메뉴 건너뛰기




Volumn 18, Issue 3, 2017, Pages 202-210

RNA modifications and structures cooperate to guide RNA-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYLADENOSINE; 5 HYDROXYMETHYLCYTOSINE; 5 METHYLCYTOSINE; 6 N METHYLADENOSINE; GUIDE RNA; PSEUDOURIDINE; RIBOSOME RNA; SERINE ARGININE RICH SPLICING FACTOR; MESSENGER RNA; PROTEIN;

EID: 85011291934     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm.2016.163     Document Type: Review
Times cited : (219)

References (113)
  • 1
    • 84916640509 scopus 로고    scopus 로고
    • The RNAissance family: SR proteins as multifaceted regulators of gene expression
    • Howard, J. M. & Sanford, J. R. The RNAissance family: SR proteins as multifaceted regulators of gene expression. Wiley Interdiscip. Rev. RNA 6, 93-110 (2015).
    • (2015) Wiley Interdiscip. Rev. RNA , vol.6 , pp. 93-110
    • Howard, J.M.1    Sanford, J.R.2
  • 2
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang, Y., Gattoni, R., Stevenin, J. & Steitz, J. A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 11, 837-843 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 3
    • 84959473078 scopus 로고    scopus 로고
    • SR proteins are NXF1 adaptors that link alternative RNA processing to mRNA export
    • Muller-McNicoll, M. et al. SR proteins are NXF1 adaptors that link alternative RNA processing to mRNA export. Genes Dev. 30, 553-566 (2016).
    • (2016) Genes Dev. , vol.30 , pp. 553-566
    • Muller-McNicoll, M.1
  • 4
    • 84877721757 scopus 로고    scopus 로고
    • SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase
    • Ji, X. et al. SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase. Cell 153, 855-868 (2013).
    • (2013) Cell , vol.153 , pp. 855-868
    • Ji, X.1
  • 5
    • 84869090905 scopus 로고    scopus 로고
    • The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus
    • Singh, G. et al. The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus. Cell 151, 750-764 (2012).
    • (2012) Cell , vol.151 , pp. 750-764
    • Singh, G.1
  • 6
    • 77950920903 scopus 로고    scopus 로고
    • Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP
    • Hafner, M. et al. Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 141, 129-141 (2010).
    • (2010) Cell , vol.141 , pp. 129-141
    • Hafner, M.1
  • 7
    • 77954387023 scopus 로고    scopus 로고
    • ICLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution
    • Konig, J. et al. iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution. Nat. Struct. Mol. Biol. 17, 909-915 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 909-915
    • Konig, J.1
  • 8
    • 84992153620 scopus 로고    scopus 로고
    • RNA sequence context effects measured in vitro predict in vivo protein binding and regulation
    • Taliaferro, J. M. et al. RNA sequence context effects measured in vitro predict in vivo protein binding and regulation. Mol. Cell 64, 294-306 (2016).
    • (2016) Mol. Cell , vol.64 , pp. 294-306
    • Taliaferro, J.M.1
  • 9
    • 84975090518 scopus 로고    scopus 로고
    • Messenger RNA modifications: Form, distribution, and function
    • Gilbert, W. V., Bell, T. A. & Schaening, C. Messenger RNA modifications: form, distribution, and function. Science 352, 1408-1412 (2016).
    • (2016) Science , vol.352 , pp. 1408-1412
    • Gilbert, W.V.1    Bell, T.A.2    Schaening, C.3
  • 10
    • 84966478699 scopus 로고    scopus 로고
    • RNA duplex map in living cells reveals higher-order transcriptome structure
    • Lu, Z. et al. RNA duplex map in living cells reveals higher-order transcriptome structure. Cell 165, 1267-1279 (2016).
    • (2016) Cell , vol.165 , pp. 1267-1279
    • Lu, Z.1
  • 11
    • 84925777836 scopus 로고    scopus 로고
    • Structural imprints in vivo decode RNA regulatory mechanisms
    • Spitale, R. C. et al. Structural imprints in vivo decode RNA regulatory mechanisms. Nature 519, 486-490 (2015).
    • (2015) Nature , vol.519 , pp. 486-490
    • Spitale, R.C.1
  • 12
    • 84925799191 scopus 로고    scopus 로고
    • HiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1
    • Sugimoto, Y. et al. hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1. Nature 519, 491-494 (2015).
    • (2015) Nature , vol.519 , pp. 491-494
    • Sugimoto, Y.1
  • 13
    • 84955695193 scopus 로고    scopus 로고
    • A-To-I editing of coding and non-coding RNAs by ADARs
    • Nishikura, K. A-To-I editing of coding and non-coding RNAs by ADARs. Nat. Rev. Mol. Cell Biol. 17, 83-96 (2016).
