al. (2012). The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments. Nat Protoc 7:1534-50.
    • (2012) Nat Protoc , vol.7 , pp. 1534-1550
    • Ingolia, N.T.1    Brar, G.A.2    Rouskin, S.3
  • 51
    • 84875129451 scopus 로고    scopus 로고
    • The current status of vertebrate cellular mRNA IRESs
    • Jackson RJ. (2013). The current status of vertebrate cellular mRNA IRESs. Cold Spring Harb Perspect Biol 5:a011569.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Jackson, R.J.1
  • 52
    • 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, et al. (1988). A segment of the 5 nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J Virol 62: 2636-43.
    • (1988) J Virol , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3
  • 53
    • 84863838830 scopus 로고    scopus 로고
    • Cap-dependent translation initiation factor eIF4E: An emerging anticancer drug target
    • Jia Y, Polunovsky V, Bitterman PB, Wagner CR. (2012). Cap-dependent translation initiation factor eIF4E: an emerging anticancer drug target. Med Res Rev 32:786-814.
    • (2012) Med Res Rev , vol.32 , pp. 786-814
    • Jia, Y.1    Polunovsky, V.2    Bitterman, P.B.3    Wagner, C.R.4
  • 54
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • Jivotovskaya AV, Valasek L, Hinnebusch AG, Nielsen KH. (2006). Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol Cell Biol 26:1355-72.
    • (2006) Mol Cell Biol , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valasek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 55
    • 2942522541 scopus 로고    scopus 로고
    • Characterization of mammalian eIF4E-family members
    • Joshi B, Cameron A, Jagus R. (2004). Characterization of mammalian eIF4E-family members. Eur J Biochem 271:2189-203.
    • (2004) Eur J Biochem , vol.271 , pp. 2189-2203
    • Joshi, B.1    Cameron, A.2    Jagus, R.3
  • 57
    • 84870936058 scopus 로고    scopus 로고
    • Genome-wide approaches to dissect the roles of RNA binding proteins in translational control: Implications for neurological diseases
    • Kapeli K, Yeo GW. (2012). Genome-wide approaches to dissect the roles of RNA binding proteins in translational control: implications for neurological diseases. Front Neurosci 6:144.
    • (2012) Front Neurosci , vol.6 , pp. 144
    • Kapeli, K.1    Yeo, G.W.2
  • 58
    • 69749116302 scopus 로고    scopus 로고
    • A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation
    • Kim KM, Cho H, Choi K, et al. (2009). A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation. Genes Dev 23:2033-45.
    • (2009) Genes Dev , vol.23 , pp. 2033-2045
    • Kim, K.M.1    Cho, H.2    Choi, K.3
  • 59
    • 43349102982 scopus 로고    scopus 로고
    • Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNA
    • Kopeina GS, Afonina ZA, Gromova KV, et al. (2008). Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNA. Nucleic Acids Res 36:2476-88.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2476-2488
    • Kopeina, G.S.1    Afonina, Z.A.2    Gromova, K.V.3
  • 60
    • 0026723117 scopus 로고
    • MRNAs containing extensive secondary structure in their 5 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas AE, Lazaris-Karatzas A, Sonenberg N. (1992). mRNAs containing extensive secondary structure in their 5 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J 11:4153-8.
    • (1992) EMBO J , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 61
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak M. (1989). The scanning model for translation: an update. J Cell Biol 108:229-41.
    • (1989) J Cell Biol , vol.108 , pp. 229-241
    • Kozak, M.1
  • 62
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M, Sabatini DM. (2012). mTOR signaling in growth control and disease. Cell 149:274-93.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 63
    • 84867618238 scopus 로고    scopus 로고
    • MRNA localization and translational control in Drosophila oogenesis
    • Lasko P. (2012). mRNA localization and translational control in Drosophila oogenesis. Cold Spring Harb Perspect Biol 4:a012294.
    • (2012) Cold Spring Harb Perspect Biol , vol.4
    • Lasko, P.1
  • 64
    • 33748354044 scopus 로고    scopus 로고
    • P97/DAP5 is a ribosome-associated factor that facilitates protein synthesis and cell proliferation by modulating the synthesis of cell cycle proteins
    • Lee SH, McCormick F. (2006). p97/DAP5 is a ribosome-associated factor that facilitates protein synthesis and cell proliferation by modulating the synthesis of cell cycle proteins. EMBO J 25:4008-19.
