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Volumn 41, Issue 1, 2013, Pages 586-598

MiRNA repression of translation in vitro takes place during 43S ribosomal scanning

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4G; MICRORNA; POLYADENYLIC ACID BINDING PROTEIN; VIRUS PROTEIN;

EID: 84871781809     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1076     Document Type: Article
Times cited : (49)

References (65)
  • 1
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • Bartel, D.P. (2009) MicroRNAs: target recognition and regulatory functions. Cell, 136, 215-233.
    • (2009) Cell , vol.136 , pp. 215-233
    • Bartel, D.P.1
  • 2
    • 60149095444 scopus 로고    scopus 로고
    • Most mammalian mRNAs are conserved targets of microRNAs
    • Friedman, R.C., Farh, K.K.-H., Burge, C.B. and Bartel, D.P. (2009) Most mammalian mRNAs are conserved targets of microRNAs. Genome Res., 19, 92-105.
    • (2009) Genome Res. , vol.19 , pp. 92-105
    • Friedman, R.C.1    Farh, K.K.-H.2    Burge, C.B.3    Bartel, D.P.4
  • 3
    • 84862778053 scopus 로고    scopus 로고
    • Ribosome profiling shows that miR-430 reduces translation before causing mRNA decay in zebrafish
    • Bazzini, A.A., Lee, M.T. and Giraldez, A.J. (2012) Ribosome profiling shows that miR-430 reduces translation before causing mRNA decay in zebrafish. Science, 336, 233-237.
    • (2012) Science , vol.336 , pp. 233-237
    • Bazzini, A.A.1    Lee, M.T.2    Giraldez, A.J.3
  • 4
    • 84864872623 scopus 로고    scopus 로고
    • Kinetic analysis reveals successive steps leading to miRNA-mediated silencing in mammalian cells
    • Bethune, J., Artus-Revel, C.G. and Filipowicz, W. (2012) Kinetic analysis reveals successive steps leading to miRNA-mediated silencing in mammalian cells. EMBO Rep., 13, 716-723.
    • (2012) EMBO Rep. , vol.13 , pp. 716-723
    • Bethune, J.1    Artus-Revel, C.G.2    Filipowicz, W.3
  • 5
    • 84859632747 scopus 로고    scopus 로고
    • MiRNA-mediated gene silencing by translational repression followed by mRNA deadenylation and decay
    • Djuranovic, S., Nahvi, A. and Green, R. (2012) miRNA-mediated gene silencing by translational repression followed by mRNA deadenylation and decay. Science, 336, 237-240.
    • (2012) Science , vol.336 , pp. 237-240
    • Djuranovic, S.1    Nahvi, A.2    Green, R.3
  • 9
    • 33845353746 scopus 로고    scopus 로고
    • Evidence that microRNAs are associated with translating messenger RNAs in human cells
    • Maroney, P.A., Yu, Y., Fisher, J. and Nilsen, T.W. (2006) Evidence that microRNAs are associated with translating messenger RNAs in human cells. Nat. Struct. Mol. Biol., 13, 1102-1107.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1102-1107
    • Maroney, P.A.1    Yu, Y.2    Fisher, J.3    Nilsen, T.W.4
  • 10
    • 1242296375 scopus 로고    scopus 로고
    • MiRNP: MRNA association in polyribosomes in a human neuronal cell line
    • Nelson, P.T., Hatzigeorgiou, A.G. and Mourelatos, Z. (2004) miRNP: mRNA association in polyribosomes in a human neuronal cell line. RNA, 10, 387-394.
    • (2004) RNA , vol.10 , pp. 387-394
    • Nelson, P.T.1    Hatzigeorgiou, A.G.2    Mourelatos, Z.3
  • 11
    • 33845354027 scopus 로고    scopus 로고
    • Human let-7a miRNA blocks protein production on actively translating polyribosomes
    • Nottrott, S., Simard, M.J. and Richter, J.D. (2006) Human let-7a miRNA blocks protein production on actively translating polyribosomes. Nat Struct. Mol. Biol., 13, 1108-1114.
