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Volumn 11, Issue 5, 2013, Pages

Control of Translation and miRNA-Dependent Repression by a Novel Poly(A) Binding Protein, hnRNP-Q

Author keywords

[No Author keywords available]

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN Q; MICRORNA; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN P68; UNCLASSIFIED DRUG;

EID: 84878295720     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001564     Document Type: Article
Times cited : (49)

References (90)
  • 1
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • Glisovic T, Bachorik JL, Yong J, Dreyfuss G, (2008) RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett 582: 1977-1986.
    • (2008) FEBS Lett , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 2
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson P, Kedersha N, (2009) RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 10: 430-436.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 3
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA biology from an atlas of mammalian mRNA-binding proteins
    • Castello A, Fischer B, Eichelbaum K, Horos R, Beckmann BM, et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149: 1393-1406.
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1    Fischer, B.2    Eichelbaum, K.3    Horos, R.4    Beckmann, B.M.5
  • 4
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV, (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11: 113-127.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 5
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N, (1999) eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 68: 913-963.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 6
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF4G
    • Tarun SZ, Sachs AB, (1996) Association of the yeast poly(A) tail binding protein with translation initiation factor eIF4G. EMBO J 15: 7168-7177.
    • (1996) EMBO J , vol.15 , pp. 7168-7177
    • Tarun, S.Z.1    Sachs, A.B.2
  • 7
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka H, Gradi A, Sonenberg N, (1998) A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J 17: 7480-7489.
    • (1998) EMBO J , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 8
    • 84869085954 scopus 로고    scopus 로고
    • Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G
    • Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, et al. (2012) Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. Mol Cell 48: 375-386.
    • (2012) Mol Cell , vol.48 , pp. 375-386
    • Safaee, N.1    Kozlov, G.2    Noronha, A.M.3    Xie, J.4    Wilds, C.J.5
  • 9
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • Sonenberg N, Hershey JWB, Mathews MB, editors, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Hershey JWB, Merrick WC (2000) Pathway and mechanism of initiation of protein synthesis. In: Sonenberg N, Hershey JWB, Mathews MB, editors. Translational control of gene expression. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. pp. 33-88.
    • (2000) Translational control of gene expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 10
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells SE, Hillner PE, Vale RD, Sachs AB, (1998) Circularization of mRNA by eukaryotic translation initiation factors. Mol Cell 2: 135-140.
    • (1998) Mol Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 11
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • Kuhn U, Wahle E, (2004) Structure and function of poly(A) binding proteins. Biochim Biophys Acta 1678: 67-84.
    • (2004) Biochim Biophys Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 12
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation: the closed-loop model
    • Hershey JWB, Mathews MB, Sonenberg N, editors, Plainview, NY: Cold Spring Harbor Laboratory Press
    • Jacobson A (1996) Poly(A) metabolism and translation: the closed-loop model. In: Hershey JWB, Mathews MB, Sonenberg N, editors. Translational control. Plainview, NY: Cold Spring Harbor Laboratory Press. pp. 451-480.
    • (1996) Translational control , pp. 451-480
    • Jacobson, A.1
  • 13
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus DA, Evans MC, Jacobson A, (2003) Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol 4: 223.
    • (2003) Genome Biol , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 14
    • 0015591267 scopus 로고
    • A protein of molecular weight 78,000 bound to the polyadenylate region of eukaryotic messenger RNAs
    • Blobel G, (1973) A protein of molecular weight 78,000 bound to the polyadenylate region of eukaryotic messenger RNAs. Proc Natl Acad Sci USA 70: 924-928.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 924-928
    • Blobel, G.1
  • 15
    • 0020638516 scopus 로고
    • The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein
    • Baer BW, Kornberg RD, (1983) The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein. J Cell Biol 96: 717-721.
    • (1983) J Cell Biol , vol.96 , pp. 717-721
    • Baer, B.W.1    Kornberg, R.D.2
  • 16
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray NK, Coller JM, Dickson KS, Wickens M, (2000) Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J 19: 4723-4733.
    • (2000) EMBO J , vol.19 , pp. 4723-4733
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 17
    • 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, Sonenberg 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    Sonenberg, N.5
  • 18
    • 0034743391 scopus 로고    scopus 로고
    • Linking the 3′ poly(A) tail to the subunit joining step of translation initiation: relations of Pab1p, eukaryotic translation initiation factor 5B (Fun12p), and Ski2p-Slh1p
    • Searfoss A, Dever TE, Wickner R, (2001) Linking the 3′ poly(A) tail to the subunit joining step of translation initiation: relations of Pab1p, eukaryotic translation initiation factor 5B (Fun12p), and Ski2p-Slh1p. Mol Cell Biol 21: 4900-4908.