    • (2006) EMBO J , vol.25 , pp. 4008-4019
    • Lee, S.H.1    McCormick, F.2
  • 65
    • 84867302560 scopus 로고    scopus 로고
    • Cryptic transcripts from a ubiquitous plasmid origin of replication confound tests for cis-regulatory function
    • Lemp NA, Hiraoka K, Kasahara N, Logg CR. (2012). Cryptic transcripts from a ubiquitous plasmid origin of replication confound tests for cis-regulatory function. Nucleic Acids Res 40:7280-90.
    • (2012) Nucleic Acids Res , vol.40 , pp. 7280-7290
    • Lemp, N.A.1    Hiraoka, K.2    Kasahara, N.3    Logg, C.R.4
  • 66
    • 0031017473 scopus 로고    scopus 로고
    • DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death
    • Levy-Strumpf N, Deiss LP, Berissi H, Kimchi A. (1997). DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death. Mol Cell Biol 17:1615-25.
    • (1997) Mol Cell Biol , vol.17 , pp. 1615-1625
    • Levy-Strumpf, N.1    Deiss, L.P.2    Berissi, H.3    Kimchi, A.4
  • 67
    • 58549092782 scopus 로고    scopus 로고
    • The translation initiation factor DAP5 is a regulator of cell survival during mitosis
    • Liberman N, Marash L, Kimchi A. (2009). The translation initiation factor DAP5 is a regulator of cell survival during mitosis. Cell Cycle 8:204-9.
    • (2009) Cell Cycle , vol.8 , pp. 204-209
    • Liberman, N.1    Marash, L.2    Kimchi, A.3
  • 68
    • 0025883162 scopus 로고
    • Internal initiation of translation mediated by the 5 leader of a cellular mRNA
    • Macejak DG, Sarnow P. (1991). Internal initiation of translation mediated by the 5 leader of a cellular mRNA. Nature 353:90-4.
    • (1991) Nature , vol.353 , pp. 90-94
    • Macejak, D.G.1    Sarnow, P.2
  • 69
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader S, Lee H, Pause A, Sonenberg N. (1995). The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol Cell Biol 15:4990-7.
    • (1995) Mol Cell Biol , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 70
    • 84885932370 scopus 로고    scopus 로고
    • HCV IRES interacts with the 18S rRNA to activate the 40S ribosome for subsequent steps of translation initiation
    • Malygin AA, Kossinova OA, Shatsky IN, Karpova GG. (2013). HCV IRES interacts with the 18S rRNA to activate the 40S ribosome for subsequent steps of translation initiation. Nucleic Acids Res 41:8706-14.
    • (2013) Nucleic Acids Res , vol.41 , pp. 8706-8714
    • Malygin, A.A.1    Kossinova, O.A.2    Shatsky, I.N.3    Karpova, G.G.4
  • 71
    • 34250755685 scopus 로고    scopus 로고
    • Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation
    • Mamane Y, Petroulakis E, Martineau Y, et al. (2007). Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation. PLoS One 2:e242.
    • (2007) PLoS One , vol.2
    • Mamane, Y.1    Petroulakis, E.2    Martineau, Y.3
  • 72
    • 80052411929 scopus 로고    scopus 로고
    • CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsense-mediated mRNA decay, and thereafter
    • Maquat LE, Hwang J, Sato H, Tang Y. (2010). CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsense-mediated mRNA decay, and thereafter. Cold Spring Harb Symp Quant Biol 75:127-34.
    • (2010) Cold Spring Harb Symp Quant Biol , vol.75 , pp. 127-134
    • Maquat, L.E.1    Hwang, J.2    Sato, H.3    Tang, Y.4
  • 73
    • 20044379571 scopus 로고    scopus 로고
    • DAP5 and IRES-mediated translation during programmed cell death
    • Marash L, Kimchi A. (2005). DAP5 and IRES-mediated translation during programmed cell death. Cell Death Differ 12:554-62.
    • (2005) Cell Death Differ , vol.12 , pp. 554-562
    • Marash, L.1    Kimchi, A.2
  • 74
    • 43449105311 scopus 로고    scopus 로고
    • DAP5 promotes cap-independent translation of Bcl-2 and CDK1 to facilitate cell survival during mitosis
    • Marash L, Liberman N, Henis-Korenblit S, et al. (2008). DAP5 promotes cap-independent translation of Bcl-2 and CDK1 to facilitate cell survival during mitosis. Mol Cell 30:447-59.