    • (2016) Nat. Rev. Mol. Cell Biol. , vol.17 , pp. 83-96
    • Nishikura, K.1
  • 15
    • 78651335915 scopus 로고    scopus 로고
    • The RNA modification database, RNAMDB: 2011 update
    • Cantara, W. A. et al. The RNA Modification Database, RNAMDB: 2011 update. Nucleic Acids Res. 39, D195-D201 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. D195-D201
    • Cantara, W.A.1
  • 16
    • 84870152928 scopus 로고    scopus 로고
    • Biosynthesis and function of posttranscriptional modifications of transfer RNAs
    • El Yacoubi, B., Bailly, M. & de Crecy-Lagard, V. Biosynthesis and function of posttranscriptional modifications of transfer RNAs. Annu. Rev. Genet. 46, 69-95 (2012).
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 69-95
    • El Yacoubi, B.1    Bailly, M.2    De Crecy-Lagard, V.3
  • 17
    • 77954053541 scopus 로고    scopus 로고
    • RNA modifications: A mechanism that modulates gene expression
    • Karijolich, J., Kantartzis, A. & Yu, Y. T. RNA modifications: a mechanism that modulates gene expression. Methods Mol. Biol. 629, 1-19 (2010).
    • (2010) Methods Mol. Biol. , vol.629 , pp. 1-19
    • Karijolich, J.1    Kantartzis, A.2    Yu, Y.T.3
  • 18
    • 77952029221 scopus 로고    scopus 로고
    • Deciphering the splicing code
    • Barash, Y. et al. Deciphering the splicing code. Nature 465, 53-59 (2010).
    • (2010) Nature , vol.465 , pp. 53-59
    • Barash, Y.1
  • 19
    • 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 485, 201-206 (2012).
    • (2012) Nature , vol.485 , pp. 201-206
    • Dominissini, D.1
  • 20
    • 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 149, 1635-1646 (2012).
    • (2012) Cell , vol.149 , pp. 1635-1646
    • Meyer, K.D.1
  • 21
    • 84904035764 scopus 로고    scopus 로고
    • Perturbation of m6A writers reveals two distinct classes of mRNA methylation at internal and 5′ sites
    • Schwartz, S. et al. Perturbation of m6A writers reveals two distinct classes of mRNA methylation at internal and 5′ sites. Cell Rep. 8, 284-296 (2014).
    • (2014) Cell Rep. , vol.8 , pp. 284-296
    • Schwartz, S.1
  • 22
    • 84864037029 scopus 로고    scopus 로고
    • RNA methylation by the MIS complex regulates a cell fate decision in yeast
    • Agarwala, S. D., Blitzblau, H. G., Hochwagen, A. & Fink, G. R. RNA methylation by the MIS complex regulates a cell fate decision in yeast. PLoS Genet. 8, e1002732 (2012).
    • (2012) PLoS Genet. , vol.8 , pp. e1002732
    • Agarwala, S.D.1    Blitzblau, H.G.2    Hochwagen, A.3    Fink, G.R.4
  • 23
    • 84887833997 scopus 로고    scopus 로고
    • Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle
    • Horiuchi, K. et al. Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle. J. Biol. Chem. 288, 33292-33302 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 33292-33302
    • Horiuchi, K.1
  • 24
    • 84897110592 scopus 로고    scopus 로고
    • A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation
    • Liu, J. et al. A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation. Nat. Chem. Biol. 10, 93-95 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 93-95
    • Liu, J.1
  • 25
    • 84988329709 scopus 로고    scopus 로고
    • M6A RNA methylation promotes XIST-mediated transcriptional repression
    • Patil, D. P. et al. m6A RNA methylation promotes XIST-mediated transcriptional repression. Nature 537, 369-373 (2016).
    • (2016) Nature , vol.537 , pp. 369-373
    • Patil, D.P.1
  • 26
    • 84893746230 scopus 로고    scopus 로고
    • Mammalian WTAP is a regulatory subunit of the RNA N6-methyladenosine methyltransferase
    • Ping, X. L. et al. Mammalian WTAP is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. Cell Res. 24, 177-189 (2014).
    • (2014) Cell Res. , vol.24 , pp. 177-189
    • Ping, X.L.1
  • 27
    • 57749089784 scopus 로고    scopus 로고
    • MTA is an Arabidopsis messenger RNA adenosine methylase and interacts with a homolog of a sex-specific splicing factor
    • Zhong, S. et al. MTA is an Arabidopsis messenger RNA adenosine methylase and interacts with a homolog of a sex-specific splicing factor. Plant Cell 20, 1278-1288 (2008).
    • (2008) Plant Cell , vol.20 , pp. 1278-1288
    • Zhong, S.1
  • 28
    • 84943570207 scopus 로고    scopus 로고
    • A majority of m6A residues are in the last exons, allowing the potential for 3′ UTR regulation
    • Ke, S. et al. A majority of m6A residues are in the last exons, allowing the potential for 3′ UTR regulation. Genes Dev. 29, 2037-2053 (2015).
    • (2015) Genes Dev. , vol.29 , pp. 2037-2053
    • Ke, S.1
  • 29
    • 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. 7, 885-887 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 885-887
    • Jia, G.1
  • 30
    • 84920273757 scopus 로고    scopus 로고
    • FTO-dependent demethylation of N6-methyladenosine regulates mRNA splicing and is required for adipogenesis
    • Zhao, X. et al. FTO-dependent demethylation of N6-methyladenosine regulates mRNA splicing and is required for adipogenesis. Cell Res. 24, 1403-1419 (2014).