    • (2001) Mol Cell Biol , vol.21 , pp. 4900-4908
    • Searfoss, A.1    Dever, T.E.2    Wickner, R.3
  • 19
    • 0037184899 scopus 로고    scopus 로고
    • A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation
    • Uchida N, Hoshino S, Imataka H, Sonenberg N, Katada T, (2002) A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation. J Biol Chem 277: 50286-50292.
    • (2002) J Biol Chem , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 20
    • 84861839851 scopus 로고    scopus 로고
    • PABP and the poly(A) tail augment microRNA repression by facilitated miRISC binding
    • Moretti F, Kaiser C, Zdanowicz-Specht A, Hentze MW, (2012) PABP and the poly(A) tail augment microRNA repression by facilitated miRISC binding. Nat Struct Mol Biol 19: 603-608.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 603-608
    • Moretti, F.1    Kaiser, C.2    Zdanowicz-Specht, A.3    Hentze, M.W.4
  • 21
    • 28544450636 scopus 로고    scopus 로고
    • Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover
    • Yamashita A, Chang TC, Yamashita Y, Zhu W, Zhong Z, et al. (2005) Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover. Nat Struct Mol Biol 12: 1054-1063.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1054-1063
    • Yamashita, A.1    Chang, T.C.2    Yamashita, Y.3    Zhu, W.4    Zhong, Z.5
  • 22
    • 67651000077 scopus 로고    scopus 로고
    • The GW182 protein family in animal cells: new insights into domains required for miRNA-mediated gene silencing
    • Eulalio A, Tritschler F, Izaurralde E, (2009) The GW182 protein family in animal cells: new insights into domains required for miRNA-mediated gene silencing. RNA 15: 1433-1442.
    • (2009) RNA , vol.15 , pp. 1433-1442
    • Eulalio, A.1    Tritschler, F.2    Izaurralde, E.3
  • 23
    • 34249810892 scopus 로고    scopus 로고
    • Argonaute proteins: mediators of RNA silencing
    • Peters L, Meister G, (2007) Argonaute proteins: mediators of RNA silencing. Mol Cell 26: 611-623.
    • (2007) Mol Cell , vol.26 , pp. 611-623
    • Peters, L.1    Meister, G.2
  • 24
    • 38349169664 scopus 로고    scopus 로고
    • Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight?
    • Filipowicz W, Bhattacharyya SN, Sonenberg N, (2008) Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight? Nat Rev Genet 9: 102-114.
    • (2008) Nat Rev Genet , vol.9 , pp. 102-114
    • Filipowicz, W.1    Bhattacharyya, S.N.2    Sonenberg, N.3
  • 25
    • 70349177026 scopus 로고    scopus 로고
    • Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-dependent deadenylation
    • Fabian MR, Mathonnet G, Sundermeier T, Mathys H, Zipprich JT, et al. (2009) Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-dependent deadenylation. Mol Cell 35: 868-880.
    • (2009) Mol Cell , vol.35 , pp. 868-880
    • Fabian, M.R.1    Mathonnet, G.2    Sundermeier, T.3    Mathys, H.4    Zipprich, J.T.5
  • 26
    • 76349104822 scopus 로고    scopus 로고
    • Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation
    • Jinek M, Fabian MR, Coyle SM, Sonenberg N, Doudna JA, (2010) Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation. Nat Struct Mol Biol 17: 238-240.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 238-240
    • Jinek, M.1    Fabian, M.R.2    Coyle, S.M.3    Sonenberg, N.4    Doudna, J.A.5
  • 27
    • 78649742020 scopus 로고    scopus 로고
    • mRNA-specific regulation of translation by poly(A)-binding proteins
    • Burgess HM, Gray NK, (2010) mRNA-specific regulation of translation by poly(A)-binding proteins. Biochem Soc Trans 38: 1517-1522.
    • (2010) Biochem Soc Trans , vol.38 , pp. 1517-1522
    • Burgess, H.M.1    Gray, N.K.2
  • 28
    • 84855911694 scopus 로고    scopus 로고
    • The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities
    • Brook M, McCracken L, Reddington JP, Lu ZL, Morrice NA, et al. (2012) The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities. Biochem J 441: 803-812.
