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Volumn 4, Issue 10, 2012, Pages

The mechanism of eukaryotic translation initiation: New insights and challenges

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR;

EID: 84863889691     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a011544     Document Type: Article
Times cited : (355)

References (137)
  • 1
    • 78650907809 scopus 로고    scopus 로고
    • Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning
    • Abaeva IS, Marintchev A, Pisareva VP, Hellen CU, Pestova TV. 2011. Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning. EMBO J 30: 115-129.
    • (2011) EMBO J , vol.30 , pp. 115-129
    • Abaeva, I.S.1    Marintchev, A.2    Pisareva, V.P.3    Hellen, C.U.4    Pestova, T.V.5
  • 2
    • 33646852583 scopus 로고    scopus 로고
    • Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining
    • Acker MG, Shin BS, Dever TE, Lorsch JR. 2006. Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining. J Bio Chem 281: 8469-8475.
    • (2006) J Bio Chem , vol.281 , pp. 8469-8475
    • Acker, M.G.1    Shin, B.S.2    Dever, T.E.3    Lorsch, J.R.4
  • 4
    • 46449083572 scopus 로고    scopus 로고
    • Bringing order to translation: The contributions of transfer RNA anticodon-domain modifications
    • Agris PF. 2008. Bringing order to translation: The contributions of transfer RNA anticodon-domain modifications. EMBO Rep 9: 629-635.
    • (2008) EMBO Rep , vol.9 , pp. 629-635
    • Agris, P.F.1
  • 6
    • 26944435515 scopus 로고    scopus 로고
    • Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • Algire MA, Maag D, Lorsch JR. 2005. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol Cell 20: 251-262.
    • (2005) Mol Cell , vol.20 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 7
    • 33744957161 scopus 로고    scopus 로고
    • Direct binding of translation initiation factor eIF2g-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B 1
    • Alone PV, Dever TE. 2006. Direct binding of translation initiation factor eIF2g-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B 1. J Biol Chem 281: 12636-12644.
    • (2006) J Biol Chem , vol.281 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 8
    • 55849085351 scopus 로고    scopus 로고
    • Translation initiation factor 2g mutant alters start codon selection independent of Met-tRNA binding
    • Alone PV, Cao C, Dever TE. 2008. Translation initiation factor 2g mutant alters start codon selection independent of Met-tRNA binding. Mol Cell Biol 28: 6877-6888.
    • (2008) Mol Cell Biol , vol.28 , pp. 6877-6888
    • Alone, P.V.1    Cao, C.2    Dever, T.E.3
  • 10
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano K, Shalev A, Phan L, Nielsen K, Clayton J, Valášek L, Donahue TF, Hinnebusch AG. 2001. Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J 20: 2326-2337.
    • (2001) EMBO J , vol.20 , pp. 2326-2337
    • Asano, K.1    Shalev, A.2    Phan, L.3    Nielsen, K.4    Clayton, J.5    Valášek, L.6    Donahue, T.F.7    Hinnebusch, A.G.8
  • 12
    • 0038719941 scopus 로고    scopus 로고
    • RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae
    • Berset C, Zurbriggen A, Djafarzadeh S, Altmann M, Trachsel H. 2003. RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae. RNA 9: 871-880.
    • (2003) RNA , vol.9 , pp. 871-880
    • Berset, C.1    Zurbriggen, A.2    Djafarzadeh, S.3    Altmann, M.4    Trachsel, H.5
  • 17
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER, McKay DB. 2000. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci 97: 13080-13085.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 19
    • 77956713468 scopus 로고    scopus 로고
    • The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotesmRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons
    • Chiu WL, Wagner S, Herrmannova A, Burela L, Zhang F, Saini AK, Valasek L, Hinnebusch AG. 2010. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotesmRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol Cell Biol 30: 4415-4434.
    • (2010) Mol Cell Biol , vol.30 , pp. 4415-4434
    • Chiu, W.L.1    Wagner, S.2    Herrmannova, A.3    Burela, L.4    Zhang, F.5    Saini, A.K.6    Valasek, L.7    Hinnebusch, A.G.8
  • 20
    • 33645677012 scopus 로고    scopus 로고
    • Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors
    • Conte MR, Kelly G, Babon J, Sanfelice D, Youell J, Smerdo SJ, Proud CG. 2006. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry 45: 4550-4558.
    • (2006) Biochemistry , vol.45 , pp. 4550-4558
    • Conte, M.R.1    Kelly, G.2    Babon, J.3    Sanfelice, D.4    Youell, J.5    Smerdo, S.J.6    Proud, C.G.7
  • 21
    • 0035794125 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein
    • Das S, Ghosh R, Maitra U. 2001. Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein. J Biol Chem 276: 6720-6726.
    • (2001) J Biol Chem , vol.276 , pp. 6720-6726
    • Das, S.1    Ghosh, R.2    Maitra, U.3
  • 23
    • 68949149110 scopus 로고    scopus 로고
    • Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components
    • Dennis MD, Person MD, Browning KS. 2009. Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components. J Biol Chem 284: 20615-20628.
    • (2009) J Biol Chem , vol.284 , pp. 20615-20628
    • Dennis, M.D.1    Person, M.D.2    Browning, K.S.3
  • 24
    • 77957825617 scopus 로고    scopus 로고
    • The b/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo
    • Dev K, Qiu H, Dong J, Zhang F, Barthlme D, Hinnebusc AG. 2010. The b/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo. Mo Cell Biol 30: 5218-5233.
