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Volumn 10, Issue 1, 2013, Pages 19-32

The DEAD-box helicase eIF4A: Paradigm or the odd one out?

Author keywords

ATP driven conformational changes; DEAD box helicase; RNA unwinding; Translation initiation

Indexed keywords

ADENOSINE TRIPHOSPHATE; INITIATION FACTOR; INITIATION FACTOR 4A; INITIATION FACTOR 4B; INITIATION FACTOR 4G; INITIATION FACTOR 4H; UNCLASSIFIED DRUG;

EID: 84875123899     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.21966     Document Type: Review
Times cited : (106)

References (158)
  • 1
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • DOI 10.1016/j.gene.2005.10.019, PII S0378111905006359
    • Cordin O, Banroques J, Tanner NK, Linder P. The DEAD-box protein family of RNA helicases. Gene 2006; 367:17-37; PMID:16337753; http://dx.doi. org/10.1016/j.gene.2005.10.019. (Pubitemid 43286737)
    • (2006) Gene , vol.367 , Issue.1-2 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 2
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • PMID:18573084
    • Pyle AM. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys 2008; 37:317-36; PMID:18573084; http://dx.doi. org/10.1146/annurev.biophys.37.032807.125908.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 3
    • 70350089113 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
    • PMID:19747077
    • Hilbert M, Karow AR, Klostermeier D. The mechanism of ATP-dependent RNA unwinding by DEAD box proteins. Biol Chem 2009; 390:1237-50; PMID:19747077; http://dx.doi.org/10.1515/BC.2009.135.
    • (2009) Biol Chem , vol.390 , pp. 1237-1250
    • Hilbert, M.1    Karow, A.R.2    Klostermeier, D.3
  • 4
    • 79960724199 scopus 로고    scopus 로고
    • From unwinding to clamping-The DEAD box RNA helicase family
    • PMID:21779027
    • Linder P, Jankowsky E. From unwinding to clamping-the DEAD box RNA helicase family. Nat Rev Mol Cell Biol 2011; 12:505-16; PMID:21779027; http://dx.doi.org/10.1038/nrm3154.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 505-516
    • Linder, P.1    Jankowsky, E.2
  • 5
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • PMID:10212190
    • Rogers GW Jr., Richter NJ, Merrick WC. Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J Biol Chem 1999; 274:12236-44; PMID:10212190; http://dx.doi. org/10.1074/jbc.274.18.12236.
    • (1999) J Biol Chem , vol.274 , pp. 12236-12244
    • Rogers Jr., G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 6
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • DOI 10.1021/bi972430g
    • Lorsch JR, Herschlag D. The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry 1998; 37:2180-93; PMID:9485364; http://dx.doi.org/10.1021/bi972430g (Pubitemid 28119291)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 7
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • PMID:11087862
    • Caruthers JM, Johnson ER, McKay DB. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA 2000; 97:13080-5; PMID:11087862; http://dx.doi.org/10.1073/pnas.97.24.13080.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 9
    • 23644449094 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of DEAD-box protein Dhh1p
    • DOI 10.1261/rna.2920905
    • Cheng Z, Coller J, Parker R, Song H. Crystal structure and functional analysis of DEAD-box protein Dhh1p. RNA 2005; 11:1258-70; PMID:15987810; http://dx.doi.org/10.1261/rna.2920905. (Pubitemid 41132397)
    • (2005) RNA , vol.11 , Issue.8 , pp. 1258-1270
    • Cheng, Z.1    Coller, J.2    Parker, R.3    Song, H.4
  • 12
    • 37749032415 scopus 로고    scopus 로고
    • The Bacillus subtilis RNA helicase YxiN is distended in solution
    • PMID:17951299
    • Wang S, Overgaard MT, Hu Y, McKay DB. The Bacillus subtilis RNA helicase YxiN is distended in solution. Biophys J 2008; 94:L01-03; PMID:17951299; http://dx.doi.org/10.1529/biophysj.107.120709.
    • (2008) Biophys J , vol.94
    • Wang, S.1    Overgaard, M.T.2    Hu, Y.3    McKay, D.B.4
  • 14
    • 67949115632 scopus 로고    scopus 로고
    • A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN
    • PMID:19474341
    • Karow AR, Klostermeier D. A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN. Nucleic Acids Res 2009; 37:4464-71; PMID:19474341; http://dx.doi.org/10.1093/ nar/gkp397.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4464-4471
    • Karow, A.R.1    Klostermeier, D.2
  • 15
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • PMID:16630817
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 2006; 125:287-300; PMID:16630817; http://dx.doi. org/10.1016/j.cell.2006.01.054.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 16
    • 33747182255 scopus 로고    scopus 로고
    • The Crystal Structure of the Exon Junction Complex Reveals How It Maintains a Stable Grip on mRNA
    • DOI 10.1016/j.cell.2006.08.006, PII S0092867406010270
    • Bono F, Ebert J, Lorentzen E, Conti E. The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 2006; 126:713-25; PMID:16923391; http://dx.doi.org/10.1016/j. cell.2006.08.006. (Pubitemid 44233638)
    • (2006) Cell , vol.126 , Issue.4 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 17
    • 0043199343 scopus 로고    scopus 로고
    • The newly identified Q motif of DEAD box helicases is involved in adenine recognition
    • PMID:12695678
    • Tanner NK. The newly identified Q motif of DEAD box helicases is involved in adenine recognition. Cell Cycle 2003; 2:18-9; PMID:12695678; http://dx.doi. org/10.4161/cc.2.1.296.
    • (2003) Cell Cycle , vol.2 , pp. 18-19
    • Tanner, N.K.1
  • 18
    • 0032562221 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes
    • DOI 10.1021/bi9724319
    • Lorsch JR, Herschlag D. The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes. Biochemistry 1998; 37:2194-206; PMID:9485365; http://dx.doi.org/10.1021/bi9724319. (Pubitemid 28119292)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 19
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-Box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • DOI 10.1016/S0092-8674(02)00771-7
    • Mohr S, Stryker JM, Lambowitz AM. A DEAD-box protein functions as an ATP-dependent RNA chaper-one in group I intron splicing. Cell 2002; 109:769-79; PMID:12086675; http://dx.doi.org/10.1016/S0092-8674(02)00771-7. (Pubitemid 34722271)
    • (2002) Cell , vol.109 , Issue.6 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 20
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • DOI 10.1021/bi012062n
    • Polach KJ, Uhlenbeck OC. Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry 2002; 41:3693-702; PMID:11888286; http://dx.doi.org/10.1021/bi012062n. (Pubitemid 34224682)
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2
  • 21
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • DOI 10.1038/sj.emboj.7600272
    • Cordin O, Tanner NK, Doère M, Linder P, Banroques J. The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J 2004; 23:2478-87; PMID:15201868; http://dx.doi.org/10.1038/sj. emboj.7600272. (Pubitemid 38988220)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 22
    • 38349186157 scopus 로고    scopus 로고
    • Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype
    • PMID:17986459
    • Elles LM, Uhlenbeck OC. Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype. Nucleic Acids Res 2008; 36:41-50; PMID:17986459; http://dx.doi. org/10.1093/nar/gkm926.
    • (2008) Nucleic Acids Res , vol.36 , pp. 41-50
    • Elles, L.M.1    Uhlenbeck, O.C.2
  • 23
    • 39649096274 scopus 로고    scopus 로고
    • The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
    • PMID:18237742
    • Henn A, Cao W, Hackney DD, De La Cruz EM. The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. J Mol Biol 2008; 377:193-205; PMID:18237742; http://dx.doi.org/10.1016/j. jmb.2007.12.046.
    • (2008) J Mol Biol , vol.377 , pp. 193-205
    • Henn, A.1    Cao, W.2    Hackney, D.D.3    De La Cruz, E.M.4
  • 24
    • 33947362880 scopus 로고    scopus 로고
    • Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA
    • DOI 10.1021/bi0619472
    • Grohman JK, Del Campo M, Bhaskaran H, Tijerina P, Lambowitz AM, Russell R. Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA. Biochemistry 2007; 46:3013-22; PMID:17311413; http://dx.doi.org/10.1021/bi0619472. (Pubitemid 46449125)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3013-3022
    • Grohman, J.K.1    Del Campo, M.2    Bhaskaran, H.3    Tijerina, P.4    Lambowitz, A.M.5    Russell, R.6
  • 25
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • PMID:18096186
    • Mohr G, Del Campo M, Mohr S, Yang Q, Jia H, Jankowsky E, et al. Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro. J Mol Biol 2008; 375:1344-64; PMID:18096186; http://dx.doi.org/10.1016/ j. jmb.2007.11.041.
    • (2008) J Mol Biol , vol.375 , pp. 1344-1364
    • Mohr, G.1    Del Campo, M.2    Mohr, S.3    Yang, Q.4    Jia, H.5    Jankowsky, E.6
  • 26
    • 84862975911 scopus 로고    scopus 로고
    • Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer
    • PMID:22713316
    • Andreou AZ, Klostermeier D. Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer. Methods Enzymol 2012; 511:75-109; PMID:22713316.