    • (2012) Biochem J , vol.441 , pp. 803-812
    • Brook, M.1    McCracken, L.2    Reddington, J.P.3    Lu, Z.L.4    Morrice, N.A.5
  • 29
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig AW, Haghighat A, Yu AT, Sonenberg N, (1998) Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392: 520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 30
    • 55449106579 scopus 로고    scopus 로고
    • Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation
    • Martineau Y, Derry MC, Wang X, Yanagiya A, Berlanga JJ, et al. (2008) Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation. Mol Cell Biol 28: 6658-6667.
    • (2008) Mol Cell Biol , vol.28 , pp. 6658-6667
    • Martineau, Y.1    Derry, M.C.2    Wang, X.3    Yanagiya, A.4    Berlanga, J.J.5
  • 31
    • 0035109013 scopus 로고    scopus 로고
    • Translational repression by a novel partner of human poly(A) binding protein, Paip2
    • Khaleghpour K, Svitkin YV, Craig AW, DeMaria CT, Deo RC, et al. (2001) Translational repression by a novel partner of human poly(A) binding protein, Paip2. Mol Cell 7: 205-216.
    • (2001) Mol Cell , vol.7 , pp. 205-216
    • Khaleghpour, K.1    Svitkin, Y.V.2    Craig, A.W.3    DeMaria, C.T.4    Deo, R.C.5
  • 32
    • 33745450501 scopus 로고    scopus 로고
    • A mechanism of translational repression by competition of Paip2 with eIF4G for poly(A) binding protein (PABP) binding
    • Karim MM, Svitkin YV, Kahvejian A, De Crescenzo G, Costa-Mattioli M, et al. (2006) A mechanism of translational repression by competition of Paip2 with eIF4G for poly(A) binding protein (PABP) binding. Proc Natl Acad Sci U S A 103: 9494-9499.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9494-9499
    • Karim, M.M.1    Svitkin, Y.V.2    Kahvejian, A.3    De Crescenzo, G.4    Costa-Mattioli, M.5
  • 33
    • 0018432123 scopus 로고
    • Ultraviolet light-induced crosslinking of mRNA to proteins
    • Greenberg JR, (1979) Ultraviolet light-induced crosslinking of mRNA to proteins. Nucleic Acids Res 6: 715-732.
    • (1979) Nucleic Acids Res , vol.6 , pp. 715-732
    • Greenberg, J.R.1
  • 34
    • 2142826526 scopus 로고    scopus 로고
    • An efficient system for cap- and poly(A)-dependent translation in vitro
    • Svitkin YV, Sonenberg N, (2004) An efficient system for cap- and poly(A)-dependent translation in vitro. Methods Mol Biol 257: 155-170.
    • (2004) Methods Mol Biol , vol.257 , pp. 155-170
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 35
    • 0032889252 scopus 로고    scopus 로고
    • A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice
    • Harris CE, Boden RA, Astell CR, (1999) A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice. J Virol 73: 72-80.
    • (1999) J Virol , vol.73 , pp. 72-80
    • Harris, C.E.1    Boden, R.A.2    Astell, C.R.3
  • 36
    • 84859715627 scopus 로고    scopus 로고
    • Negative regulation of RhoA translation and signaling by hnRNP-Q1 affects cellular morphogenesis
    • Xing L, Yao X, Williams KR, Bassell GJ, (2011) Negative regulation of RhoA translation and signaling by hnRNP-Q1 affects cellular morphogenesis. Mol Biol Cell 23: 1500-1509.
    • (2011) Mol Biol Cell , vol.23 , pp. 1500-1509
    • Xing, L.1    Yao, X.2    Williams, K.R.3    Bassell, G.J.4
  • 37
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G, (2001) SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J 20: 5443-5452.
    • (2001) EMBO J , vol.20 , pp. 5443-5452
    • Mourelatos, Z.1    Abel, L.2    Yong, J.3    Kataoka, N.4    Dreyfuss, G.5
  • 38
    • 0034730324 scopus 로고    scopus 로고
    • A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex
    • Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, et al. (2000) A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell 103: 29-40.
    • (2000) Cell , vol.103 , pp. 29-40
    • Grosset, C.1    Chen, C.Y.2    Xu, N.3    Sonenberg, N.4    Jacquemin-Sablon, H.5
  • 39
    • 0035971213 scopus 로고    scopus 로고
    • Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing
    • Blanc V, Navaratnam N, Henderson JO, Anant S, Kennedy S, et al. (2001) Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing. J Biol Chem 276: 10272-10283.
    • (2001) J Biol Chem , vol.276 , pp. 10272-10283
    • Blanc, V.1    Navaratnam, N.2    Henderson, J.O.3    Anant, S.4    Kennedy, S.5
  • 40
    • 55849144692 scopus 로고    scopus 로고
    • The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene
    • Chen HH, Chang JG, Lu RM, Peng TY, Tarn WY, (2008) The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene. Mol Cell Biol 28: 6929-6938.
