{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T05:23:46Z","timestamp":1791350626637,"version":"4.3.1"},"reference-count":56,"publisher":"Springer Science and Business Media LLC","issue":"7584","license":[{"start":{"date-parts":[[2015,12,23]],"date-time":"2015-12-23T00:00:00Z","timestamp":1450828800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2016,1]]},"DOI":"10.1038\/nature16469","type":"journal-article","created":{"date-parts":[[2015,12,23]],"date-time":"2015-12-23T16:21:48Z","timestamp":1450887708000},"page":"48-53","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":257,"title":["SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination"],"prefix":"10.1038","volume":"529","author":[{"given":"Dorothy","family":"Yanling Zhao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerald","family":"Gish","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Braunschweig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yue","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zuyao","family":"Ni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank W.","family":"Schmitges","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guoqing","family":"Zhong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ke","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weiguo","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jason","family":"Moffat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masoud","family":"Vedadi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinrong","family":"Min","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tony J.","family":"Pawson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin J.","family":"Blencowe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack F.","family":"Greenblatt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,12,23]]},"reference":[{"key":"BFnature16469_CR1","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.molcel.2009.10.019","volume":"36","author":"S Buratowski","year":"2009","unstructured":"Buratowski, S. Progression through the RNA polymerase II CTD cycle. Mol. Cell 36, 541\u2013546 (2009)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1038\/nrm3953","volume":"16","author":"I Jonkers","year":"2015","unstructured":"Jonkers, I. & Lis, J. T. Getting up to speed with transcription elongation by RNA polymerase II. Nature Rev. Mol. Cell Biol. 16, 167\u2013177 (2015)","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"BFnature16469_CR3","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1038\/nrm3943","volume":"16","author":"O Porrua","year":"2015","unstructured":"Porrua, O. & Libri, D. Transcription termination and the control of the transcriptome: why, where and how to stop. Nature Rev. Mol. Cell Biol. 16, 190\u2013202 (2015)","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"BFnature16469_CR4","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1038\/nrm3941","volume":"16","author":"S Venkatesh","year":"2015","unstructured":"Venkatesh, S. & Workman, J. L. Histone exchange, chromatin structure and the regulation of transcription. Nature Rev. Mol. Cell Biol. 16, 178\u2013189 (2015)","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"BFnature16469_CR5","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1126\/science.1219651","volume":"336","author":"A Mayer","year":"2012","unstructured":"Mayer, A. et al. CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II. Science 336, 1723\u20131725 (2012)","journal-title":"Science"},{"key":"BFnature16469_CR6","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1126\/science.1206034","volume":"334","author":"JP Hsin","year":"2011","unstructured":"Hsin, J. P., Sheth, A. & Manley, J. L. RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3\u2032 end processing. Science 334, 683\u2013686 (2011)","journal-title":"Science"},{"key":"BFnature16469_CR7","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1126\/science.1202663","volume":"332","author":"RJ Sims III","year":"2011","unstructured":"Sims, R. J. III et al. The C-terminal domain of RNA polymerase II is modified by site-specific methylation. Science 332, 99\u2013103 (2011)","journal-title":"Science"},{"key":"BFnature16469_CR8","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.molcel.2014.01.011","volume":"53","author":"Y Yang","year":"2014","unstructured":"Yang, Y. et al. Arginine methylation facilitates the recruitment of TOP3B to chromatin to prevent R loop accumulation. Mol. Cell 53, 484\u2013497 (2014)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR9","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.molcel.2010.11.024","volume":"40","author":"Y Yang","year":"2010","unstructured":"Yang, Y. et al. TDRD3 is an effector molecule for arginine-methylated histone marks. Mol. Cell 40, 1016\u20131023 (2010)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR10","doi-asserted-by":"crossref","first-page":"6428","DOI":"10.1038\/ncomms7428","volume":"6","author":"Y Yang","year":"2015","unstructured":"Yang, Y. et al. PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145. Nat. Commun. 