    • (2012) Methods Enzymol , vol.511 , pp. 75-109
    • Andreou, A.Z.1    Klostermeier, D.2
  • 27
    • 0032883203 scopus 로고    scopus 로고
    • Effects of oligonucleotide length and atomic composition on stimulation of the ATPase activity of translation initiation factor eIF4A
    • DOI 10.1017/S1355838299990817
    • Peck ML, Herschlag D. Effects of oligonucleotide length and atomic composition on stimulation of the ATPase activity of translation initiation factor elF4A. RNA 1999; 5:1210-21; PMID:10496222; http://dx.doi.org/10.1017/ S1355838299990817. (Pubitemid 29422763)
    • (1999) RNA , vol.5 , Issue.9 , pp. 1210-1221
    • Peck, M.L.1    Herschlag, D.2
  • 28
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA
    • PMID:19748356
    • Del Campo M, Lambowitz AM. Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell 2009; 35:598-609; PMID:19748356; http://dx.doi.org/10.1016/j.mol-cel.2009.07.032.
    • (2009) Mol Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 29
    • 70449584733 scopus 로고    scopus 로고
    • The DEAD box heli-case YxiN maintains a closed conformation during ATP hydrolysis
    • PMID:19839642
    • Aregger R, Klostermeier D. The DEAD box heli-case YxiN maintains a closed conformation during ATP hydrolysis. Biochemistry 2009; 48:10679-81; PMID:19839642; http://dx.doi.org/10.1021/bi901278p.
    • (2009) Biochemistry , vol.48 , pp. 10679-10681
    • Aregger, R.1    Klostermeier, D.2
  • 30
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • PMID:19088201
    • Liu F, Putnam A, Jankowsky E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc Natl Acad Sci USA 2008; 105:20209-14; PMID:19088201; http://dx.doi. org/10.1073/pnas.0811115106.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 31
    • 58149503706 scopus 로고    scopus 로고
    • DEAD-box proteins can completely separate an RNA duplex using a single ATP
    • PMID:19088196
    • Chen Y, Potratz J P, Tijerina P, Del Campo M, Lambowitz AM, Russell R. DEAD-box proteins can completely separate an RNA duplex using a single ATP. Proc Natl Acad Sci USA 2008; 105:20203-8; PMID:19088196; http://dx.doi.org/10.1073/ pnas.0811075106.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20203-20208
    • Chen, Y.1    Potratz, J.P.2    Tijerina, P.3    Del Campo, M.4    Lambowitz, A.M.5    Russell, R.6
  • 32
    • 62549164363 scopus 로고    scopus 로고
    • Crystal structure of the eIF4A-PDCD4 complex
    • PMID:19204291
    • Chang JH, Cho YH, Sohn SY, Choi JM, Kim A, Kim YC, et al. Crystal structure of the eIF4A-PDCD4 complex. Proc Natl Acad Sci USA 2009; 106:3148-53; PMID:19204291; http://dx.doi.org/10.1073/pnas.0808275106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3148-3153
    • Chang, J.H.1    Cho, Y.H.2    Sohn, S.Y.3    Choi, J.M.4    Kim, A.5    Kim, Y.C.6
  • 33
    • 0037378193 scopus 로고    scopus 로고
    • RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis
    • DOI 10.1261/rna.2161303
    • Oguro A, Ohtsu T, Svitkin YV, Sonenberg N, Nakamura Y. RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis. RNA 2003; 9:394-407; PMID:12649492; http://dx.doi.org/10.1261/rna. 2161303. (Pubitemid 36356727)
    • (2003) RNA , vol.9 , Issue.4 , pp. 394-407
    • Oguro, A.1    Ohtsu, T.2    Svitkin, Y.V.3    Sonenberg, N.4    Nakamura, Y.5
  • 34
    • 58149092125 scopus 로고    scopus 로고
    • Mechanism of ATP turnover inhibition in the EJC
    • PMID:19033377
    • Nielsen KH, Chamieh H, Andersen CB, Fredslund F, Hamborg K, Le Hir H, et al. Mechanism of ATP turnover inhibition in the EJC. RNA 2009; 15:67-75; PMID:19033377; http://dx.doi.org/10.1261/rna.1283109.
    • (2009) RNA , vol.15 , pp. 67-75
    • Nielsen, K.H.1    Chamieh, H.2    Andersen, C.B.3    Fredslund, F.4    Hamborg, K.5    Le Hir, H.6
  • 36
    • 79953675393 scopus 로고    scopus 로고
    • EIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
    • PMID:21062831
    • Hilbert M, Kebbel F, Gubaev A, Klostermeier D. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res 2011; 39:2260-70; PMID:21062831; http://dx.doi.org/10.1093/ nar/gkq1127.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 37
    • 67449105353 scopus 로고    scopus 로고
    • The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch
    • PMID:19244245
    • Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, et al. The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch. J Biol Chem 2009; 284:10296-300; PMID:19244245; http://dx.doi.org/10.1074/jbc.C900018200.
    • (2009) J Biol Chem , vol.284 , pp. 10296-10300
    • Collins, R.1    Karlberg, T.2    Lehtiö, L.3    Schütz, P.4    Van Den Berg, S.5    Dahlgren, L.G.6
  • 38
    • 63649159790 scopus 로고    scopus 로고
    • Solution and crystal structures of mRNA exporter Dbp5p and its interaction with nucleotides
    • PMID:19281819
    • Fan JS, Cheng Z, Zhang J, Noble C, Zhou Z, Song H, et al. Solution and crystal structures of mRNA exporter Dbp5p and its interaction with nucleotides. J Mol Biol 2009; 388:1-10; PMID:19281819; http://dx.doi. org/10.1016/j.jmb.2009. 03.004.
    • (2009) J Mol Biol , vol.388 , pp. 1-10
    • Fan, J.S.1    Cheng, Z.2    Zhang, J.3    Noble, C.4    Zhou, Z.5    Song, H.6
  • 39
    • 62549108142 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19
    • PMID:19208808
    • Napetschnig J, Kassube SA, Debler EW, Wong RW, Blobel G, Hoelz A. Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19. Proc Natl Acad Sci USA 2009; 106:3089-94; PMID:19208808; http://dx.doi.org/10.1073/pnas.0813267106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3089-3094
    • Napetschnig, J.1    Kassube, S.A.2    Debler, E.W.3    Wong, R.W.4    Blobel, G.5    Hoelz, A.6
  • 40
    • 62049084648 scopus 로고    scopus 로고
    • The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleo-porin NUP214 in a mutually exclusive manner
    • PMID:19219046
    • von Moeller H, Basquin C, Conti E. The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleo-porin NUP214 in a mutually exclusive manner. Nat Struct Mol Biol 2009; 16:247-54; PMID:19219046; http://dx.doi.org/10.1038/nsmb. 1561.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 247-254
    • Von Moeller, H.1    Basquin, C.2    Conti, E.3
  • 41
    • 0036927393 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the DExD/H protein YxiN is sufficient to confer specificity for 23 S rRNA
    • DOI 10.1016/S0022-2836(02)01140-3
    • Kossen K, Karginov FV, Uhlenbeck OC. The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA. J Mol Biol 2002; 324:625-36; PMID:12460566; http://dx.doi. org/10.1016/S0022-2836(02)01140- 3. (Pubitemid 36044102)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.4 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 42
    • 54549123661 scopus 로고    scopus 로고
    • The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity
    • PMID:18782831
    • Linden MH, Hartmann RK, Klostermeier D. The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity. Nucleic Acids Res 2008; 36:5800-11; PMID:18782831; http://dx.doi.org/10.1093/nar/gkn581.
    • (2008) Nucleic Acids Res , vol.36 , pp. 5800-5811
    • Linden, M.H.1    Hartmann, R.K.2    Klostermeier, D.3
  • 43
    • 0037215580 scopus 로고    scopus 로고
    • A novel domain within the DEAD-box protein DP103 is essential for transcriptional repression and helicase activity
    • DOI 10.1128/MCB.23.1.414-423.2003
    • Yan X, Mouillet J F, Ou Q, Sadovsky Y. A novel domain within the DEAD-box protein DP103 is essential for transcriptional repression and helicase activity. Mol Cell Biol 2003; 23:414-23; PMID:12482992; http://dx.doi.org/10. 1128/MCB.23.1.414-423.2003. (Pubitemid 36008531)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.1 , pp. 414-423
    • Yan, X.1    Mouillet, J.-F.2    Ou, Q.3    Sadovsky, Y.4
  • 44
    • 59649110939 scopus 로고    scopus 로고
    • A novel dimeriza-tion motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility
    • PMID:19050012
    • Klostermeier D, Rudolph MG. A novel dimeriza-tion motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. Nucleic Acids Res 2009; 37:421-30; PMID:19050012; http://dx.doi.org/10.1093/nar/gkn947.