    • (2008) Mol Cell , vol.30 , pp. 447-459
    • Marash, L.1    Liberman, N.2    Henis-Korenblit, S.3
  • 75
    • 84877923058 scopus 로고    scopus 로고
    • Roles of helicases in translation initiation: A mechanistic view
    • Marintchev A. (2013). Roles of helicases in translation initiation: a mechanistic view. Biochim Biophys Acta 1829:799-809.
    • (2013) Biochim Biophys Acta , pp. 799-809
    • Marintchev, A.1
  • 76
    • 55449106579 scopus 로고    scopus 로고
    • Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation
    • Martineau Y, Derry MC, Wang X, et al. (2008). Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation. Mol Cell Biol 28:6658-67.
    • (2008) Mol Cell Biol , vol.28 , pp. 6658-6667
    • Martineau, Y.1    Derry, M.C.2    Wang, X.3
  • 77
    • 37749006919 scopus 로고    scopus 로고
    • The amazing diversity of cap-independent translation elements in the 3-untranslated regions of plant viral RNAs
    • Miller WA, Wang Z, Treder K. (2007). The amazing diversity of cap-independent translation elements in the 3-untranslated regions of plant viral RNAs. Biochem Soc Trans 35:1629-33.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1629-1633
    • Miller, W.A.1    Wang, Z.2    Treder, K.3
  • 78
    • 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 SF, Walker SE, Algire MA, et al. (2010). The 5-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway. Mol Cell 39:950-62.
    • (2010) Mol Cell , vol.39 , pp. 950-962
    • Mitchell, S.F.1    Walker, S.E.2    Algire, M.A.3
  • 79
    • 84866274906 scopus 로고    scopus 로고
    • A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian development
    • Morita M, Ler LW, Fabian MR, et al. (2012). A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian development. Mol Cell Biol 32:3585-93.
    • (2012) Mol Cell Biol , vol.32 , pp. 3585-3593
    • Morita, M.1    Ler, L.W.2    Fabian, M.R.3
  • 80
    • 0034057277 scopus 로고    scopus 로고
    • Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    • Mothe-Satney I, Yang D, Fadden P, et al. (2000). Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression. Mol Cell Biol 20:3558-67.
    • (2000) Mol Cell Biol , vol.20 , pp. 3558-3567
    • Mothe-Satney, I.1    Yang, D.2    Fadden, P.3
  • 81
    • 84861404431 scopus 로고    scopus 로고
    • INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation
    • Neusiedler J, Mocquet V, Limousin T, et al. (2012). INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation. RNA 18:1163-77.
    • (2012) RNA , vol.18 , pp. 1163-1177
    • Neusiedler, J.1    Mocquet, V.2    Limousin, T.3
  • 82
    • 77953641910 scopus 로고    scopus 로고
    • Tombusvirus recruitment of host translational machinery via the 3 UTR
    • Nicholson BL, Wu B, Chevtchenko I, White KA. (2010). Tombusvirus recruitment of host translational machinery via the 3 UTR. RNA 16: 1402-19.
    • (2010) RNA , vol.16 , pp. 1402-1419
    • Nicholson, B.L.1    Wu, B.2    Chevtchenko, I.3    White, K.A.4
  • 83
    • 33847336023 scopus 로고    scopus 로고
    • The eIF4G-homolog p97 can activate translation independent of caspase cleavage
    • Nousch M, Reed V, Bryson-Richardson RJ, et al. (2007). The eIF4G-homolog p97 can activate translation independent of caspase cleavage. RNA 13:374-84.
    • (2007) RNA , vol.13 , pp. 374-384
    • Nousch, M.1    Reed, V.2    Bryson-Richardson, R.J.3
  • 84
    • 84874631075 scopus 로고    scopus 로고
    • EIF4E3 acts as a tumor suppressor by utilizing an atypical mode of methyl-7-guanosine cap recognition
    • Osborne MJ, Volpon L, Kornblatt JA, et al. (2013). eIF4E3 acts as a tumor suppressor by utilizing an atypical mode of methyl-7-guanosine cap recognition. Proc Natl Acad Sci USA 110: 3877-82.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 3877-3882
    • Osborne, M.J.1    Volpon, L.2    Kornblatt, J.A.3
  • 85
    • 46549088588 scopus 로고    scopus 로고
    • Death-associated protein 5 (DAP5/p97/NAT1) contributes to retinoic acid-induced granulocytic differentiation and arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • Ozpolat B, Akar U, Zorrilla-Calancha I, et al. (2008). Death-associated protein 5 (DAP5/p97/NAT1) contributes to retinoic acid-induced granulocytic differentiation and arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Apoptosis 13:915-28.
