{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:31:50Z","timestamp":1791207110669,"version":"4.1.0"},"reference-count":60,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2015,1,27]],"date-time":"2015-01-27T00:00:00Z","timestamp":1422316800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2015,1,27]],"date-time":"2015-01-27T00:00:00Z","timestamp":1422316800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"DOI":"10.1038\/ncomms7171","type":"journal-article","created":{"date-parts":[[2015,1,27]],"date-time":"2015-01-27T09:52:18Z","timestamp":1422352338000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":216,"title":["ALS-causative mutations in FUS\/TLS confer gain and loss of function by altered association with SMN and U1-snRNP"],"prefix":"10.1038","volume":"6","author":[{"given":"Shuying","family":"Sun","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuo-Chien","family":"Ling","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinsong","family":"Qiu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudio P.","family":"Albuquerque","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seiya","family":"Tokunaga","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hairi","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haiyan","family":"Qiu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anh","family":"Bui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gene W.","family":"Yeo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric J.","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin","family":"Eggan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huilin","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang-Dong","family":"Fu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clotilde","family":"Lagier-Tourenne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Don W.","family":"Cleveland","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,1,27]]},"reference":[{"key":"BFncomms7171_CR1","doi-asserted-by":"publisher","first-page":"R46","DOI":"10.1093\/hmg\/ddq137","volume":"19","author":"C Lagier-Tourenne","year":"2010","unstructured":"Lagier-Tourenne, C., Polymenidou, M. & Cleveland, D. W. TDP-43 and FUS\/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 19, R46\u2013R64 (2010).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR2","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1126\/science.1166066","volume":"323","author":"TJ Kwiatkowski Jr","year":"2009","unstructured":"Kwiatkowski, T. J. Jr et al. Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205\u20131208 (2009).","journal-title":"Science"},{"key":"BFncomms7171_CR3","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1126\/science.1165942","volume":"323","author":"C Vance","year":"2009","unstructured":"Vance, C. et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323, 1208\u20131211 (2009).","journal-title":"Science"},{"key":"BFncomms7171_CR4","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1038\/ng.132","volume":"40","author":"E Kabashi","year":"2008","unstructured":"Kabashi, E. et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 40, 572\u2013574 (2008).","journal-title":"Nat. Genet."},{"key":"BFncomms7171_CR5","doi-asserted-by":"publisher","first-page":"1668","DOI":"10.1126\/science.1154584","volume":"319","author":"J Sreedharan","year":"2008","unstructured":"Sreedharan, J. et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1668\u20131672 (2008).","journal-title":"Science"},{"key":"BFncomms7171_CR6","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","volume":"351","author":"T Arai","year":"2006","unstructured":"Arai, T. et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602\u2013611 (2006).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BFncomms7171_CR7","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1126\/science.1134108","volume":"314","author":"M Neumann","year":"2006","unstructured":"Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130\u2013133 (2006).","journal-title":"Science"},{"key":"BFncomms7171_CR8","doi-asserted-by":"publisher","first-page":"904","DOI":"10.1016\/j.conb.2011.05.029","volume":"21","author":"S Da Cruz","year":"2011","unstructured":"Da Cruz, S. & Cleveland, D. W. Understanding the role of TDP-43 and FUS\/TLS in ALS and beyond. Curr. Opin. Neurobiol. 21, 904\u2013919 (2011).","journal-title":"Curr. Opin. Neurobiol."