{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T05:30:16Z","timestamp":1790487016547,"version":"4.1.0"},"reference-count":52,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2003,11,1]],"date-time":"2003-11-01T00:00:00Z","timestamp":1067644800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Experimental Neurology"],"published-print":{"date-parts":[[2003,11]]},"DOI":"10.1016\/j.expneurol.2003.07.004","type":"journal-article","created":{"date-parts":[[2003,10,31]],"date-time":"2003-10-31T09:44:47Z","timestamp":1067593487000},"page":"436-446","source":"Crossref","is-referenced-by-count":96,"title":["SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease"],"prefix":"10.1016","volume":"184","author":[{"given":"D.L","family":"Pountney","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R.J","family":"Burns","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E","family":"Haan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.D","family":"Thompson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.C","family":"Blumbergs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W.P","family":"Gai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.expneurol.2003.07.004_BIB1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0960-9822(01)00650-9","article-title":"Directed proteomic analysis of the human nucleolus","volume":"12","author":"Andersen","year":"2002","journal-title":"Curr. Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB2","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the ubiquitin-proteasome system by protein aggregation","volume":"292","author":"Bence","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB3","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/S1097-2765(02)00699-8","article-title":"SUMO-1 protease-1 regulates gene transcription through PML","volume":"10","author":"Best","year":"2002","journal-title":"Mol. Cell."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB4","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1083\/jcb.152.5.1099","article-title":"The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body","volume":"152","author":"Boisvert","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB5","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1126\/science.1077209","article-title":"Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism","volume":"299","author":"Bonifati","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB6","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/S1097-2765(00)80133-1","article-title":"SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation","volume":"2","author":"Desterro","year":"1998","journal-title":"Mol. Cell"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB7","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB8","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s004010050975","article-title":"Nuclear inclusions in spinocerebellar ataxia type 1","volume":"97","author":"Duyckaerts","year":"1999","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB9","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1139\/o02-079","article-title":"The promyelocytic leukemia nuclear body","volume":"80","author":"Eskiw","year":"2002","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB10","doi-asserted-by":"crossref","first-page":"6185","DOI":"10.1093\/emboj\/19.22.6185","article-title":"Regulation of p53 activity in nuclear bodies by a specific PML isoform","volume":"19","author":"Fogal","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB11","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB12","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1111\/j.1755-3768.1986.tb00680.x","article-title":"Neuronal intranuclear inclusion disease","volume":"64","author":"Haltia","year":"1986","journal-title":"Acta Ophthalmol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB13","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/S0968-0004(01)01849-7","article-title":"Protein modification by SUMO","volume":"26","author":"Hay","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB14","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1086\/301991","article-title":"Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies","volume":"63","author":"Hodges","year":"1998","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB15","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0022-510X(96)00024-X","article-title":"Age-related ubiquitin-positive granular structures in non-demented subjects and neurodegenerative disorders","volume":"142","author":"Iseki","year":"1996","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB16","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/j.1365-2990.1979.tb00630.x","article-title":"Widespread intranuclear neuronal corpuscles (Marinesco bodies) associated with a familial spinal degeneration with cranial and nerve involvement","volume":"5","author":"Janota","year":"1979","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB17","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/S0962-8924(00)01785-2","article-title":"Ubiquitin and its kin","volume":"10","author":"Jentsch","year":"2000","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB18","doi-asserted-by":"crossref","first-page":"3449","DOI":"10.1038\/sj.onc.1204446","article-title":"DNA microarray analysis of genes involved in P53 mediated apoptosis","volume":"20","author":"Kannan","year":"2001","journal-title":"Oncogene"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB19","doi-asserted-by":"crossref","first-page":"14102","DOI":"10.1074\/jbc.275.19.14102","article-title":"A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs","volume":"275","author":"Kim","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB20","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0022-510X(98)00169-5","article-title":"Familial neuronal intranuclear inclusion disease with ubiquitin positive inclusions","volume":"160","author":"Kimber","year":"1998","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB21","doi-asserted-by":"crossref","first-page":"2771","DOI":"10.1091\/mbc.E02-03-0122","article-title":"Clastosome","volume":"13","author":"Lafarga","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB22","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1016\/S0140-6736(05)70296-8","article-title":"Polyglutamine-containing aggregates in neuronal intranuclear inclusion disease","volume":"351","author":"Lieberman","year":"1998","journal-title":"Lancet"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB23","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1002\/1531-8249(199908)46:2<271::AID-ANA21>3.0.CO;2-M","article-title":"Ataxin 1 and ataxin 3 in neuronal intranuclear inclusion disease","volume":"46","author":"Lieberman","year":"1999","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB24","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1007\/BF00690510","article-title":"A light and electron microscopy study of an unusual widespread nuclear inclusion body disease. A possible residuum of an old herpesvirus infection","volume":"10","author":"Lindenberg","year":"1968","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB25","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1083\/jcb.140.2.259","article-title":"Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association","volume":"140","author":"Mahajan","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB26","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1073\/pnas.031566998","article-title":"Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation","volume":"98","author":"Mattsson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB27","doi-asserted-by":"crossref","first-page":"2197","DOI":"10.1093\/hmg\/9.14.2197","article-title":"CREB-binding protein sequestration by expanded