{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T22:37:14Z","timestamp":1790807834416,"version":"4.1.0"},"reference-count":53,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2013,4,19]],"date-time":"2013-04-19T00:00:00Z","timestamp":1366329600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0061576","type":"journal-article","created":{"date-parts":[[2013,4,19]],"date-time":"2013-04-19T21:09:41Z","timestamp":1366405781000},"page":"e61576","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":105,"title":["Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo"],"prefix":"10.1371","volume":"8","author":[{"given":"Chiara","family":"Scaramuzzino","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Monaghan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carmelo","family":"Milioto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas A.","family":"Lanson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Astha","family":"Maltare","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanya","family":"Aggarwal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian","family":"Casci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank O.","family":"Fackelmayer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Pennuto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Udai Bhan","family":"Pandey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2013,4,19]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nrn1971","article-title":"Molecular biology of amyotrophic lateral sclerosis: insights from genetics","volume":"7","author":"P Pasinelli","year":"2006","journal-title":"Nat Rev Neurosci"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1750-1172-4-3","article-title":"Amyotrophic lateral sclerosis","volume":"4","author":"LC Wijesekera","year":"2009","journal-title":"Orphanet J Rare Dis"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1111\/j.1460-9568.2010.07260.x","article-title":"The neurobiology of amyotrophic lateral sclerosis","volume":"31","author":"A Bento-Abreu","year":"2010","journal-title":"Eur J Neurosci"},{"key":"ref4","first-page":"65","article-title":"Genetics of familial Amyotrophic lateral sclerosis","volume":"149","author":"N Ticozzi","year":"2011","journal-title":"Arch Ital Biol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1126\/science.1166066","article-title":"Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis","volume":"323","author":"TJ Kwiatkowski Jr","year":"2009","journal-title":"Science"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"C Vance","year":"2009","journal-title":"Science"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1038\/ng1742","article-title":"ANG mutations segregate with familial and \u2018sporadic\u2019 amyotrophic lateral sclerosis","volume":"38","author":"MJ Greenway","year":"2006","journal-title":"Nat Genet"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/ana.21344","article-title":"TDP-43 A315T mutation in familial motor neuron disease","volume":"63","author":"MA Gitcho","year":"2008","journal-title":"Ann Neurol"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/ng.132","article-title":"TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis","volume":"40","author":"E Kabashi","year":"2008","journal-title":"Nat Genet"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1126\/science.1154584","article-title":"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"319","author":"J Sreedharan","year":"2008","journal-title":"Science"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1002\/ana.21392","article-title":"TDP-43 mutation in familial amyotrophic lateral sclerosis","volume":"63","author":"A Yokoseki","year":"2008","journal-title":"Ann Neurol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"R46","DOI":"10.1093\/hmg\/ddq137","article-title":"TDP-43 and FUS\/TLS: emerging roles in RNA processing and neurodegeneration","volume":"19","author":"C Lagier-Tourenne","year":"2010","journal-title":"Hum Mol Genet"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1002\/wrna.111","article-title":"RNA-binding proteins in neurodegenerative disease: TDP-43 and beyond","volume":"3","author":"KA Hanson","year":"2012","journal-title":"Wiley Interdiscip Rev RNA"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1093\/jmcb\/mjp025","article-title":"The TET family of proteins: functions and roles in disease","volume":"1","author":"AY Tan","year":"2009","journal-title":"J Mol Cell Biol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/geno.1996.0513","article-title":"Expression patterns of the human sarcoma-associated genes FUS and EWS and the genomic structure of FUS","volume":"37","author":"P Aman","year":"1996","journal-title":"Genomics"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"4160","DOI":"10.1093\/hmg\/ddq335","article-title":"Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules","volume":"19","author":"DA Bosco","year":"2010","journal-title":"Hum Mol Genet"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1002\/ana.22246","article-title":"Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS\/TLS","volume":"69","author":"D Ito","year":"2011","journal-title":"Ann Neurol"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1093\/nar\/gkq1162","article-title":"Intracellular localization and splicing regulation of FUS\/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations","volume":"39","author":"Y Kino","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"ref19","article-title":"RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations","author":"JG Daigle","year":"2013","journal-title":"Hum Mol Genet"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"2510","DOI":"10.1093\/hmg\/ddr150","article-title":"A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43","volume":"20","author":"NA Lanson Jr","year":"2011","journal-title":"Hum Mol Genet"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.tibs.2005.10.002","article-title":"Protein arginine methyltransferases: guardians of the Arg?","volume":"30","author":"FO Fackelmayer","year":"2005","journal-title":"Trends Biochem Sci"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2008.12.013","article-title":"Protein arginine methylation in mammals: who, what, and why","volume":"33","author":"MT Bedford","year":"2009","journal-title":"Mol Cell"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1210\/me.2008-0380","article-title":"Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation","volume":"23","author":"YH Lee","year":"2009","journal-title":"Mol Endocrinol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"2109","DOI":"10.1007\/s00018-009-0010-x","article-title":"The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans","volume":"66","author":"SS Wolf","year":"2009","journal-title":"Cell Mol Life Sci"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"3107","DOI":"10.1021\/ac026283q","article-title":"Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode","volume":"75","author":"J Rappsilber","year":"2003","journal-title":"Anal Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/j.bbrc.2010.12.097","article-title":"TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation","volume":"404","author":"K