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Volumn 23, Issue 10, 2013, Pages 504-510

Emerging roles for ribonucleoprotein modification and remodeling in controlling RNA fate

Author keywords

Post translational modification; Ribonucleotidyltransferase; RNA decay; RNA helicase; RNA modification; RNA tailing; RNP modification; Uridylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MESSENGER RNA; RIBONUCLEOPROTEIN; RNA HELICASE; UNTRANSLATED RNA;

EID: 84884418135     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2013.05.001     Document Type: Review
Times cited : (39)

References (90)
  • 1
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • Glisovic T., et al. RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett. 2008, 582:1977-1986.
    • (2008) FEBS Lett. , vol.582 , pp. 1977-1986
    • Glisovic, T.1
  • 2
    • 48949115091 scopus 로고    scopus 로고
    • RNA-binding proteins in human genetic disease
    • Lukong K.E., et al. RNA-binding proteins in human genetic disease. Trends Genet. 2008, 24:416-425.
    • (2008) Trends Genet. , vol.24 , pp. 416-425
    • Lukong, K.E.1
  • 3
    • 60149093432 scopus 로고    scopus 로고
    • RNA and disease
    • Cooper T., et al. RNA and disease. Cell 2009, 136:777-793.
    • (2009) Cell , vol.136 , pp. 777-793
    • Cooper, T.1
  • 4
    • 84876806808 scopus 로고    scopus 로고
    • RNA-binding proteins in Mendelian disease
    • Castello A., et al. RNA-binding proteins in Mendelian disease. Trends Genet. 2013, 29:318-327.
    • (2013) Trends Genet. , vol.29 , pp. 318-327
    • Castello, A.1
  • 5
    • 84856223380 scopus 로고    scopus 로고
    • MRNP quality control goes regulatory
    • Mühlemann O., Jensen T.H. mRNP quality control goes regulatory. Trends Genet. 2012, 28:70-77.
    • (2012) Trends Genet. , vol.28 , pp. 70-77
    • Mühlemann, O.1    Jensen, T.H.2
  • 6
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: the complex lives of eukaryotic mRNAs
    • Moore M.J. From birth to death: the complex lives of eukaryotic mRNAs. Science 2005, 309:1514-1518.
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 8
    • 84864393412 scopus 로고    scopus 로고
    • The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover
    • Brook M., Gray N.K. The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover. Biochem. Soc. Trans. 2012, 40:856-864.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 856-864
    • Brook, M.1    Gray, N.K.2
  • 9
    • 84860723984 scopus 로고    scopus 로고
    • From conformational chaos to robust regulation: the structure and function of the multi-enzyme RNA degradosome
    • Górna M.W., et al. From conformational chaos to robust regulation: the structure and function of the multi-enzyme RNA degradosome. Q. Rev. Biophys. 2012, 45:105-145.
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 105-145
    • Górna, M.W.1
  • 10
    • 84862501232 scopus 로고    scopus 로고
    • Nuclear noncoding RNA surveillance: is the end in sight?
    • Wolin S.L., et al. Nuclear noncoding RNA surveillance: is the end in sight?. Trends Genet. 2012, 28:306-313.
    • (2012) Trends Genet. , vol.28 , pp. 306-313
    • Wolin, S.L.1
  • 11
    • 80051730960 scopus 로고    scopus 로고
    • Interaction profiling identifies the human nuclear exosome targeting complex
    • Lubas M., et al. Interaction profiling identifies the human nuclear exosome targeting complex. Mol. Cell 2011, 43:624-637.
    • (2011) Mol. Cell , vol.43 , pp. 624-637
    • Lubas, M.1
  • 12
    • 22744459614 scopus 로고    scopus 로고
    • A new yeast poly(A) polymerase complex involved in RNA quality control
    • Vanácová S., et al. A new yeast poly(A) polymerase complex involved in RNA quality control. PLoS Biol. 2005, 3:e189.