    • (2010) Mo Cell Biol , vol.30 , pp. 5218-5233
    • Dev, K.1    Qiu, H.2    Dong, J.3    Zhang, F.4    Barthlme, D.5    Hinnebusc, A.G.6
  • 26
    • 0345060297 scopus 로고    scopus 로고
    • Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 50 untranslated regions
    • Cold SpringHarbor Laboratory Press, Cold SpringHarbor N. Y
    • Cold SpringHarbor Laboratory Press, Cold SpringHarbor, NY. Dmitriev SE, Terenin IM, Dunaevsky YE, MerrickWC, Shatsk IN. 2003. Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 50 untranslated regions. Mol Cell Biol 23: 8925-8933.
    • (2003) Mol Cell Biol , vol.23 , pp. 8925-8933
    • Dmitriev, S.E.1    Terenin, I.M.2    Dunaevsky, Y.E.3    Merrick, W.C.4    Shatsk, I.N.5
  • 28
    • 0002538063 scopus 로고    scopus 로고
    • Genetic approaches to translation initiation in Saccharomyces cerevisiae
    • (ed. Sonenberg N, Hershey JWB, Mathews MB)
    • Donahue T. 2000. Genetic approaches to translation initiation in Saccharomyces cerevisiae. In Translational control of gene expression (ed. Sonenberg N, Hershey JWB, Mathews MB), pp. 487-502.
    • (2000) Translational control of gene expression , pp. 487-502
    • Donahue, T.1
  • 29
    • 50049130690 scopus 로고    scopus 로고
    • Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Dong J, Nanda JS, Rahman H, Pruitt MR, Shin BS, Won CM, Lorsch JR, Hinnebusch AG. 2008. Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection. Genes Dev 22: 2242-2255.
    • (2008) Genes Dev , vol.22 , pp. 2242-2255
    • Dong, J.1    Nanda, J.S.2    Rahman, H.3    Pruitt, M.R.4    Shin, B.S.5    Won, C.M.6    Lorsch, J.R.7    Hinnebusch, A.G.8
  • 33
    • 33947245582 scopus 로고    scopus 로고
    • Coupled release of eukaryotic translation initiation factors 5B and 1A from 80S ribosomes following subunit joining
    • Fringer JM, Acker MG, Fekete CA, Lorsch JR, Dever TE. 2007. Coupled release of eukaryotic translation initiation factors 5B and 1A from 80S ribosomes following subunit joining. Mol Cell Biol 27: 2384-2397.
    • (2007) Mol Cell Biol , vol.27 , pp. 2384-2397
    • Fringer, J.M.1    Acker, M.G.2    Fekete, C.A.3    Lorsch, J.R.4    Dever, T.E.5
  • 34
    • 0034024628 scopus 로고    scopus 로고
    • Identification of domains and residues within the 1 subunit of eukaryotic translation initiation factor 2B (eIF2b) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation
    • Gomez E, Pavitt GD. 2000. Identification of domains and residues within the 1 subunit of eukaryotic translation initiation factor 2B (eIF2b) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol Cell Biol 20: 3965-3976.
    • (2000) Mol Cell Biol , vol.20 , pp. 3965-3976
    • Gomez, E.1    Pavitt, G.D.2
  • 35
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez E, Mohammad SS, Pavitt GD. 2002. Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation. EMBO J 21: 5292-5301.
    • (2002) EMBO J , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 36
    • 0041589832 scopus 로고    scopus 로고
    • The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection
    • He H, von der Haar T, Singh CR, Ii M, Li B, Hinnebusch AG, McCarthy JE, Asano K. 2003. The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection. Mol Cell Biol 23: 5431-5445.
    • (2003) Mol Cell Biol , vol.23 , pp. 5431-5445
    • He, H.1    von der Haar, T.2    Singh, C.R.3    Ii, M.4    Li, B.5    Hinnebusch, A.G.6    McCarthy, J.E.7    Asano, K.8
  • 37
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • (ed. Sonenberg N, Hershey JWB, Mathews MB), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hershey JWB, MerrickWC. 2000. Pathway and mechanism of initiation of protein synthesis. In Translational control of gene expression (ed. Sonenberg N, Hershey JWB, Mathews MB), pp. 33-88. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational control of gene expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 38
    • 79953675393 scopus 로고    scopus 로고
    • eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
    • Hilbert M, Kebbel F, Gubaev A, KlostermeierD. 2011. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res 39: 2260-2270.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 39
    • 80053022305 scopus 로고    scopus 로고
    • The DEADbox protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex
    • Hilliker A, Gao Z, Jankowsky E, Parker R. 2011. The DEADbox protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol Cell 43: 962-972.
    • (2011) Mol Cell , vol.43 , pp. 962-972
    • Hilliker, A.1    Gao, Z.2    Jankowsky, E.3    Parker, R.4
  • 40
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • Hinnebusch AG. 2011. Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol Mol Biol Rev 75: 434-467.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 41
    • 34249665243 scopus 로고    scopus 로고
    • Mechanism of translation initiation in the yeast Saccharomyces cerevisiae
    • (ed. Mathews M, Sonenberg N, Hershey JWB)
    • Hinnebusch AG, Dever TE, Asano K. 2007. Mechanism of translation initiation in the yeast Saccharomyces cerevisiae. In Translational control in biology and medicine (ed. Mathews M, Sonenberg N, Hershey JWB), pp. 225-268.