    • (2009) Nucleic Acids Res , vol.37 , pp. 421-430
    • Klostermeier, D.1    Rudolph, M.G.2
  • 45
    • 0024967639 scopus 로고
    • Birth of the D-E-A-D box. [erratum appears in Nature 1989 Jul 20;340(6230):246]
    • PMID:2563148
    • Linder P, Lasko P F, Ashburner M, Leroy P, Nielsen PJ, Nishi K, et al. Birth of the D-E-A-D box. [erratum appears in Nature 1989 Jul 20;340(6230):246]. Nature 1989; 337:121-2; PMID:2563148; http://dx.doi.org/10.1038/337121a0.
    • (1989) Nature , vol.337 , pp. 121-122
    • Linder, P.1    Lasko, P.F.2    Ashburner, M.3    Leroy, P.4    Nielsen, P.J.5    Nishi, K.6
  • 46
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • PMID:1552844
    • Schmid SR, Linder P. D-E-A-D protein family of putative RNA helicases. Mol Microbiol 1992; 6:283-91; PMID:1552844; http://dx.doi. org/10.1111/j.1365- 2958.1992.tb01470.x.
    • (1992) Mol Microbiol , vol.6 , pp. 283-291
    • Schmid, S.R.1    Linder, P.2
  • 47
    • 0036048086 scopus 로고    scopus 로고
    • EIF4A: The godfather of the DEAD box helicases
    • PMID:12206455
    • Rogers GW Jr., Komar AA, Merrick WC. eIF4A: the godfather of the DEAD box helicases. Prog Nucleic Acid Res Mol Biol 2002; 72:307-31; PMID:12206455; http://dx.doi.org/10.1016/S0079-6603(02)72073-4.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.72 , pp. 307-331
    • Rogers Jr., G.W.1    Komar, A.A.2    Merrick, W.C.3
  • 48
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • PMID:1378397
    • Pause A, Sonenberg N. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J 1992; 11:2643-54; PMID:1378397.
    • (1992) EMBO J , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 49
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause A, Méthot N, Sonenberg N. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol Cell Biol 1993; 13:6789-98; PMID:8413273. (Pubitemid 23321132)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.11 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 51
    • 0032763657 scopus 로고    scopus 로고
    • Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase
    • PMID:10606264
    • Johnson ER, McKay DB. Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase. RNA 1999; 5:1526-34; PMID:10606264; http://dx.doi. org/10.1017/ S1355838299991410.
    • (1999) RNA , vol.5 , pp. 1526-1534
    • Johnson, E.R.1    McKay, D.B.2
  • 52
    • 0010456859 scopus 로고    scopus 로고
    • Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae - The prototype of the DEAD box protein family
    • DOI 10.1016/S0969-2126(99)80088-4
    • Benz J, Trachsel H, Baumann U. Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae-the prototype of the DEAD box protein family. Structure 1999; 7:671-9; PMID:10404596; http://dx.doi.org/10.1016/S0969-2126(99)80088-4. (Pubitemid 29277420)
    • (1999) Structure , vol.7 , Issue.6 , pp. 671-679
    • Benz, J.1    Trachsel, H.2    Baumann, U.3
  • 53
    • 59049092956 scopus 로고    scopus 로고
    • Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
    • PMID:19203580
    • Marintchev A, Edmonds KA, Marintcheva B, Hendrickson E, Oberer M, Suzuki C, et al. Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 2009; 136:447-60; PMID:19203580; http://dx.doi.org/10.1016/j. cell.2009.01.014.
    • (2009) Cell , vol.136 , pp. 447-460
    • Marintchev, A.1    Edmonds, K.A.2    Marintcheva, B.3    Hendrickson, E.4    Oberer, M.5    Suzuki, C.6
  • 54
    • 0024039480 scopus 로고
    • The mouse protein synthesis initiation factor 4A gene family includes two related functional genes which are differentially expressed
    • PMID:3046931
    • Nielsen PJ, Trachsel H. The mouse protein synthesis initiation factor 4A gene family includes two related functional genes which are differentially expressed. EMBO J 1988; 7:2097-105; PMID:3046931.
    • (1988) EMBO J , vol.7 , pp. 2097-2105
    • Nielsen, P.J.1    Trachsel, H.2
  • 55
    • 0030913841 scopus 로고    scopus 로고
    • Differential expression of the murine eukaryotic translation initiation factor isogenes eIF4A(I) and eIF4A(II) is dependent upon cellular growth status
    • DOI 10.1006/abbi.1996.9804
    • Williams-Hill DM, Duncan R F, Nielsen PJ, Tahara SM. Differential expression of the murine eukaryotic translation initiation factor isogenes eIF4A(I) and eIF4A(II) is dependent upon cellular growth status. Arch Biochem Biophys 1997; 338:111-20; PMID:9015395; http://dx.doi.org/10.1006/abbi.1996. 9804. (Pubitemid 27200301)
    • (1997) Archives of Biochemistry and Biophysics , vol.338 , Issue.1 , pp. 111-120
    • Williams-Hill, D.M.1    Duncan, R.F.2    Nielsen, P.J.3    Tahara, S.M.4
  • 56
    • 84862520790 scopus 로고    scopus 로고
    • A cellular response linking eIF4AI activity to eIF4AII transcription
    • PMID:22589333
    • Galicia-Vázquez G, Cencic R, Robert F, Agenor AQ, Pelletier J. A cellular response linking eIF4AI activity to eIF4AII transcription. RNA 2012; 18:1373-84; PMID:22589333; http://dx.doi.org/10.1261/rna.033209.112.
    • (2012) RNA , vol.18 , pp. 1373-1384
    • Galicia-Vázquez, G.1    Cencic, R.2    Robert, F.3    Agenor, A.Q.4    Pelletier, J.5
  • 57
    • 0026091681 scopus 로고
    • Divergent genes for translation initiation factor elF-4A are coordinately expressed in tobacco
    • Owttrim GW, Hofmann S, Kuhlemeier C. Divergent genes for translation initiation factor eIF-4A are coor-dinately expressed in tobacco. Nucleic Acids Res 1991; 19:5491-6; PMID:1719476; http://dx.doi. org/10.1093/nar/19.20.5491. (Pubitemid 21912945)
    • (1991) Nucleic Acids Research , vol.19 , Issue.20 , pp. 5491-5496
    • Owttrim, G.W.1    Hofmann, S.2    Kuhlemeier, C.3
  • 59
    • 1842577707 scopus 로고    scopus 로고
    • EIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay
    • DOI 10.1038/nsmb750
    • Shibuya T, Tange TO, Sonenberg N, Moore MJ. eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay. Nat Struct Mol Biol 2004; 11:346-51; PMID:15034551; http://dx.doi.org/10.1038/ nsmb750. (Pubitemid 38436799)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.4 , pp. 346-351
    • Shibuya, T.1    Tange, T.O.2    Sonenberg, N.3    Moore, M.J.4
  • 61
    • 1442354190 scopus 로고    scopus 로고
    • An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay
    • DOI 10.1038/nature02351
    • Palacios IM, Gatfield D, St Johnston D, Izaurralde E. An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay. Nature 2004; 427:753-7; PMID:14973490; http://dx.doi.org/10.1038/ nature02351. (Pubitemid 38294596)
    • (2004) Nature , vol.427 , Issue.6976 , pp. 753-757
    • Palacios, I.M.1    Gatfield, D.2    St. Johnston, D.3    Izaurralde, E.4
  • 62
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: An additional function of the exon junction complex
    • DOI 10.1101/gad.1163204
    • Nott A, Le Hir H, Moore MJ. Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev 2004; 18:210-22; PMID:14752011; http://dx.doi.org/10.1101/gad.1163204. (Pubitemid 38141788)
    • (2004) Genes and Development , vol.18 , Issue.2 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 63
    • 0035687504 scopus 로고    scopus 로고
    • The protein Mago provides a link between splicing and mRNA localization
    • DOI 10.1093/embo-reports/kve245
    • Le Hir H, Gatfield D, Braun IC, Forler D, Izaurralde E. The protein Mago provides a link between splicing and mRNA localization. EMBO Rep 2001; 2:1119-24; PMID:11743026; http://dx.doi.org/10.1093/embo-reports/kve245. (Pubitemid 34055959)
    • (2001) EMBO Reports , vol.2 , Issue.12 , pp. 1119-1124
    • Le Hir, H.1    Gatfield, D.2    Braun, I.C.3    Forler, D.4    Izaurralde, E.5
  • 64
    • 18144441468 scopus 로고
    • Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding for a translation initiation factor
    • PMID:3057442
    • Linder P, Slonimski P P. Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding for a translation initiation factor. Nucleic Acids Res 1988; 16:10359; PMID:3057442; http://dx.doi. org/10.1093/nar/16.21. 10359.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10359
    • Linder, P.1    Slonimski, P.P.2
  • 67
    • 0021099436 scopus 로고
    • New initiation factor activity required for globin mRNA translation
    • PMID:6853548
    • Grifo JA, Tahara SM, Morgan MA, Shatkin AJ, Merrick WC. New initiation factor activity required for globin mRNA translation. J Biol Chem 1983; 258:5804-10; PMID:6853548.