    • (2005) PLoS Biol. , vol.3
    • Vanácová, S.1
  • 13
    • 20444368818 scopus 로고    scopus 로고
    • RNA degradation by the exosome is promoted by a nuclear polyadenylation complex
    • LaCava J., et al. RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 2005, 121:713-724.
    • (2005) Cell , vol.121 , pp. 713-724
    • LaCava, J.1
  • 14
    • 20444368036 scopus 로고    scopus 로고
    • Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase
    • Wyers F., et al. Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 2005, 121:725-737.
    • (2005) Cell , vol.121 , pp. 725-737
    • Wyers, F.1
  • 15
    • 34447300418 scopus 로고    scopus 로고
    • The exosome subunit Rrp44 plays a direct role in RNA substrate recognition
    • Schneider C., et al. The exosome subunit Rrp44 plays a direct role in RNA substrate recognition. Mol. Cell 2007, 27:324-331.
    • (2007) Mol. Cell , vol.27 , pp. 324-331
    • Schneider, C.1
  • 16
    • 77950509943 scopus 로고    scopus 로고
    • TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6
    • Callahan K.P., Butler J.S. TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6. J. Biol. Chem. 2010, 285:3540-3547.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3540-3547
    • Callahan, K.P.1    Butler, J.S.2
  • 17
    • 68249083958 scopus 로고    scopus 로고
    • Distinct roles of non-canonical poly(A) polymerases in RNA metabolism
    • San Paolo S., et al. Distinct roles of non-canonical poly(A) polymerases in RNA metabolism. PLoS Genet. 2009, 5:e1000555.
    • (2009) PLoS Genet. , vol.5
    • San Paolo, S.1
  • 18
    • 38049069276 scopus 로고    scopus 로고
    • Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p
    • Wang X., et al. Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p. RNA 2008, 14:107-116.
    • (2008) RNA , vol.14 , pp. 107-116
    • Wang, X.1
  • 19
    • 41949126822 scopus 로고    scopus 로고
    • Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome
    • Bernstein J., et al. Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome. J. Biol. Chem. 2008, 283:4930-4942.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4930-4942
    • Bernstein, J.1
  • 20
    • 77955453339 scopus 로고    scopus 로고
    • Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance
    • Weir J.R., et al. Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:12139-12144.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 12139-12144
    • Weir, J.R.1
  • 21
    • 84860806396 scopus 로고    scopus 로고
    • RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex
    • Jia H., Wang X. RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:7292-7297.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 7292-7297
    • Jia, H.1    Wang, X.2
  • 22
    • 79955587252 scopus 로고    scopus 로고
    • The nuclear RNA polymerase II surveillance system targets polymerase III transcripts
    • Wlotzka W., et al. The nuclear RNA polymerase II surveillance system targets polymerase III transcripts. EMBO J. 2011, 30:1790-1803.
    • (2011) EMBO J. , vol.30 , pp. 1790-1803
    • Wlotzka, W.1
  • 23
    • 84869082850 scopus 로고    scopus 로고
    • Transcriptome-wide analysis of exosome targets
    • Schneider C., et al. Transcriptome-wide analysis of exosome targets. Mol. Cell 2012, 48:422-433.
    • (2012) Mol. Cell , vol.48 , pp. 422-433
    • Schneider, C.1
  • 24
    • 84861911071 scopus 로고    scopus 로고
    • Translational control by changes in poly(A) tail length: recycling mRNAs
    • Weill L., et al. Translational control by changes in poly(A) tail length: recycling mRNAs. Nat. Struct. Mol. Biol. 2012, 19:577-585.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 577-585
    • Weill, L.1
  • 25
    • 84864388068 scopus 로고    scopus 로고
    • Cytoplasmic mRNA 3' tagging in eukaryotes: does it spell the end?
    • Morozov I.Y., Caddick M.X. Cytoplasmic mRNA 3' tagging in eukaryotes: does it spell the end?. Biochem. Soc. Trans. 2012, 40:810-814.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 810-814
    • Morozov, I.Y.1    Caddick, M.X.2
  • 26
    • 78650433004 scopus 로고    scopus 로고
    • Polyadenylation and beyond: emerging roles for noncanonical poly(A) polymerases
    • Schmidt M-J., Norbury C.J. Polyadenylation and beyond: emerging roles for noncanonical poly(A) polymerases. Wiley Interdiscip. Rev. RNA 2010, 1:142-151.