    • (2007) Translational control in biology and medicine , pp. 225-268
    • Hinnebusch, A.G.1    Dever, T.E.2    Asano, K.3
  • 42
    • 33847332134 scopus 로고    scopus 로고
    • Functional analysis of individual binding activities of the scaffold protein eIF4G
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Hinton TM, Coldwell MJ, Carpenter GA, Morley SJ, Pai VM. 2007. Functional analysis of individual binding activities of the scaffold protein eIF4G. J Biol Chem 282: 1695-1708.
    • (2007) J Biol Chem , vol.282 , pp. 1695-1708
    • Hinton, T.M.1    Coldwell, M.J.2    Carpenter, G.A.3    Morley, S.J.4    Pai, V.M.5
  • 43
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • Ingolia NT, Ghaemmaghami S, Newman JR, Weissman JS. 2009. Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324: 218-223.
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.3    Weissman, J.S.4
  • 44
    • 78149277351 scopus 로고    scopus 로고
    • Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1)
    • Ivanov IP, Loughran G, Sachs MS, Atkins JF. 2010. Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1). Proc Natl Acad Sci 107: 18056-18060.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 18056-18060
    • Ivanov, I.P.1    Loughran, G.2    Sachs, M.S.3    Atkins, J.F.4
  • 45
    • 77952734403 scopus 로고    scopus 로고
    • eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
    • Jennings MD, Pavitt GD. 2010. eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature 465: 378-381.
    • (2010) Nature , vol.465 , pp. 378-381
    • Jennings, M.D.1    Pavitt, G.D.2
  • 46
    • 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: 1355-1372.
    • (2006) Mol Cell Biol , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valasek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 47
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • Kahvejian A, Svitkin YV, Sukarieh R, M'Boutchou MN, Sonenber N. 2005. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev 19: 104-113.
    • (2005) Genes Dev , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.N.4    Sonenber, N.5
  • 48
    • 0347123543 scopus 로고    scopus 로고
    • GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2
    • Kapp LD, Lorsch JR. 2004. GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2. J Mol Biol 335: 923-936.
    • (2004) J Mol Biol , vol.335 , pp. 923-936
    • Kapp, L.D.1    Lorsch, J.R.2
  • 49
    • 33646168052 scopus 로고    scopus 로고
    • Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation
    • Kapp LD, Kolitz SE, Lorsch JR. 2006. Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation. RNA 12: 751-764.
    • (2006) RNA , vol.12 , pp. 751-764
    • Kapp, L.D.1    Kolitz, S.E.2    Lorsch, J.R.3
  • 50
    • 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
    • Kaye NM, Emmett KJ, Merrick WC, Jankowsky E. 2009. Intrinsic RNA binding by the eukaryotic initiation factor 4F depends on a minimal RNA length but not on the m7G cap. J Biol Chem 284: 17742-17750.
    • (2009) J Biol Chem , vol.284 , pp. 17742-17750
    • Kaye, N.M.1    Emmett, K.J.2    Merrick, W.C.3    Jankowsky, E.4
  • 51
    • 79958804665 scopus 로고    scopus 로고
    • eIF2A mediates translation of hepatitis C viral mRNA under stress conditions
    • Kim JH, Park SM, Park JH, Keum SJ, Jang SK. 2011. eIF2A mediates translation of hepatitis C viral mRNA under stress conditions. EMBO J 30: 2454-2464.
    • (2011) EMBO J , vol.30 , pp. 2454-2464
    • Kim, J.H.1    Park, S.M.2    Park, J.H.3    Keum, S.J.4    Jang, S.K.5
  • 52
    • 58149104495 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation
    • Kolitz SE, Takacs JE, Lorsch JR. 2009. Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation. RNA 15: 138-152.
    • (2009) RNA , vol.15 , pp. 138-152
    • Kolitz, S.E.1    Takacs, J.E.2    Lorsch, J.R.3
  • 53
    • 10644277580 scopus 로고    scopus 로고
    • Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association
    • Kolupaeva VG, Unbehaun A, Lomakin IB, Hellen CU, Pestov TV. 2005. Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association. RNA 11: 470-486.
    • (2005) RNA , vol.11 , pp. 470-486
    • Kolupaeva, V.G.1    Unbehaun, A.2    Lomakin, I.B.3    Hellen, C.U.4    Pestov, T.V.5
  • 54
    • 0034731347 scopus 로고    scopus 로고
    • Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1
    • Korneeva NL, Lamphear BJ, Hennigan FL, Rhoads RE. 2000. Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J Biol Chem 275: 41369-41376.
    • (2000) J Biol Chem , vol.275 , pp. 41369-41376
    • Korneeva, N.L.1    Lamphear, B.J.2    Hennigan, F.L.3    Rhoads, R.E.4
  • 55
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated a subunit of initiation factor 2 (eIF2a) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
    • Krishnamoorthy T, Pavitt GD, Zhang F, Dever TE, Hinnebusc AG. 2001. Tight binding of the phosphorylated a subunit of initiation factor 2 (eIF2a) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol Cel Biol 21: 5018-5030.
    • (2001) Mol Cel Biol , vol.21 , pp. 5018-5030
    • Krishnamoorthy, T.1    Pavitt, G.D.2    Zhang, F.3    Dever, T.E.4    Hinnebusc, A.G.5
  • 57
    • 0037168583 scopus 로고    scopus 로고
    • Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation
    • Lee JH, Pestova TV, Shin BS, Cao C, Choi SK, Dever TE. 2002. Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation. Pro Natl Acad Sci 99: 16689-16694.