},{"key":"BFncomms7171_CR9","doi-asserted-by":"publisher","first-page":"2841","DOI":"10.1038\/emboj.2010.143","volume":"29","author":"D Dormann","year":"2010","unstructured":"Dormann, D. et al. ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J. 29, 2841\u20132857 (2010).","journal-title":"EMBO J."},{"key":"BFncomms7171_CR10","doi-asserted-by":"publisher","first-page":"995","DOI":"10.1016\/S1474-4422(10)70195-2","volume":"9","author":"IR Mackenzie","year":"2010","unstructured":"Mackenzie, I. R., Rademakers, R. & Neumann, M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol. 9, 995\u20131007 (2010).","journal-title":"Lancet Neurol."},{"key":"BFncomms7171_CR11","doi-asserted-by":"publisher","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. Nat. Neurosci. 15, 1488\u20131497 (2012).","journal-title":"Nat. Neurosci."},{"key":"BFncomms7171_CR12","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1038\/srep00529","volume":"2","author":"S Ishigaki","year":"2012","unstructured":"Ishigaki, S. et al. Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions. Sci. Rep. 2, 529 (2012).","journal-title":"Sci. Rep."},{"key":"BFncomms7171_CR13","doi-asserted-by":"publisher","first-page":"1428","DOI":"10.1038\/nsmb.2163","volume":"18","author":"JI Hoell","year":"2011","unstructured":"Hoell, J. I. et al. RNA targets of wild-type and mutant FET family proteins. Nat. Struct. Mol. Biol. 18, 1428\u20131431 (2011).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFncomms7171_CR14","doi-asserted-by":"publisher","first-page":"15635","DOI":"10.1074\/jbc.M111.333450","volume":"287","author":"C Colombrita","year":"2012","unstructured":"Colombrita, C. et al. TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells. J. Biol. Chem. 287, 15635\u201315647 (2012).","journal-title":"J. Biol. Chem."},{"key":"BFncomms7171_CR15","doi-asserted-by":"publisher","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":"BFncomms7171_CR16","doi-asserted-by":"publisher","first-page":"498","DOI":"10.1261\/rna.037804.112","volume":"19","author":"T Nakaya","year":"2013","unstructured":"Nakaya, T., Alexiou, P., Maragkakis, M., Chang, A. & Mourelatos, Z. FUS regulates genes coding for RNA-binding proteins in neurons by binding to their highly conserved introns. RNA 19, 498\u2013509 (2013).","journal-title":"RNA"},{"key":"BFncomms7171_CR17","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1016\/j.ceb.2009.02.004","volume":"21","author":"A Chari","year":"2009","unstructured":"Chari, A., Paknia, E. & Fischer, U. The role of RNP biogenesis in spinal muscular atrophy. Curr. Opin. Cell Biol. 21, 387\u2013393 (2009).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFncomms7171_CR18","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/j.tcb.2004.03.010","volume":"14","author":"J Yong","year":"2004","unstructured":"Yong, J., Wan, L. & Dreyfuss, G. Why do cells need an assembly machine for RNA-protein complexes? Trends Cell Biol. 14, 226\u2013232 (2004).","journal-title":"Trends Cell Biol."},{"key":"BFncomms7171_CR19","doi-asserted-by":"publisher","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":"BFncomms7171_CR20","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1016\/S0962-8924(02)02371-1","volume":"12","author":"G Meister","year":"2002","unstructured":"Meister, G., Eggert, C. & Fischer, U. SMN-mediated assembly of RNPs: a complex story. Trends Cell Biol. 12, 472\u2013478 (2002).","journal-title":"Trends Cell Biol."},{"key":"BFncomms7171_CR21","doi-asserted-by":"publisher","first-page":"a003707","DOI":"10.1101\/cshperspect.a003707","volume":"3","author":"CL Will","year":"2011","unstructured":"Will, C. L. & Luhrmann, R. Spliceosome structure and function. Cold Spring Harb. Perspect. Biol. 3, a003707 (2011).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"BFncomms7171_CR22","doi-asserted-by":"publisher","first-page":"5543","DOI":"10.1128\/MCB.25.13.5543-5551.2005","volume":"25","author":"L Wan","year":"2005","unstructured":"Wan, L. et al. The survival of motor neurons protein determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy. Mol. Cell. Biol. 25, 5543\u20135551 (2005).","journal-title":"Mol. Cell. Biol."},{"key":"BFncomms7171_CR23","doi-asserted-by":"publisher","first-page":"17372","DOI":"10.1073\/pnas.0508947102","volume":"102","author":"KB Shpargel","year":"2005","unstructured":"Shpargel, K. B. & Matera, A. G. Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins. Proc. Natl Acad. Sci. USA 102, 17372\u201317377 (2005).