    • (1983) J Biol Chem , vol.258 , pp. 5804-5810
    • Grifo, J.A.1    Tahara, S.M.2    Morgan, M.A.3    Shatkin, A.J.4    Merrick, W.C.5
  • 68
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • PMID:20094052
    • Jackson RJ, Hellen CU, Pestova T V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 2010; 11:113-27; PMID:20094052; http://dx.doi.org/10.1038/nrm2838.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 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
    • PMID:7651417
    • Mader S, Lee H, Pause A, Sonenberg N. 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 1995; 15:4990-7; PMID:7651417.
    • (1995) Mol Cell Biol , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 70
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picorna-viral proteases. Implications for cap-dependent and cap-independent translational initiation
    • PMID:7665619
    • Lamphear BJ, Kirchweger R, Skern T, Rhoads RE. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picorna-viral proteases. Implications for cap-dependent and cap-independent translational initiation. J Biol Chem 1995; 270:21975-83; PMID:7665619.
    • (1995) J Biol Chem , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 71
    • 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
    • DOI 10.1128/MCB.26.4.1355-1372.2006
    • Jivotovskaya AV, Valásek L, Hinnebusch AG, Nielsen KH. Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S sub-units independently of eIF4G in yeast. Mol Cell Biol 2006; 26:1355-72; PMID:16449648; http://dx.doi. org/10.1128/MCB.26.4.1355-1372.2006. (Pubitemid 43202562)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valasek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 72
    • 11844292767 scopus 로고    scopus 로고
    • MRNA heli-case activity of the ribosome
    • PMID:15652481
    • Takyar S, Hickerson R P, Noller H F. mRNA heli-case activity of the ribosome. Cell 2005; 120:49-58; PMID:15652481; http://dx.doi.org/10.1016/j. cell.2004.11.042.
    • (2005) Cell , vol.120 , pp. 49-58
    • Takyar, S.1    Hickerson, R.P.2    Noller, H.F.3
  • 73
    • 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
    • DOI 10.1017/S135583820100108X
    • Svitkin YV, Pause A, Haghighat A, Pyronnet S, Witherell G, Belsham GJ, et al. The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure. RNA 2001; 7:382-94; PMID:11333019; http://dx.doi.org/10.1017/S135583820100108X. (Pubitemid 32381914)
    • (2001) RNA , vol.7 , Issue.3 , pp. 382-394
    • Svitkin, Y.V.1    Pause, A.2    Haghighat, A.3    Pyronnet, S.4    Witherell, G.5    Belsham, G.J.6    Sonenberg, N.7
  • 75
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4 F
    • PMID:2304461
    • Rozen F, Edery I, Meerovitch K, Dever TE, Merrick WC, Sonenberg N. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4 F. Mol Cell Biol 1990; 10:1134-44; PMID:2304461.
    • (1990) Mol Cell Biol , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 76
    • 0021875798 scopus 로고
    • ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors
    • Ray BK, Lawson TG, Kramer JC, Cladaras MH, Grifo JA, Abramson RD, et al. ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors. J Biol Chem 1985; 260:7651-8; PMID:3838990. (Pubitemid 15063051)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.12 , pp. 7651-7658
    • Ray, B.K.1    Lawson, T.G.2    Kramer, J.C.3
  • 77
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian translation initiation factor elF-4A define a critical role for elF-4F in cap-dependent and cap-independent initiation of translation
    • Pause A, Méthot N, Svitkin Y, Merrick WC, Sonenberg N. Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation. EMBO J 1994; 13:1205-15; PMID:8131750. (Pubitemid 24074727)
    • (1994) EMBO Journal , vol.13 , Issue.5 , pp. 1205-1215
    • Pause, A.1    Methot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 78
    • 42449155947 scopus 로고    scopus 로고
    • Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking
    • DOI 10.1261/rna.971208
    • Lindqvist L, Imataka H, Pelletier J. Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking. RNA 2008; 14:960-9; PMID:18367715; http://dx.doi.org/10.1261/rna.971208. (Pubitemid 351574917)
    • (2008) RNA , vol.14 , Issue.5 , pp. 960-969
    • Lindqvist, L.1    Imataka, H.2    Pelletier, J.3
  • 79
    • 0037029091 scopus 로고    scopus 로고
    • Ribosome as a molecular machine
    • DOI 10.1016/S0014-5793(02)02309-8, PII S0014579302023098
    • Spirin AS. Ribosome as a molecular machine. FEBS Lett 2002; 514:2-10; PMID:11904172; http://dx.doi. org/10.1016/S0014-5793(02)02309-8. (Pubitemid 34251233)
    • (2002) FEBS Letters , vol.514 , Issue.1 , pp. 2-10
    • Spirin, A.S.1
  • 80
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • DOI 10.1126/science.291.5501.121
    • Jankowsky E, Gross CH, Shuman S, Pyle AM. Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 2001; 291:121-5; PMID:11141562; http://dx.doi.org/10.1126/sci-ence.291.5501.121. (Pubitemid 32056679)
    • (2001) Science , vol.291 , Issue.5501 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 81
    • 0037781588 scopus 로고    scopus 로고
    • Yeast RNA helicases of the DEAD-box family involved in translation initiation
    • DOI 10.1016/S0248-4900(03)00032-7
    • Linder P. Yeast RNA helicases of the DEAD-box family involved in translation initiation. Biol Cell 2003; 95:157-67; PMID:12867080; http://dx.doi. org/10.1016/S0248-4900(03)00032-7. (Pubitemid 36889218)
    • (2003) Biology of the Cell , vol.95 , Issue.3-4 , pp. 157-167
    • Linder, P.1
  • 83
    • 42349090351 scopus 로고    scopus 로고
    • Translational control by a small RNA: Dendritic BC1 RNA targets the eukaryotic initiation factor 4A helicase mechanism
    • DOI 10.1128/MCB.01800-07
    • Lin D, Pestova TV, Hellen CU, Tiedge H. Translational control by a small RNA: dendritic BC1 RNA targets the eukaryotic initiation factor 4A helicase mechanism. Mol Cell Biol 2008; 28:3008-19; PMID:18316401; http://dx.doi.org/10. 1128/MCB.01800-07. (Pubitemid 351556532)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.9 , pp. 3008-3019
    • Lin, D.1    Pestova, T.V.2    Hellen, C.U.T.3    Tiedge, H.4
  • 84
    • 77953422876 scopus 로고    scopus 로고
    • Inhibitors of translation initiation as cancer therapeutics
    • PMID:21425987
    • Lindqvist L, Pelletier J. Inhibitors of translation initiation as cancer therapeutics. Future Med Chem 2009; 1:1709-22; PMID:21425987; http://dx.doi. org/10.4155/fmc.09.122.
    • (2009) Future Med Chem , vol.1 , pp. 1709-1722
    • Lindqvist, L.1    Pelletier, J.2
  • 85
    • 0030919560 scopus 로고    scopus 로고
    • Translation initiation factor eIF-4A1 mRNA is consistently overexpressed in human melanoma cells in vitro
    • DOI 10.1002/(SICI)1097-0215(19970502)71:3<396::AID-IJC16>3.0.CO;2-E
    • Eberle J, Krasagakis K, Orfanos CE. Translation initiation factor eIF-4A1 mRNA is consistently overexpressed in human melanoma cells in vitro. Int J Cancer 1997; 71:396-401; PMID:9139875; http://dx.doi.org/10.1002/(SICI)1097- 0215(19970502)71:33.0.CO;2-E. (Pubitemid 27224304)
    • (1997) International Journal of Cancer , vol.71 , Issue.3 , pp. 396-401
    • Eberle, J.1    Krasagakis, K.2    Orfanos, C.E.3
  • 87
    • 33749868662 scopus 로고    scopus 로고
    • Involvement of programmed cell death 4 in transforming growth factor-β1-induced apoptosis in human hepatocellular carcinoma
    • DOI 10.1038/sj.onc.1209634, PII 1209634
    • Zhang H, Ozaki I, Mizuta T, Hamajima H, Yasutake T, Eguchi Y, et al. Involvement of programmed cell death 4 in transforming growth factor-beta1-induced apop-tosis in human hepatocellular carcinoma. Oncogene 2006; 25:6101-12; PMID:16682950; http://dx.doi. org/10.1038/sj.onc.1209634. (Pubitemid 44562408)
    • (2006) Oncogene , vol.25 , Issue.45 , pp. 6101-6112
    • Zhang, H.1    Ozaki, I.2    Mizuta, T.3    Hamajima, H.4    Yasutake, T.5    Eguchi, Y.6    Ideguchi, H.7    Yamamoto, K.8    Matsuhashi, S.9
  • 88
    • 0042524204 scopus 로고    scopus 로고
    • Loss of PDCD4 expression in human lung cancer correlates with tumour progression and prognosis
    • DOI 10.1002/path.1378
    • Chen Y, Knösel T, Kristiansen G, Pietas A, Garber ME, Matsuhashi S, et al. Loss of PDCD4 expression in human lung cancer correlates with tumour progression and prognosis. J Pathol 2003; 200:640-6; PMID:12898601; http://dx.doi.org/10.1002/path.1378. (Pubitemid 36987314)
    • (2003) Journal of Pathology , vol.200 , Issue.5 , pp. 640-646
    • Chen, Y.1    Knosel, T.2    Kristiansen, G.3    Pietas, A.4    Garber, M.E.5    Matsuhashi, S.6    Ozaki, I.7    Petersen, I.8
  • 89
    • 38449088795 scopus 로고    scopus 로고
    • Alterations in the expression of PDCD4 in ductal carcinoma of the breast
    • PMID:17982621
    • Wen YH, Shi X, Chiriboga L, Matsahashi S, Yee H, Afonja O. Alterations in the expression of PDCD4 in ductal carcinoma of the breast. Oncol Rep 2007; 18:1387-93; PMID:17982621.