    • (2002) Pro Natl Acad Sci , vol.99 , pp. 16689-16694
    • Lee, J.H.1    Pestova, T.V.2    Shin, B.S.3    Cao, C.4    Choi, S.K.5    Dever, T.E.6
  • 59
    • 73549090572 scopus 로고    scopus 로고
    • The Sua5 protein is essential for normal translational regulation in yeast
    • LinCA, Ellis SR, True HL. 2009. The Sua5 protein is essential for normal translational regulation in yeast. Mol Cell Biol 30: 354-363.
    • (2009) Mol Cell Biol , vol.30 , pp. 354-363
    • Lin, C.A.1    Ellis, S.R.2    True, H.L.3
  • 60
    • 42449155947 scopus 로고    scopus 로고
    • Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking
    • Lindqvist L, Imataka H, Pelletier J. 2008. Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking. RNA 14: 960-969.
    • (2008) RNA , vol.14 , pp. 960-969
    • Lindqvist, L.1    Imataka, H.2    Pelletier, J.3
  • 61
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F, Putnam A, Jankowsky E. 2008. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc Natl Acad Sci 105: 20209-20214.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 62
    • 0345305759 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
    • Lomakin IB, Kolupaeva VG, Marintchev A, Wagner G, Pestov TV. 2003. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev 17: 2786-2797.
    • (2003) Genes Dev , vol.17 , pp. 2786-2797
    • Lomakin, I.B.1    Kolupaeva, V.G.2    Marintchev, A.3    Wagner, G.4    Pestov, T.V.5
  • 63
    • 30444454334 scopus 로고    scopus 로고
    • The fidelity of translation initiation: Reciprocal activities of eIF1, IF3 and YciH
    • Lomakin IB, Shirokikh NE, Yusupov MM, Hellen CU, Pestov TV. 2006. The fidelity of translation initiation: Reciprocal activities of eIF1, IF3 and YciH. EMBO J 25: 196-210.
    • (2006) EMBO J , vol.25 , pp. 196-210
    • Lomakin, I.B.1    Shirokikh, N.E.2    Yusupov, M.M.3    Hellen, C.U.4    Pestov, T.V.5
  • 64
    • 77954373163 scopus 로고    scopus 로고
    • Molecular view of 43 S complex formation and start site selection in eukaryotic translation initiation
    • Lorsch JR, Dever TE. 2010. Molecular view of 43 S complex formation and start site selection in eukaryotic translation initiation. J Biol Chem 285: 21203-21207.
    • (2010) J Biol Chem , vol.285 , pp. 21203-21207
    • Lorsch, J.R.1    Dever, T.E.2
  • 65
    • 84860181797 scopus 로고    scopus 로고
    • Stringency of start codon selection modulates autoregulation of translation initiation factor eIF5
    • Loughran G, Sachs MS, Atkins JF, Ivanov IP. 2012. Stringency of start codon selection modulates autoregulation of translation initiation factor eIF5. Nucleic Acids Res 40: 2898-2906.
    • (2012) Nucleic Acids Res , vol.40 , pp. 2898-2906
    • Loughran, G.1    Sachs, M.S.2    Atkins, J.F.3    Ivanov, I.P.4
  • 66
    • 0037675905 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit
    • Maag D, Lorsch JR. 2003. Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit. J Mol Biol 330: 917-924.
    • (2003) J Mol Biol , vol.330 , pp. 917-924
    • Maag, D.1    Lorsch, J.R.2
  • 67
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • Maag D, Fekete CA, Gryczynski Z, Lorsch JR. 2005. A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol Cell 17: 265-275.
    • (2005) Mol Cell , vol.17 , pp. 265-275
    • Maag, D.1    Fekete, C.A.2    Gryczynski, Z.3    Lorsch, J.R.4
  • 68
    • 31344481752 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection
    • Maag D, Algire MA, Lorsch JR. 2006. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J Mol Biol 356: 724-737.
    • (2006) J Mol Biol , vol.356 , pp. 724-737
    • Maag, D.1    Algire, M.A.2    Lorsch, J.R.3
  • 69
    • 0037458626 scopus 로고    scopus 로고
    • Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex
    • Majumdar R, Bandyopadhyay A, Maitra U. 2003. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex. J Biol Chem 278: 6580-6587.
    • (2003) J Biol Chem , vol.278 , pp. 6580-6587
    • Majumdar, R.1    Bandyopadhyay, A.2    Maitra, U.3
  • 70
    • 0036792830 scopus 로고    scopus 로고
    • tRNomics: Analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and bacteria reveals anticodon-sparing strategies and domain-specific features
    • Marck C, Grosjean H. 2002. tRNomics: Analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and bacteria reveals anticodon-sparing strategies and domain-specific features. RNA 8: 1189-1232.
    • (2002) RNA , vol.8 , pp. 1189-1232
    • Marck, C.1    Grosjean, H.2
  • 71
    • 0037452587 scopus 로고    scopus 로고
    • Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: A new interaction between old partners
    • Marintchev A, Kolupaeva VG, Pestova TV, Wagner G. 2003. Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: A new interaction between old partners. Proc Natl Acad Sci 100: 1535-1540.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 1535-1540
    • Marintchev, A.1    Kolupaeva, V.G.2    Pestova, T.V.3    Wagner, G.4
  • 73
    • 67649646602 scopus 로고    scopus 로고
    • GTP hydrolysis by IF2 guides progression of the ribosome into elongation
    • Marshall RA, Aitken CE, Puglisi JD. 2009. GTP hydrolysis by IF2 guides progression of the ribosome into elongation. Mol Cell 35: 37-47.