    • (2008) Apoptosis , vol.13 , pp. 915-928
    • Ozpolat, B.1    Akar, U.2    Zorrilla-Calancha, I.3
  • 86
    • 78751609906 scopus 로고    scopus 로고
    • Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1*PABP mRNPs in vivo
    • Park EH, Walker SE, Lee JM, et al. (2011a). Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1*PABP mRNPs in vivo. EMBO J 30:302-16.
    • (2011) EMBO J , vol.30 , pp. 302-316
    • Park, E.H.1    Walker, S.E.2    Lee, J.M.3
  • 87
    • 79251570260 scopus 로고    scopus 로고
    • Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide
    • Park EH, Zhang F, Warringer J, et al. (2011b). Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide. BMC Genomics 12:68.
    • (2011) BMC Genomics , vol.12 , pp. 68
    • Park, E.H.1    Zhang, F.2    Warringer, J.3
  • 88
    • 79953052296 scopus 로고    scopus 로고
    • MRNA helicases: The tacticians of translational control
    • Parsyan A, Svitkin Y, Shahbazian D, et al. (2011). mRNA helicases: the tacticians of translational control. Nat Rev Mol Cell Biol 12: 235-45.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 235-245
    • Parsyan, A.1    Svitkin, Y.2    Shahbazian, D.3
  • 89
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J, Sonenberg N. (1988). Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 334:320-5.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 90
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova TV, Hellen CU, Shatsky IN. (1996a). Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol Cell Biol 16:6859-69.
    • (1996) Mol Cell Biol , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 91
    • 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 TV, Shatsky IN, Fletcher SP, et al. (1998). 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 12:67-83.
    • (1998) Genes Dev , vol.12 , pp. 67-83
    • Pestova, T.V.1    Shatsky, I.N.2    Fletcher, S.P.3
  • 92
    • 0029968997 scopus 로고    scopus 로고
    • Functional dissection of eukaryotic initiation factor 4F: The 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes
    • Pestova TV, Shatsky IN, Hellen CU. (1996b). Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes. Mol Cell Biol 16:6870-8.
    • (1996) Mol Cell Biol , vol.16 , pp. 6870-6878
    • Pestova, T.V.1    Shatsky, I.N.2    Hellen, C.U.3
  • 93
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 5UTRs requires DExH-box protein DHX29
    • Pisareva VP, Pisarev AV, Komar AA, et al. (2008). Translation initiation on mammalian mRNAs with structured 5UTRs requires DExH-box protein DHX29. Cell 135:1237-50.
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3
  • 94
    • 0345373936 scopus 로고    scopus 로고
    • Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning
    • Prevot D, Decimo D, Herbreteau CH, et al. (2003). Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning. EMBO J 22:1909-21.
    • (2003) EMBO J , vol.22 , pp. 1909-1921
    • Prevot, D.1    Decimo, D.2    Herbreteau, C.H.3
  • 95
    • 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 EH, Hinnebusch AG, Lorsch JR. (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 287:20301-12.
    • (2012) J Biol Chem , vol.287 , pp. 20301-20312
    • Rajagopal, V.1    Park, E.H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 96
    • 42449138319 scopus 로고    scopus 로고
    • EIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy
    • Ramirez-Valle F, Braunstein S, Zavadil J, et al. (2008). eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy. J Cell Biol 181:293-307.
    • (2008) J Cell Biol , vol.181 , pp. 293-307
    • Ramirez-Valle, F.1    Braunstein, S.2    Zavadil, J.3
  • 97
    • 67650543838 scopus 로고    scopus 로고
    • EIF4E: New family members, new binding partners, new roles
    • Rhoads RE. (2009). eIF4E: new family members, new binding partners, new roles. J Biol Chem 284:16711-15.