    • (2014) Cell Res. , vol.24 , pp. 1403-1419
    • Zhao, X.1
  • 31
    • 84893310526 scopus 로고    scopus 로고
    • N6-methyladenosine modification destabilizes developmental regulators in embryonic stem cells
    • Wang, Y. et al. N6-methyladenosine modification destabilizes developmental regulators in embryonic stem cells. Nat. Cell Biol. 16, 191-198 (2014).
    • (2014) Nat. Cell Biol. , vol.16 , pp. 191-198
    • Wang, Y.1
  • 32
    • 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 49, 18-29 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 18-29
    • Zheng, G.1
  • 33
    • 61449176062 scopus 로고    scopus 로고
    • Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones
    • Zhong, X. Y., Ding, J. H., Adams, J. A., Ghosh, G. & Fu, X. D. Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones. Genes Dev. 23, 482-495 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 482-495
    • Zhong, X.Y.1    Ding, J.H.2    Adams, J.A.3    Ghosh, G.4    Fu, X.D.5
  • 34
    • 67649671966 scopus 로고    scopus 로고
    • SR proteins in vertical integration of gene expression from transcription to RNA processing to translation
    • Zhong, X. Y., Wang, P., Han, J., Rosenfeld, M. G. & Fu, X. D. SR proteins in vertical integration of gene expression from transcription to RNA processing to translation. Mol. Cell 35, 1-10 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 1-10
    • Zhong, X.Y.1    Wang, P.2    Han, J.3    Rosenfeld, M.G.4    Fu, X.D.5
  • 35
    • 84958624251 scopus 로고    scopus 로고
    • Nuclear m6A reader YTHDC1 regulates mRNA splicing
    • Xiao, W. et al. Nuclear m6A reader YTHDC1 regulates mRNA splicing. Mol. Cell 61, 507-519 (2016).
    • (2016) Mol. Cell , vol.61 , pp. 507-519
    • Xiao, W.1
  • 36
    • 85017163153 scopus 로고    scopus 로고
    • M6A potentiates Sxl alternative pre-mRNA splicing for robust Drosophila sex determination
    • Haussmann, I.U. et al. m6A potentiates Sxl alternative pre-mRNA splicing for robust Drosophila sex determination. Nature 540, 301-304 (2016).
    • (2016) Nature , vol.540 , pp. 301-304
    • Haussmann, I.U.1
  • 37
    • 85017161112 scopus 로고    scopus 로고
    • M6A modulates neuronal functions and sex determination in Drosophila
    • Lence, T. et al. m6A modulates neuronal functions and sex determination in Drosophila. Nature 540, 242-247 (2016).
    • (2016) Nature , vol.540 , pp. 242-247
    • Lence, T.1
  • 38
    • 84941424170 scopus 로고    scopus 로고
    • HNRNPA2B1 is a mediator of m6A-dependent nuclear RNA processing events
    • Alarcon, C. R. et al. HNRNPA2B1 is a mediator of m6A-dependent nuclear RNA processing events. Cell 162, 1299-1308 (2015).
    • (2015) Cell , vol.162 , pp. 1299-1308
    • Alarcon, C.R.1
  • 39
    • 84922180958 scopus 로고    scopus 로고
    • Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells
    • Carlile, T. M. et al. Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells. Nature 515, 143-146 (2014).
    • (2014) Nature , vol.515 , pp. 143-146
    • Carlile, T.M.1
  • 40
    • 84937514684 scopus 로고    scopus 로고
    • Chemical pulldown reveals dynamic pseudouridylation of the mammalian transcriptome
    • Li, X. et al. Chemical pulldown reveals dynamic pseudouridylation of the mammalian transcriptome. Nat. Chem. Biol. 11, 592-597 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 592-597
    • Li, X.1
  • 41
    • 84908626586 scopus 로고    scopus 로고
    • Transcriptome-wide mapping of pseudouridines: Pseudouridine synthases modify specific mRNAs in S. Cerevisiae
    • Lovejoy, A. F., Riordan, D. P. & Brown, P. O. Transcriptome-wide mapping of pseudouridines: pseudouridine synthases modify specific mRNAs in S. cerevisiae. PLoS ONE 9, e110799 (2014).
    • (2014) PLoS One , vol.9 , pp. e110799
    • Lovejoy, A.F.1    Riordan, D.P.2    Brown, P.O.3
  • 42
    • 84907527348 scopus 로고    scopus 로고
    • Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA
    • Schwartz, S. et al. Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA. Cell 159, 148-162 (2014).
    • (2014) Cell , vol.159 , pp. 148-162
    • Schwartz, S.1
  • 43
    • 0018188778 scopus 로고
    • The absolute frequency of labeled N-6-methyladenosine in HeLa cell messenger RNA decreases with label time
    • Sommer, S., Lavi, U. & Darnell, J. E. Jr. The absolute frequency of labeled N-6-methyladenosine in HeLa cell messenger RNA decreases with label time. J. Mol. Biol. 124, 487-499 (1978).