    • (2009) Mol Cell , vol.35 , pp. 37-47
    • Marshall, R.A.1    Aitken, C.E.2    Puglisi, J.D.3
  • 74
    • 34548249070 scopus 로고    scopus 로고
    • Ribosomal protein L33 is required for ribosome biogenesis, subunit joining and repression of GCN4 translation
    • Martin-Marcos P, Hinnebusch AG, Tamame M. 2007. Ribosomal protein L33 is required for ribosome biogenesis, subunit joining and repression of GCN4 translation. Mo Cell Biol 27: 5968-5985.
    • (2007) Mo Cell Biol , vol.27 , pp. 5968-5985
    • Martin-Marcos, P.1    Hinnebusch, A.G.2    Tamame, M.3
  • 75
    • 83255187893 scopus 로고    scopus 로고
    • Functional elements in initiation factors 1, 1A and 2b discriminate against poor AUG context and non-AUG start codons
    • Martin-Marcos P, Cheung YN, Hinnebusch AG. 2011. Functional elements in initiation factors 1, 1A and 2b discriminate against poor AUG context and non-AUG start codons. Mol Cell Biol 31: 4814-4831.
    • (2011) Mol Cell Biol , vol.31 , pp. 4814-4831
    • Martin-Marcos, P.1    Cheung, Y.N.2    Hinnebusch, A.G.3
  • 76
    • 77956940474 scopus 로고    scopus 로고
    • The 50-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and block an alternative pathway
    • Mitchell SF, Walker SE, Algire MA, Park EH, Hinnebusc AG, Lorsch JR. 2010. The 50-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and block an alternative pathway. Mol Cell 39: 950-962.
    • (2010) Mol Cell , vol.39 , pp. 950-962
    • Mitchell, S.F.1    Walker, S.E.2    Algire, M.A.3    Park, E.H.4    Hinnebusc, A.G.5    Lorsch, J.R.6
  • 78
    • 77957676706 scopus 로고    scopus 로고
    • tRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculi
    • Naveau M, Lazennec-Schurdevin C, Panvert M, Mechula Y, Schmitt E. 2010. tRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculi. Biochemistry 49: 8680-8688.
    • (2010) Biochemistry , vol.49 , pp. 8680-8688
    • Naveau, M.1    Lazennec-Schurdevin, C.2    Panvert, M.3    Mechula, Y.4    Schmitt, E.5
  • 79
    • 77957813917 scopus 로고    scopus 로고
    • Yeast 18 S rRNA is directly involved in the ribosomal response to stringent AUG selection during translation initiation
    • Nemoto N, Singh CR, Udagawa T, Wang S, Thorson E, Winter Z, Ohira T, Ii M, Valasek L, Brown SJ, et al. 2010. Yeast 18 S rRNA is directly involved in the ribosomal response to stringent AUG selection during translation initiation. J Biol Chem 285: 32200-32212.
    • (2010) J Biol Chem , vol.285 , pp. 32200-32212
    • Nemoto, N.1    Singh, C.R.2    Udagawa, T.3    Wang, S.4    Thorson, E.5    Winter, Z.6    Ohira, T.7    Ii, M.8    Valasek, L.9    Brown, S.J.10
  • 80
    • 1842576663 scopus 로고    scopus 로고
    • Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
    • Nielsen KH, Szamecz B, Valasek L, Jivotovskaya A, Shin BS, Hinnebusch AG. 2004. Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control. EMBO J 23: 1166-1177.
    • (2004) EMBO J , vol.23 , pp. 1166-1177
    • Nielsen, K.H.1    Szamecz, B.2    Valasek, L.3    Jivotovskaya, A.4    Shin, B.S.5    Hinnebusch, A.G.6
  • 82
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • Oberer M, Marintchev A, Wagner G. 2005. Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev 19: 2212-2223.
    • (2005) Genes Dev , vol.19 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 83
    • 0037439198 scopus 로고    scopus 로고
    • Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
    • Olsen DS, EM S, Mathew A, Zhang F, Krishnamoorthy T, Phan L, Hinnebusch AG. 2003. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J 22: 193-204.
    • (2003) EMBO J , vol.22 , pp. 193-204
    • Olsen, D.S.1    Em, S.2    Mathew, A.3    Zhang, F.4    Krishnamoorthy, T.5    Phan, L.6    Hinnebusch, A.G.7
  • 84
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B
    • Ozes AR, Feoktistova K, Avanzino BC, Fraser CS. 2011. Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. JMol Biol 412: 674-687.
    • (2011) JMol Biol , vol.412 , pp. 674-687
    • Ozes, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 85
    • 78751609906 scopus 로고    scopus 로고
    • Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1 PABP mRNPs in vivo
    • Park E, Walker S, Lee J, Rothenburg S, Lorsch J, Hinnebusc A. 2011a. Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1 PABP mRNPs in vivo. EMBO J 30: 302-316.
    • (2011) EMBO J , vol.30 , pp. 302-316
    • Park, E.1    Walker, S.2    Lee, J.3    Rothenburg, S.4    Lorsch, J.5    Hinnebusc, A.6
  • 86
    • 79960741740 scopus 로고    scopus 로고
    • Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide
    • Park EH, Zhang F, Warringer J, Sunnerhagen P, Hinnebusc AG. 2011b. Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide. BMC Genomics 12: 1-18.
    • (2011) BMC Genomics , vol.12 , pp. 1-18
    • Park, E.H.1    Zhang, F.2    Warringer, J.3    Sunnerhagen, P.4    Hinnebusc, A.G.5
  • 90
    • 0035191271 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein
    • Paulin FE, Campbell LE, O'Brien K, Loughlin J, Proud CG. 2001. Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr Biol 11: 55-59.