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms7171_CR24","doi-asserted-by":"publisher","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":"BFncomms7171_CR25","doi-asserted-by":"publisher","first-page":"440","DOI":"10.1016\/j.cell.2012.09.012","volume":"151","author":"F Lotti","year":"2012","unstructured":"Lotti, F. et al. An SMN-dependent U12 splicing event essential for motor circuit function. Cell 151, 440\u2013454 (2012).","journal-title":"Cell"},{"key":"BFncomms7171_CR26","doi-asserted-by":"publisher","first-page":"2320","DOI":"10.1101\/gad.342005","volume":"19","author":"C Winkler","year":"2005","unstructured":"Winkler, C. et al. Reduced U snRNP assembly causes motor axon degeneration in an animal model for spinal muscular atrophy. Genes Dev. 19, 2320\u20132330 (2005).","journal-title":"Genes Dev."},{"key":"BFncomms7171_CR27","doi-asserted-by":"publisher","first-page":"e921","DOI":"10.1371\/journal.pone.0000921","volume":"2","author":"F Gabanella","year":"2007","unstructured":"Gabanella, F. et al. Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs. PLoS ONE 2, e921 (2007).","journal-title":"PLoS ONE"},{"key":"BFncomms7171_CR28","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1093\/hmg\/9.1.47","volume":"9","author":"S Pagliardini","year":"2000","unstructured":"Pagliardini, S. et al. Subcellular localization and axonal transport of the survival motor neuron (SMN) protein in the developing rat spinal cord. Hum. Mol. Genet. 9, 47\u201356 (2000).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR29","doi-asserted-by":"publisher","first-page":"16325","DOI":"10.1073\/pnas.1003459107","volume":"107","author":"X Shan","year":"2010","unstructured":"Shan, X., Chiang, P. M., Price, D. L. & Wong, P. C. Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl Acad. Sci. USA 107, 16325\u201316330 (2010).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms7171_CR30","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1097\/NEN.0b013e318244b635","volume":"71","author":"B Gertz","year":"2012","unstructured":"Gertz, B., Wong, M. & Martin, L. J. Nuclear localization of human SOD1 and mutant SOD1-specific disruption of survival motor neuron protein complex in transgenic amyotrophic lateral sclerosis mice. J. Neuropathol. Exp. Neurol. 71, 162\u2013177 (2012).","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"BFncomms7171_CR31","doi-asserted-by":"publisher","first-page":"3421","DOI":"10.1093\/hmg\/dds174","volume":"21","author":"S Kariya","year":"2012","unstructured":"Kariya, S. et al. Mutant superoxide dismutase 1 (SOD1), a cause of amyotrophic lateral sclerosis, disrupts the recruitment of SMN, the spinal muscular atrophy protein to nuclear Cajal bodies. Hum. Mol. Genet. 21, 3421\u20133434 (2012).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR32","doi-asserted-by":"publisher","first-page":"4136","DOI":"10.1093\/hmg\/ddt262","volume":"22","author":"T Ishihara","year":"2013","unstructured":"Ishihara, T. et al. Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis. Hum. Mol. Genet. 22, 4136\u20134147 (2013).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR33","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1016\/j.celrep.2012.08.025","volume":"2","author":"T Yamazaki","year":"2012","unstructured":"Yamazaki, T. et al. FUS-SMN protein interactions link the motor neuron diseases ALS and SMA. Cell Rep. 2, 799\u2013806 (2012).","journal-title":"Cell Rep."},{"key":"BFncomms7171_CR34","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1002\/emmm.201202303","volume":"5","author":"H Tsuiji","year":"2013","unstructured":"Tsuiji, H. et al. Spliceosome integrity is defective in the motor neuron diseases ALS and SMA. EMBO Mol. Med. 5, 221\u2013234 (2013).","journal-title":"EMBO Mol. Med."},{"key":"BFncomms7171_CR35","doi-asserted-by":"publisher","first-page":"3690","DOI":"10.1093\/hmg\/ddt222","volume":"22","author":"EJ Groen","year":"2013","unstructured":"Groen, E. J. et al. ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN. Hum. Mol. Genet. 22, 3690\u20133704 (2013).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR36","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1016\/j.nbd.2013.03.003","volume":"55","author":"V Gerbino","year":"2013","unstructured":"Gerbino, V., Carri, M. T., Cozzolino, M. & Achsel, T. Mislocalised FUS mutants stall spliceosomal snRNPs in the cytoplasm. Neurobiol. Dis. 55, 120\u2013128 (2013).","journal-title":"Neurobiol. Dis."