    • (2007) Oncol Rep , vol.18 , pp. 1387-1393
    • Wen, Y.H.1    Shi, X.2    Chiriboga, L.3    Matsahashi, S.4    Yee, H.5    Afonja, O.6
  • 90
    • 35248889933 scopus 로고    scopus 로고
    • Loss of programmed cell death 4 expression marks adenoma-carcinoma transition, correlates inversely with phosphorylated protein kinase B, and is an independent prognostic factor in resected colorectal cancer
    • DOI 10.1002/cncr.22983
    • Mudduluru G, Medved F, Grobholz R, Jost C, Gruber A, Leupold JH, et al. Loss of programmed cell death 4 expression marks adenoma-carcinoma transition, correlates inversely with phosphorylated protein kinase B, and is an independent prognostic factor in resected colorectal cancer. Cancer 2007; 110:1697-707; PMID:17849461; http://dx.doi.org/10.1002/cncr.22983. (Pubitemid 47558956)
    • (2007) Cancer , vol.110 , Issue.8 , pp. 1697-1707
    • Mudduluru, G.1    Medved, F.2    Grobholz, R.3    Jost, C.4    Gruber, A.5    Leupold, J.H.6    Post, S.7    Jansen, A.8    Colburn, N.H.9    Allgayer, H.10
  • 91
    • 38149139712 scopus 로고    scopus 로고
    • Frequent loss of PDCD4 expression in human glioma: Possible role in the tumorigenesis of glioma
    • PMID:17143488
    • Gao F, Zhang P, Zhou C, Li J, Wang Q, Zhu F, et al. Frequent loss of PDCD4 expression in human glioma: possible role in the tumorigenesis of glioma. Oncol Rep 2007; 17:123-8; PMID:17143488.
    • (2007) Oncol Rep , vol.17 , pp. 123-128
    • Gao, F.1    Zhang, P.2    Zhou, C.3    Li, J.4    Wang, Q.5    Zhu, F.6
  • 92
    • 84863450258 scopus 로고    scopus 로고
    • RNA helicases in infection and disease
    • PMID:22699555
    • Steimer L, Klostermeier D. RNA helicases in infection and disease. RNA Biol 2012; 9; PMID:22699555; http://dx.doi.org/10.4161/rna.20090.
    • (2012) RNA Biol , vol.9
    • Steimer, L.1    Klostermeier, D.2
  • 93
    • 0024415732 scopus 로고
    • A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity
    • Rozen F, Pelletier J, Trachsel H, Sonenberg N. A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity. Mol Cell Biol 1989; 9:4061-3; PMID:2506440. (Pubitemid 19216300)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.9 , pp. 4061-4063
    • Rozen, F.1    Pelletier, J.2    Trachsel, H.3    Sonenberg, N.4
  • 94
    • 0025898593 scopus 로고
    • Translation initiation factor 4A from Saccharomyces cerevisiae: Analysis of residues conserved in the D-E-A-D family of RNA helicases
    • Schmid SR, Linder P. Translation initiation factor 4A from Saccharomyces cerevisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases. Mol Cell Biol 1991; 11:3463-71; PMID:2046664. (Pubitemid 21895733)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.7 , pp. 3463-3471
    • Schmid, S.R.1    Linder, P.2
  • 95
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • DOI 10.1016/S1097-2765(03)00006-6
    • Tanner NK, Cordin O, Banroques J, Doère M, Linder P. The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol Cell 2003; 11:127-38; PMID:12535527; http://dx.doi.org/10.1016/ S1097-2765(03)00006-6. (Pubitemid 36126596)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 96
    • 0026668609 scopus 로고
    • ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae
    • PMID:1502180
    • Blum S, Schmid SR, Pause A, Buser P, Linder P, Sonenberg N, et al. ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 1992; 89:7664-8; PMID:1502180; http://dx.doi. org/10.1073/pnas.89.16.7664.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7664-7668
    • Blum, S.1    Schmid, S.R.2    Pause, A.3    Buser, P.4    Linder, P.5    Sonenberg, N.6
  • 97
    • 79954598438 scopus 로고    scopus 로고
    • A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export
    • PMID:21441902
    • Montpetit B, Thomsen ND, Helmke KJ, Seeliger MA, Berger JM, Weis K. A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export. Nature 2011; 472:238-42; PMID:21441902; http://dx.doi.org/10.1038/ nature09862.
    • (2011) Nature , vol.472 , pp. 238-242
    • Montpetit, B.1    Thomsen, N.D.2    Helmke, K.J.3    Seeliger, M.A.4    Berger, J.M.5    Weis, K.6
  • 98
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith CA, Rayment I. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys J 1996; 70:1590-602; PMID:8785318; http://dx.doi.org/10.1016/S0006-3495(96)79745-X. (Pubitemid 26103931)
    • (1996) Biophysical Journal , vol.70 , Issue.4 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 100
    • 0023146671 scopus 로고
    • A fluorescence study of the binding of eucaryotic initiation factors to messenger RNA and messenger RNA analogues
    • DOI 10.1021/bi00380a009
    • Goss DJ, Woodley CL, Wahba AJ. A fluorescence study of the binding of eucaryotic initiation factors to messenger RNA and messenger RNA analogues. Biochemistry 1987; 26:1551-6; PMID:3593677; http://dx.doi.org/10.1021/ bi00380a009. (Pubitemid 17047624)
    • (1987) Biochemistry , vol.26 , Issue.6 , pp. 1551-1556
    • Goss, D.J.1    Woodley, C.L.2    Wahba, A.J.3
  • 101
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • PMID:11278350
    • Rogers GW Jr., Lima WF, Merrick WC. Further characterization of the helicase activity of eIF4A. Substrate specificity. J Biol Chem 2001; 276:12598-608; PMID:11278350; http://dx.doi.org/10.1074/jbc. M007560200.
    • (2001) J Biol Chem , vol.276 , pp. 12598-12608
    • Rogers Jr., G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 102
    • 84862000545 scopus 로고    scopus 로고
    • Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 5'-overhangs
    • PMID:22467875
    • Rajagopal V, Park EH, Hinnebusch AG, Lorsch JR. Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 5'-overhangs. J Biol Chem 2012; 287:20301-12; PMID:22467875; http://dx.doi. org/10.1074/jbc.M112.347278.
    • (2012) J Biol Chem , vol.287 , pp. 20301-20312
    • Rajagopal, V.1    Park, E.H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 103
    • 70449553011 scopus 로고    scopus 로고
    • How does a scanning ribosomal particle move along the 5'-untranslated region of eukaryot-ic mRNA? Brownian Ratchet model
    • PMID:19835415
    • Spirin AS. How does a scanning ribosomal particle move along the 5'-untranslated region of eukaryot-ic mRNA? Brownian Ratchet model. Biochemistry 2009; 48:10688-92; PMID:19835415; http://dx.doi. org/10.1021/bi901379a.
    • (2009) Biochemistry , vol.48 , pp. 10688-10692
    • Spirin, A.S.1
  • 104
    • 0141856111 scopus 로고    scopus 로고
    • Adenosine 5'-O-(3-thio)triphosphate (ATPγS) is a substrate for the nucleotide hydrolysis and RNA unwinding activities of eukaryotic translation initiation factor eIF4A
    • DOI 10.1261/rna.2103703
    • Peck ML, Herschlag D. Adenosine 5'-O-(3-thio) triphosphate (ATPgammaS) is a substrate for the nucleotide hydrolysis and RNA unwinding activities of eukaryotic translation initiation factor eIF4A. RNA 2003; 9:1180-7; PMID:13130132; http://dx.doi. org/10.1261/rna.2103703. (Pubitemid 37151673)
    • (2003) RNA , vol.9 , Issue.10 , pp. 1180-1187
    • Peck, M.L.1    Herschlag, D.2
  • 105
    • 84864491902 scopus 로고    scopus 로고
    • The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase
    • PMID:22457067
    • Sun Y, Atas E, Lindqvist L, Sonenberg N, Pelletier J, Meller A. The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase. Nucleic Acids Res 2012; 40:6199-207; PMID:22457067; http://dx.doi. org/10.1093/nar/gks278.