    • (2008) Mol Cell Biol , vol.28 , pp. 6929-6938
    • Chen, H.H.1    Chang, J.G.2    Lu, R.M.3    Peng, T.Y.4    Tarn, W.Y.5
  • 41
    • 4444361515 scopus 로고    scopus 로고
    • A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon
    • Kim JH, Paek KY, Ha SH, Cho S, Choi K, et al. (2004) A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon. Mol Cell Biol 24: 7878-7890.
    • (2004) Mol Cell Biol , vol.24 , pp. 7878-7890
    • Kim, J.H.1    Paek, K.Y.2    Ha, S.H.3    Cho, S.4    Choi, K.5
  • 42
    • 33845760911 scopus 로고    scopus 로고
    • BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1
    • Cho S, Park SM, Kim TD, Kim JH, Kim KT, et al. (2007) BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1. Mol Cell Biol 27: 368-383.
    • (2007) Mol Cell Biol , vol.27 , pp. 368-383
    • Cho, S.1    Park, S.M.2    Kim, T.D.3    Kim, J.H.4    Kim, K.T.5
  • 43
    • 34147166984 scopus 로고    scopus 로고
    • Rhythmic control of AANAT translation by hnRNP Q in circadian melatonin production
    • Kim TD, Woo KC, Cho S, Ha DC, Jang SK, et al. (2007) Rhythmic control of AANAT translation by hnRNP Q in circadian melatonin production. Genes Dev 21: 797-810.
    • (2007) Genes Dev , vol.21 , pp. 797-810
    • Kim, T.D.1    Woo, K.C.2    Cho, S.3    Ha, D.C.4    Jang, S.K.5
  • 44
    • 84872308008 scopus 로고    scopus 로고
    • hnRNP Q regulates translation of p53 in normal and stress conditions
    • doi 10.1038/cdd.2012.109
    • Kim DY, Kim W, Lee KH, Kim SH, Lee HR, et al. (2012) hnRNP Q regulates translation of p53 in normal and stress conditions. Cell Death Differ doi:10.1038/cdd.2012.109.
    • (2012) Cell Death Differ
    • Kim, D.Y.1    Kim, W.2    Lee, K.H.3    Kim, S.H.4    Lee, H.R.5
  • 45
    • 80053194321 scopus 로고    scopus 로고
    • Translation-competent 48S complex formation on HCV IRES requires the RNA-binding protein NSAP1
    • Park SM, Paek KY, Hong KY, Jang CJ, Cho S, et al. (2011) Translation-competent 48S complex formation on HCV IRES requires the RNA-binding protein NSAP1. Nucleic Acids Res 39: 7791-7802.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7791-7802
    • Park, S.M.1    Paek, K.Y.2    Hong, K.Y.3    Jang, C.J.4    Cho, S.5
  • 46
    • 0037067732 scopus 로고    scopus 로고
    • Identification of pp68 as the tyrosine-phosphorylated form of SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein
    • Hresko RC, Mueckler M, (2002) Identification of pp68 as the tyrosine-phosphorylated form of SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein. J Biol Chem 277: 25233-25238.
    • (2002) J Biol Chem , vol.277 , pp. 25233-25238
    • Hresko, R.C.1    Mueckler, M.2
  • 47
    • 33745162529 scopus 로고    scopus 로고
    • The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization
    • Passos DO, Quaresma AJ, Kobarg J, (2006) The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization. Biochem Biophys Res Commun 346: 517-525.
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 517-525
    • Passos, D.O.1    Quaresma, A.J.2    Kobarg, J.3
  • 48
    • 0034737604 scopus 로고    scopus 로고
    • SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms
    • Mizutani A, Fukuda M, Ibata K, Shiraishi Y, Mikoshiba K, (2000) SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms. J Biol Chem 275: 9823-9831.
    • (2000) J Biol Chem , vol.275 , pp. 9823-9831
    • Mizutani, A.1    Fukuda, M.2    Ibata, K.3    Shiraishi, Y.4    Mikoshiba, K.5
  • 49
    • 0001409429 scopus 로고    scopus 로고
    • Masked and translatable messenger ribonucleoproteins in higher eukariotes
    • Hershey JWB, Mathews MB, Sonenberg N, editors, Plainview, NY: Cold Spring Harbor Laboratory Press
    • Spirin AS (1996) Masked and translatable messenger ribonucleoproteins in higher eukariotes. In: Hershey JWB, Mathews MB, Sonenberg N, editors. Translational control. Plainview, NY: Cold Spring Harbor Laboratory Press. pp. 319-334.