    • (2006) Nat Struct. Mol. Biol. , vol.13 , pp. 1108-1114
    • Nottrott, S.1    Simard, M.J.2    Richter, J.D.3
  • 12
    • 32444436121 scopus 로고    scopus 로고
    • Short RNAs repress translation after initiation in mammalian cells
    • Petersen, C.P., Bordeleau, M.-E., Pelletier, J. and Sharp, P.A. (2006) Short RNAs repress translation after initiation in mammalian cells. Mol. Cell, 21, 533-542.
    • (2006) Mol. Cell , vol.21 , pp. 533-542
    • Petersen, C.P.1    Bordeleau, M.-E.2    Pelletier, J.3    Sharp, P.A.4
  • 14
    • 28044457883 scopus 로고    scopus 로고
    • MicroRNAs control translation initiation by inhibiting eukaryotic initiation factor 4E/cap and poly(A) tail function
    • Humphreys, D.T., Westman, B.J., Martin, D.I. and Preiss, T. (2005) MicroRNAs control translation initiation by inhibiting eukaryotic initiation factor 4E/cap and poly(A) tail function. Proc. Natl Acad. Sci. USA, 102, 16961-16966.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16961-16966
    • Humphreys, D.T.1    Westman, B.J.2    Martin, D.I.3    Preiss, T.4
  • 15
    • 63649105975 scopus 로고    scopus 로고
    • Drosophila argonaute1 and argonaute2 employ distinct mechanisms for translational repression
    • Iwasaki, S., Kawamata, T. and Tomari, Y. (2009) Drosophila argonaute1 and argonaute2 employ distinct mechanisms for translational repression. Mol. Cell, 34, 58-67.
    • (2009) Mol. Cell , vol.34 , pp. 58-67
    • Iwasaki, S.1    Kawamata, T.2    Tomari, Y.3
  • 18
    • 34249282243 scopus 로고    scopus 로고
    • Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation
    • Thermann, R. and Hentze, M.W. (2007) Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation. Nature, 447, 875-878.
    • (2007) Nature , vol.447 , pp. 875-878
    • Thermann, R.1    Hentze, M.W.2
  • 19
    • 33646522366 scopus 로고    scopus 로고
    • Recapitulation of short RNA-directed translational gene silencing in vitro
    • Wang, B., Love, T.M., Call, M.E., Doench, J.G. and Novina, C.D. (2006) Recapitulation of short RNA-directed translational gene silencing in vitro. Mol. Cell, 22, 553-560.
    • (2006) Mol. Cell , vol.22 , pp. 553-560
    • Wang, B.1    Love, T.M.2    Call, M.E.3    Doench, J.G.4    Novina, C.D.5
  • 20
    • 44449164346 scopus 로고    scopus 로고
    • MicroRNA-repressed mRNAs contain 40S but not 60S components
    • Wang, B., Yanez, A. and Novina, C.D. (2008) MicroRNA-repressed mRNAs contain 40S but not 60S components. Proc. Natl Acad. Sci. USA, 105, 5343-5348.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5343-5348
    • Wang, B.1    Yanez, A.2    Novina, C.D.3
  • 21
    • 75649096055 scopus 로고    scopus 로고
    • Poly(A)-binding protein modulates mRNA susceptibility to cap-dependent miRNA-mediated repression
    • Walters, R.W., Bradrick, S.S. and Gromeier, M. (2010) Poly(A)-binding protein modulates mRNA susceptibility to cap-dependent miRNA-mediated repression. RNA, 16, 239-250.
    • (2010) RNA , vol.16 , pp. 239-250
    • Walters, R.W.1    Bradrick, S.S.2    Gromeier, M.3
  • 24
    • 33645119514 scopus 로고    scopus 로고
    • MicroRNAs direct rapid deadenylation of mRNA
    • Wu, L., Fan, J. and Belasco, J.G. (2006) MicroRNAs direct rapid deadenylation of mRNA. Proc. Natl Acad. Sci. USA, 103, 4034-4039.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4034-4039
    • Wu, L.1    Fan, J.2    Belasco, J.G.3
  • 25
    • 80053580757 scopus 로고    scopus 로고
    • GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets
    • Braun, J.E., Huntzinger, E., Fauser, M. and Izaurralde, E. (2011) GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets. Mol. Cell, 44, 120-133.