6, 6428 (2015)","journal-title":"Nat. Commun."},{"key":"BFnature16469_CR11","doi-asserted-by":"crossref","first-page":"16723","DOI":"10.1074\/jbc.M115.659433","volume":"290","author":"A Hadjikyriacou","year":"2015","unstructured":"Hadjikyriacou, A., Yang, Y., Espejo, A., Bedford, M. T. & Clarke, S. G. Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2. J. Biol. Chem. 290, 16723\u201316743 (2015)","journal-title":"J. Biol. Chem."},{"key":"BFnature16469_CR12","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1093\/nar\/gkg197","volume":"31","author":"P Licciardo","year":"2003","unstructured":"Licciardo, P. et al. The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP. Nucleic Acids Res. 31, 999\u20131005 (2003)","journal-title":"Nucleic Acids Res."},{"key":"BFnature16469_CR13","doi-asserted-by":"crossref","first-page":"17960","DOI":"10.1073\/pnas.1209814109","volume":"109","author":"S Antonysamy","year":"2012","unstructured":"Antonysamy, S. et al. Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl Acad. Sci. USA 109, 17960\u201317965 (2012)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature16469_CR14","doi-asserted-by":"crossref","first-page":"8243","DOI":"10.1074\/jbc.M109984200","volume":"277","author":"WJ Friesen","year":"2002","unstructured":"Friesen, W. J. et al. A novel WD repeat protein component of the methylosome binds Sm proteins. J. Biol. Chem. 277, 8243\u20138247 (2002)","journal-title":"J. Biol. Chem."},{"key":"BFnature16469_CR15","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1038\/nrm3185","volume":"12","author":"C Chen","year":"2011","unstructured":"Chen, C., Nott, T. J., Jin, J. & Pawson, T. Deciphering arginine methylation: Tudor tells the tale. Nature Rev. Mol. Cell Biol. 12, 629\u2013642 (2011)","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"BFnature16469_CR16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2008.12.013","volume":"33","author":"MT Bedford","year":"2009","unstructured":"Bedford, M. T. & Clarke, S. G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33, 1\u201313 (2009)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR17","doi-asserted-by":"crossref","first-page":"11748","DOI":"10.1093\/nar\/gks929","volume":"40","author":"T Sikorsky","year":"2012","unstructured":"Sikorsky, T. et al. Recognition of asymmetrically dimethylated arginine by TDRD3. Nucleic Acids Res. 40, 11748\u201311755 (2012)","journal-title":"Nucleic Acids Res."},{"key":"BFnature16469_CR18","doi-asserted-by":"crossref","first-page":"3384","DOI":"10.1093\/hmg\/ddp278","volume":"18","author":"A Suraweera","year":"2009","unstructured":"Suraweera, A. et al. Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation. Hum. Mol. Genet. 18, 3384\u20133396 (2009)","journal-title":"Hum. Mol. Genet."},{"key":"BFnature16469_CR19","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.molcel.2011.04.026","volume":"42","author":"K Skourti-Stathaki","year":"2011","unstructured":"Skourti-Stathaki, K., Proudfoot, N. J. & Gromak, N. Human senataxin resolves RNA\/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination. Mol. Cell 42, 794\u2013805 (2011)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR20","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/nature03035","volume":"432","author":"S West","year":"2004","unstructured":"West, S., Gromak, N. & Proudfoot, N. J. Human 5\u2032\u21923\u2032 exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432, 522\u2013525 (2004)","journal-title":"Nature"},{"key":"BFnature16469_CR21","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1126\/science.1162228","volume":"322","author":"LJ Core","year":"2008","unstructured":"Core, L. J., Waterfall, J. J. & Lis, J. T . Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters. Science 322, 1845\u20131848 (2008)","journal-title":"Science"},{"key":"BFnature16469_CR22","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1038\/nature13374","volume":"511","author":"V Bhatia","year":"2014","unstructured":"Bhatia, V. et al. BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export factor PCID2. Nature 511, 362\u2013365 (2014)","journal-title":"Nature"},{"key":"BFnature16469_CR23","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1101\/sqb.2006.71.001","volume":"71","author":"DJ Battle","year":"2006","unstructured":"Battle, D. J. et al. The SMN complex: an assembly machine for RNPs. Cold Spring Harb. Symp. Quant. Biol. 71, 313\u2013320 (2006)","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"BFnature16469_CR24","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/nrn2670","volume":"10","author":"AH Burghes","year":"2009","unstructured":"Burghes, A. H. & Beattie, C. E. Spinal muscular atrophy: why do low levels of survival motor neuron protein make motor neurons sick? Nature Rev. Neurosci. 10, 597\u2013609 (2009)","journal-title":"Nature Rev. Neurosci."},{"key":"BFnature16469_CR25","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.cell.2008.03.031","volume":"133","author":"Z Zhang","year":"2008","unstructured":"Zhang, Z. et al. SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell 133, 585\u2013600 (2008)","journal-title":"Cell"},{"key":"BFnature16469_CR26","doi-asserted-by":"crossref","first-page":"e1000773","DOI":"10.1371\/journal.pgen.1000773","volume":"5","author":"D B\u00e4umer","year":"2009","unstructured":"B\u00e4umer, D. et al. Alternative splicing events are a late feature of pathology in a mouse model of spinal muscular atrophy. PLoS Genet. 5, e1000773 (2009)","journal-title":"PLoS Genet."},{"key":"BFnature16469_CR27","doi-asserted-by":"crossref","first-page":"19348","DOI":"10.1073\/pnas.1319280110","volume":"110","author":"Z Zhang","year":"2013","unstructured":"Zhang, Z. et al. Dysregulation of synaptogenesis genes antecedes motor neuron pathology in spinal muscular atrophy. Proc. Natl Acad. Sci. USA 110, 19348\u201319353 (2013)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature16469_CR28","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.cell.2009.03.010","volume":"137","author":"MJ Mu\u00f1oz","year":"2009","unstructured":"Mu\u00f1oz, M. J. et al. DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation. Cell 137, 708\u2013720 (2009)","journal-title":"Cell"},{"key":"BFnature16469_CR29","doi-asserted-by":"crossref","first-page":"13318","DOI":"10.1073\/pnas.1008227107","volume":"107","author":"SC Ling","year":"2010","unstructured":"Ling, S. C. et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS\/TLS. Proc. Natl Acad. Sci. USA 107, 13318\u201313323 (2010)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature16469_CR30","doi-asserted-by":"crossref","first-page":"34097","DOI":"10.1074\/jbc.M110.154831","volume":"285","author":"SH Kim","year":"2010","unstructured":"Kim, S. H., Shanware, N. P., Bowler, M. J. & Tibbetts, R. S. Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS\/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J. Biol. Chem. 285, 34097\u201334105 (2010)","journal-title":"J. Biol. Chem."},{"key":"BFnature16469_CR31","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/j.celrep.2012.08.025","volume":"2","author":"T Yamazaki","year":"2012","unstructured":"Yamazaki, T. et al. FUS\u2013SMN protein interactions link the motor neuron diseases ALS and SMA. Cell Rep . 2, 799\u2013806 (2012)","journal-title":"Cell Rep"},{"key":"BFnature16469_CR32","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1038\/nn.3230","volume":"15","author":"C Lagier-Tourenne","year":"2012","unstructured":"Lagier-Tourenne, C. et al. Divergent roles of ALS-linked proteins FUS\/TLS and TDP-43 intersect in processing long pre-mRNAs. Nature Neurosci. 15, 1488\u20131497 (2012)","journal-title":"Nature Neurosci."},{"key":"BFnature16469_CR33","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/nn.2779","volume":"14","author":"M Polymenidou","year":"2011","unstructured":"Polymenidou, M. et al. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nature Neurosci. 14, 459\u2013468 (2011)","journal-title":"Nature Neurosci."},{"key":"BFnature16469_CR34","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/srep00529","volume":"2","author":"S Ishigaki","year":"2012","unstructured":"Ishigaki, S. et al. Position-dependent FUS\u2013RNA interactions regulate alternative splicing events and transcriptions. Sci. Rep. 2, 529 (2012)","journal-title":"Sci. Rep."