    • (2012) Nucleic Acids Res , vol.40 , pp. 6199-6207
    • Sun, Y.1    Atas, E.2    Lindqvist, L.3    Sonenberg, N.4    Pelletier, J.5    Meller, A.6
  • 106
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • PMID:11418588
    • Rogers GW Jr., Richter NJ, Lima WF, Merrick WC. Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J Biol Chem 2001; 276:30914-22; PMID:11418588; http://dx.doi.org/10.1074/jbc. M100157200.
    • (2001) J Biol Chem , vol.276 , pp. 30914-30922
    • Rogers Jr., G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 107
    • 12544253991 scopus 로고    scopus 로고
    • Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity
    • PMID:15528191
    • Korneeva NL, First EA, Benoit CA, Rhoads RE. Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity. J Biol Chem 2005; 280:1872-81; PMID:15528191; http://dx.doi. org/10.1074/jbc.M406168200.
    • (2005) J Biol Chem , vol.280 , pp. 1872-1881
    • Korneeva, N.L.1    First, E.A.2    Benoit, C.A.3    Rhoads, R.E.4
  • 108
    • 52949097997 scopus 로고    scopus 로고
    • Interactions between eIF4AI and its accessory factors eIF4B and eIF4H
    • PMID:18719248
    • Rozovsky N, Butterworth AC, Moore MJ. Interactions between eIF4AI and its accessory factors eIF4B and eIF4H. RNA 2008; 14:2136-48; PMID:18719248; http://dx.doi.org/10.1261/rna.1049608.
    • (2008) RNA , vol.14 , pp. 2136-2148
    • Rozovsky, N.1    Butterworth, A.C.2    Moore, M.J.3
  • 109
    • 0021099528 scopus 로고
    • Identification and quantita-tion of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional poly-acrylamide gel electrophoresis
    • PMID:6853516
    • Duncan R, Hershey JW. Identification and quantita-tion of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional poly-acrylamide gel electrophoresis. J Biol Chem 1983; 258:7228-35; PMID:6853516.
    • (1983) J Biol Chem , vol.258 , pp. 7228-7235
    • Duncan, R.1    Hershey, J.W.2
  • 110
    • 0033590182 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4B from wheat and Arabidopsis thaliana is a member of a multigene family
    • DOI 10.1006/bbrc.1999.1814
    • Metz AM, Wong KC, Malmström SA, Browning KS. Eukaryotic initiation factor 4B from wheat and Arabidopsis thaliana is a member of a multigene family. Biochem Biophys Res Commun 1999; 266:314-21; PMID:10600500; http://dx.doi.org/10.1006/bbrc.1999.1814. (Pubitemid 30028665)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.2 , pp. 314-321
    • Metz, A.M.1    Wong, K.C.H.2    Malmstrom, S.A.3    Browning, K.S.4
  • 111
    • 0029805730 scopus 로고    scopus 로고
    • In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: The role of the RNA recognition motif
    • Méthot N, Pickett G, Keene JD, Sonenberg N. In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: the role of the RNA remotif. RNA 1996; 2:38-50; PMID:8846295. (Pubitemid 26371310)
    • (1996) RNA , vol.2 , Issue.1 , pp. 38-50
    • Methot, N.1    Pickett, G.2    Keene, J.D.3    Sonenberg, N.4
  • 112
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • Méthot N, Song MS, Sonenberg N. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol Cell Biol 1996; 16:5328-34; PMID:8816444. (Pubitemid 26315051)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5328-5334
    • Methot, N.1    Song, M.S.2    Sonenberg, N.3
  • 113
    • 33747697785 scopus 로고    scopus 로고
    • Wheat eukaryotic initiation factor 4B organizes assembly of RNA and eIFiso4G, eIF4A, and poly(A)-binding protein
    • DOI 10.1074/jbc.M605404200
    • Cheng S, Gallie DR. Wheat eukaryotic initiation factor 4B organizes assembly of RNA and eIFiso4G, eIF4A, and poly(A)-binding protein. J Biol Chem 2006; 281:24351-64; PMID:16803875; http://dx.doi. org/10.1074/jbc.M605404200. (Pubitemid 44274207)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24351-24364
    • Cheng, S.1    Gallie, D.R.2
  • 114
    • 0042666838 scopus 로고    scopus 로고
    • Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B
    • DOI 10.1021/bi034506g
    • Fleming K, Ghuman J, Yuan X, Simpson P, Szendröi A, Matthews S, et al. Solution structure and RNA interactions of the RNA recognition motif from eukary-otic translation initiation factor 4B. Biochemistry 2003; 42:8966-75; PMID:12885229; http://dx.doi. org/10.1021/bi034506g. (Pubitemid 36935404)
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 8966-8975
    • Fleming, K.1    Ghuman, J.2    Yuan, X.3    Simpson, P.4    Szendroi, A.5    Matthews, S.6    Curry, S.7
  • 115
    • 0028685657 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1
    • Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, et al. Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res 1994; 1:27-35; PMID:7584026; http://dx.doi. org/10.1093/dnares/1.1.27. (Pubitemid 124000596)
    • (1994) DNA Research , vol.1 , Issue.1 , pp. 27-35
    • Nomura, N.1    Miyajima, N.2    Sazuka, T.3    Tanaka, A.4    Kawarabayasi, Y.5    Sato, S.6    Nagase, T.7    Seki, N.8    Ishikawa, K.-I.9    Tabata, S.10
  • 116
    • 0033544894 scopus 로고    scopus 로고
    • Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H
    • Richter NJ, Rogers GW Jr., Hensold JO, Merrick WC. Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H. J Biol Chem 1999; 274:35415-24; PMID:10585411; http://dx.doi. org/10.1074/jbc.274.50. 35415. (Pubitemid 129512832)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35415-35424
    • Richter, N.J.1    Rogers Jr., G.W.2    Hensold, J.O.3    Merrick, W.C.4
  • 117
    • 22544452431 scopus 로고    scopus 로고
    • MRNA decay during herpes simplex virus (HSV) infections: Protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A
    • DOI 10.1128/JVI.79.15.9651-9664.2005
    • Feng P, Everly DN Jr., Read GS. mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A. J Virol 2005; 79:9651-64; PMID:16014927; http://dx.doi. org/10.1128/JVI.79.15.9651-9664.2005. (Pubitemid 41022308)
    • (2005) Journal of Virology , vol.79 , Issue.15 , pp. 9651-9664
    • Feng, P.1    Everly Jr., D.N.2    Read, G.S.3
  • 118
    • 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
    • DOI 10.1128/MCB.23.24.8925-8933.2003
    • Dmitriev SE, Terenin IM, Dunaevsky YE, Merrick WC, Shatsky IN. Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5' untranslated regions. Mol Cell Biol 2003; 23:8925-33; PMID:14645505; http://dx.doi.org/10.1128/MCB.23.24.8925-8933. 2003. (Pubitemid 37499783)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 8925-8933
    • Dmitriev, S.E.1    Terenin, I.M.2    Dunaevsky, Y.E.3    Merrick, W.C.4    Shatsky, I.N.5
  • 120
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B
    • PMID:21840318
    • Özes AR, Feoktistova K, Avanzino BC, Fraser CS. Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. J Mol Biol 2011; 412:674-87; PMID:21840318; http://dx.doi.org/10.1016/j. jmb.2011.08.004.
    • (2011) J Mol Biol , vol.412 , pp. 674-687
    • Özes, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 121
    • 67650566334 scopus 로고    scopus 로고
    • Intrinsic RNA binding by the eukaryotic initiation factor 4F depends on a minimal RNA length but not on the m7G cap
    • PMID:19414591
    • Kaye NM, Emmett KJ, Merrick WC, Jankowsky E. Intrinsic RNA binding by the eukaryotic initiation factor 4F depends on a minimal RNA length but not on the m7G cap. J Biol Chem 2009; 284:17742-50; PMID:19414591; http://dx.doi.org/10. 1074/jbc. M109.009001.
    • (2009) J Biol Chem , vol.284 , pp. 17742-17750
    • Kaye, N.M.1    Emmett, K.J.2    Merrick, W.C.3    Jankowsky, E.4
  • 122
    • 0029086291 scopus 로고
    • The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity
    • PMID:7543843
    • Altmann M, Wittmer B, Méthot N, Sonenberg N, Trachsel H. The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity. EMBO J 1995; 14:3820-7; PMID:7543843.
