{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T21:53:26Z","timestamp":1788386006464,"version":"build-2803163510"},"reference-count":59,"publisher":"Oxford University Press (OUP)","issue":"16","license":[{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002960","name":"V\u00e4sterbotten County Council","doi-asserted-by":"publisher","award":["56103\u20137002829"],"award-info":[{"award-number":["56103\u20137002829"]}],"id":[{"id":"10.13039\/501100002960","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Torsten and Ragnar S\u00f6derberg Foundation, Ume\u00e5 University Insamlingsstiftelsen","award":["223\u20132808-12"],"award-info":[{"award-number":["223\u20132808-12"]}]},{"name":"Torsten and Ragnar S\u00f6derberg Foundation, Ume\u00e5 University Insamlingsstiftelsen","award":["223\u20131881-13"],"award-info":[{"award-number":["223\u20131881-13"]}]},{"name":"Torsten and Ragnar S\u00f6derberg Foundation, Ume\u00e5 University Insamlingsstiftelsen","award":["2.1.12\u20131605-14"],"award-info":[{"award-number":["2.1.12\u20131605-14"]}]},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","award":["2012.0091"],"award-info":[{"award-number":["2012.0091"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","award":["2014.0305"],"award-info":[{"award-number":["2014.0305"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","award":["2020.0232"],"award-info":[{"award-number":["2020.0232"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["2012\u20133167"],"award-info":[{"award-number":["2012\u20133167"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["2017\u201303100"],"award-info":[{"award-number":["2017\u201303100"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2012\u20130262"],"award-info":[{"award-number":["2012\u20130262"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2012\u20130305"],"award-info":[{"award-number":["2012\u20130305"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2013\u20130279"],"award-info":[{"award-number":["2013\u20130279"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2016\u20130303"],"award-info":[{"award-number":["2016\u20130303"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2018\u20130310"],"award-info":[{"award-number":["2018\u20130310"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2020\u20130353"],"award-info":[{"award-number":["2020\u20130353"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003792","name":"Swedish Brain Foundation","doi-asserted-by":"crossref","award":["2022\u20130309"],"award-info":[{"award-number":["2022\u20130309"]}],"id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,8,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Mutations in superoxide dismutase-1 (SOD1) are a common cause of amyotrophic lateral sclerosis (ALS). Inheritance is as a rule dominant, but in carriers of the most common mutation, D90A, disease can develop in both homozygous and, more rarely, in heterozygous individuals with unexplained differences in clinical presentation. There is mounting evidence that prion-like spread of SOD1 aggregation is the primary cause of the disease. Two different strains of aggregates have been found to arise in human SOD1 (hSOD1) transgenic mouse models of ALS. Strain A is formed by most mutants including hSOD1G85R and hSOD1WT, whereas hSOD1D90A transgenic mice form a distinct strain B in addition to A. To explore the effects of aggregate strain propensities when hSOD1 variants are coexpressed, we generated digenic hSOD1G85R\/WT and hSOD1G85R\/D90A mice. Coexpression of hSOD1WT considerably shortened the lifespan of hSOD1G85R mice to the extent expected from the neurotoxicities of the variants alone. In contrast, coexpression of hSOD1D90A had a minimal effect on survival, far smaller than expected. Moreover, time from onset to the end stage was markedly prolonged in the hSOD1G85R\/D90A mice. Aggregation of hSOD1 developed concomitantly with motor neuron disease, and the aggregates contained large amounts of both coexpressed variants in both digenic models. Our findings suggest that hSOD1WT has high a capacity to coaggregate with mutants and enhance neurotoxicity. Such interactions may be restricted by differences in strain propensities, which may contribute to the primarily recessive inheritance associated with the hSOD1D90A mutation.<\/jats:p>","DOI":"10.1093\/hmg\/ddaf088","type":"journal-article","created":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T08:45:11Z","timestamp":1748767511000},"page":"1380-1391","source":"Crossref","is-referenced-by-count":2,"title":["Diverse effects of coexpression of human SOD1 variants on motor neuron disease"],"prefix":"10.1093","volume":"34","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7690-3025","authenticated-orcid":false,"given":"Eiichi","family":"Tokuda","sequence":"first","affiliation":[{"name":"Department of Medical Biosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]},{"name":"Laboratory of Clinical Medicine, School of Pharmacy, Nihon University , 7-7-1, Narashinodai, Funabashi, Chiba 274-8555 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-9020-3817","authenticated-orcid":false,"given":"Laura","family":"Leykam","sequence":"additional","affiliation":[{"name":"Department of Medical Biosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8718-3249","authenticated-orcid":false,"given":"Per","family":"Zetterstr\u00f6m","sequence":"additional","affiliation":[{"name":"Department