    • (1978) J. Mol. Biol. , vol.124 , pp. 487-499
    • Sommer, S.1    Lavi, U.2    Darnell, J.E.3
  • 44
    • 84919457819 scopus 로고    scopus 로고
    • M6A RNA modification controls cell fate transition in mammalian embryonic stem cells
    • Batista, P. J. et al. m6A RNA modification controls cell fate transition in mammalian embryonic stem cells. Cell Stem Cell 15, 707-719 (2014).
    • (2014) Cell Stem Cell , vol.15 , pp. 707-719
    • Batista, P.J.1
  • 45
    • 84922342926 scopus 로고    scopus 로고
    • Stem cells. M6A mRNA methylation facilitates resolution of naive pluripotency toward differentiation
    • Geula, S. et al. Stem cells. m6A mRNA methylation facilitates resolution of naive pluripotency toward differentiation. Science 347, 1002-1006 (2015).
    • (2015) Science , vol.347 , pp. 1002-1006
    • Geula, S.1
  • 46
    • 84983728274 scopus 로고    scopus 로고
    • YTHDF2 destabilizes m6A-containing RNA through direct recruitment of the CCR4-NOT deadenylase complex
    • Du, H. et al. YTHDF2 destabilizes m6A-containing RNA through direct recruitment of the CCR4-NOT deadenylase complex. Nat. Commun. 7, 12626 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 12626
    • Du, H.1
  • 47
    • 84892372347 scopus 로고    scopus 로고
    • N6-methyladenosine-dependent regulation of messenger RNA stability
    • Wang, X. et al. N6-methyladenosine-dependent regulation of messenger RNA stability. Nature 505, 117-120 (2014).
    • (2014) Nature , vol.505 , pp. 117-120
    • Wang, X.1
  • 48
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth, U. & Parker, R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300, 805-808 (2003).
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 49
    • 84963960245 scopus 로고    scopus 로고
    • Posttranscriptional m6A editing of HIV-1 mRNAs enhances viral gene expression
    • Kennedy, E. M. et al. Posttranscriptional m6A editing of HIV-1 mRNAs enhances viral gene expression. Cell Host Microbe 19, 675-685 (2016).
    • (2016) Cell Host Microbe , vol.19 , pp. 675-685
    • Kennedy, E.M.1
  • 50
    • 84924283323 scopus 로고    scopus 로고
    • M6A RNA methylation is regulated by microRNAs and promotes reprogramming to pluripotency
    • Chen, T. et al. m6A RNA methylation is regulated by microRNAs and promotes reprogramming to pluripotency. Cell Stem Cell 16, 289-301 (2015).
    • (2015) Cell Stem Cell , vol.16 , pp. 289-301
    • Chen, T.1
  • 51
    • 84925796024 scopus 로고    scopus 로고
    • N6-methyladenosine marks primary microRNAs for processing
    • Alarcon, C. R., Lee, H., Goodarzi, H., Halberg, N. & Tavazoie, S. F. N6-methyladenosine marks primary microRNAs for processing. Nature 519, 482-485 (2015).
    • (2015) Nature , vol.519 , pp. 482-485
    • Alarcon, C.R.1    Lee, H.2    Goodarzi, H.3    Halberg, N.4    Tavazoie, S.F.5
  • 52
    • 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. 40, 5023-5033 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5023-5033
    • Squires, J.E.1
  • 53
    • 85018194065 scopus 로고    scopus 로고
    • Reversible methylation of m6Am in the 5′ cap controls mRNA stability
    • Mauer, J. et al. Reversible methylation of m6Am in the 5′ cap controls mRNA stability. Nature http://dx.doi.org/10.1038/nature21022 (2016).
    • (2016) Nature
    • Mauer, J.1
  • 54
    • 2442466927 scopus 로고    scopus 로고
    • Cap-dependent and cap-independent translation in eukaryotic systems
    • Merrick, W. C. Cap-dependent and cap-independent translation in eukaryotic systems. Gene 332, 1-11 (2004).
    • (2004) Gene , vol.332 , pp. 1-11
    • Merrick, W.C.1
  • 55
    • 84930621650 scopus 로고    scopus 로고
    • N6-methyladenosine modulates messenger RNA translation efficiency
    • Wang, X. et al. N6-methyladenosine modulates messenger RNA translation efficiency. Cell 161, 1388-1399 (2015).
    • (2015) Cell , vol.161 , pp. 1388-1399
    • Wang, X.1
  • 56
    • 84979556508 scopus 로고    scopus 로고
    • N6-methyladenosine of HIV-1 RNA regulates viral infection and HIV-1 Gag protein expression
    • Tirumuru, N. et al. N6-methyladenosine of HIV-1 RNA regulates viral infection and HIV-1 Gag protein expression. Elife 5 e15528 (2016).
    • (2016) Elife , vol.5 , pp. e15528
    • Tirumuru, N.1
  • 57
    • 84946228509 scopus 로고    scopus 로고
    • 5′ UTR m6A promotes cap-independent translation
    • Meyer, K. D. et al. 5′ UTR m6A promotes cap-independent translation. Cell 163, 999-1010 (2015).