},{"key":"BFncomms7171_CR37","doi-asserted-by":"publisher","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":"BFncomms7171_CR38","doi-asserted-by":"publisher","first-page":"e1003895","DOI":"10.1371\/journal.pgen.1003895","volume":"9","author":"Y Zhou","year":"2013","unstructured":"Zhou, Y., Liu, S., Liu, G., Ozturk, A. & Hicks, G. G. ALS-associated FUS mutations result in compromised FUS alternative splicing and autoregulation. PLoS Genet. 9, e1003895 (2013).","journal-title":"PLoS Genet."},{"key":"BFncomms7171_CR39","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1111\/j.2517-6161.1995.tb02031.x","volume":"57","author":"Y Benjamini","year":"1995","unstructured":"Benjamini, Y. & Hochberg, Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R Statist. Soc. Ser. B 57, 289\u2013300 (1995).","journal-title":"J. R Statist. Soc. Ser. B"},{"key":"BFncomms7171_CR40","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1093\/hmg\/ddr448","volume":"21","author":"ML Tradewell","year":"2012","unstructured":"Tradewell, M. L. et al. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS\/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 21, 136\u2013149 (2012).","journal-title":"Hum. Mol. Genet."},{"key":"BFncomms7171_CR41","doi-asserted-by":"publisher","first-page":"R666","DOI":"10.1016\/j.cub.2010.05.056","volume":"20","author":"P Lasko","year":"2010","unstructured":"Lasko, P. Tudor domain. Curr. Biol. 20, R666\u2013R667 (2010).","journal-title":"Curr. Biol."},{"key":"BFncomms7171_CR42","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.molbrainres.2003.08.011","volume":"119","author":"PJ Young","year":"2003","unstructured":"Young, P. J. et al. The Ewing's sarcoma protein interacts with the Tudor domain of the survival motor neuron protein. Brain Res. Mol. Brain Res. 119, 37\u201349 (2003).","journal-title":"Brain Res. Mol. Brain Res."},{"key":"BFncomms7171_CR43","doi-asserted-by":"publisher","first-page":"3555","DOI":"10.1002\/j.1460-2075.1996.tb00725.x","volume":"15","author":"Q Liu","year":"1996","unstructured":"Liu, Q. & Dreyfuss, G. A novel nuclear structure containing the survival of motor neurons protein. EMBO J. 15, 3555\u20133565 (1996).","journal-title":"EMBO J."},{"key":"BFncomms7171_CR44","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1086\/301992","volume":"63","author":"AG Matera","year":"1998","unstructured":"Matera, A. G. & Frey, M. R. Coiled bodies and gems: Janus or gemini? Am. J. Hum. Genet. 63, 317\u2013321 (1998).","journal-title":"Am. J. Hum. Genet."},{"key":"BFncomms7171_CR45","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1083\/jcb.147.4.715","volume":"147","author":"T Carvalho","year":"1999","unstructured":"Carvalho, T. et al. The spinal muscular atrophy disease gene product, SMN: a link between snRNP biogenesis and the Cajal (coiled) body. J. Cell Biol. 147, 715\u2013728 (1999).","journal-title":"J. Cell Biol."},{"key":"BFncomms7171_CR46","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1146\/annurev.cellbio.20.010403.103738","volume":"21","author":"M Cioce","year":"2005","unstructured":"Cioce, M. & Lamond, A. I. Cajal bodies: a long history of discovery. Annu. Rev. Cell Dev. Biol. 21, 105\u2013131 (2005).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFncomms7171_CR47","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1172\/JCI72723","volume":"124","author":"H Qiu","year":"2014","unstructured":"Qiu, H. et al. ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects. J. Clin. Invest. 124, 981\u2013999 (2014).","journal-title":"J. Clin. Invest."},{"key":"BFncomms7171_CR48","doi-asserted-by":"publisher","first-page":"664","DOI":"10.1038\/nature09479","volume":"468","author":"D Kaida","year":"2010","unstructured":"Kaida, D. et al. U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation. Nature 468, 664\u2013668 (2010).","journal-title":"Nature"},{"key":"BFncomms7171_CR49","first-page":"11","volume":"Chapter 4","author":"H Li","year":"2012","unstructured":"Li, H., Qiu, J. & Fu, X. D. RASL-seq for massively parallel and quantitative analysis of gene expression. Curr. Protoc. Mol. Biol. Chapter 4, Unit 4 1311\u201319 (2012).","journal-title":"Curr. Protoc. Mol. Biol."