polyglutamine","volume":"9","author":"McCampbell","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB28","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/S0306-4522(01)00113-0","article-title":"\u03b1-Synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive incusions in primary neurons","volume":"104","author":"McClean","year":"2001","journal-title":"Neuroscience"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB29","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1146\/annurev.cellbio.16.1.591","article-title":"SUMO\u2014nonclassical ubiquitin","volume":"16","author":"Melchior","year":"2000","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB30","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/35056591","article-title":"SUMO, ubiquitin's mysterious cousin","volume":"2","author":"Muller","year":"2001","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB31","doi-asserted-by":"crossref","first-page":"39060","DOI":"10.1074\/jbc.M103955200","article-title":"Characterization of a novel mammalian SUMO\/Smt3-specific isopeptidase, a homologue of rat Axam, which is an Axin-binding protein promoting b-catenin degradation","volume":"276","author":"Nishida","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB32","doi-asserted-by":"crossref","first-page":"12038","DOI":"10.1073\/pnas.201112398","article-title":"Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection","volume":"98","author":"Nollen","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB33","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1002\/1531-8257(200009)15:5<990::AID-MDS1035>3.0.CO;2-I","article-title":"Neuronal intranuclear inclusion disease and juvenile parkinsonism","volume":"15","author":"O'Sullivan","year":"2000","journal-title":"Mov. Disord."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB34","doi-asserted-by":"crossref","first-page":"12957","DOI":"10.1073\/pnas.210395797","article-title":"Polyglutamine disease and neuronal cell death","volume":"97","author":"Paulson","year":"2000","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB35","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1002\/ana.410410408","article-title":"Machado-Joseph Disease Gene Product is a cytoplasmic protein widely expressed in brain","volume":"41","author":"Paulson","year":"1997","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB36","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0896-6273(00)80943-5","article-title":"Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3","volume":"19","author":"Paulson","year":"1997","journal-title":"Neuron"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB37","doi-asserted-by":"crossref","first-page":"2377","DOI":"10.1093\/hmg\/8.13.2377","article-title":"Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix","volume":"8","author":"Perez","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB38","unstructured":"Pountney, D.L., Blumbergs, P.C., Gai, W.P., (2002). Neuropathological Intranuclear Protein Aggregates Containing SUMO-1 Modified Ataxin-3 with Exposed Polyglutamine. The 27th Annual Lorne Conference on Protein Structure and Function, Lorne, Australia, ISSN 1034\u20133180, C-7"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB39","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1046\/j.1471-4159.2001.00474.x","article-title":"Proteasomal inhibition leads to formation of ubiquitin\/alpha-synuclein-immunoreactive inclusions in PC12 cells","volume":"8","author":"Rideout","year":"2001","journal-title":"J. Neurochem."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB40","doi-asserted-by":"crossref","first-page":"21664","DOI":"10.1074\/jbc.M100006200","article-title":"The SUMO-1 consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification","volume":"276","author":"Sampson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB41","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0896-6273(01)00177-5","article-title":"Cellular defenses against unfolded proteins","volume":"29","author":"Sherman","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB42","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/978-1-4615-0117-6_3","article-title":"Spinocerebellar ataxias caused by polyglutamine expansions","volume":"516","author":"Stevanin","year":"2002","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB43","doi-asserted-by":"crossref","first-page":"9134","DOI":"10.1074\/jbc.M210440200","article-title":"A synergy control motif within the attenuator domain of C\/EBPalpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3","volume":"278","author":"Subramanian","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB44","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1110\/ps.8.4.905","article-title":"Nucleolar protein B23 has molecular chaperone activities","volume":"8","author":"Szebeni","year":"1999","journal-title":"Protein Sci."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB45","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1093\/jnen\/60.4.369","article-title":"Recruitment of non-expanded polyglutamine proteins to intranuclear aggregates in neuronal intranuclear hyaline inclusion disease","volume":"60","author":"Takahashi","year":"2001","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB46","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1097\/00001756-200212030-00038","article-title":"SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death","volume":"13","author":"Terashima","year":"2002","journal-title":"Neuroreport"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB47","doi-asserted-by":"crossref","first-page":"6037","DOI":"10.1093\/emboj\/18.21.6037","article-title":"Human Daxx regulates Fas induced apoptosis from nuclear PML oncogenic domains (PODs)","volume":"18","author":"Torii","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB48","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0006-291X(02)00211-5","article-title":"Enhanced SUMOylation in polyglutamine diseases","volume":"293","author":"Ueda","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB49","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1091\/mbc.12.5.1393","article-title":"Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation","volume":"12","author":"Waelter","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.expneurol.2003.07.004_BIB50","first-page":"93","article-title":"Intranuclear inclusion bodies in an elderly demented woman","volume":"14","author":"Weidenheim","year":"1995","journal-title":"Clin. Neuropathol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB51","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1001\/archneur.59.8.1319","article-title":"Hereditary neuronal intranuclear inclusion disease with autonomic failure and cerebellar degeneration","volume":"59","author":"Zannolli","year":"2002","journal-title":"Arch. Neurol."},{"key":"10.1016\/j.expneurol.2003.07.004_BIB52","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1146\/annurev.neuro.23.1.217","article-title":"Glutamine repeats and neurodegeneration","volume":"23","author":"Zoghbi","year":"2000","journal-title":"Annu. Rev. Neurosci."}],"container-title":["Experimental Neurology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014488603003959?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014488603003959?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,2,18]],"date-time":"2019-02-18T12:24:29Z","timestamp":1550492669000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0014488603003959"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,11]]},"references-count":52,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,11]]}},"alternative-id":["S0014488603003959"],"URL":"https:\/\/doi.org\/10.1016\/j.expneurol.2003.07.004","relation":{},"ISSN":["0014-4886"],"issn-type":[{"value":"0014-4886","type":"print"}],"subject":[],"published":{"date-parts":[[2003,11]]}}}