    • (2001) Curr Biol , vol.11 , pp. 55-59
    • Paulin, F.E.1    Campbell, L.E.2    O'Brien, K.3    Loughlin, J.4    Proud, C.G.5
  • 91
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova TV, Kolupaeva VG. 2002. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev 16: 2906-2922.
    • (2002) Genes Dev , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 94
    • 33644779804 scopus 로고    scopus 로고
    • Specific functional interactions of nucleotides at key 23 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pisarev AV, Kolupaeva VG, Pisareva VP, MerrickWC, Helle CU, Pestova TV. 2006. Specific functional interactions of nucleotides at key 23 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev 20: 624-636.
    • (2006) Genes Dev , vol.20 , pp. 624-636
    • Pisarev, A.V.N.Y.1    Kolupaeva, V.G.2    Pisareva, V.P.3    Merrick, W.C.4    Helle, C.U.5    Pestova, T.V.6
  • 95
    • 44649095899 scopus 로고    scopus 로고
    • Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
    • Pisarev AV, Kolupaeva VG, Yusupov MM, Hellen CU, Pestov TV. 2008. Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes. EMBO J 27: 1609-1621.
    • (2008) EMBO J , vol.27 , pp. 1609-1621
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Yusupov, M.M.3    Hellen, C.U.4    Pestov, T.V.5
  • 96
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 50UTRs requires DExH-box protein DHX29
    • Pisareva VP, Pisarev AV, Komar AA, Hellen CU, Pestova TV. 2008. Translation initiation on mammalian mRNAs with structured 50UTRs requires DExH-box protein DHX29. Cell 135: 1237-1250.
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3    Hellen, C.U.4    Pestova, T.V.5
  • 97
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. 2011. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331: 730-736.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 98
    • 84862000545 scopus 로고    scopus 로고
    • Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 50-overhangs
    • doi: 10.1074/jbc.M112.347278
    • Rajagopal V, Park EH, Hinnebusch AG, Lorsch JR. 2012. Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 50-overhangs. J Biol Chem doi: 10.1074/jbc.M112.347278.
    • (2012) J Biol Chem
    • Rajagopal, V.1    Park, E.H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 100
    • 38149140938 scopus 로고    scopus 로고
    • Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection
    • Reibarkh M, Yamamoto Y, Singh CR, del Rio F, Fahmy A, Le B, Luna RE, Ii M, Wagner G, Asano K. 2008. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J Biol Chem 283: 1094-1103.
    • (2008) J Biol Chem , vol.283 , pp. 1094-1103
    • Reibarkh, M.1    Yamamoto, Y.2    Singh, C.R.3    del Rio, F.4    Fahmy, A.5    Le, B.6    Luna, R.E.7    Ii, M.8    Wagner, G.9    Asano, K.10
  • 101
    • 52949097997 scopus 로고    scopus 로고
    • Interactions between eIF4AI and its accessory factors eIF4B and eIF4H
    • Rozovsky N, Butterworth AC, Moore MJ. 2008. Interactions between eIF4AI and its accessory factors eIF4B and eIF4H. RNA 14: 2136-2148.
    • (2008) RNA , vol.14 , pp. 2136-2148
    • Rozovsky, N.1    Butterworth, A.C.2    Moore, M.J.3
  • 102
    • 73549103606 scopus 로고    scopus 로고
    • Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNA(i)(Met) binding to the ribosome
    • Saini AK, Nanda JS, Lorsch JR, Hinnebusch AG. 2010. Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNA(i)(Met) binding to the ribosome. Genes Dev 24: 97-110.
    • (2010) Genes Dev , vol.24 , pp. 97-110
    • Saini, A.K.1    Nanda, J.S.2    Lorsch, J.R.3    Hinnebusch, A.G.4
  • 103
    • 71849102917 scopus 로고    scopus 로고
    • Eukaryotic and archaeal translation initiation factor 2: A heterotrimeric tRNA carrier
    • Schmitt E, Naveau M, Mechulam Y. 2010. Eukaryotic and archaeal translation initiation factor 2: A heterotrimeric tRNA carrier. FEBS Lett 584: 405-412.
    • (2010) FEBS Lett , vol.584 , pp. 405-412
    • Schmitt, E.1    Naveau, M.2    Mechulam, Y.3
  • 105
  • 107
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyam S. 2006. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125: 287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyam, S.5
  • 108
    • 3042668591 scopus 로고    scopus 로고
    • Comparative analysis of orthologous eukaryotic mRNAs: Potential hidden functional signals
    • Shabalina SA, Ogurtsov AY, Rogozin IB, Koonin EV, Lipma DJ. 2004. Comparative analysis of orthologous eukaryotic mRNAs: Potential hidden functional signals. Nuclei Acids Res 32: 1774-1782.
    • (2004) Nuclei Acids Res , vol.32 , pp. 1774-1782
    • Shabalina, S.A.1    Ogurtsov, A.Y.2    Rogozin, I.B.3    Koonin, E.V.4    Lipma, D.J.5
  • 109
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin BS, Maag D, Roll-Mecak A, Arefin MS, Burley SK, Lorsch JR, Dever TE. 2002. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 111: 1015-1025.
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1    Maag, D.2    Roll-Mecak, A.3    Arefin, M.S.4    Burley, S.K.5    Lorsch, J.R.6    Dever, T.E.7
  • 110
    • 33847224854 scopus 로고    scopus 로고
    • Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant
    • Shin BS, Acker MG, Maag D, Kim JR, Lorsch JR, Dever TE. 2007. Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant. Mol Cell Biol 27: 1677-1685.