of Medical Biosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4201-8204","authenticated-orcid":false,"given":"Thomas","family":"Br\u00e4nnstr\u00f6m","sequence":"additional","affiliation":[{"name":"Department of Medical Biosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0094-5429","authenticated-orcid":false,"given":"Peter M","family":"Andersen","sequence":"additional","affiliation":[{"name":"Department of Clinical Science, Neurosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3270-2854","authenticated-orcid":false,"given":"Stefan L","family":"Marklund","sequence":"additional","affiliation":[{"name":"Department of Medical Biosciences, Ume\u00e5 University , Ume\u00e5, SE 901 85 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2025,6,1]]},"reference":[{"key":"2025081901162956300_ref1","first-page":"341","article-title":"De la scl\u00e9rose lat\u00e9rale amyotrophique","volume":"2","author":"Charcot","year":"1874","journal-title":"Prog Med"},{"key":"2025081901162956300_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":"Rosen","year":"1993","journal-title":"Nature"},{"key":"2025081901162956300_ref3","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1038\/nrneurol.2011.150","article-title":"Clinical genetics of amyotrophic lateral sclerosis: what do we really know?","volume":"7","author":"Andersen","year":"2011","journal-title":"Nat Rev Neurol"},{"key":"2025081901162956300_ref4","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1080\/17482960802146106","article-title":"ALSOD: the amyotrophic lateral sclerosis online database","volume":"9","author":"Wroe","year":"2008","journal-title":"Amyotroph Lateral Scler"},{"key":"2025081901162956300_ref5","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1093\/brain\/119.4.1153","article-title":"Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. A clinical and genealogical study of 36 patients","volume":"119","author":"Andersen","year":"1996","journal-title":"Brain"},{"key":"2025081901162956300_ref6","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":"Andersen","year":"1995","journal-title":"Nat Genet"},{"key":"2025081901162956300_ref7","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1212\/WNL.47.5.1336","article-title":"D90A heterozygosity in the SOD1 gene is associated with familial and apparently sporadic amyotrophic lateral sclerosis","volume":"47","author":"Robberecht","year":"1996","journal-title":"Neurology"},{"key":"2025081901162956300_ref8","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/s11910-996-0008-9","article-title":"Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene","volume":"6","author":"Andersen","year":"2006","journal-title":"Curr Neurol Neurosci Rep"},{"key":"2025081901162956300_ref9","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":"Kato","year":"2000","journal-title":"Amyotroph Lateral Scler Other Motor Neuron Disord"},{"key":"2025081901162956300_ref10","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1093\/hmg\/dds399","article-title":"Expression of wild-type human superoxide dismutase-1 in mice causes amyotrophic lateral sclerosis","volume":"22","author":"Graffmo","year":"2013","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref11","doi-asserted-by":"crossref","first-page":"4489","DOI":"10.1073\/pnas.1419228112","article-title":"Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping","volume":"112","author":"Bergh","year":"2015","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref12","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1172\/JCI84360","article-title":"Two superoxide dismutase prion strains transmit amyotrophic lateral sclerosis-like disease","volume":"126","author":"Bidhendi","year":"2016","journal-title":"J Clin Invest"},{"key":"2025081901162956300_ref13","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1007\/s00401-016-1623-4","article-title":"Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS","volume":"132","author":"Ayers","year":"2016","journal-title":"Acta Neuropathol"},{"key":"2025081901162956300_ref14","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1007\/s00401-014-1342-7","article-title":"Experimental transmissibility of mutant SOD1 motor neuron disease","volume":"128","author":"Ayers","year":"2014","journal-title":"Acta Neuropathol"},{"key":"2025081901162956300_ref15","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1007\/s00401-015-1514-0","article-title":"Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathways","volume":"131","author":"Ayers","year":"2016","journal-title":"Acta Neuropathol"},{"key":"2025081901162956300_ref16","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1186\/s40478-021-01191-w","article-title":"Variation in the vulnerability of mice expressing human superoxide dismutase 1 to prion-like seeding: a study of the influence of primary amino acid sequence","volume":"9","author":"Ayers","year":"2021","journal-title":"Acta Neuropathol Commun"},{"key":"2025081901162956300_ref17","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1186\/2051-5960-2-55","article-title":"Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases","volume":"2","author":"Ayers","year":"2014","journal-title":"Acta Neuropathol Commun"},{"key":"2025081901162956300_ref18","doi-asserted-by":"crossref","first-page":"e10627","DOI":"10.1371\/journal.pone.0010627","article-title":"Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis","volume":"5","author":"Chia","year":"2010","journal-title":"PLoS