    • (1996) Translational control , pp. 319-334
    • Spirin, A.S.1
  • 50
    • 42749087550 scopus 로고    scopus 로고
    • Modulation of enteroviral proteinase cleavage of poly(A)-binding protein (PABP) by conformation and PABP-associated factors
    • Rivera CI, Lloyd RE, (2008) Modulation of enteroviral proteinase cleavage of poly(A)-binding protein (PABP) by conformation and PABP-associated factors. Virology 375: 59-72.
    • (2008) Virology , vol.375 , pp. 59-72
    • Rivera, C.I.1    Lloyd, R.E.2
  • 51
    • 0030836448 scopus 로고    scopus 로고
    • Overexpression in COS cells of p50, the major core protein associated with mRNA, results in translation inhibition
    • Davydova EK, Evdokimova VM, Ovchinnikov LP, Hershey JW, (1997) Overexpression in COS cells of p50, the major core protein associated with mRNA, results in translation inhibition. Nucleic Acids Res 25: 2911-2916.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2911-2916
    • Davydova, E.K.1    Evdokimova, V.M.2    Ovchinnikov, L.P.3    Hershey, J.W.4
  • 52
    • 0038063499 scopus 로고    scopus 로고
    • Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction
    • Kuhn U, Pieler T, (1996) Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction. J Mol Biol 256: 20-30.
    • (1996) J Mol Biol , vol.256 , pp. 20-30
    • Kuhn, U.1    Pieler, T.2
  • 53
    • 0028340737 scopus 로고
    • The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity
    • Görlach M, Burd CG, Dreyfuss G, (1994) The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity. Exp Cell Res 211: 400-407.
    • (1994) Exp Cell Res , vol.211 , pp. 400-407
    • Görlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 54
    • 58149330117 scopus 로고    scopus 로고
    • General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation
    • Svitkin YV, Evdokimova VM, Brasey A, Pestova TV, Fantus D, et al. (2009) General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation. EMBO J 28: 58-68.
    • (2009) EMBO J , vol.28 , pp. 58-68
    • Svitkin, Y.V.1    Evdokimova, V.M.2    Brasey, A.3    Pestova, T.V.4    Fantus, D.5
  • 55
    • 0038529622 scopus 로고    scopus 로고
    • The mRNA-binding protein YB-1 (p50) prevents association of the eukaryotic initiation factor eIF4G with mRNA and inhibits protein synthesis at the initiation stage
    • Nekrasov MP, Ivshina MP, Chernov KG, Kovrigina EA, Evdokimova VM, et al. (2003) The mRNA-binding protein YB-1 (p50) prevents association of the eukaryotic initiation factor eIF4G with mRNA and inhibits protein synthesis at the initiation stage. J Biol Chem 278: 13936-13943.
    • (2003) J Biol Chem , vol.278 , pp. 13936-13943
    • Nekrasov, M.P.1    Ivshina, M.P.2    Chernov, K.G.3    Kovrigina, E.A.4    Evdokimova, V.M.5
  • 56
    • 35548996750 scopus 로고    scopus 로고
    • Back to basics: the untreated rabbit reticulocyte lysate as a competitive system to recapitulate cap/poly(A) synergy and the selective advantage of IRES-driven translation
    • Rifo RS, Ricci EP, Decimo D, Moncorge O, Ohlmann T, (2007) Back to basics: the untreated rabbit reticulocyte lysate as a competitive system to recapitulate cap/poly(A) synergy and the selective advantage of IRES-driven translation. Nucleic Acids Res 35: e121.
    • (2007) Nucleic Acids Res , vol.35
    • Rifo, R.S.1    Ricci, E.P.2    Decimo, D.3    Moncorge, O.4    Ohlmann, T.5
  • 57
    • 0031414570 scopus 로고    scopus 로고
    • Poly(A) dependent translation in rabbit reticulocyte lysate
    • Wakiyama M, Futami T, Miura K, (1997) Poly(A) dependent translation in rabbit reticulocyte lysate. Biochimie 79: 781-785.
    • (1997) Biochimie , vol.79 , pp. 781-785
    • Wakiyama, M.1    Futami, T.2    Miura, K.3
  • 58
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • Svitkin YV, Ovchinnikov LP, Dreyfuss G, Sonenberg N, (1996) General RNA binding proteins render translation cap dependent. EMBO J 15: 7147-7155.