    • (2007) Mol Cell Biol , vol.27 , pp. 1677-1685
    • Shin, B.S.1    Acker, M.G.2    Maag, D.3    Kim, J.R.4    Lorsch, J.R.5    Dever, T.E.6
  • 111
    • 80555131009 scopus 로고    scopus 로고
    • Initiation factor eIF2g promotes eIF2-GTP-MettRNA(i)(Met) ternary complex binding to the 40S ribosome
    • Shin BS, Kim JR, Walker SE, Dong J, Lorsch JR, Dever TE. 2011. Initiation factor eIF2g promotes eIF2-GTP-MettRNA(i)(Met) ternary complex binding to the 40S ribosome. Nat Struct Mol Biol 18: 1227-1234.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1227-1234
    • Shin, B.S.1    Kim, J.R.2    Walker, S.E.3    Dong, J.4    Lorsch, J.R.5    Dever, T.E.6
  • 112
    • 3843096103 scopus 로고    scopus 로고
    • Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo
    • Singh CR, He H, Ii M, Yamamoto Y, Asano K. 2004. Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo. J Biol Chem 279: 31910-31920.
    • (2004) J Biol Chem , vol.279 , pp. 31910-31920
    • Singh, C.R.1    He, H.2    Ii, M.3    Yamamoto, Y.4    Asano, K.5
  • 113
    • 20744451862 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation
    • Singh CR, Curtis C, Yamamoto Y, Hall NS, Kruse DS, He H, Hannig EM, Asano K. 2005. Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation. Mol Cell Biol 25: 5480-5491.
    • (2005) Mol Cell Biol , vol.25 , pp. 5480-5491
    • Singh, C.R.1    Curtis, C.2    Yamamoto, Y.3    Hall, N.S.4    Kruse, D.S.5    He, H.6    Hannig, E.M.7    Asano, K.8
  • 114
    • 33749340583 scopus 로고    scopus 로고
    • An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
    • Singh CR, Lee B, Udagawa T, Mohammad-Qureshi SS, Yamamot Y, PavittGD, Asano K. 2006. An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J 25: 4537-4546.
    • (2006) EMBO J , vol.25 , pp. 4537-4546
    • Singh, C.R.1    Lee, B.2    Udagawa, T.3    Mohammad-Qureshi, S.S.4    Yamamot, Y.5    Pavitt, G.D.6    Asano, K.7
  • 115
    • 34249699125 scopus 로고    scopus 로고
    • Change in nutritional status modulates the abundance of critical preinitiation intermediate complexes during translation initiation in vivo
    • Singh CR, Udagawa T, Lee B, Wassink S, He H, Yamamoto Y, Anderson JT, Pavitt GD, Asano K. 2007. Change in nutritional status modulates the abundance of critical preinitiation intermediate complexes during translation initiation in vivo. J Mol Biol 370: 315-330.
    • (2007) J Mol Biol , vol.370 , pp. 315-330
    • Singh, C.R.1    Udagawa, T.2    Lee, B.3    Wassink, S.4    He, H.5    Yamamoto, Y.6    Anderson, J.T.7    Pavitt, G.D.8    Asano, K.9
  • 116
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok B, Fraser CS, Hall RJ, Doudna JA, Nogales E. 2005. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310: 1513-1515.
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1    Fraser, C.S.2    Hall, R.J.3    Doudna, J.A.4    Nogales, E.5
  • 117
    • 77955862748 scopus 로고    scopus 로고
    • Activities of Ligatin and MCT-1/ DENR in eukaryotic translation initiation and ribosomal recycling
    • Skabkin MA, Skabkina OV, Dhote V, Komar AA, Hellen CU, Pestova TV. 2010. Activities of Ligatin and MCT-1/ DENR in eukaryotic translation initiation and ribosomal recycling. Genes Dev 24: 1787-1801.
    • (2010) Genes Dev , vol.24 , pp. 1787-1801
    • Skabkin, M.A.1    Skabkina, O.V.2    Dhote, V.3    Komar, A.A.4    Hellen, C.U.5    Pestova, T.V.6
  • 118
    • 84855867417 scopus 로고    scopus 로고
    • The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit
    • Sokabe M, Fraser CS, Hershey JW. 2011. The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit. Nucleic Acids Res 40: 905-913.
    • (2011) Nucleic Acids Res , vol.40 , pp. 905-913
    • Sokabe, M.1    Fraser, C.S.2    Hershey, J.W.3
  • 119
    • 70449553011 scopus 로고    scopus 로고
    • How does a scanning ribosomal particle move along the 50-untranslated region of eukaryotic mRNA? Brownian ratchetmodel
    • Spirin AS. 2009. How does a scanning ribosomal particle move along the 50-untranslated region of eukaryotic mRNA? Brownian ratchetmodel. Biochemistry 48: 10688-10692.
    • (2009) Biochemistry , vol.48 , pp. 10688-10692
    • Spirin, A.S.1
  • 120
    • 79952280840 scopus 로고    scopus 로고
    • The highly conserved KEOPS/ EKC complex is essential for a universal tRNA modification, t6A
    • Srinivasan M, Mehta P, Yu Y, Prugar E, Koonin EV, Karza AW, Sternglanz R. 2011. The highly conserved KEOPS/ EKC complex is essential for a universal tRNA modification, t6A. EMBO J 30: 873-881.