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 142-151
    • Schmidt, M.-J.1    Norbury, C.J.2
  • 27
    • 33845957402 scopus 로고    scopus 로고
    • Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts
    • Ibrahim F., et al. Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts. Science 2006, 314:1893.
    • (2006) Science , vol.314 , pp. 1893
    • Ibrahim, F.1
  • 28
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen B., Goodman H.M. Uridine addition after microRNA-directed cleavage. Science 2004, 306:997.
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 29
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'
    • Mullen T.E., Marzluff W.F. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev. 2008, 22:50-65.
    • (2008) Genes Dev. , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 30
    • 79251485649 scopus 로고    scopus 로고
    • Modifications of small RNAs and their associated proteins
    • Kim Y-K., et al. Modifications of small RNAs and their associated proteins. Cell 2010, 143:703-709.
    • (2010) Cell , vol.143 , pp. 703-709
    • Kim, Y.-K.1
  • 31
    • 84862803181 scopus 로고    scopus 로고
    • Regulation of small RNA stability: methylation and beyond
    • Ji L., Chen X. Regulation of small RNA stability: methylation and beyond. Cell Res. 2012, 22:624-636.
    • (2012) Cell Res. , vol.22 , pp. 624-636
    • Ji, L.1    Chen, X.2
  • 32
    • 81055122667 scopus 로고    scopus 로고
    • TRNAs marked with CCACCA are targeted for degradation
    • Wilusz J.E., et al. tRNAs marked with CCACCA are targeted for degradation. Science 2011, 334:817-821.
    • (2011) Science , vol.334 , pp. 817-821
    • Wilusz, J.E.1
  • 33
    • 66849122924 scopus 로고    scopus 로고
    • Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover
    • Rissland O.S., Norbury C.J. Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover. Nat. Struct. Mol. Biol. 2009, 16:616-623.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 616-623
    • Rissland, O.S.1    Norbury, C.J.2
  • 34
    • 73549112185 scopus 로고    scopus 로고
    • CUCU modification of mRNA promotes decapping and transcript degradation in Aspergillus nidulans
    • Morozov I.Y., et al. CUCU modification of mRNA promotes decapping and transcript degradation in Aspergillus nidulans. Mol. Cell. Biol. 2010, 30:460-469.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 460-469
    • Morozov, I.Y.1
  • 35
    • 84863994303 scopus 로고    scopus 로고
    • MRNA 3' tagging is induced by nonsense-mediated decay and promotes ribosome dissociation
    • Morozov I.Y., et al. mRNA 3' tagging is induced by nonsense-mediated decay and promotes ribosome dissociation. Mol. Cell. Biol. 2012, 32:2585-2595.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2585-2595
    • Morozov, I.Y.1
  • 36
    • 36248947229 scopus 로고    scopus 로고
    • 3' Terminal oligo U-tract-mediated stimulation of decapping
    • Song M-G., Kiledjian M. 3' Terminal oligo U-tract-mediated stimulation of decapping. RNA 2007, 13:2356-2365.
    • (2007) RNA , vol.13 , pp. 2356-2365
    • Song, M.-G.1    Kiledjian, M.2
  • 37
    • 34250804009 scopus 로고    scopus 로고
    • The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs
    • Chowdhury A., et al. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA 2007, 13:998-1016.
    • (2007) RNA , vol.13 , pp. 998-1016
    • Chowdhury, A.1
  • 38
    • 84872026333 scopus 로고    scopus 로고
    • Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay
    • Hoefig K.P., et al. Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay. Nat. Struct. Mol. Biol. 2013, 20:73-81.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 73-81
    • Hoefig, K.P.1
  • 39
    • 84880245419 scopus 로고    scopus 로고
    • The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway
    • Malecki M., et al. The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway. EMBO J. 2013, 32:1842-1854.