    • (1996) EMBO J , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4
  • 59
    • 0017882570 scopus 로고
    • Translational recognition of the 5′-terminal 7-methylguanosine of globin messenger RNA as a function of ionic strength
    • Chu LY, Rhoads RE, (1978) Translational recognition of the 5′-terminal 7-methylguanosine of globin messenger RNA as a function of ionic strength. Biochemistry 17: 2450-2455.
    • (1978) Biochemistry , vol.17 , pp. 2450-2455
    • Chu, L.Y.1    Rhoads, R.E.2
  • 60
    • 0019319074 scopus 로고
    • Inhibition of cell-free messenger ribonucleic acid translation by 7-methylguanosine 5′-triphosphate: effect of messenger ribonucleic acid concentration
    • Chu LY, Rhoads RE, (1980) Inhibition of cell-free messenger ribonucleic acid translation by 7-methylguanosine 5′-triphosphate: effect of messenger ribonucleic acid concentration. Biochemistry 19: 184-191.
    • (1980) Biochemistry , vol.19 , pp. 184-191
    • Chu, L.Y.1    Rhoads, R.E.2
  • 61
    • 0034327417 scopus 로고    scopus 로고
    • Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end
    • Borman AM, Michel YM, Kean KM, (2000) Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end. Nucleic Acids Res 28: 4068-4075.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4068-4075
    • Borman, A.M.1    Michel, Y.M.2    Kean, K.M.3
  • 62
    • 34547944309 scopus 로고    scopus 로고
    • MicroRNA inhibition of translation initiation in vitro by targeting the cap-binding complex eIF4F
    • Mathonnet G, Fabian MR, Svitkin YV, Parsyan A, Huck L, et al. (2007) MicroRNA inhibition of translation initiation in vitro by targeting the cap-binding complex eIF4F. Science 317: 1764-1767.
    • (2007) Science , vol.317 , pp. 1764-1767
    • Mathonnet, G.1    Fabian, M.R.2    Svitkin, Y.V.3    Parsyan, A.4    Huck, L.5
  • 63
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast
    • Preiss T, Hentze MW, (1998) Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature 392: 516-520.
    • (1998) Nature , vol.392 , pp. 516-520
    • Preiss, T.1    Hentze, M.W.2
  • 64
    • 27944483724 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation
    • Svitkin YV, Herdy B, Costa-Mattioli M, Gingras AC, Raught B, et al. (2005) Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation. Mol Cell Biol 25: 10556-10565.
    • (2005) Mol Cell Biol , vol.25 , pp. 10556-10565
    • Svitkin, Y.V.1    Herdy, B.2    Costa-Mattioli, M.3    Gingras, A.C.4    Raught, B.5
  • 65
    • 79960273121 scopus 로고    scopus 로고
    • Activation of a microRNA response in trans reveals a new role for poly(A) in translational repression
    • Ricci EP, Limousin T, Soto-Rifo R, Allison R, Poyry T, et al. (2011) Activation of a microRNA response in trans reveals a new role for poly(A) in translational repression. Nucleic Acids Res 39: 5215-5231.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5215-5231
    • Ricci, E.P.1    Limousin, T.2    Soto-Rifo, R.3    Allison, R.4    Poyry, T.5
  • 66
    • 33646353201 scopus 로고    scopus 로고
    • Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A
    • Bordeleau ME, Mori A, Oberer M, Lindqvist L, Chard LS, et al. (2006) Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. Nat Chem Biol 2: 213-220.
    • (2006) Nat Chem Biol , vol.2 , pp. 213-220
    • Bordeleau, M.E.1    Mori, A.2    Oberer, M.3    Lindqvist, L.4    Chard, L.S.5
  • 67
    • 77953629046 scopus 로고    scopus 로고
    • Regulation of mRNA translation and stability by microRNAs
    • Fabian MR, Sonenberg N, Filipowicz W, (2010) Regulation of mRNA translation and stability by microRNAs. Annu Rev Biochem 79: 351-379.
    • (2010) Annu Rev Biochem , vol.79 , pp. 351-379
    • Fabian, M.R.1    Sonenberg, N.2    Filipowicz, W.3
  • 68
    • 71949121493 scopus 로고    scopus 로고
    • The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release
    • Zekri L, Huntzinger E, Heimstadt S, Izaurralde E, (2009) The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release. Mol Cell Biol 29: 6220-6231.
    • (2009) Mol Cell Biol , vol.29 , pp. 6220-6231
    • Zekri, L.1    Huntzinger, E.2    Heimstadt, S.3    Izaurralde, E.4
  • 69
    • 24644480213 scopus 로고    scopus 로고
    • Inhibition of translational initiation by Let-7 MicroRNA in human cells
    • Pillai RS, Bhattacharyya SN, Artus CG, Zoller T, Cougot N, et al. (2005) Inhibition of translational initiation by Let-7 MicroRNA in human cells. Science 309: 1573-1576.
