{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T23:09:16Z","timestamp":1793315356385,"version":"4.5.0"},"reference-count":44,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2010,7,14]],"date-time":"2010-07-14T00:00:00Z","timestamp":1279065600000},"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.0011552","type":"journal-article","created":{"date-parts":[[2010,7,14]],"date-time":"2010-07-14T17:40:42Z","timestamp":1279129242000},"page":"e11552","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":292,"title":["Novel Antibodies Reveal Inclusions Containing Non-Native SOD1 in Sporadic ALS Patients"],"prefix":"10.1371","volume":"5","author":[{"given":"Karin","family":"Forsberg","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P. Andreas","family":"Jonsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter M.","family":"Andersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Bergemalm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin S.","family":"Graffmo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magnus","family":"Hultdin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan","family":"Jacobsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roland","family":"Rosquist","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan L.","family":"Marklund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Br\u00e4nnstr\u00f6m","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2010,7,14]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1093\/brain\/118.3.707","article-title":"Natural history of amyotrophic lateral sclerosis in a database population. Validation of a scoring system and a model for survival prediction.","volume":"118 (Pt3)","author":"LJ Haverkamp","year":"1995","journal-title":"Brain"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.","volume":"362","author":"DR Rosen","year":"1993","journal-title":"Nature"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1126\/science.8209258","article-title":"Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation.","volume":"264","author":"ME Gurney","year":"1994","journal-title":"Science"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1038\/ng0595-61","article-title":"Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase.","volume":"10","author":"PM Andersen","year":"1995","journal-title":"Nat Genet"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1038\/ng0596-43","article-title":"Motor neurons in Cu\/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury.","volume":"13","author":"AG Reaume","year":"1996","journal-title":"Nat Genet"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1080\/14660820310011700","article-title":"Sixteen novel mutations in the Cu\/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes.","volume":"4","author":"PM Andersen","year":"2003","journal-title":"Amyotroph Lateral Scler Other Motor Neuron Disord"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1038\/nm1113","article-title":"Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs.","volume":"10","author":"MS Forman","year":"2004","journal-title":"Nat Med"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"3617","DOI":"10.1073\/pnas.0730423100","article-title":"Misfolded CuZnSOD and amyotrophic lateral sclerosis.","volume":"100","author":"JS Valentine","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1093\/brain\/awh005","article-title":"Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis.","volume":"127","author":"PA Jonsson","year":"2004","journal-title":"Brain"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"9754","DOI":"10.1073\/pnas.0501957102","article-title":"Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants.","volume":"102","author":"MJ Lindberg","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/j.nbd.2005.06.005","article-title":"Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA.","volume":"20","author":"J Wang","year":"2005","journal-title":"Neurobiol Dis"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1093\/brain\/awh704","article-title":"Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models.","volume":"129","author":"PA Jonsson","year":"2006","journal-title":"Brain"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"2366","DOI":"10.1046\/j.1471-4159.1995.64052366.x","article-title":"Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis.","volume":"64","author":"AC Bowling","year":"1995","journal-title":"J Neurochem"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1212\/01.wnl.0000188760.53922.05","article-title":"Rapid disease progression correlates with instability of mutant SOD1 in familial ALS.","volume":"65","author":"T Sato","year":"2005","journal-title":"Neurology"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.nbd.2009.08.006","article-title":"Superoxide dismutase in amyotrophic lateral sclerosis patients homozygous for the D90A mutation.","volume":"36","author":"PA Jonsson","year":"2009","journal-title":"Neurobiol Dis"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1097\/01.jnen.0000248545.36046.3c","article-title":"Motor neuron disease in mice expressing the wild type-like D90A mutant superoxide dismutase-1.","volume":"65","author":"PA Jonsson","year":"2006","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1006\/nbdi.2000.0299","article-title":"Human Cu\/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1.","volume":"7","author":"D Jaarsma","year":"2000","journal-title":"Neurobiol Dis"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"7142","DOI":"10.1073\/pnas.0602046103","article-title":"Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.","volume":"103","author":"HX Deng","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"15499","DOI":"10.1074\/jbc.M313295200","article-title":"Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.","volume":"279","author":"R Rakhit","year":"2004","journal-title":"J Biol Chem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1111\/j.1471-4159.2007.04531.x","article-title":"Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation.","volume":"102","author":"SA Ezzi","year":"2007","journal-title":"J Neurochem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"12524","DOI":"10.1073\/pnas.0705044104","article-title":"Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis.","volume":"104","author":"A Gruzman","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0304-3940(94)90956-3","article-title":"Cu\/Zn superoxide dismutase-like immunoreactivity in Lewy body-like inclusions of sporadic amyotrophic lateral sclerosis.","volume":"179","author":"N Shibata","year":"1994","journal-title":"Neurosci