    • (2013) EMBO J. , vol.32 , pp. 1842-1854
    • Malecki, M.1
  • 40
    • 0034732089 scopus 로고    scopus 로고
    • Yeast Sm-like proteins function in mRNA decapping and decay
    • Tharun S., et al. Yeast Sm-like proteins function in mRNA decapping and decay. Nature 2000, 404:515-518.
    • (2000) Nature , vol.404 , pp. 515-518
    • Tharun, S.1
  • 41
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J., Parker R. General translational repression by activators of mRNA decapping. Cell 2005, 122:875-886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 42
    • 84877757514 scopus 로고    scopus 로고
    • A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7 pathway
    • Chang H-M., et al. A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7 pathway. Nature 2013, 497:244-248.
    • (2013) Nature , vol.497 , pp. 244-248
    • Chang, H.-M.1
  • 43
    • 84860307087 scopus 로고    scopus 로고
    • Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis
    • Ren G., et al. Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis. Curr. Biol. 2012, 22:695-700.
    • (2012) Curr. Biol. , vol.22 , pp. 695-700
    • Ren, G.1
  • 44
    • 84860301401 scopus 로고    scopus 로고
    • The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated small RNAs to trigger their degradation
    • Zhao Y., et al. The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated small RNAs to trigger their degradation. Curr. Biol. 2012, 22:689-694.
    • (2012) Curr. Biol. , vol.22 , pp. 689-694
    • Zhao, Y.1
  • 45
    • 61449186404 scopus 로고    scopus 로고
    • Selective stabilization of mammalian microRNAs by 3' adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2
    • Katoh T., et al. Selective stabilization of mammalian microRNAs by 3' adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2. Genes Dev. 2009, 23:433-438.
    • (2009) Genes Dev. , vol.23 , pp. 433-438
    • Katoh, T.1
  • 46
    • 79955599925 scopus 로고    scopus 로고
    • CPEB and two poly(A) polymerases control miR-122 stability and p53 mRNA translation
    • Burns D.M., et al. CPEB and two poly(A) polymerases control miR-122 stability and p53 mRNA translation. Nature 2011, 473:105-108.
    • (2011) Nature , vol.473 , pp. 105-108
    • Burns, D.M.1
  • 47
    • 84871690215 scopus 로고    scopus 로고
    • Specific miRNA stabilization by Gld2-catalyzed monoadenylation
    • D'Ambrogio A., et al. Specific miRNA stabilization by Gld2-catalyzed monoadenylation. Cell Rep. 2012, 2:1537-1545.
    • (2012) Cell Rep. , vol.2 , pp. 1537-1545
    • D'Ambrogio, A.1
  • 48
    • 78651335915 scopus 로고    scopus 로고
    • The RNA Modification Database, RNAMDB: 2011 update
    • Cantara W., et al. The RNA Modification Database, RNAMDB: 2011 update. Nucleic Acids Res. 2011, 39:D195-D201.
    • (2011) Nucleic Acids Res. , vol.39
    • Cantara, W.1
  • 49
    • 84875692043 scopus 로고    scopus 로고
    • MODOMICS: a database of RNA modification pathways--2013 update
    • Machnicka M., et al. MODOMICS: a database of RNA modification pathways--2013 update. Nucleic Acids Res. 2013, 41:D262-D267.
    • (2013) Nucleic Acids Res. , vol.41
    • Machnicka, M.1
  • 50
    • 77952293063 scopus 로고    scopus 로고
    • Functions and regulation of RNA editing by ADAR deaminases
    • Nishikura K. Functions and regulation of RNA editing by ADAR deaminases. Annu. Rev. Biochem. 2010, 79:321-349.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 321-349
    • Nishikura, K.1
  • 51
    • 84860751168 scopus 로고    scopus 로고
    • Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA
    • Squires J.E., et al. Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA. Nucleic Acids Res. 2012, 40:5023-5033.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5023-5033
    • Squires, J.E.1
  • 52
    • 84860779086 scopus 로고    scopus 로고
    • Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq
    • Dominissini D., et al. Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq. Nature 2012, 485:201-206.