    • (2015) Cell , vol.163 , pp. 999-1010
    • Meyer, K.D.1
  • 58
    • 84945288814 scopus 로고    scopus 로고
    • Dynamic m6A mRNA methylation directs translational control of heat shock response
    • Zhou, J. et al. Dynamic m6A mRNA methylation directs translational control of heat shock response. Nature 526, 591-594 (2015).
    • (2015) Nature , vol.526 , pp. 591-594
    • Zhou, J.1
  • 59
    • 0029791354 scopus 로고    scopus 로고
    • Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation
    • Feigenblum, D. & Schneider, R. J. Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation. Mol. Cell. Biol. 16, 5450-5457 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5450-5457
    • Feigenblum, D.1    Schneider, R.J.2
  • 60
    • 84958156997 scopus 로고    scopus 로고
    • NSun2 delays replicative senescence by repressing p27KIP1 translation and elevating CDK1 translation
    • Tang, H. et al. NSun2 delays replicative senescence by repressing p27KIP1 translation and elevating CDK1 translation. Aging (Albany NY) 7, 1143-1158 (2015).
    • (2015) Aging (Albany NY) , vol.7 , pp. 1143-1158
    • Tang, H.1
  • 61
    • 84946232216 scopus 로고    scopus 로고
    • NSun2 promotes cell growth via elevating cyclin-dependent kinase 1 translation
    • Xing, J. et al. NSun2 promotes cell growth via elevating cyclin-dependent kinase 1 translation. Mol. Cell. Biol. 35, 4043-4052 (2015).
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 4043-4052
    • Xing, J.1
  • 62
    • 84906342396 scopus 로고    scopus 로고
    • Tet-mediated formation of 5-hydroxymethylcytosine in RNA
    • Fu, L. et al. Tet-mediated formation of 5-hydroxymethylcytosine in RNA. J. Am. Chem. Soc. 136, 11582-11585 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 11582-11585
    • Fu, L.1
  • 63
    • 84954349048 scopus 로고    scopus 로고
    • RNA biochemistry. Transcriptome-wide distribution and function of RNA hydroxymethylcytosine
    • Delatte, B. et al. RNA biochemistry. Transcriptome-wide distribution and function of RNA hydroxymethylcytosine. Science 351, 282-285 (2016).
    • (2016) Science , vol.351 , pp. 282-285
    • Delatte, B.1
  • 64
    • 84959386536 scopus 로고    scopus 로고
    • The dynamic N1-methyladenosine methylome in eukaryotic messenger RNA
    • Dominissini, D. et al. The dynamic N1-methyladenosine methylome in eukaryotic messenger RNA. Nature 530, 441-446 (2016).
    • (2016) Nature , vol.530 , pp. 441-446
    • Dominissini, D.1
  • 65
    • 84957828213 scopus 로고    scopus 로고
    • Transcriptome-wide mapping reveals reversible and dynamic N1-methyladenosine methylome
    • Li, X. et al. Transcriptome-wide mapping reveals reversible and dynamic N1-methyladenosine methylome. Nat. Chem. Biol. 12, 311-316 (2016).
    • (2016) Nat. Chem. Biol. , vol.12 , pp. 311-316
    • Li, X.1
  • 66
    • 84942293253 scopus 로고    scopus 로고
    • Transcriptome-wide dynamics of RNA pseudouridylation
    • Karijolich, J., Yi, C. & Yu, Y. T. Transcriptome-wide dynamics of RNA pseudouridylation. Nat. Rev. Mol. Cell Biol. 16, 581-585 (2015).
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 581-585
    • Karijolich, J.1    Yi, C.2    Yu, Y.T.3
  • 68
    • 84857080591 scopus 로고    scopus 로고
    • Functional complexity and regulation through RNA dynamics
    • Dethoff, E. A., Chugh, J., Mustoe, A. M. & Al-Hashimi, H. M. Functional complexity and regulation through RNA dynamics. Nature 482, 322-330 (2012).
    • (2012) Nature , vol.482 , pp. 322-330
    • Dethoff, E.A.1    Chugh, J.2    Mustoe, A.M.3    Al-Hashimi, H.M.4
  • 69
    • 84897128298 scopus 로고    scopus 로고
    • The noncoding RNA revolution - Trashing old rules to forge new ones
    • Cech, T. R. & Steitz, J. A. The noncoding RNA revolution - trashing old rules to forge new ones. Cell 157, 77-94 (2014).
    • (2014) Cell , vol.157 , pp. 77-94
    • Cech, T.R.1    Steitz, J.A.2
  • 70
    • 60149103676 scopus 로고    scopus 로고
    • The centrality of RNA
    • Sharp, P. A. The centrality of RNA. Cell 136, 577-580 (2009).