    • (1995) EMBO J , vol.14 , pp. 3820-3827
    • Altmann, M.1    Wittmer, B.2    Méthot, N.3    Sonenberg, N.4    Trachsel, H.5
  • 123
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • DOI 10.1146/annurev.biochem.73.030403.080419
    • Kapp LD, Lorsch JR. The molecular mechanics of eukaryotic translation. Annu Rev Biochem 2004; 73:657-704; PMID:15189156; http://dx.doi. org/10.1146/annurev.biochem.73.030403.080419. (Pubitemid 39050383)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 124
    • 0037781584 scopus 로고    scopus 로고
    • Conducting the initiation of protein synthesis: The role of eIF4G
    • DOI 10.1016/S0248-4900(03)00031-5
    • Prévôt D, Darlix JL, Ohlmann T. Conducting the initiation of protein synthesis: the role of eIF4G. Biol Cell 2003; 95:141-56; PMID:12867079; http://dx.doi.org/10.1016/S0248-4900(03)00031-5. (Pubitemid 36889217)
    • (2003) Biology of the Cell , vol.95 , Issue.3-4 , pp. 141-156
    • Prevot, D.1    Darlix, J.-L.2    Ohlmann, T.3
  • 125
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H, Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol Cell Biol 1997; 17:6940-7; PMID:9372926. (Pubitemid 27505924)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 126
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
    • DOI 10.1016/S0092-8674(03)00975-9
    • Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, et al. Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell 2003; 115:739-50; PMID:14675538; http://dx.doi.org/10.1016/S0092-8674(03)00975-9. (Pubitemid 38030302)
    • (2003) Cell , vol.115 , Issue.6 , pp. 739-750
    • Gross, J.D.1    Moerke, N.J.2    Von Der Haar, T.3    Lugovskoy, A.A.4    Sachs, A.B.5    McCarthy, J.E.G.6    Wagner, G.7
  • 127
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain within eIF4G Directs Assembly of the Translation Initiation Machinery
    • DOI 10.1016/S1097-2765(01)00167-8
    • Marcotrigiano J, Lomakin IB, Sonenberg N, Pestova TV, Hellen CU, Burley SK. A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery. Mol Cell 2001; 7:193-203; PMID:11172724; http://dx.doi.org/10.1016/S1097-2765(01)00167-8. (Pubitemid 32162912)
    • (2001) Molecular Cell , vol.7 , Issue.1 , pp. 193-203
    • Marcotrigiano, J.1    Lomakin, I.B.2    Sonenberg, N.3    Pestova, T.V.4    Hellen, C.U.T.5    Burley, S.K.6
  • 128
    • 33646341222 scopus 로고    scopus 로고
    • Two Structurally Atypical HEAT Domains in the C-Terminal Portion of Human eIF4G Support Binding to eIF4A and Mnk1
    • DOI 10.1016/j.str.2006.03.012, PII S0969212606001808
    • Bellsolell L, Cho-Park P F, Poulin F, Sonenberg N, Burley SK. Tw o structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Structure 2006; 14:913-23; PMID:16698552; http://dx.doi.org/10.1016/j. str.2006.03.012. (Pubitemid 43674101)
    • (2006) Structure , vol.14 , Issue.5 , pp. 913-923
    • Bellsolell, L.1    Cho-Park, P.F.2    Poulin, F.3    Sonenberg, N.4    Burley, S.K.5
  • 129
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • DOI 10.1101/gad.1335305
    • Oberer M, Marintchev A, Wagner G. Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev 2005; 19:2212-23; PMID:16166382; http://dx.doi.org/10.1101/gad.1335305. (Pubitemid 41330322)
    • (2005) Genes and Development , vol.19 , Issue.18 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 130
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • DOI 10.1128/MCB.20.2.468-477.2000
    • Morino S, Imataka H, Svitkin YV, Pestova T V, Sonenberg N. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol Cell Biol 2000; 20:468-77; PMID:10611225; http://dx.doi.org/10.1128/MCB.20.2.468-477.2000. (Pubitemid 30023088)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.2 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 131
    • 78751609906 scopus 로고    scopus 로고
    • Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1•PABP mRNPs in vivo
    • PMID:21139564
    • Park EH, Walker SE, Lee JM, Rothenburg S, Lorsch JR, Hinnebusch AG. Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1•PABP mRNPs in vivo. EMBO J 2011; 30:302-16; PMID:21139564; http://dx.doi.org/10.1038/ emboj.2010.312.
    • (2011) EMBO J , vol.30 , pp. 302-316
    • Park, E.H.1    Walker, S.E.2    Lee, J.M.3    Rothenburg, S.4    Lorsch, J.R.5    Hinnebusch, A.G.6
  • 132
    • 0037216626 scopus 로고    scopus 로고
    • The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation
    • DOI 10.1128/MCB.23.1.26-37.2003
    • Yang HS, Jansen A P, Komar AA, Zheng X, Merrick WC, Costes S, et al. The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Mol Cell Biol 2003; 23:26-37; PMID:12482958; http://dx.doi. org/10.1128/MCB.23.1.26-37.2003. (Pubitemid 36008498)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.1 , pp. 26-37
    • Yang, H.-S.1    Jansen, A.P.2    Komar, A.A.3    Zheng, X.4    Merrick, W.C.5    Costes, S.6    Lockett, S.J.7    Sonenberg, N.8    Colburn, N.H.9
  • 133
    • 0026044572 scopus 로고
    • Pateamine-A Potent Cytotoxin from the New-Zealand Marine Sponge, Mycale Sp
    • Northcote PT, Blunt JW, Munro MHG. Pateamine-a Potent Cytotoxin from the New-Zealand Marine Sponge, Mycale Sp. Tetrahedron Lett 1991; 32:6411-4; http://dx.doi.org/10.1016/0040-4039(91)80182-6.
    • (1991) Tetrahedron Lett , vol.32 , pp. 6411-6414
    • Northcote, P.T.1    Blunt, J.W.2    Munro, M.H.G.3
  • 134
    • 34250328209 scopus 로고    scopus 로고
    • Substrate-Dependent Targeting of Eukaryotic Translation Initiation Factor 4A by Pateamine A: Negation of Domain-Linker Regulation of Activity
    • DOI 10.1016/j.chembiol.2007.05.012, PII S1074552107001810
    • Low WK, Dang Y, Bhat S, Romo D, Liu JO. Substrate-dependent targeting of eukaryotic translation initiation factor 4A by pateamine A: negation of domain-linker regulation of activity. Chem Biol 2007; 14:715-27; PMID:17584618; http://dx.doi.org/10.1016/j.chem-biol.2007.05.012. (Pubitemid 46920988)
    • (2007) Chemistry and Biology , vol.14 , Issue.6 , pp. 715-727
    • Low, W.-K.1    Dang, Y.2    Bhat, S.3    Romo, D.4    Liu, J.O.5
  • 135
    • 28444448743 scopus 로고    scopus 로고
    • Inhibition of eukaryotic translation initiation by the marine natural product pateamine A
    • DOI 10.1016/j.molcel.2005.10.008, PII S1097276505016783
    • Low WK, Dang Y, Schneider-Poetsch T, Shi Z, Choi NS, Merrick WC, et al. Inhibition of eukaryotic translation initiation by the marine natural product pateamine A. Mol Cell 2005; 20:709-22; PMID:16337595; http://dx.doi.org/10.1016/ j.molcel.2005.10.008. (Pubitemid 41740693)
    • (2005) Molecular Cell , vol.20 , Issue.5 , pp. 709-722
    • Low, W.-K.1    Dang, Y.2    Schneider-Poetsch, T.3    Shi, Z.4    Choi, N.S.5    Merrick, W.C.6    Romo, D.7    Liu, J.O.8
  • 136
    • 27144445082 scopus 로고    scopus 로고
    • The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity
    • DOI 10.1038/nsmb990, PII N990
    • Ballut L, Marchadier B, Baguet A, Tomasetto C, Séraphin B, Le Hir H. The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. Nat Struct Mol Biol 2005; 12:861-9; PMID:16170325; http://dx.doi.org/10.1038/nsmb990. (Pubitemid 41486709)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 861-869
    • Ballut, L.1    Marchadier, B.2    Baguet, A.3    Tomasetto, C.4    Seraphin, B.5    Le Hir, H.6
  • 137
    • 34547194577 scopus 로고    scopus 로고
    • MLN51 stimulates the RNA-helicase activity of eIF4AIII
    • PMID:17375189
    • Noble CG, Song H. MLN51 stimulates the RNA-helicase activity of eIF4AIII. PLoS ONE 2007; 2:e303; PMID:17375189; http://dx.doi.org/10.1371/journal. pone.0000303.