Du","year":"2011","journal-title":"Biochem Biophys Res Commun"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"e49267","DOI":"10.1371\/journal.pone.0049267","article-title":"The Effect of PRMT1-Mediated Arginine Methylation on the Subcellular Localization, Stress Granules, and Detergent-Insoluble Aggregates of FUS\/TLS","volume":"7","author":"A Yamaguchi","year":"2012","journal-title":"PLoS One"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"4258","DOI":"10.1038\/emboj.2012.261","article-title":"Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS","volume":"31","author":"D Dormann","year":"2012","journal-title":"EMBO J"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1093\/hmg\/ddr448","article-title":"Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS\/TLS harbouring ALS-linked mutations","volume":"21","author":"ML Tradewell","year":"2012","journal-title":"Hum Mol Genet"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"32890","DOI":"10.1074\/jbc.M506944200","article-title":"PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family","volume":"280","author":"J Lee","year":"2005","journal-title":"J Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.brainres.2007.03.086","article-title":"Specific regional distribution of protein arginine methyltransferase 8 (PRMT8) in the mouse brain","volume":"1155","author":"T Taneda","year":"2007","journal-title":"Brain Res"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1016\/j.neuroscience.2009.06.061","article-title":"The distribution and characterization of endogenous protein arginine N-methyltransferase 8 in mouse CNS","volume":"163","author":"A Kousaka","year":"2009","journal-title":"Neuroscience"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1097\/00001756-199109000-00002","article-title":"Embryonic mouse spinal cord motor neuron hybrid cells","volume":"2","author":"EF Salazar-Grueso","year":"1991","journal-title":"Neuroreport"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1093\/hmg\/ddm109","article-title":"Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity","volume":"16","author":"I Palazzolo","year":"2007","journal-title":"Hum Mol Genet"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.1002\/jnr.22389","article-title":"B2 attenuates polyglutamine-expanded androgen receptor toxicity in cell and fly models of spinal and bulbar muscular atrophy","volume":"88","author":"I Palazzolo","year":"2010","journal-title":"J Neurosci Res"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1038\/nature05853","article-title":"HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS","volume":"447","author":"UB Pandey","year":"2007","journal-title":"Nature"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1242\/jcs.039933","article-title":"Human protein arginine methyltransferases in vivo\u2013distinct properties of eight canonical members of the PRMT family","volume":"122","author":"F Herrmann","year":"2009","journal-title":"J Cell Sci"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"30888","DOI":"10.1074\/jbc.M505831200","article-title":"Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions","volume":"280","author":"AE McBride","year":"2005","journal-title":"J Biol Chem"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1128\/EC.00074-07","article-title":"Protein arginine methylation in Candida albicans: role in nuclear transport","volume":"6","author":"AE McBride","year":"2007","journal-title":"Eukaryot Cell"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1126\/science.1067122","article-title":"Toxic proteins in neurodegenerative disease","volume":"296","author":"JP Taylor","year":"2002","journal-title":"Science"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1172\/JCI24761","article-title":"The genetic epidemiology of neurodegenerative disease","volume":"115","author":"L Bertram","year":"2005","journal-title":"J Clin Invest"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"M Arrasate","year":"2004","journal-title":"Nature"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1212\/WNL.0b013e3181bbfeef","article-title":"Mutations in FUS cause FALS and SALS in French and French Canadian populations","volume":"73","author":"VV Belzil","year":"2009","journal-title":"Neurology"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1007\/s00401-009-0581-5","article-title":"Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease","volume":"118","author":"M Neumann","year":"2009","journal-title":"Acta Neuropathol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1136\/jmg.2009.071027","article-title":"Mutations of FUS gene in sporadic amyotrophic lateral sclerosis","volume":"47","author":"L Corrado","year":"2010","journal-title":"J Med Genet"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"C Vance","year":"2009","journal-title":"Science"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"2922","DOI":"10.1093\/brain\/awp214","article-title":"A new subtype of frontotemporal lobar degeneration with FUS pathology","volume":"132","author":"M Neumann","year":"2009","journal-title":"Brain"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/j.bbrc.2005.02.018","article-title":"Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1","volume":"329","author":"N Araya","year":"2005","journal-title":"Biochem Biophys Res Commun"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1016\/j.yexcr.2008.12.008","article-title":"PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function","volume":"315","author":"L Jobert","year":"2009","journal-title":"Exp Cell Res"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/72842","article-title":"Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death","volume":"24","author":"GG Hicks","year":"2000","journal-title":"Nat Genet"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1093\/emboj\/19.3.453","article-title":"Male sterility and enhanced radiation sensitivity in TLS(\u2212\/\u2212) mice","volume":"19","author":"M Kuroda","year":"2000","journal-title":"EMBO J"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"5022","DOI":"10.1002\/j.1460-2075.1996.tb00882.x","article-title":"hTAF(II)68, a novel RNA\/ssDNA-binding protein with homology to the pro-oncoproteins TLS\/FUS and EWS is associated with both TFIID and RNA polymerase II","volume":"15","author":"A Bertolotti","year":"1996","journal-title":"EMBO J"},{"key":"ref53","first-page":"2323 e2327","article-title":"Nuclear localization sequence of FUS and induction of stress granules by ALS mutants","volume":"32","author":"J Gal","year":"2011","journal-title":"Neurobiol Aging"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0061576","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,7,12]],"date-time":"2019-07-12T21:27:14Z","timestamp":1562966834000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0061576"}},"subtitle":[],"editor":[{"given":"Diego E.","family":"Rincon-Limas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,4,19]]},"references-count":53,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2013,4,19]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0061576","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,4,19]]}}}