One"},{"key":"2025081901162956300_ref19","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1186\/s40478-021-01211-9","article-title":"Peripheral administration of SOD1 aggregates does not transmit pathogenic aggregation to the CNS of SOD1 transgenic mice","volume":"9","author":"Keskin","year":"2021","journal-title":"Acta Neuropathol Commun"},{"key":"2025081901162956300_ref20","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1186\/s40478-020-01032-2","article-title":"Aggregate-selective antibody attenuates seeded aggregation but not spontaneously evolving disease in SOD1 ALS model mice","volume":"8","author":"Lehmann","year":"2020","journal-title":"Acta Neuropathol Commun"},{"key":"2025081901162956300_ref21","doi-asserted-by":"crossref","first-page":"e0184384","DOI":"10.1371\/journal.pone.0184384","article-title":"Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells","volume":"12","author":"Pokrishevsky","year":"2017","journal-title":"PLoS One"},{"key":"2025081901162956300_ref22","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1007\/s00401-018-1915-y","article-title":"Mutant superoxide dismutase aggregates from human spinal cord transmit amyotrophic lateral sclerosis","volume":"136","author":"Ekhtiari Bidhendi","year":"2018","journal-title":"Acta Neuropathol"},{"key":"2025081901162956300_ref23","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":"Deng","year":"2006","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref24","doi-asserted-by":"crossref","first-page":"4774","DOI":"10.1093\/hmg\/ddq408","article-title":"An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1","volume":"19","author":"Prudencio","year":"2010","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref25","doi-asserted-by":"crossref","first-page":"1642","DOI":"10.1093\/hmg\/ddp085","article-title":"Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouse","volume":"18","author":"Wang","year":"2009","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref26","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":"Jaarsma","year":"2000","journal-title":"Neurobiol Dis"},{"key":"2025081901162956300_ref27","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.1046\/j.0953-816x.2001.01828.x","article-title":"Stabilization of mutant Cu\/Zn superoxide dismutase (SOD1) protein by coexpressed wild SOD1 protein accelerates the disease progression in familial amyotrophic lateral sclerosis mice","volume":"14","author":"Fukada","year":"2001","journal-title":"Eur J Neurosci"},{"key":"2025081901162956300_ref28","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1093\/hmg\/ddu517","article-title":"Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice","volume":"24","author":"Xu","year":"2015","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref29","doi-asserted-by":"crossref","first-page":"2310","DOI":"10.1093\/hmg\/ddn131","article-title":"Molecular dissection of ALS-associated toxicity of SOD1 in transgenic mice using an exon-fusion approach","volume":"17","author":"Deng","year":"2008","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref30","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":"Bruijn","year":"1998","journal-title":"Science"},{"key":"2025081901162956300_ref31","doi-asserted-by":"crossref","first-page":"4147","DOI":"10.1523\/JNEUROSCI.5461-05.2006","article-title":"Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models","volume":"26","author":"Bergemalm","year":"2006","journal-title":"J Neurosci"},{"key":"2025081901162956300_ref32","doi-asserted-by":"crossref","first-page":"18663","DOI":"10.1073\/pnas.0807058105","article-title":"Initiation and elongation in fibrillation of ALS-linked superoxide dismutase","volume":"105","author":"Chattopadhyay","year":"2008","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref33","doi-asserted-by":"crossref","first-page":"30624","DOI":"10.1074\/jbc.M115.666503","article-title":"The Disulfide bond, but not zinc or dimerization, controls initiation and seeded growth in amyotrophic lateral sclerosis-linked Cu,Zn superoxide dismutase (SOD1) fibrillation","volume":"290","author":"Chattopadhyay","year":"2015","journal-title":"J Biol Chem"},{"key":"2025081901162956300_ref34","doi-asserted-by":"crossref","first-page":"7774","DOI":"10.1073\/pnas.0902505106","article-title":"Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS","volume":"106","author":"Karch","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref35","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1111\/j.1471-4159.2010.06753.x","article-title":"Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice","volume":"114","author":"Bergemalm","year":"2010","journal-title":"J Neurochem"},{"key":"2025081901162956300_ref36","doi-asserted-by":"crossref","first-page":"E6939","DOI":"10.1073\/pnas.1611418113","article-title":"Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy","volume":"113","author":"Sekhar","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref37","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1007\/s00018-016-2416-6","article-title":"Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis","volume":"74","author":"Santamaria","year":"2017","journal-title":"Cell Mol Life Sci"},{"key":"2025081901162956300_ref38","doi-asserted-by":"crossref","first-page":"106844","DOI":"10.1016\/j.bpc.2022.106844","article-title":"Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes","volume":"288","author":"Deol","year":"2022","journal-title":"Biophys