    • (2011) Mol. Cell , vol.44 , pp. 120-133
    • Braun, J.E.1    Huntzinger, E.2    Fauser, M.3    Izaurralde, E.4
  • 26
    • 78650258635 scopus 로고    scopus 로고
    • Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing
    • Huntzinger, E., Braun, J.E., Heimstadt, S., Zekri, L. and Izaurralde, E. (2010) Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing. EMBO J., 29, 4146-4160.
    • (2010) EMBO J. , vol.29 , pp. 4146-4160
    • Huntzinger, E.1    Braun, J.E.2    Heimstadt, S.3    Zekri, L.4    Izaurralde, E.5
  • 27
    • 76349104822 scopus 로고    scopus 로고
    • Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation
    • Jinek, M., Fabian, M.R., Coyle, S.M., Sonenberg, N. and Doudna, J.A. (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
  • 28
    • 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. and 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
  • 30
    • 84856375470 scopus 로고    scopus 로고
    • Translational inhibition by deadenylation-independent mechanisms is central to microRNA-mediated silencing in zebrafish
    • Mishima, Y., Fukao, A., Kishimoto, T., Sakamoto, H., Fujiwara, T. and Inoue, K. (2012) Translational inhibition by deadenylation-independent mechanisms is central to microRNA-mediated silencing in zebrafish. Proc. Natl Acad. Sci. USA, 109, 1104-1109.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 1104-1109
    • Mishima, Y.1    Fukao, A.2    Kishimoto, T.3    Sakamoto, H.4    Fujiwara, T.5    Inoue, K.6
  • 31
    • 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. and Hentze, M.W. (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
  • 32
    • 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
    • Soto Rifo, R., Ricci, E.P., Decimo, D., Moncorge, O. and 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
    • Soto Rifo, R.1    Ricci, E.P.2    Decimo, D.3    Moncorge, O.4    Ohlmann, T.5
  • 33
    • 0033053004 scopus 로고    scopus 로고
    • The properties of chimeric picornavirus IRESes show that discrimination between internal translation initiation sites is influenced by the identity of the IRES and not just the context of the AUG codon
    • Ohlmann, T. and Jackson, R.J. (1999) The properties of chimeric picornavirus IRESes show that discrimination between internal translation initiation sites is influenced by the identity of the IRES and not just the context of the AUG codon. RNA, 5, 764-778.
    • (1999) RNA , vol.5 , pp. 764-778
    • Ohlmann, T.1    Jackson, R.J.2
  • 34
    • 0036241453 scopus 로고    scopus 로고
    • Pestivirus internal ribosome entry site (IRES) structure and function: Elements in the 5′ untranslated region important for IRES function
    • Fletcher, S.P. and Jackson, R.J. (2002) Pestivirus internal ribosome entry site (IRES) structure and function: elements in the 5′ untranslated region important for IRES function. J. Virol., 76, 5024-5033.
    • (2002) J. Virol. , vol.76 , pp. 5024-5033
    • Fletcher, S.P.1    Jackson, R.J.2
  • 35
    • 38849184624 scopus 로고    scopus 로고
    • The picornavirus avian encephalomyelitis virus possesses a hepatitis C virus-like internal ribosome entry site element
    • Bakhshesh, M., Groppelli, E., Willcocks, M.M., Royall, E., Belsham, G.J. and Roberts, L.O. (2008) The picornavirus avian encephalomyelitis virus possesses a hepatitis C virus-like internal ribosome entry site element. J. Virol., 82, 1993-2003.
    • (2008) J. Virol. , vol.82 , pp. 1993-2003
    • Bakhshesh, M.1    Groppelli, E.2    Willcocks, M.M.3    Royall, E.4    Belsham, G.J.5    Roberts, L.O.6
  • 37
    • 83555161676 scopus 로고    scopus 로고
    • PABP is not essential for microRNA-mediated translational repression and deadenylation in vitro
    • Fukaya, T. and Tomari, Y. (2011) PABP is not essential for microRNA-mediated translational repression and deadenylation in vitro. EMBO J., 30, 4998-5009.