    • (2009) Cell , vol.136 , pp. 577-580
    • Sharp, P.A.1
  • 71
    • 44949246374 scopus 로고    scopus 로고
    • "Nought may endure but mutability": Spliceosome dynamics and the regulation of splicing
    • Smith, D. J., Query, C. C. & Konarska, M. M. "Nought may endure but mutability": spliceosome dynamics and the regulation of splicing. Mol. Cell 30, 657-666 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 657-666
    • Smith, D.J.1    Query, C.C.2    Konarska, M.M.3
  • 72
    • 84893427735 scopus 로고    scopus 로고
    • In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features
    • Ding, Y. et al. In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features. Nature 505, 696-700 (2014).
    • (2014) Nature , vol.505 , pp. 696-700
    • Ding, Y.1
  • 73
    • 84893351549 scopus 로고    scopus 로고
    • Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo
    • Rouskin, S., Zubradt, M., Washietl, S., Kellis, M. & Weissman, J. S. Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo. Nature 505, 701-705 (2014).
    • (2014) Nature , vol.505 , pp. 701-705
    • Rouskin, S.1    Zubradt, M.2    Washietl, S.3    Kellis, M.4    Weissman, J.S.5
  • 74
    • 84985946078 scopus 로고    scopus 로고
    • Regulatory effects of cotranscriptional RNA structure formation and transitions
    • Liu, S. R., Hu, C. G. & Zhang, J. Z. Regulatory effects of cotranscriptional RNA structure formation and transitions. Wiley Interdiscip. Rev. RNA 7, 562-574 (2016).
    • (2016) Wiley Interdiscip. Rev. RNA , vol.7 , pp. 562-574
    • Liu, S.R.1    Hu, C.G.2    Zhang, J.Z.3
  • 75
    • 84955600694 scopus 로고    scopus 로고
    • Two-way street: Regulatory interplay between RNA polymerase and nascent RNA structure
    • Zhang, J. & Landick, R. A. Two-way street: regulatory interplay between RNA polymerase and nascent RNA structure. Trends Biochem. Sci. 41, 293-310 (2016).
    • (2016) Trends Biochem. Sci. , vol.41 , pp. 293-310
    • Zhang, J.1    Landick, R.A.2
  • 77
    • 0141888375 scopus 로고    scopus 로고
    • A slow RNA polymerase II affects alternative splicing in vivo
    • de la Mata, M. et al. A slow RNA polymerase II affects alternative splicing in vivo. Mol. Cell 12, 525-532 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 525-532
    • De La-Mata, M.1
  • 78
    • 79958859723 scopus 로고    scopus 로고
    • RNA polymerase II kinetics in polo polyadenylation signal selection
    • Pinto, P. A. et al. RNA polymerase II kinetics in polo polyadenylation signal selection. EMBO J. 30, 2431-2444 (2011).
    • (2011) EMBO J. , vol.30 , pp. 2431-2444
    • Pinto, P.A.1
  • 79
    • 79956067688 scopus 로고    scopus 로고
    • New insights into RNA secondary structure in the alternative splicing of pre-mRNAs
    • Jin, Y., Yang, Y. & Zhang, P. New insights into RNA secondary structure in the alternative splicing of pre-mRNAs. RNA Biol. 8, 450-457 (2011).
    • (2011) RNA Biol. , vol.8 , pp. 450-457
    • Jin, Y.1    Yang, Y.2    Zhang, P.3
  • 80
    • 84893358533 scopus 로고    scopus 로고
    • Landscape and variation of RNA secondary structure across the human transcriptome
    • Wan, Y. et al. Landscape and variation of RNA secondary structure across the human transcriptome. Nature 505, 706-709 (2014).
    • (2014) Nature , vol.505 , pp. 706-709
    • Wan, Y.1
  • 81
    • 84890132388 scopus 로고    scopus 로고
    • Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges
    • Lovci, M. T. et al. Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges. Nat. Struct. Mol. Biol. 20, 1434-1442 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1434-1442
    • Lovci, M.T.1
  • 82
    • 84966553306 scopus 로고    scopus 로고
    • In vivo mapping of eukaryotic RNA interactomes reveals principles of higher-order organization and regulation
    • Aw, J. G. et al. In vivo mapping of eukaryotic RNA interactomes reveals principles of higher-order organization and regulation. Mol. Cell 62, 603-617 (2016).
    • (2016) Mol. Cell , vol.62 , pp. 603-617
    • Aw, J.G.1
  • 84
    • 84924072927 scopus 로고    scopus 로고
    • N6-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions
    • Liu, N. et al. N6-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions. Nature 518, 560-564 (2015).
    • (2015) Nature , vol.518 , pp. 560-564
    • Liu, N.1
  • 85
    • 84859115602 scopus 로고    scopus 로고
    • HnRNP C tetramer measures RNA length to classify RNA polymerase II transcripts for export
    • McCloskey, A., Taniguchi, I., Shinmyozu, K. & Ohno, M. hnRNP C tetramer measures RNA length to classify RNA polymerase II transcripts for export. Science 335, 1643-1646 (2012).
    • (2012) Science , vol.335 , pp. 1643-1646
    • McCloskey, A.1    Taniguchi, I.2    Shinmyozu, K.3    Ohno, M.4
  • 86
    • 84873323035 scopus 로고    scopus 로고
    • Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements
    • Zarnack, K. et al. Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements. Cell 152, 453-466 (2013).