    • (2007) PLoS ONE , vol.2
    • Noble, C.G.1    Song, H.2
  • 138
    • 28344456363 scopus 로고    scopus 로고
    • Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core
    • DOI 10.1261/rna.2155905
    • Tange TO, Shibuya T, Jurica MS, Moore MJ. Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core. RNA 2005; 11:1869-83; PMID:16314458; http://dx.doi. org/10.1261/rna.2155905. (Pubitemid 41720036)
    • (2005) RNA , vol.11 , Issue.12 , pp. 1869-1883
    • Tange, T.O.1    Shibuya, T.2    Jurica, M.S.3    Moore, M.J.4
  • 139
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • DOI 10.1093/emboj/19.24.6860
    • Le Hir H, Izaurralde E, Maquat LE, Moore MJ. The spliceosome deposits multiple proteins 20-24 nucleo-tides upstream of mRNA exon-exon junctions. EMBO J 2000; 19:6860-9; PMID:11118221; http://dx.doi. org/10.1093/emboj/19.24.6860. (Pubitemid 32011679)
    • (2000) EMBO Journal , vol.19 , Issue.24 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 140
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • Le Hir H, Moore MJ, Maquat LE. Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev 2000; 14:1098-108; PMID:10809668. (Pubitemid 30324423)
    • (2000) Genes and Development , vol.14 , Issue.9 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 141
    • 77953370114 scopus 로고    scopus 로고
    • Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex
    • PMID:20479275
    • Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, et al. Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. Proc Natl Acad Sci USA 2010; 107:10050-5; PMID:20479275; http://dx.doi.org/10.1073/pnas.1000993107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10050-10055
    • Buchwald, G.1    Ebert, J.2    Basquin, C.3    Sauliere, J.4    Jayachandran, U.5    Bono, F.6
  • 142
    • 0035823247 scopus 로고    scopus 로고
    • Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1
    • DOI 10.1126/science.1062786
    • Lykke-Andersen J, Shu MD, Steitz JA. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 2001; 293:1836-9; PMID:11546874; http://dx.doi. org/10.1126/science. 1062786. (Pubitemid 32845782)
    • (2001) Science , vol.293 , Issue.5536 , pp. 1836-1839
    • Lykke-Andersen, J.1    Shu, M.-D.2    Steitz, J.A.3
  • 143
    • 0042025014 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Drosophila: At the intersection of the yeast and mammalian pathways
    • DOI 10.1093/emboj/cdg371
    • Gatfield D, Unterholzner L, Ciccarelli FD, Bork P, Izaurralde E. Nonsense-mediated mRNA decay in Drosophila: at the intersection of the yeast and mammalian pathways. EMBO J 2003; 22:3960-70; PMID:12881430; http://dx.doi.org/10.1093/emboj/cdg371. (Pubitemid 36975722)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 3960-3970
    • Gatfield, D.1    Unterholzner, L.2    Ciccarelli, F.D.3    Bork, P.4    Izaurralde, E.5
  • 144
    • 34247556560 scopus 로고    scopus 로고
    • Mechanistic insights and identification of two novel factors in the C. elegans NMD pathway
    • DOI 10.1101/gad.417707
    • Longman D, Plasterk RH, Johnstone IL, Cáceres J F. Mechanistic insights and identification of two novel factors in the C. elegans NMD pathway. Genes Dev 2007; 21:1075-85; PMID:17437990; http://dx.doi. org/10.1101/gad. 417707. (Pubitemid 46686476)
    • (2007) Genes and Development , vol.21 , Issue.9 , pp. 1075-1085
    • Longman, D.1    Plasterk, R.H.A.2    Johnstone, I.L.3    Caceres, J.F.4
  • 145
    • 0035934166 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Saccharomyces cerevisiae
    • DOI 10.1016/S0378-1119(01)00552-2, PII S0378111901005522
    • González CI, Bhattacharya A, Wang W, Peltz SW. Nonsense-mediated mRNA decay in Saccharomyces cerevisiae. Gene 2001; 274:15-25; PMID:11674994; http://dx.doi.org/10.1016/S0378-1119(01)00552-2. (Pubitemid 32817119)
    • (2001) Gene , vol.274 , Issue.1-2 , pp. 15-25
    • Gonzalez, C.I.1    Bhattacharya, A.2    Wang, W.3    Peltz, S.W.4
  • 146
    • 79956302113 scopus 로고    scopus 로고
    • Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex
    • PMID:21576267
    • Alexandrov A, Colognori D, Steitz JA. Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex. Genes Dev 2011; 25:1078-90; PMID:21576267; http://dx.doi.org/10.1101/gad.2045411.
    • (2011) Genes Dev , vol.25 , pp. 1078-1090
    • Alexandrov, A.1    Colognori, D.2    Steitz, J.A.3
  • 147
    • 0030679565 scopus 로고    scopus 로고
    • Fal1p is an essential DEAD-box protein involved in 40S-ribosomal- subunit biogenesis in Saccharomyces cerevisiae
    • Kressler D, de la Cruz J, Rojo M, Linder P. Fal1p is an essential DEAD-box protein involved in 40S-ribosomal-subunit biogenesis in Saccharomyces cerevisiae. Mol Cell Biol 1997; 17:7283-94; PMID:9372960. (Pubitemid 27505958)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 7283-7294
    • Kressler, D.1    De La Cruz, J.2    Rojo, M.3    Linder, P.4
  • 148
    • 68949200868 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation
    • PMID:19716792
    • Budiman ME, Bubenik JL, Miniard AC, Middleton LM, Gerber CA, Cash A, et al. Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation. Mol Cell 2009; 35:479-89; PMID:19716792; http://dx.doi.org/10.1016/j.molcel.2009.06.026.
    • (2009) Mol Cell , vol.35 , pp. 479-489
    • Budiman, M.E.1    Bubenik, J.L.2    Miniard, A.C.3    Middleton, L.M.4    Gerber, C.A.5    Cash, A.6
  • 149
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3' untranslated region
    • Berry MJ, Banu L, Chen YY, Mandel SJ, Kieffer JD, Harney JW, et al. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region. Nature 1991; 353:273-6; PMID:1832744; http://dx.doi. org/10.1038/353273a0. (Pubitemid 21896772)
    • (1991) Nature , vol.353 , Issue.6341 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 150
    • 80053204231 scopus 로고    scopus 로고
    • Identification of a signature motif for the eIF4a3-SECIS interaction
    • PMID:21685449
    • Budiman ME, Bubenik JL, Driscoll DM. Identification of a signature motif for the eIF4a3-SECIS interaction. Nucleic Acids Res 2011; 39:7730-9; PMID:21685449; http://dx.doi.org/10.1093/nar/gkr446.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7730-7739
    • Budiman, M.E.1    Bubenik, J.L.2    Driscoll, D.M.3
  • 151
    • 80054720123 scopus 로고    scopus 로고
    • Analyses of the functional regions of DEAD-box RNA "helicases" with deletion and chimera constructs tested in vivo and in vitro
    • PMID:21884706
    • Banroques J, Cordin O, Doère M, Linder P, Tanner NK. Analyses of the functional regions of DEAD-box RNA "helicases" with deletion and chimera constructs tested in vivo and in vitro. J Mol Biol 2011; 413:451-72; PMID:21884706; http://dx.doi.org/10.1016/j. jmb.2011.08.032.
    • (2011) J Mol Biol , vol.413 , pp. 451-472
    • Banroques, J.1    Cordin, O.2    Doère, M.3    Linder, P.4    Tanner, N.K.5
  • 152
    • 79961099216 scopus 로고    scopus 로고
    • Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail
    • PMID:21746911
    • Mallam AL, Jarmoskaite I, Tijerina P, Del Campo M, Seifert S, Guo L, et al. Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail. Proc Natl Acad Sci USA 2011; 108:12254-9; PMID:21746911; http://dx.doi.org/10.1073/pnas.1109566108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12254-12259
    • Mallam, A.L.1    Jarmoskaite, I.2    Tijerina, P.3    Del Campo, M.4    Seifert, S.5    Guo, L.6
  • 153
    • 27444442034 scopus 로고    scopus 로고
    • H core and a specific RNA-binding domain
    • DOI 10.1074/jbc.M506815200
    • Karginov F V, Caruthers JM, Hu Y, McKay DB, Uhlenbeck OC. YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. J Biol Chem 2005; 280:35499-505; PMID:16118224; http://dx.doi.org/10.1074/jbc. M506815200. (Pubitemid 41532740)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 154
    • 0033214805 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: Delineation of a novel sub-family of bacterial DEAD proteins
    • DOI 10.1093/nar/27.19.3811
    • Kossen K, Uhlenbeck OC. Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: delineation of a novel sub-family of bacterial DEAD proteins. Nucleic Acids Res 1999; 27:3811-20; PMID:10481020; http://dx.doi.org/10.1093/nar/27.19.3811. (Pubitemid 29454429)
    • (1999) Nucleic Acids Research , vol.27 , Issue.19 , pp. 3811-3820
    • Kossen, K.1    Uhlenbeck, O.C.2
  • 155
    • 33745406566 scopus 로고    scopus 로고
    • The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis
    • DOI 10.1093/nar/gkl419
    • Granneman S, Lin C, Champion EA, Nandineni MR, Zorca C, Baserga SJ. The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis. Nucleic Acids Res 2006; 34:3189-99; PMID:16772403; http://dx.doi. org/10.1093/nar/gkl419. (Pubitemid 44540444)
    • (2006) Nucleic Acids Research , vol.34 , Issue.10 , pp. 3189-3199
    • Granneman, S.1    Lin, C.Y.2    Champion, E.A.3    Nandineni, M.R.4    Zorca, C.5    Baserga, S.J.6


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