    • (2011) EMBO J. , vol.30 , pp. 4998-5009
    • Fukaya, T.1    Tomari, Y.2
  • 38
    • 41649115420 scopus 로고    scopus 로고
    • GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay
    • Eulalio, A., Huntzinger, E. and Izaurralde, E. (2008) GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay. Nat. Struct. Mol. Biol., 15, 346-353.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 346-353
    • Eulalio, A.1    Huntzinger, E.2    Izaurralde, E.3
  • 40
    • 47649133501 scopus 로고    scopus 로고
    • Nondestructive analysis of senescence in mesophyll cells by spectral resolution of protein synthesis-dependent pigment metabolism
    • Gay, A., Thomas, H., Roca, M., James, C., Taylor, J., Rowland, J. and Ougham, H. (2008) Nondestructive analysis of senescence in mesophyll cells by spectral resolution of protein synthesis-dependent pigment metabolism. New Phytol., 179, 663-674.
    • (2008) New Phytol. , vol.179 , pp. 663-674
    • Gay, A.1    Thomas, H.2    Roca, M.3    James, C.4    Taylor, J.5    Rowland, J.6    Ougham, H.7
  • 41
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R.J., Hellen, C.U. and Pestova, T.V. (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
  • 42
    • 0021828136 scopus 로고
    • Protein synthesis in rabbit reticulocytes. Purification and properties of an Mr 80, 000 polypeptide (Co-eIF-2A80) with Co-eIF-2A activity
    • Chakravarty, I., Bagchi, M.K., Roy, R., Banerjee, A.C. and Gupta, N.K. (1985) Protein synthesis in rabbit reticulocytes. Purification and properties of an Mr 80, 000 polypeptide (Co-eIF-2A80) with Co-eIF-2A activity. J. Biol. Chem., 260, 6945-6949.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6945-6949
    • Chakravarty, I.1    Bagchi, M.K.2    Roy, R.3    Banerjee, A.C.4    Gupta, N.K.5
  • 44
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation
    • Pause, A., Methot, N., Svitkin, Y., Merrick, W.C. and Sonenberg, N. (1994) Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation. EMBO J., 13, 1205-1215.
    • (1994) EMBO J. , vol.13 , pp. 1205-1215
    • Pause, A.1    Methot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 46
    • 0035968267 scopus 로고    scopus 로고
    • Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase-and viral protease-mediated cleavages
    • Bushell, M., Wood, W., Carpenter, G., Pain, V.M., Morley, S.J. and Clemens, M.J. (2001) Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase-and viral protease-mediated cleavages. J. Biol. Chem., 276, 23922-23928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23922-23928
    • Bushell, M.1    Wood, W.2    Carpenter, G.3    Pain, V.M.4    Morley, S.J.5    Clemens, M.J.6
  • 47
    • 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. and 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
  • 48
    • 0036308653 scopus 로고    scopus 로고
    • In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system
    • Ohlmann, T., Prevot, D., Decimo, D., Roux, F., Garin, J., Morley, S.J. and Darlix, J.L. (2002) In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system. J. Mol. Biol., 318, 9-20.
    • (2002) J. Mol. Biol. , vol.318 , pp. 9-20
    • Ohlmann, T.1    Prevot, D.2    Decimo, D.3    Roux, F.4    Garin, J.5    Morley, S.J.6    Darlix, J.L.7
  • 49
    • 0345373936 scopus 로고    scopus 로고
    • Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning
    • Prevot, D., Decimo, D., Herbreteau, C.H., Roux, F., Garin, J., Darlix, J.L. and Ohlmann, T. (2003) Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning. EMBO J., 22, 1909-1921.
    • (2003) EMBO J. , vol.22 , pp. 1909-1921
    • Prevot, D.1    Decimo, D.2    Herbreteau, C.H.3    Roux, F.4    Garin, J.5    Darlix, J.L.6    Ohlmann, T.7
  • 51
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • first page of table of contents
    • Hinnebusch, A.G. (2011) Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol. Mol. Biol. Rev., 75, 434-467, first page of table of contents.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 52
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 5′UTRs requires DExH-box protein DHX29
    • Pisareva, V.P., Pisarev, A.V., Komar, A.A., Hellen, C.U. and Pestova, T.V. (2008) Translation initiation on mammalian mRNAs with structured 5′UTRs 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
  • 53
    • 84866361659 scopus 로고    scopus 로고
    • DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs
    • Soto-Rifo, R., Rubilar, P.S., Limousin, T., de Breyne, S., Decimo, D. and Ohlmann, T. (2012) DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs. EMBO J., 31, 3745-3756.