    • (2005) Science , vol.309 , pp. 1573-1576
    • Pillai, R.S.1    Bhattacharyya, S.N.2    Artus, C.G.3    Zoller, T.4    Cougot, N.5
  • 70
    • 78751477191 scopus 로고    scopus 로고
    • Gene silencing by microRNAs: contributions of translational repression and mRNA decay
    • Huntzinger E, Izaurralde E, (2011) Gene silencing by microRNAs: contributions of translational repression and mRNA decay. Nat Rev Genet 12: 99-110.
    • (2011) Nat Rev Genet , vol.12 , pp. 99-110
    • Huntzinger, E.1    Izaurralde, E.2
  • 71
    • 0021920897 scopus 로고
    • Reconstitution of functional mRNA-protein complexes in a rabbit reticulocyte cell-free translation system
    • Greenberg JR, Carroll E, (1985) Reconstitution of functional mRNA-protein complexes in a rabbit reticulocyte cell-free translation system. Mol Cell Biol 5: 342-351.
    • (1985) Mol Cell Biol , vol.5 , pp. 342-351
    • Greenberg, J.R.1    Carroll, E.2
  • 72
    • 0019415355 scopus 로고
    • Proteins associated with poly(A) and other regions of mRNA and hnRNA molecules as investigated by crosslinking
    • Setyono B, Greenberg JR, (1981) Proteins associated with poly(A) and other regions of mRNA and hnRNA molecules as investigated by crosslinking. Cell 24: 775-783.
    • (1981) Cell , vol.24 , pp. 775-783
    • Setyono, B.1    Greenberg, J.R.2
  • 73
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G, Kim VN, Kataoka N, (2002) Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 3: 195-205.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 74
    • 61849143823 scopus 로고    scopus 로고
    • Human hnRNP Q re-localizes to cytoplasmic granules upon PMA, thapsigargin, arsenite and heat-shock treatments
    • Quaresma AJ, Bressan GC, Gava LM, Lanza DC, Ramos CH, et al. (2009) Human hnRNP Q re-localizes to cytoplasmic granules upon PMA, thapsigargin, arsenite and heat-shock treatments. Exp Cell Res 315: 968-980.
    • (2009) Exp Cell Res , vol.315 , pp. 968-980
    • Quaresma, A.J.1    Bressan, G.C.2    Gava, L.M.3    Lanza, D.C.4    Ramos, C.H.5
  • 75
    • 67651095905 scopus 로고    scopus 로고
    • Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity
    • Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, et al. (2009) Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity. Mol Cell 35: 164-180.
    • (2009) Mol Cell , vol.35 , pp. 164-180
    • Arif, A.1    Jia, J.2    Mukhopadhyay, R.3    Willard, B.4    Kinter, M.5
  • 77
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U, (2007) P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 78
    • 22344455246 scopus 로고    scopus 로고
    • Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
    • Kedersha N, Stoecklin G, Ayodele M, Yacono P, Lykke-Andersen J, et al. (2005) Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol 169: 871-884.
    • (2005) J Cell Biol , vol.169 , pp. 871-884
    • Kedersha, N.1    Stoecklin, G.2    Ayodele, M.3    Yacono, P.4    Lykke-Andersen, J.5
  • 79
    • 11144229414 scopus 로고    scopus 로고
    • An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites
    • Bannai H, Fukatsu K, Mizutani A, Natsume T, Iemura S, et al. (2004) An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites. J Biol Chem 279: 53427-53434.
    • (2004) J Biol Chem , vol.279 , pp. 53427-53434
    • Bannai, H.1    Fukatsu, K.2    Mizutani, A.3    Natsume, T.4    Iemura, S.5
  • 80
    • 58149092016 scopus 로고    scopus 로고
    • Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs
    • Weidensdorfer D, Stohr N, Baude A, Lederer M, Kohn M, et al. (2009) Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs. RNA 15: 104-115.
    • (2009) RNA , vol.15 , pp. 104-115
    • Weidensdorfer, D.1    Stohr, N.2    Baude, A.3    Lederer, M.4    Kohn, M.5
  • 81
    • 38449123748 scopus 로고    scopus 로고
    • Assembly and analysis of eukaryotic translation initiation complexes
    • Pisarev AV, Unbehaun A, Hellen CU, Pestova TV, (2007) Assembly and analysis of eukaryotic translation initiation complexes. Methods Enzymol 430: 147-177.