    • (2009) J Biol Chem , vol.284 , pp. 16711-16715
    • Rhoads, R.E.1
  • 98
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: A life in translation
    • Richter JD. (2007). CPEB: a life in translation. Trends Biochem Sci 32: 279-85.
    • (2007) Trends Biochem Sci , vol.32 , pp. 279-285
    • Richter, J.D.1
  • 100
    • 84866425291 scopus 로고    scopus 로고
    • Translational control in cancer etiology
    • Ruggero D. (2013). Translational control in cancer etiology. Cold Spring Harb Perspect Biol 5:a012336.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Ruggero, D.1
  • 101
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • Schwanhausser B, Busse D, Li N, et al. (2011). Global quantification of mammalian gene expression control. Nature 473:337-42.
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhausser, B.1    Busse, D.2    Li, N.3
  • 102
    • 84868210924 scopus 로고    scopus 로고
    • In vitro activity of human translation initiation factor eIF4B is not affected by phosphomimetic amino acid substitutions S422D and S422E
    • Shagam LI, Terenin IM, Andreev DE, et al. (2012). In vitro activity of human translation initiation factor eIF4B is not affected by phosphomimetic amino acid substitutions S422D and S422E. Biochimie 94:2484-90.
    • (2012) Biochimie , vol.94 , pp. 2484-2490
    • Shagam, L.I.1    Terenin, I.M.2    Andreev, D.E.3
  • 103
    • 84861216902 scopus 로고    scopus 로고
    • Thriving under stress: Selective translation of HIV-1 structural protein mRNA during Vpr-mediated impairment of eIF4E translation activity
    • Sharma A, Yilmaz A, Marsh K, et al. (2012). Thriving under stress: selective translation of HIV-1 structural protein mRNA during Vpr-mediated impairment of eIF4E translation activity. PLoS Pathog 8: e1002612.
    • (2012) PLoS Pathog , vol.8
    • Sharma, A.1    Yilmaz, A.2    Marsh, K.3
  • 104
    • 78650427660 scopus 로고    scopus 로고
    • Cap-and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs
    • Shatsky IN, Dmitriev SE, Terenin IM, Andreev DE. (2010). Cap-and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs. Mol Cells 30:285-93.
    • (2010) Mol Cells , vol.30 , pp. 285-293
    • Shatsky, I.N.1    Dmitriev, S.E.2    Terenin, I.M.3    Andreev, D.E.4
  • 105
    • 0031568258 scopus 로고    scopus 로고
    • CDNA cloning, expression analysis, and chromosomal localization of a gene with high homology to wheat eIF-(iso)4F and mammalian eIF-4G
    • Shaughnessy Jr JD, Jenkins NA, Copeland NG. (1997). cDNA cloning, expression analysis, and chromosomal localization of a gene with high homology to wheat eIF-(iso)4F and mammalian eIF-4G. Genomics 39:192-7.
    • (1997) Genomics , vol.39 , pp. 192-197
    • Shaughnessy Jr., J.D.1    Jenkins, N.A.2    Copeland, N.G.3
  • 106
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. (2009). Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136:731-45.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 107
    • 84866361659 scopus 로고    scopus 로고
    • DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs
    • Soto-Rifo R, Rubilar PS, Limousin T, et al. (2012). DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs. EMBO J 31:3745-56.
    • (2012) EMBO J , vol.31 , pp. 3745-3756
    • Soto-Rifo, R.1    Rubilar, P.S.2    Limousin, T.3
  • 108
    • 84859741492 scopus 로고    scopus 로고
    • Regulation of neuronal mRNA translation by CaM-kinase i phosphorylation of eIF4GII
    • Srivastava T, Fortin DA, Nygaard S, et al. (2012). Regulation of neuronal mRNA translation by CaM-kinase I phosphorylation of eIF4GII. J Neurosci 32:5620-30.
    • (2012) J Neurosci , vol.32 , pp. 5620-5630
    • Srivastava, T.1    Fortin, D.A.2    Nygaard, S.3
  • 109
    • 55549137084 scopus 로고    scopus 로고
    • The 3 proximal translational enhancer of Turnip crinkle virus binds to 60S ribosomal subunits
    • Stupina VA, Meskauskas A, Mccormack JC, et al. (2008). The 3 proximal translational enhancer of Turnip crinkle virus binds to 60S ribosomal subunits. RNA 14:2379-93.