    • (2012) EMBO J. , vol.31 , pp. 3745-3756
    • Soto-Rifo, R.1    Rubilar, P.S.2    Limousin, T.3    De Breyne, S.4    Decimo, D.5    Ohlmann, T.6
  • 54
    • 28844476749 scopus 로고    scopus 로고
    • Alternative mechanisms of initiating translation of mammalian mRNAs
    • Jackson, R.J. (2005) Alternative mechanisms of initiating translation of mammalian mRNAs. Biochem. Soc. Trans., 33, 1231-1241.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1231-1241
    • Jackson, R.J.1
  • 55
    • 0029008576 scopus 로고
    • Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin
    • Ziegler, E., Borman, A.M., Kirchweger, R., Skern, T. and Kean, K.M. (1995) Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin. J. Virol., 69, 3465-3474.
    • (1995) J. Virol. , vol.69 , pp. 3465-3474
    • Ziegler, E.1    Borman, A.M.2    Kirchweger, R.3    Skern, T.4    Kean, K.M.5
  • 56
    • 0031905698 scopus 로고    scopus 로고
    • A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs
    • Pestova, T.V., Shatsky, I.N., Fletcher, S.P., Jackson, R.J. and Hellen, C.U. (1998) A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs. Genes Dev., 12, 67-83.
    • (1998) Genes Dev. , vol.12 , pp. 67-83
    • Pestova, T.V.1    Shatsky, I.N.2    Fletcher, S.P.3    Jackson, R.J.4    Hellen, C.U.5
  • 57
    • 34547623022 scopus 로고    scopus 로고
    • Let-7 microRNA-mediated mRNA deadenylation and translational repression in a mammalian cell-free system
    • Wakiyama, M., Takimoto, K., Ohara, O. and Yokoyama, S. (2007) Let-7 microRNA-mediated mRNA deadenylation and translational repression in a mammalian cell-free system. Genes Dev., 21, 1857-1862.
    • (2007) Genes Dev. , vol.21 , pp. 1857-1862
    • Wakiyama, M.1    Takimoto, K.2    Ohara, O.3    Yokoyama, S.4
  • 58
    • 34547441263 scopus 로고    scopus 로고
    • Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′UTR as in the 3′ UTR
    • Lytle, J.R., Yario, T.A. and Steitz, J.A. (2007) Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′UTR as in the 3′ UTR. Proc. Natl Acad. Sci. USA, 104, 9667-9672.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 9667-9672
    • Lytle, J.R.1    Yario, T.A.2    Steitz, J.A.3
  • 61
    • 0030949304 scopus 로고    scopus 로고
    • Translational controls impinging on the 5′-untranslated region and initiation factor proteins
    • Jackson, R.J. and Wickens, M. (1997) Translational controls impinging on the 5′-untranslated region and initiation factor proteins. Curr. Opin. Genet. Dev., 7, 233-241.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 233-241
    • Jackson, R.J.1    Wickens, M.2
  • 62
    • 0029437960 scopus 로고
    • Internal initiation of translation in eukaryotes: The picornavirus paradigm and beyond
    • Jackson, R.J. and Kaminski, A. (1995) Internal initiation of translation in eukaryotes: the picornavirus paradigm and beyond. RNA, 1, 985-1000.
    • (1995) RNA , vol.1 , pp. 985-1000
    • Jackson, R.J.1    Kaminski, A.2
  • 63
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig, A.W., Haghighat, A., Yu, A.T. and 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
  • 65
    • 77951596454 scopus 로고    scopus 로고
    • Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein
    • Kozlov, G., Safaee, N., Rosenauer, A. and Gehring, K. (2010) Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. J. Biol. Chem., 285, 13599-13606.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13599-13606
    • Kozlov, G.1    Safaee, N.2    Rosenauer, A.3    Gehring, K.4


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