    • (2007) Methods Enzymol , vol.430 , pp. 147-177
    • Pisarev, A.V.1    Unbehaun, A.2    Hellen, C.U.3    Pestova, T.V.4
  • 82
    • 0035674431 scopus 로고    scopus 로고
    • Poly(A)-binding protein interaction with eIF4G stimulates picornavirus IRES-dependent translation
    • Svitkin YV, Imataka H, Khaleghpour K, Kahvejian A, Liebig HD, et al. (2001) Poly(A)-binding protein interaction with eIF4G stimulates picornavirus IRES-dependent translation. RNA 7: 1743-1752.
    • (2001) RNA , vol.7 , pp. 1743-1752
    • Svitkin, Y.V.1    Imataka, H.2    Khaleghpour, K.3    Kahvejian, A.4    Liebig, H.D.5
  • 83
    • 36248948743 scopus 로고    scopus 로고
    • A highly efficient and robust in vitro translation system for expression of picornavirus and hepatitis C virus RNA genomes
    • Svitkin YV, Sonenberg N, (2007) A highly efficient and robust in vitro translation system for expression of picornavirus and hepatitis C virus RNA genomes. Methods Enzymol 429: 53-82.
    • (2007) Methods Enzymol , vol.429 , pp. 53-82
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 84
    • 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
    • Morino S, Imataka H, Svitkin YV, Pestova TV, Sonenberg N, (2000) 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 20: 468-477.
    • (2000) Mol Cell Biol , vol.20 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 85
    • 0021112566 scopus 로고
    • Involvement of eukaryotic initiation factor 4A in the cap recognition process
    • Edery I, Humbelin M, Darveau A, Lee KA, Milburn S, et al. (1983) Involvement of eukaryotic initiation factor 4A in the cap recognition process. J Biol Chem 258: 11398-11403.
    • (1983) J Biol Chem , vol.258 , pp. 11398-11403
    • Edery, I.1    Humbelin, M.2    Darveau, A.3    Lee, K.A.4    Milburn, S.5
  • 86
    • 77749323441 scopus 로고    scopus 로고
    • Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B
    • Shahbazian D, Parsyan A, Petroulakis E, Topisirovic I, Martineau Y, et al. (2010) Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B. Mol Cell Biol 30: 1478-1485.
    • (2010) Mol Cell Biol , vol.30 , pp. 1478-1485
    • Shahbazian, D.1    Parsyan, A.2    Petroulakis, E.3    Topisirovic, I.4    Martineau, Y.5
  • 87
    • 0019876737 scopus 로고
    • ATP/Mg++-dependent cross-linking of cap binding proteins to the 5′ end of eukaryotic mRNA
    • Sonenberg N, (1981) ATP/Mg++-dependent cross-linking of cap binding proteins to the 5′ end of eukaryotic mRNA. Nucleic Acids Res 9: 1643-1656.
    • (1981) Nucleic Acids Res , vol.9 , pp. 1643-1656
    • Sonenberg, N.1
  • 88
    • 0021111551 scopus 로고
    • mRNA secondary structure as a determinant in cap recognition and initiation complex formation. ATP-Mg2+ independent cross-linking of cap binding proteins to m7I-capped inosine-substituted reovirus mRNA
    • Lee KA, Guertin D, Sonenberg N, (1983) mRNA secondary structure as a determinant in cap recognition and initiation complex formation. ATP-Mg2+ independent cross-linking of cap binding proteins to m7I-capped inosine-substituted reovirus mRNA. J Biol Chem 258: 707-710.
    • (1983) J Biol Chem , vol.258 , pp. 707-710
    • Lee, K.A.1    Guertin, D.2    Sonenberg, N.3
  • 89
    • 0030920579 scopus 로고    scopus 로고
    • Assays for eukaryotic translation factors that bind mRNA
    • Merrick WC, Sonenberg N, (1997) Assays for eukaryotic translation factors that bind mRNA. Methods 11: 333-342.
    • (1997) Methods , vol.11 , pp. 333-342
    • Merrick, W.C.1    Sonenberg, N.2
  • 90
    • 33744973775 scopus 로고    scopus 로고
    • Relief of microRNA-mediated translational repression in human cells subjected to stress
    • Bhattacharyya SN, Habermacher R, Martine U, Closs EI, Filipowicz W, (2006) Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125: 1111-1124.
    • (2006) Cell , vol.125 , pp. 1111-1124
    • Bhattacharyya, S.N.1    Habermacher, R.2    Martine, U.3    Closs, E.I.4    Filipowicz, W.5


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