},{"key":"BFncomms7171_CR50","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1016\/j.molcel.2012.05.014","volume":"47","author":"Z Zhou","year":"2012","unstructured":"Zhou, Z. et al. The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus. Mol. Cell 47, 422\u2013433 (2012).","journal-title":"Mol. Cell"},{"key":"BFncomms7171_CR51","doi-asserted-by":"publisher","first-page":"2720","DOI":"10.1101\/gad.908401","volume":"15","author":"MD Hebert","year":"2001","unstructured":"Hebert, M. D., Szymczyk, P. W., Shpargel, K. B. & Matera, A. G. Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein. Genes Dev. 15, 2720\u20132729 (2001).","journal-title":"Genes Dev."},{"key":"BFncomms7171_CR52","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1083\/jcb.201302044","volume":"201","author":"YR Li","year":"2013","unstructured":"Li, Y. R., King, O. D., Shorter, J. & Gitler, A. D. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201, 361\u2013372 (2013).","journal-title":"J. Cell Biol."},{"key":"BFncomms7171_CR53","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1007\/s00401-012-1020-6","volume":"124","author":"M Neumann","year":"2012","unstructured":"Neumann, M. et al. Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol. 124, 705\u2013716 (2012).","journal-title":"Acta Neuropathol."},{"key":"BFncomms7171_CR54","doi-asserted-by":"publisher","first-page":"436","DOI":"10.3109\/17482960902759162","volume":"10","author":"P Corcia","year":"2009","unstructured":"Corcia, P. et al. The importance of the SMN genes in the genetics of sporadic ALS. Amyotroph. Lateral Scler. 10, 436\u2013440 (2009).","journal-title":"Amyotroph. Lateral Scler."},{"key":"BFncomms7171_CR55","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1212\/WNL.0b013e3181ed9cde","volume":"75","author":"D Baumer","year":"2010","unstructured":"Baumer, D. et al. Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75, 611\u2013618 (2010).","journal-title":"Neurology"},{"key":"BFncomms7171_CR56","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1001\/archneurol.2011.2499","volume":"69","author":"VV Belzil","year":"2012","unstructured":"Belzil, V. V. et al. Novel FUS deletion in a patient with juvenile amyotrophic lateral sclerosis. Arch. Neurol. 69, 653\u2013656 (2012).","journal-title":"Arch. Neurol."},{"key":"BFncomms7171_CR57","doi-asserted-by":"publisher","first-page":"E736","DOI":"10.1073\/pnas.1222809110","volume":"110","author":"ES Arnold","year":"2013","unstructured":"Arnold, E. S. et al. ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43. Proc. Natl Acad. Sci. USA 110, E736\u2013E745 (2013).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms7171_CR58","doi-asserted-by":"publisher","first-page":"282","DOI":"10.1074\/mcp.M700342-MCP200","volume":"7","author":"U Rothbauer","year":"2008","unstructured":"Rothbauer, U. et al. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteom. 7, 282\u2013289 (2008).","journal-title":"Mol. Cell. Proteom."},{"key":"BFncomms7171_CR59","doi-asserted-by":"publisher","first-page":"R25","DOI":"10.1186\/gb-2009-10-3-r25","volume":"10","author":"B Langmead","year":"2009","unstructured":"Langmead, B., Trapnell, C., Pop, M. & Salzberg, S. L. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome. Biol. 10, R25 (2009).","journal-title":"Genome. Biol."},{"key":"BFncomms7171_CR60","doi-asserted-by":"publisher","first-page":"14863","DOI":"10.1073\/pnas.95.25.14863","volume":"95","author":"MB Eisen","year":"1998","unstructured":"Eisen, M. B., Spellman, P. T., Brown, P. O. & Botstein, D. Cluster analysis and display of genome-wide expression patterns. Proc. Natl Acad. Sci. USA 95, 14863\u201314868 (1998).","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/ncomms7171.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/ncomms7171","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/ncomms7171.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,6]],"date-time":"2024-06-06T17:12:17Z","timestamp":1717693937000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ncomms7171"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,1,27]]},"references-count":60,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2015,5,5]]}},"alternative-id":["BFncomms7171"],"URL":"https:\/\/doi.org\/10.1038\/ncomms7171","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,1,27]]},"assertion":[{"value":"8 March 2014","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 December 2014","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 January 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"}}],"article-number":"6171"}}