    • (2012) Nature , vol.485 , pp. 201-206
    • Dominissini, D.1
  • 53
    • 84862649489 scopus 로고    scopus 로고
    • Comprehensive analysis of mRNA methylation reveals enrichment in 3' UTRs and near stop codons
    • Meyer K.D., et al. Comprehensive analysis of mRNA methylation reveals enrichment in 3' UTRs and near stop codons. Cell 2012, 149:1635-1646.
    • (2012) Cell , vol.149 , pp. 1635-1646
    • Meyer, K.D.1
  • 54
    • 84875530060 scopus 로고    scopus 로고
    • N6-methyl-adenosine modification in messenger and long non-coding RNA
    • Pan T. N6-methyl-adenosine modification in messenger and long non-coding RNA. Trends Biochem. Sci. 2013, 38:204-209.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 204-209
    • Pan, T.1
  • 55
    • 0021487958 scopus 로고
    • Mapping of N6-methyladenosine residues in bovine prolactin mRNA
    • Horowitz S., et al. Mapping of N6-methyladenosine residues in bovine prolactin mRNA. Proc. Natl. Acad. Sci. U.S.A. 1984, 81:5667-5671.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 5667-5671
    • Horowitz, S.1
  • 56
    • 84872274463 scopus 로고    scopus 로고
    • ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility
    • Zheng G., et al. ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility. Mol. Cell 2013, 49:18-29.
    • (2013) Mol. Cell , vol.49 , pp. 18-29
    • Zheng, G.1
  • 57
    • 81355146483 scopus 로고    scopus 로고
    • N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
    • Jia G., et al. N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO. Nat. Chem. Biol. 2011, 7:885-887.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 885-887
    • Jia, G.1
  • 58
    • 84859168499 scopus 로고    scopus 로고
    • 4 mRNA by methylating the 3'-untranslated region of p16
    • 4 mRNA by methylating the 3'-untranslated region of p16. Nat. Commun. 2012, 10.1038/ncomms1692.
    • (2012) Nat. Commun.
    • Zhang, X.1
  • 59
    • 35549008047 scopus 로고    scopus 로고
    • Identification of recognition residues for ligation-based detection and quantitation of pseudouridine and N6-methyladenosine
    • Dai Q., et al. Identification of recognition residues for ligation-based detection and quantitation of pseudouridine and N6-methyladenosine. Nucleic Acids Res. 2007, 35:6322-6329.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6322-6329
    • Dai, Q.1
  • 60
    • 84867850145 scopus 로고    scopus 로고
    • NMD: a multifaceted response to premature translational termination
    • Kervestin S., Jacobson A. NMD: a multifaceted response to premature translational termination. Nat. Rev. Mol. Cell Biol. 2012, 13:700-712.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 700-712
    • Kervestin, S.1    Jacobson, A.2
  • 61
    • 79958265483 scopus 로고    scopus 로고
    • SnapShot: nonsense-mediated mRNA decay
    • 324-324.e2
    • Durand S., Lykke-Andersen J. SnapShot: nonsense-mediated mRNA decay. Cell 2011, 145. 324-324.e2.
    • (2011) Cell , vol.145
    • Durand, S.1    Lykke-Andersen, J.2
  • 62
    • 84856858152 scopus 로고    scopus 로고
    • N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD
    • Okada-Katsuhata Y., et al. N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD. Nucleic Acids Res. 2012, 40:1251-1266.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1251-1266
    • Okada-Katsuhata, Y.1
  • 63
    • 58149291462 scopus 로고    scopus 로고
    • Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex
    • Cho H., et al. Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex. Mol. Cell 2009, 33:75-86.
    • (2009) Mol. Cell , vol.33 , pp. 75-86
    • Cho, H.1
  • 64
    • 41949113083 scopus 로고    scopus 로고
    • Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay
    • Isken O., et al. Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay. Cell 2008, 133:314-327.