Lett"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/s004010050535","article-title":"Familial amyotrophic lateral sclerosis with a mutation in exon 4 of the Cu\/Zn superoxide dismutase gene: pathological and immunocytochemical changes.","volume":"92","author":"PG Ince","year":"1996","journal-title":"Acta Neuropathol (Berl)"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1212\/WNL.49.6.1612","article-title":"Familial amyotrophic lateral sclerosis. Molecular pathology of a patient with a SOD1 mutation.","volume":"49","author":"CE Shaw","year":"1997","journal-title":"Neurology"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S0022-510X(96)05316-6","article-title":"Immunocytochemical study of the distribution of the free radical scavenging enzymes Cu\/Zn superoxide dismutase (SOD1); MN superoxide dismutase (MN SOD) and catalase in the normal human spinal cord and in motor neuron disease.","volume":"147","author":"PJ Shaw","year":"1997","journal-title":"J Neurol Sci"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1097\/00005072-199810000-00002","article-title":"Amyotrophic lateral sclerosis associated with genetic abnormalities in the gene encoding Cu\/Zn superoxide dismutase: molecular pathology of five new cases, and comparison with previous reports and 73 sporadic cases of ALS.","volume":"57","author":"PG Ince","year":"1998","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s004010050766","article-title":"CuZnSOD and MnSOD immunoreactivity in brain stem motor neurons from amyotrophic lateral sclerosis patients.","volume":"95","author":"Y Liu","year":"1998","journal-title":"Acta Neuropathol (Berl)"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1080\/14660820050515160","article-title":"New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: inclusions containing SOD1 in neurons and astrocytes.","volume":"1","author":"S Kato","year":"2000","journal-title":"Amyotroph Lateral Scler Other Motor Neuron Disord"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1111\/j.1440-1789.1998.tb00132.x","article-title":"Neuropathology of familial amyotrophic lateral sclerosis patients with superoxide dismutase 1 gene mutations.","volume":"18","author":"A Hirano","year":"1998","journal-title":"Neuropathology"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1002\/mus.20495","article-title":"Clinicopathological phenotype of ALS with a novel G72C SOD1 gene mutation mimicking a myopathy.","volume":"33","author":"HG Stewart","year":"2006","journal-title":"Muscle Nerve"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1097\/00005072-199604000-00011","article-title":"Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement.","volume":"55","author":"N Shibata","year":"1996","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1046\/j.1471-4159.1997.69020675.x","article-title":"Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients.","volume":"69","author":"SL Marklund","year":"1997","journal-title":"J Neurochem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1002\/ana.21704","article-title":"Lack of evidence of monomer\/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis.","volume":"66","author":"HN Liu","year":"2009","journal-title":"Ann Neurol"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1126\/science.281.5384.1851","article-title":"Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1.","volume":"281","author":"LI Bruijn","year":"1998","journal-title":"Science"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1006\/nbdi.2002.0498","article-title":"Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site.","volume":"10","author":"J Wang","year":"2002","journal-title":"Neurobiol Dis"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1146\/annurev.neuro.27.070203.144244","article-title":"Unraveling the mechanisms involved in motor neuron degeneration in ALS.","volume":"27","author":"LI Bruijn","year":"2004","journal-title":"Annu Rev Neurosci"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"14157","DOI":"10.1073\/pnas.0700477104","article-title":"Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models.","volume":"104","author":"P Zetterstrom","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/4553","article-title":"Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons.","volume":"2","author":"TL Williamson","year":"1999","journal-title":"Nat Neurosci"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"13901","DOI":"10.1073\/pnas.240305897","article-title":"Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis.","volume":"97","author":"P Pasinelli","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1002\/mus.1176","article-title":"Presymptomatic motor neuron loss and reactive astrocytosis in the SOD1 mouse model of amyotrophic lateral sclerosis.","volume":"24","author":"SJ Feeney","year":"2001","journal-title":"Muscle Nerve"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1002\/mus.20228","article-title":"Gait analysis detects early changes in transgenic SOD1(G93A) mice.","volume":"32","author":"CM Wooley","year":"2005","journal-title":"Muscle Nerve"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1172\/JCI111550","article-title":"Extracellular superoxide dismutase in human tissues and human cell lines.","volume":"74","author":"SL Marklund","year":"1984","journal-title":"J Clin Invest"},{"key":"ref43","first-page":"1","article-title":"Papers from the 3rd International Symposium on Amyotrophic Lateral Sclerosis\/Motor Neurone Disease. Genetics and Cell Biology of the Motor Neurone. Birmingham, United Kingdom, November 2-4, 1992.","volume":"124","year":"1994"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1093\/brain\/124.7.1461","article-title":"Superoxide dismutase in CSF from amyotrophic lateral sclerosis patients with and without CuZn-superoxide dismutase mutations.","volume":"124","author":"J Jacobsson","year":"2001","journal-title":"Brain"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0011552","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,22]],"date-time":"2018-10-22T10:06:19Z","timestamp":1540202779000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0011552"}},"subtitle":[],"editor":[{"given":"Per","family":"Westermark","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2010,7,14]]},"references-count":44,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2010,7,14]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0011552","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.12796974.14073076","asserted-by":"object"}]},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,7,14]]}}}