    • (2008) RNA , vol.14 , pp. 2379-2393
    • Stupina, V.A.1    Meskauskas, A.2    McCormack, J.C.3
  • 110
    • 79953171531 scopus 로고    scopus 로고
    • PI3K-mTORC1 attenuates stress response by inhibiting cap-independent Hsp70 translation
    • Sun J, Conn CS, Han Y, et al. (2011). PI3K-mTORC1 attenuates stress response by inhibiting cap-independent Hsp70 translation. J Biol Chem 286:6791-800.
    • (2011) J Biol Chem , vol.286 , pp. 6791-6800
    • Sun, J.1    Conn, C.S.2    Han, Y.3
  • 111
    • 0035032444 scopus 로고    scopus 로고
    • The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5 secondary structure
    • Svitkin YV, Pause A, Haghighat A, et al. (2001). The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5 secondary structure. RNA 7: 382-94.
    • (2001) RNA , vol.7 , pp. 382-394
    • Svitkin, Y.V.1    Pause, A.2    Haghighat, A.3
  • 112
    • 33847199335 scopus 로고    scopus 로고
    • EIF4E function in somatic cells modulates ageing in Caenorhabditis elegans
    • Syntichaki P, Troulinaki K, Tavernarakis N. (2007). eIF4E function in somatic cells modulates ageing in Caenorhabditis elegans. Nature 445:922-6.
    • (2007) Nature , vol.445 , pp. 922-926
    • Syntichaki, P.1    Troulinaki, K.2    Tavernarakis, N.3
  • 113
    • 13844255528 scopus 로고    scopus 로고
    • Evolutionarily conserved non-AUG translation initiation in NAT1/p97/DAP5 (EIF4G2)
    • Takahashi K, Maruyama M, Tokuzawa Y, et al. (2005). Evolutionarily conserved non-AUG translation initiation in NAT1/p97/DAP5 (EIF4G2). Genomics 85:360-71.
    • (2005) Genomics , vol.85 , pp. 360-371
    • Takahashi, K.1    Maruyama, M.2    Tokuzawa, Y.3
  • 114
    • 84873621295 scopus 로고    scopus 로고
    • A novel mechanism of eukaryotic translation initiation that is neither m7G-cap-, nor IRES-dependent
    • Terenin IM, Andreev DE, Dmitriev SE, Shatsky IN. (2013). A novel mechanism of eukaryotic translation initiation that is neither m7G-cap-, nor IRES-dependent. Nucleic Acids Res 41: 1807-16.
    • (2013) Nucleic Acids Res , vol.41 , pp. 1807-1816
    • Terenin, I.M.1    Andreev, D.E.2    Dmitriev, S.E.3    Shatsky, I.N.4
  • 115
    • 23844558098 scopus 로고    scopus 로고
    • A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry
    • Terenin IM, Dmitriev SE, Andreev DE, et al. (2005). A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry. Mol Cell Biol 25:7879-88.
    • (2005) Mol Cell Biol , vol.25 , pp. 7879-7888
    • Terenin, I.M.1    Dmitriev, S.E.2    Andreev, D.E.3
  • 116
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation of mRNA translation
    • Thoreen CC, Chantranupong L, Keys HR, et al. (2012). A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485:109-13.
    • (2012) Nature , vol.485 , pp. 109-113
    • Thoreen, C.C.1    Chantranupong, L.2    Keys, H.R.3
  • 117
    • 38049016441 scopus 로고    scopus 로고
    • The 3 cap-independent translation element of Barley yellow dwarf virus binds eIF4F via the eIF4G subunit to initiate translation
    • Treder K, Kneller EL, Allen EM, et al. (2008). The 3 cap-independent translation element of Barley yellow dwarf virus binds eIF4F via the eIF4G subunit to initiate translation. RNA 14:134-47.
    • (2008) RNA , vol.14 , pp. 134-147
    • Treder, K.1    Kneller, E.L.2    Allen, E.M.3
  • 118
    • 84861944874 scopus 로고    scopus 로고
    • An oxygen-regulated switch in the protein synthesis machinery
    • Uniacke J, Holterman CE, Lachance G, et al. (2012). An oxygen-regulated switch in the protein synthesis machinery. Nature 486: 126-9.