    • (2013) Cell , vol.152 , pp. 453-466
    • Zarnack, K.1
  • 87
    • 77956306662 scopus 로고    scopus 로고
    • Genome-wide measurement of RNA secondary structure in yeast
    • Kertesz, M. et al. Genome-wide measurement of RNA secondary structure in yeast. Nature 467, 103-107 (2010).
    • (2010) Nature , vol.467 , pp. 103-107
    • Kertesz, M.1
  • 88
    • 84868009378 scopus 로고    scopus 로고
    • Genome-wide measurement of RNA folding energies
    • Wan, Y. et al. Genome-wide measurement of RNA folding energies. Mol. Cell 48, 169-181 (2012).
    • (2012) Mol. Cell , vol.48 , pp. 169-181
    • Wan, Y.1
  • 89
    • 84862229118 scopus 로고    scopus 로고
    • 5′-UTR RNA G-quadruplexes: Translation regulation and targeting
    • Bugaut, A. & Balasubramanian, S. 5′-UTR RNA G-quadruplexes: translation regulation and targeting. Nucleic Acids Res. 40, 4727-4741 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4727-4741
    • Bugaut, A.1    Balasubramanian, S.2
  • 90
    • 84989267452 scopus 로고    scopus 로고
    • RNA G-quadruplexes are globally unfolded in eukaryotic cells and depleted in bacteria
    • Guo, J. U. & Bartel, D. P. RNA G-quadruplexes are globally unfolded in eukaryotic cells and depleted in bacteria. Science 353 (2016).
    • (2016) Science , vol.353
    • Guo, J.U.1    Bartel, D.P.2
  • 92
    • 84907221438 scopus 로고    scopus 로고
    • RNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer
    • Wolfe, A. L. et al. RNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer. Nature 513, 65-70 (2014).
    • (2014) Nature , vol.513 , pp. 65-70
    • Wolfe, A.L.1
  • 93
    • 84915814905 scopus 로고    scopus 로고
    • MOV10 and FMRP regulate AGO2 association with microRNA recognition elements
    • Kenny, P. J. et al. MOV10 and FMRP regulate AGO2 association with microRNA recognition elements. Cell Rep. 9, 1729-1741 (2014).
    • (2014) Cell Rep. , vol.9 , pp. 1729-1741
    • Kenny, P.J.1
  • 95
    • 84894131718 scopus 로고    scopus 로고
    • Global analysis of mRNA isoform half-lives reveals stabilizing and destabilizing elements in yeast
    • Geisberg, J. V., Moqtaderi, Z., Fan, X., Ozsolak, F. & Struhl, K. Global analysis of mRNA isoform half-lives reveals stabilizing and destabilizing elements in yeast. Cell 156, 812-824 (2014).
    • (2014) Cell , vol.156 , pp. 812-824
    • Geisberg, J.V.1    Moqtaderi, Z.2    Fan, X.3    Ozsolak, F.4    Struhl, K.5
  • 96
    • 84985887596 scopus 로고    scopus 로고
    • Secondary structures involving the poly(A) tail and other 3′ sequences are major determinants of mRNA isoform stability in yeast
    • Moqtaderi, Z., Geisberg, J. V. & Struhl, K. Secondary structures involving the poly(A) tail and other 3′ sequences are major determinants of mRNA isoform stability in yeast. Microb. Cell 1, 137-139 (2014).
    • (2014) Microb. Cell , vol.1 , pp. 137-139
    • Moqtaderi, Z.1    Geisberg, J.V.2    Struhl, K.3
  • 97
    • 84890494960 scopus 로고    scopus 로고
    • 3′ UTR-isoform choice has limited influence on the stability and translational efficiency of most mRNAs in mouse fibroblasts
    • Spies, N., Burge, C. B. & Bartel, D. P. 3′ UTR-isoform choice has limited influence on the stability and translational efficiency of most mRNAs in mouse fibroblasts. Genome Res. 23, 2078-2090 (2013).
    • (2013) Genome Res. , vol.23 , pp. 2078-2090
    • Spies, N.1    Burge, C.B.2    Bartel, D.P.3
  • 99
    • 54149091257 scopus 로고    scopus 로고
    • Metabolism and regulation of canonical histone mRNAs: Life without a poly(A) tail
    • Marzluff, W. F., Wagner, E. J. & Duronio, R. J. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat. Rev. Genet. 9, 843-854 (2008).