    • (2011) EMBO J , vol.30 , pp. 873-881
    • Srinivasan, M.1    Mehta, P.2    Yu, Y.3    Prugar, E.4    Koonin, E.V.5    Karza, A.W.6    Sternglanz, R.7
  • 121
    • 50149109434 scopus 로고    scopus 로고
    • Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the a-and b-subunits
    • Stolboushkina E, Nikonov S, Nikulin A, Blasi U, Manstei DJ, Fedorov R, Garber M, Nikonov O. 2008. Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the a-and b-subunits. J Mol Biol 382: 680-691.
    • (2008) J Mol Biol , vol.382 , pp. 680-691
    • Stolboushkina, E.1    Nikonov, S.2    Nikulin, A.3    Blasi, U.4    Manstei, D.J.5    Fedorov, R.6    Garber, M.7    Nikonov, O.8
  • 123
    • 0035032444 scopus 로고    scopus 로고
    • The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 50 secondary structure
    • Svitkin Y, Pause A, Haghighat A, Pyronnet S, Witherell GW, Belsham G, Sonenberg N. 2001. The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 50 secondary structure. RNA 7: 382-394.
    • (2001) RNA , vol.7 , pp. 382-394
    • Svitkin, Y.1    Pause, A.2    Haghighat, A.3    Pyronnet, S.4    Witherell, G.W.5    Belsham, G.6    Sonenberg, N.7
  • 126
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly (A) tail-dependent translation
    • Tarun SZ, Wells SE, Deardorff JA, Sachs AB. 1997. Translation initiation factor eIF4G mediates in vitro poly (A) tail-dependent translation. Proc Natl Acad Sci 94: 9046-9051.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1    Wells, S.E.2    Deardorff, J.A.3    Sachs, A.B.4
  • 127
    • 10644249220 scopus 로고    scopus 로고
    • Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP
    • Unbehaun A, Borukhov SI, Hellen CU, Pestova TV. 2004. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev 18: 3078-3093.
    • (2004) Genes Dev , vol.18 , pp. 3078-3093
    • Unbehaun, A.1    Borukhov, S.I.2    Hellen, C.U.3    Pestova, T.V.4
  • 128
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valášek L, Nielsen KH, Hinnebusch AG. 2002. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J 21: 5886-5898.
    • (2002) EMBO J , vol.21 , pp. 5886-5898
    • Valášek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 129
    • 0037444342 scopus 로고    scopus 로고
    • The Yeast eIF3 subunits TIF32/a and NIP1/c and eIF5 make critical connections with the 40S ribosome in vivo
    • Valášek L, Mathew A, Shin BS, Nielsen KH, Szamecz B, Hinnebusch AG. 2003. The Yeast eIF3 subunits TIF32/a and NIP1/c and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev 17: 786-799.
    • (2003) Genes Dev , vol.17 , pp. 786-799
    • Valášek, L.1    Mathew, A.2    Shin, B.S.3    Nielsen, K.H.4    Szamecz, B.5    Hinnebusch, A.G.6
  • 130
    • 6344291066 scopus 로고    scopus 로고
    • Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
    • Valášek L, Nielsen KH, Zhang F, Fekete CA, Hinnebusch AG. 2004. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol Cell Biol 24: 9437-9455.
    • (2004) Mol Cell Biol , vol.24 , pp. 9437-9455
    • Valášek, L.1    Nielsen, K.H.2    Zhang, F.3    Fekete, C.A.4    Hinnebusch, A.G.5
  • 131
    • 80052212313 scopus 로고    scopus 로고
    • Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation
    • Vassilenko KS, Alekhina OM, Dmitriev SE, Shatsky IN, Spirin AS. 2011. Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation. Nucleic Acids Res 39: 5555-5567.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5555-5567
    • Vassilenko, K.S.1    Alekhina, O.M.2    Dmitriev, S.E.3    Shatsky, I.N.4    Spirin, A.S.5
  • 132
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • von der Haar T, McCarthy JE. 2002. Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function. Mol Microbiol 46: 531-544.
    • (2002) Mol Microbiol , vol.46 , pp. 531-544
    • von der Haar, T.1    McCarthy, J.E.2
  • 133
    • 62849126891 scopus 로고    scopus 로고
    • Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap
    • Yanagiya A, Svitkin YV, Shibata S, Mikami S, Imataka H, Sonenberg N. 2009. Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap. Mol Cell Biol 29: 1661-1669.
    • (2009) Mol Cell Biol , vol.29 , pp. 1661-1669
    • Yanagiya, A.1    Svitkin, Y.V.2    Shibata, S.3    Mikami, S.4    Imataka, H.5    Sonenberg, N.6
  • 134
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the g subunit in an archaeal aIF2ag heterodimer
    • Yatime L, Mechulam Y, Blanquet S, Schmitt E. 2006. Structural switch of the g subunit in an archaeal aIF2ag heterodimer. Structure 14: 119-128.
    • (2006) Structure , vol.14 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 135
    • 36749037829 scopus 로고    scopus 로고
    • Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
    • Yatime L, Mechulam Y, Blanquet S, Schmitt E. 2007. Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proc Natl Acad Sci 104: 18445-18450.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 18445-18450
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 137
    • 79959452628 scopus 로고    scopus 로고
    • Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors
    • Yu Y, Abaeva IS, Marintchev A, Pestova TV, HellenCU. 2011. Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors. Nuclei Acids Res 39: 4851-4865.
    • (2011) Nuclei Acids Res , vol.39 , pp. 4851-4865
    • Yu, Y.1    Abaeva, I.S.2    Marintchev, A.3    Pestova, T.V.4    Hellen, C.U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.