    • (2008) Cell , vol.133 , pp. 314-327
    • Isken, O.1
  • 65
    • 84860320152 scopus 로고    scopus 로고
    • The regulation of mRNA stability in mammalian cells: 2.0
    • Wu X., Brewer G. The regulation of mRNA stability in mammalian cells: 2.0. Gene 2012, 500:10-21.
    • (2012) Gene , vol.500 , pp. 10-21
    • Wu, X.1    Brewer, G.2
  • 66
    • 84867599479 scopus 로고    scopus 로고
    • Perspectives on the ARE as it turns 25 years old
    • Beisang D., Bohjanen P.R. Perspectives on the ARE as it turns 25 years old. Wiley Interdiscip. Rev. RNA 2012, 3:719-731.
    • (2012) Wiley Interdiscip. Rev. RNA , vol.3 , pp. 719-731
    • Beisang, D.1    Bohjanen, P.R.2
  • 67
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment
    • Clement S.L., et al. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol. Cell. Biol. 2011, 31:256-266.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 256-266
    • Clement, S.L.1
  • 68
    • 77956261147 scopus 로고    scopus 로고
    • MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment
    • Marchese F.P., et al. MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment. J. Biol. Chem. 2010, 285:27590-27600.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27590-27600
    • Marchese, F.P.1
  • 69
    • 84856198547 scopus 로고    scopus 로고
    • Regulation of an RNA granule during spermatogenesis: acetylation of MVH in the chromatoid body of germ cells
    • Nagamori I., et al. Regulation of an RNA granule during spermatogenesis: acetylation of MVH in the chromatoid body of germ cells. J. Cell Sci. 2011, 124:4346-4355.
    • (2011) J. Cell Sci. , vol.124 , pp. 4346-4355
    • Nagamori, I.1
  • 70
    • 77956382385 scopus 로고    scopus 로고
    • Sirtuin 1 regulation of developmental genes during differentiation of stem cells
    • Calvanese V. Sirtuin 1 regulation of developmental genes during differentiation of stem cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:13736-13741.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13736-13741
    • Calvanese, V.1
  • 71
    • 33644769540 scopus 로고    scopus 로고
    • CARM1 regulates proliferation of PC12 cells by methylating HuD CARM1 regulates proliferation of PC12 cells by methylating HuD
    • Fujiwara T., et al. CARM1 regulates proliferation of PC12 cells by methylating HuD CARM1 regulates proliferation of PC12 cells by methylating HuD. Mol. Cell. Biol. 2006, 26:2273-2285.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2273-2285
    • Fujiwara, T.1
  • 72
    • 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., et al. 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. 2012, 441:803-812.
    • (2012) Biochem. J. , vol.441 , pp. 803-812
    • Brook, M.1
  • 73
    • 84864379832 scopus 로고    scopus 로고
    • RGG motif proteins: modulators of mRNA functional states
    • Rajyaguru P., Parker R. RGG motif proteins: modulators of mRNA functional states. Cell Cycle 2012, 11:2594-2599.
    • (2012) Cell Cycle , vol.11 , pp. 2594-2599
    • Rajyaguru, P.1    Parker, R.2
  • 74
    • 84856270385 scopus 로고    scopus 로고
    • Scd6 targets eIF4G to repress translation: RGG motif proteins as a class of eIF4G-binding proteins
    • Rajyaguru P., et al. Scd6 targets eIF4G to repress translation: RGG motif proteins as a class of eIF4G-binding proteins. Mol. Cell 2012, 45:244-254.
    • (2012) Mol. Cell , vol.45 , pp. 244-254
    • Rajyaguru, P.1
  • 75
    • 84857195774 scopus 로고    scopus 로고
    • Arginine methylation of RNA-binding proteins regulates cell function and differentiation
    • Blackwell E., Ceman S. Arginine methylation of RNA-binding proteins regulates cell function and differentiation. Mol. Reprod. Dev. 2012, 79:163-175.