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 843-854
    • Marzluff, W.F.1    Wagner, E.J.2    Duronio, R.J.3
  • 100
    • 33845662140 scopus 로고    scopus 로고
    • Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element
    • Conrad, N. K., Mili, S., Marshall, E. L., Shu, M. D. & Steitz, J. A. Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element. Mol. Cell 24, 943-953 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 943-953
    • Conrad, N.K.1    Mili, S.2    Marshall, E.L.3    Shu, M.D.4    Steitz, J.A.5
  • 101
    • 34547510230 scopus 로고    scopus 로고
    • Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail
    • Conrad, N. K., Shu, M. D., Uyhazi, K. E. & Steitz, J. A. Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail. Proc. Natl Acad. Sci. USA 104, 10412-10417 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10412-10417
    • Conrad, N.K.1    Shu, M.D.2    Uyhazi, K.E.3    Steitz, J.A.4
  • 102
    • 20044369601 scopus 로고    scopus 로고
    • Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts
    • Conrad, N. K. & Steitz, J. A. A. Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts. EMBO J. 24, 1831-1841 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1831-1841
    • Conrad, N.K.1    Steitz, J.A.A.2
  • 103
    • 84869846717 scopus 로고    scopus 로고
    • Formation of triple-helical structures by the 3′-end sequences of MALAT1 and MENβ noncoding RNAs
    • Brown, J. A., Valenstein, M. L., Yario, T. A., Tycowski, K. T. & Steitz, J. A. Formation of triple-helical structures by the 3′-end sequences of MALAT1 and MENβ noncoding RNAs. Proc. Natl Acad. Sci. USA 109, 19202-19207 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 19202-19207
    • Brown, J.A.1    Valenstein, M.L.2    Yario, T.A.3    Tycowski, K.T.4    Steitz, J.A.5
  • 104
    • 84868519473 scopus 로고    scopus 로고
    • A triple helix stabilizes the 3′ ends of long noncoding RNAs that lack poly(A) tails
    • Wilusz, J. E. et al. A triple helix stabilizes the 3′ ends of long noncoding RNAs that lack poly(A) tails. Genes Dev. 26, 2392-2407 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 2392-2407
    • Wilusz, J.E.1
  • 105
    • 61849113891 scopus 로고    scopus 로고
    • MEN ∈/β nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles
    • Sunwoo, H. et al. MEN ∈/β nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles. Genome Res. 19, 347-359 (2009).
    • (2009) Genome Res. , vol.19 , pp. 347-359
    • Sunwoo, H.1
  • 106
    • 56349113455 scopus 로고    scopus 로고
    • 3′ end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA
    • Wilusz, J. E., Freier, S. M. & Spector, D. L. 3′ end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA. Cell 135, 919-932 (2008).
    • (2008) Cell , vol.135 , pp. 919-932
    • Wilusz, J.E.1    Freier, S.M.2    Spector, D.L.3
  • 107
    • 84964612350 scopus 로고    scopus 로고
    • Myriad triple-helix-forming structures in the transposable element RNAs of plants and fungi
    • Tycowski, K. T., Shu, M. D. & Steitz, J. A. Myriad triple-helix-forming structures in the transposable element RNAs of plants and fungi. Cell Rep. 15, 1266-1276 (2016).
    • (2016) Cell Rep. , vol.15 , pp. 1266-1276
    • Tycowski, K.T.1    Shu, M.D.2    Steitz, J.A.3
  • 108
    • 0042161864 scopus 로고    scopus 로고
    • The thermodynamic stability of RNA duplexes and hairpins containing N6-alkyladenosines and 2-methylthio-N6-alkyladenosines
    • Kierzek, E. & Kierzek, R. The thermodynamic stability of RNA duplexes and hairpins containing N6-alkyladenosines and 2-methylthio-N6-alkyladenosines. Nucleic Acids Res. 31, 4472-4480 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4472-4480
    • Kierzek, E.1    Kierzek, R.2
  • 109
    • 84922780316 scopus 로고    scopus 로고
    • Structure and thermodynamics of N6-methyladenosine in RNA: A spring-loaded base modification
    • Roost, C. et al. Structure and thermodynamics of N6-methyladenosine in RNA: a spring-loaded base modification. J. Am. Chem. Soc. 137, 2107-2115 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 2107-2115
    • Roost, C.1
  • 110
    • 84925767325 scopus 로고    scopus 로고
    • The multifunctional Staufen proteins: Conserved roles from neurogenesis to synaptic plasticity
    • Heraud-Farlow, J. E. & Kiebler, M. A. The multifunctional Staufen proteins: conserved roles from neurogenesis to synaptic plasticity. Trends Neurosci. 37, 470-479 (2014).
    • (2014) Trends Neurosci. , vol.37 , pp. 470-479
    • Heraud-Farlow, J.E.1    Kiebler, M.A.2
  • 111
    • 0025245501 scopus 로고
    • Sequence specificity of mRNA N6-adenosine methyltransferase
    • Csepany, T., Lin, A., Baldick, C. J. Jr & Beemon, K. Sequence specificity of mRNA N6-adenosine methyltransferase. J. Biol. Chem. 265, 20117-20122 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 20117-20122
    • Csepany, T.1    Lin, A.2    Baldick, C.J.3    Beemon, K.4
  • 113
    • 84888423912 scopus 로고    scopus 로고
    • Probing N6-methyladenosine RNA modification status at single nucleotide resolution in mRNA and long noncoding RNA
    • Liu, N. et al. Probing N6-methyladenosine RNA modification status at single nucleotide resolution in mRNA and long noncoding RNA. RNA 19, 1848-1856 (2013).
    • (2013) RNA , vol.19 , pp. 1848-1856
    • Liu, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.