},{"key":"BFnature16469_CR35","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1038\/srep00603","volume":"2","author":"B Rogelj","year":"2012","unstructured":"Rogelj, B. et al. Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain. Sci. Rep. 2, 603 (2012)","journal-title":"Sci. Rep."},{"key":"BFnature16469_CR36","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.molcel.2012.04.009","volume":"46","author":"A Aguilera","year":"2012","unstructured":"Aguilera, A. & Garcia-Muse, T. R loops: from transcription byproducts to threats to genome stability. Mol. Cell 46, 115\u2013124 (2012)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR37","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.molcel.2015.01.011","volume":"57","author":"E Hatchi","year":"2015","unstructured":"Hatchi, E. et al. BRCA1 recruitment to transcriptional pause sites is required for R-loop-driven DNA damage repair. Mol. Cell 57, 636\u2013647 (2015)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR38","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/j.molcel.2014.10.020","volume":"56","author":"J Sollier","year":"2014","unstructured":"Sollier, J. et al. Transcription-coupled nucleotide excision repair factors promote R-loop-induced genome instability. Mol. Cell 56, 777\u2013785 (2014)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR39","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1038\/srep01311","volume":"3","author":"S Dhar","year":"2013","unstructured":"Dhar, S. et al. Loss of the major type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs. Sci. Rep. 3, 1311 (2013)","journal-title":"Sci. Rep."},{"key":"BFnature16469_CR40","doi-asserted-by":"crossref","first-page":"9630","DOI":"10.1128\/MCB.24.21.9630-9645.2004","volume":"24","author":"S Pal","year":"2004","unstructured":"Pal, S., Vishwanath, S. N., Erdjument-Bromage, H., Tempst, P. & Sif, S. Human SWI\/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 24, 9630\u20139645 (2004)","journal-title":"Mol. Cell. Biol."},{"key":"BFnature16469_CR41","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1002\/jcp.21180","volume":"213","author":"S Pal","year":"2007","unstructured":"Pal, S. & Sif, S. Interplay between chromatin remodelers and protein arginine methyltransferases. J. Cell. Physiol. 213, 306\u2013315 (2007)","journal-title":"J. Cell. Physiol."},{"key":"BFnature16469_CR42","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/S1097-2765(03)00101-1","volume":"11","author":"YT Kwak","year":"2003","unstructured":"Kwak, Y. T. et al. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol. Cell 11, 1055\u20131066 (2003)","journal-title":"Mol. Cell"},{"key":"BFnature16469_CR43","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1093\/hmg\/6.3.497","volume":"6","author":"K Talbot","year":"1997","unstructured":"Talbot, K. et al. Missense mutation clustering in the survival motor neuron gene: a role for a conserved tyrosine and glycine rich region of the protein in RNA metabolism? Hum. Mol. Genet. 6, 497\u2013500 (1997)","journal-title":"Hum. Mol. Genet."},{"key":"BFnature16469_CR44","doi-asserted-by":"crossref","first-page":"2869","DOI":"10.1093\/hmg\/9.19.2869","volume":"9","author":"PJ Young","year":"2000","unstructured":"Young, P. J. et al. The exon 2b region of the spinal muscular atrophy protein, SMN, is involved in self-association and SIP1 binding. Hum. Mol. Genet. 9, 2869\u20132877 (2000)","journal-title":"Hum. Mol. Genet."},{"key":"BFnature16469_CR45","doi-asserted-by":"crossref","first-page":"re2","DOI":"10.1126\/stke.2712005re2","volume":"2005","author":"FM Boisvert","year":"2005","unstructured":"Boisvert, F. M., Chenard, C. A. & Richard, S. Protein interfaces in signaling regulated by arginine methylation. Sci. STKE 2005, re2 (2005)","journal-title":"Sci. STKE"},{"key":"BFnature16469_CR46","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1074\/mcp.M300088-MCP200","volume":"2","author":"FM Boisvert","year":"2003","unstructured":"Boisvert, F. M., Cote, J., Boulanger, M. C. & Richard, S. A proteomic analysis of arginine-methylated protein complexes. Mol. Cell. Proteomics 2, 1319\u20131330 (2003)","journal-title":"Mol. Cell. Proteomics"},{"key":"BFnature16469_CR47","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1074\/mcp.M112.020743","volume":"11","author":"T Uhlmann","year":"2012","unstructured":"Uhlmann, T. et al. A method for large-scale identification of protein arginine methylation. Mol. Cell. Proteomics 11, 