    • (2012) Mol. Reprod. Dev. , vol.79 , pp. 163-175
    • Blackwell, E.1    Ceman, S.2
  • 76
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
    • Ruthenburg A.J., et al. Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol. Cell 2007, 25:15-30.
    • (2007) Mol. Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1
  • 77
    • 79952304472 scopus 로고    scopus 로고
    • Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs
    • Schaeffer D., Van Hoof A. Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:2366-2371.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2366-2371
    • Schaeffer, D.1    Van Hoof, A.2
  • 78
    • 84055217962 scopus 로고    scopus 로고
    • The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome
    • Halbach F., et al. The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome. RNA 2012, 18:124-134.
    • (2012) RNA , vol.18 , pp. 124-134
    • Halbach, F.1
  • 79
    • 78649949096 scopus 로고    scopus 로고
    • Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay
    • Franks T., et al. Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay. Cell 2010, 143:938-950.
    • (2010) Cell , vol.143 , pp. 938-950
    • Franks, T.1
  • 80
    • 0029791449 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein
    • Weng Y., et al. Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein. Mol. Cell. Biol. 1996, 16:5477-5490.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5477-5490
    • Weng, Y.1
  • 81
    • 79952686670 scopus 로고    scopus 로고
    • Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2
    • Chakrabarti S., et al. Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. Mol. Cell 2011, 41:693-703.
    • (2011) Mol. Cell , vol.41 , pp. 693-703
    • Chakrabarti, S.1
  • 82
    • 37849005006 scopus 로고    scopus 로고
    • NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity
    • Chamieh H., et al. NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity. Nat. Struct. Mol. Biol. 2008, 15:85-93.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 85-93
    • Chamieh, H.1
  • 83
    • 33745159015 scopus 로고    scopus 로고
    • Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation
    • Weston A., Sommerville J. Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation. Nucleic Acids Res. 2006, 34:3082-3094.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3082-3094
    • Weston, A.1    Sommerville, J.2
  • 84
    • 80052642129 scopus 로고    scopus 로고
    • The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics
    • Carroll J.S., et al. The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics. J. Cell Biol. 2011, 194:527-537.
    • (2011) J. Cell Biol. , vol.194 , pp. 527-537
    • Carroll, J.S.1
  • 85
    • 84863688029 scopus 로고    scopus 로고
    • The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement
    • Sweet T., et al. The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement. PLoS Biol. 2012, 10:e1001342.
    • (2012) PLoS Biol. , vol.10
    • Sweet, T.1
  • 86
    • 79961016813 scopus 로고    scopus 로고
    • Intermolecular interactions within the abundant DEAD-box protein Dhh1 regulate its activity in vivo
    • Dutta A., et al. Intermolecular interactions within the abundant DEAD-box protein Dhh1 regulate its activity in vivo. J. Biol. Chem. 2011, 286:27454-27470.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27454-27470
    • Dutta, A.1
  • 87
    • 62549144414 scopus 로고    scopus 로고
    • The current understanding of Ded1p/DDX3 homologs from yeast to human
    • Tarn W., Chang T. The current understanding of Ded1p/DDX3 homologs from yeast to human. RNA Biol. 2009, 6:17-20.
    • (2009) RNA Biol. , vol.6 , pp. 17-20
    • Tarn, W.1    Chang, T.2
  • 88
    • 80053022305 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex
    • Hilliker A., et al. The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol. Cell 2011, 43:962-972.
    • (2011) Mol. Cell , vol.43 , pp. 962-972
    • Hilliker, A.1
  • 89
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA biology from an atlas of mammalian mRNA-binding proteins
    • Castello A., et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 2012, 149:1393-1406.
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1
  • 90
    • 84872051030 scopus 로고    scopus 로고
    • Global analysis of yeast mRNPs
    • Mitchell S.F., et al. Global analysis of yeast mRNPs. Nat. Struct. Mol. Biol. 2012, 20:127-133.
    • (2012) Nat. Struct. Mol. Biol. , vol.20 , pp. 127-133
    • Mitchell, S.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.