    • (2012) Nature , vol.486 , pp. 126-129
    • Uniacke, J.1    Holterman, C.E.2    Lachance, G.3
  • 119
    • 84875906203 scopus 로고    scopus 로고
    • Structural analysis of the DAP5 MIF4G domain and its interaction with eIF4A
    • Virgili G, Frank F, Feoktistova K, et al. (2013). Structural analysis of the DAP5 MIF4G domain and its interaction with eIF4A. Structure 21: 517-27.
    • (2013) Structure , vol.21 , pp. 517-527
    • Virgili, G.1    Frank, F.2    Feoktistova, K.3
  • 120
    • 0034730734 scopus 로고    scopus 로고
    • Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5-Cap by domains of eIF4G
    • Von Der Haar T, Ball PD, McCarthy JE. (2000). Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5-Cap by domains of eIF4G. J Biol Chem 275:30551-5.
    • (2000) J Biol Chem , vol.275 , pp. 30551-30555
    • Von Der Haar, T.1    Ball, P.D.2    McCarthy, J.E.3
  • 121
    • 84884849501 scopus 로고    scopus 로고
    • Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins
    • Von Moeller H, Lerner R, Ricciardi A, et al. (2013). Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins. Nucleic Acids Res 41:7960-71.
    • (2013) Nucleic Acids Res , vol.41 , pp. 7960-7971
    • Von Moeller, H.1    Lerner, R.2    Ricciardi, A.3
  • 122
    • 77950671415 scopus 로고    scopus 로고
    • The nematode eukaryotic translation initiation factor 4E/G complex works with a trans-spliced leader stem-loop to enable efficient translation of trimethylguanosine-capped RNAs
    • Wallace A, Filbin ME, Veo B, et al. (2010). The nematode eukaryotic translation initiation factor 4E/G complex works with a trans-spliced leader stem-loop to enable efficient translation of trimethylguanosine-capped RNAs. Mol Cell Biol 30:1958-70.
    • (2010) Mol Cell Biol , vol.30 , pp. 1958-1970
    • Wallace, A.1    Filbin, M.E.2    Veo, B.3
  • 123
    • 80051637832 scopus 로고    scopus 로고
    • MTORC1 signaling: What we still don't know
    • Wang X, Proud CG. (2011). mTORC1 signaling: what we still don't know. J Mol Cell Biol 3:206-20.
    • (2011) J Mol Cell Biol , vol.3 , pp. 206-220
    • Wang, X.1    Proud, C.G.2
  • 124
    • 0031048641 scopus 로고    scopus 로고
    • A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme
    • Yamanaka S, Poksay KS, Arnold KS, Innerarity TL. (1997). A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme. Genes Dev 11:321-33.
    • (1997) Genes Dev , vol.11 , pp. 321-333
    • Yamanaka, S.1    Poksay, K.S.2    Arnold, K.S.3    Innerarity, T.L.4
  • 125
    • 0034676036 scopus 로고    scopus 로고
    • Essential role of NAT1/p97/DAP5 in embryonic differentiation and the retinoic acid pathway
    • Yamanaka S, Zhang XY, Maeda M, et al. (2000). Essential role of NAT1/p97/DAP5 in embryonic differentiation and the retinoic acid pathway. EMBO J 19:5533-41.
    • (2000) EMBO J , vol.19 , pp. 5533-5541
    • Yamanaka, S.1    Zhang, X.Y.2    Maeda, M.3
  • 126
    • 84862979524 scopus 로고    scopus 로고
    • Translational homeostasis via the mRNA cap-binding protein, eIF4E
    • Yanagiya A, Suyama E, Adachi H, et al. (2012). Translational homeostasis via the mRNA cap-binding protein, eIF4E. Mol Cell 46:847-58.
    • (2012) Mol Cell , vol.46 , pp. 847-858
    • Yanagiya, A.1    Suyama, E.2    Adachi, H.3
  • 127
    • 70349438679 scopus 로고    scopus 로고
    • 4E-BP extends lifespan upon dietary restriction by enhancing mitochondrial activity in Drosophila
    • Zid BM, Rogers AN, Katewa SD, et al. (2009). 4E-BP extends lifespan upon dietary restriction by enhancing mitochondrial activity in Drosophila. Cell 139:149-60.
    • (2009) Cell , vol.139 , pp. 149-160
    • Zid, B.M.1    Rogers, A.N.2    Katewa, S.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.