1489\u20131499 (2012)","journal-title":"Mol. Cell. Proteomics"},{"key":"BFnature16469_CR48","doi-asserted-by":"crossref","first-page":"e30375","DOI":"10.1371\/journal.pone.0030375","volume":"7","author":"K Liu","year":"2012","unstructured":"Liu, K. et al. Crystal structure of TDRD3 and methyl-arginine binding characterization of TDRD3, SMN and SPF30. PLoS ONE 7, e30375 (2012)","journal-title":"PLoS ONE"},{"key":"BFnature16469_CR49","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1074\/mcp.M000002-MCP201","volume":"9","author":"AB Mak","year":"2010","unstructured":"Mak, A. B. et al. A lentiviral functional proteomics approach identifies chromatin remodeling complexes important for the induction of pluripotency. Mol. Cell. Proteomics 9, 811\u2013823 (2010)","journal-title":"Mol. Cell. Proteomics"},{"key":"BFnature16469_CR50","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1101\/gad.573310","volume":"24","author":"A El Hage","year":"2010","unstructured":"El Hage, A., French, S. L., Beyer, A. L. & Tollervey, D. Loss of topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis. Genes Dev. 24, 1546\u20131558 (2010)","journal-title":"Genes Dev."},{"key":"BFnature16469_CR51","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0022-1759(86)90040-2","volume":"89","author":"SJ Boguslawski","year":"1986","unstructured":"Boguslawski, S. J. et al. Characterization of monoclonal antibody to DNA.RNA and its application to immunodetection of hybrids. J. Immunol. Methods 89, 123\u2013130 (1986)","journal-title":"J. Immunol. Methods"},{"key":"BFnature16469_CR52","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nsmb1352","volume":"15","author":"K Glover-Cutter","year":"2008","unstructured":"Glover-Cutter, K., Kim, S., Espinosa, J. & Bentley, D. L. RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes. Nature Struct. Mol. Biol . 15, 71\u201378 (2008)","journal-title":"Nature Struct. Mol. Biol"},{"key":"BFnature16469_CR53","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.ymeth.2009.03.001","volume":"48","author":"D Schmidt","year":"2009","unstructured":"Schmidt, D. et al. ChIP-seq: using high-throughput sequencing to discover protein\u2013DNA interactions. Methods 48, 240\u2013248 (2009)","journal-title":"Methods"},{"key":"BFnature16469_CR54","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1101\/gr.177790.114","volume":"24","author":"U Braunschweig","year":"2014","unstructured":"Braunschweig, U. et al. Widespread intron retention in mammals functionally tunes transcriptomes. Genome Res. 24, 1774\u20131786 (2014)","journal-title":"Genome Res."},{"key":"BFnature16469_CR55","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/nmeth.1923","volume":"9","author":"B Langmead","year":"2012","unstructured":"Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nature Methods 9, 357\u2013359 (2012)","journal-title":"Nature Methods"},{"key":"BFnature16469_CR56","doi-asserted-by":"crossref","first-page":"1684","DOI":"10.1128\/MCB.22.6.1684-1692.2002","volume":"22","author":"K Ryan","year":"2002","unstructured":"Ryan, K., Murthy, K. G., Kaneko, S. & Manley, J. L. Requirements of the RNA polymerase II C-terminal domain for reconstituting pre-mRNA 3\u2032 cleavage. Mol. Cell. Biol. 22, 1684\u20131692 (2002)","journal-title":"Mol. Cell. Biol."}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature16469.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature16469","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature16469.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T13:49:00Z","timestamp":1684417740000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature16469"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,12,23]]},"references-count":56,"journal-issue":{"issue":"7584","published-print":{"date-parts":[[2016,1]]}},"alternative-id":["BFnature16469"],"URL":"https:\/\/doi.org\/10.1038\/nature16469","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.726037485.793517540","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.726037485.793513041","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.726037485.793517959","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.726037485.793518689","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12,23]]},"assertion":[{"value":"6 January 2014","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 November 2015","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 December 2015","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}