Chem"},{"key":"2025081901162956300_ref39","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1111\/jnc.15718","article-title":"Mutant SOD1 aggregates formed in vitro and in cultured cells are polymorphic and differ from those arising in the CNS","volume":"164","author":"Nordstr\u00f6m","year":"2023","journal-title":"J Neurochem"},{"key":"2025081901162956300_ref40","doi-asserted-by":"crossref","first-page":"eado8499","DOI":"10.1126\/sciadv.ado8499","article-title":"Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations","volume":"10","author":"Wang","year":"2024","journal-title":"Sci Adv"},{"key":"2025081901162956300_ref41","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":"Jonsson","year":"2004","journal-title":"Brain"},{"key":"2025081901162956300_ref42","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":"Jonsson","year":"2006","journal-title":"J Neuropathol Exp Neurol"},{"key":"2025081901162956300_ref43","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":"Jonsson","year":"2006","journal-title":"Brain"},{"key":"2025081901162956300_ref44","doi-asserted-by":"crossref","first-page":"8292","DOI":"10.1073\/pnas.91.17.8292","article-title":"Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity","volume":"91","author":"Borchelt","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref45","doi-asserted-by":"crossref","first-page":"15923","DOI":"10.1074\/jbc.M112087200","article-title":"Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis","volume":"277","author":"Hayward","year":"2002","journal-title":"J Biol Chem"},{"key":"2025081901162956300_ref46","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/S0896-6273(00)80272-X","article-title":"ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions","volume":"18","author":"Bruijn","year":"1997","journal-title":"Neuron"},{"key":"2025081901162956300_ref47","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.nbd.2010.05.031","article-title":"Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1 G86R","volume":"40","author":"Audet","year":"2010","journal-title":"Neurobiol Dis"},{"key":"2025081901162956300_ref48","doi-asserted-by":"crossref","first-page":"16398","DOI":"10.1073\/pnas.1102645108","article-title":"Intermolecular transmission of superoxide dismutase 1 misfolding in living cells","volume":"108","author":"Grad","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref49","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/1750-1326-8-46","article-title":"Features of wild-type human SOD1 limit interactions with misfolded aggregates of mouse G86R Sod1","volume":"8","author":"Qualls","year":"2013","journal-title":"Mol Neurodegener"},{"key":"2025081901162956300_ref50","doi-asserted-by":"crossref","first-page":"8774","DOI":"10.1523\/JNEUROSCI.2315-06.2006","article-title":"Complete dissociation of motor neuron death from motor dysfunction by Bax deletion in a mouse model of ALS","volume":"26","author":"Gould","year":"2006","journal-title":"J Neurosci"},{"key":"2025081901162956300_ref51","doi-asserted-by":"crossref","first-page":"20","DOI":"10.4161\/pri.4.1.11378","article-title":"Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters","volume":"4","author":"Xue","year":"2010","journal-title":"Prion"},{"key":"2025081901162956300_ref52","doi-asserted-by":"crossref","first-page":"a004374","DOI":"10.1101\/cshperspect.a004374","article-title":"Cellular strategies of protein quality control","volume":"3","author":"Chen","year":"2011","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"2025081901162956300_ref53","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1021\/acschemneuro.6b00048","article-title":"Stochastic formation of Fibrillar and amorphous superoxide dismutase oligomers linked to amyotrophic lateral sclerosis","volume":"7","author":"Abdolvahabi","year":"2016","journal-title":"ACS Chem Neurosci"},{"key":"2025081901162956300_ref54","doi-asserted-by":"crossref","first-page":"17868","DOI":"10.1073\/pnas.1201795109","article-title":"Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium","volume":"109","author":"Lang","year":"2012","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025081901162956300_ref55","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":"Gurney","year":"1994","journal-title":"Science"},{"key":"2025081901162956300_ref56","doi-asserted-by":"crossref","first-page":"4201","DOI":"10.1093\/hmg\/ddq338","article-title":"A novel SOD1 splice site mutation associated with familial ALS revealed by SOD activity analysis","volume":"19","author":"Birve","year":"2010","journal-title":"Hum Mol Genet"},{"key":"2025081901162956300_ref57","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1126\/science.1123511","article-title":"Onset and progression in inherited ALS determined by motor neurons and microglia","volume":"312","author":"Boill\u00e9e","year":"2006","journal-title":"Science"},{"key":"2025081901162956300_ref58","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s40478-016-0274-y","article-title":"Low autophagy capacity implicated in motor system vulnerability to mutant superoxide dismutase","volume":"4","author":"Tokuda","year":"2016","journal-title":"Acta Neuropathol Commun"},{"key":"2025081901162956300_ref59","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.nbd.2013.01.001","article-title":"Dysregulation of intracellular copper homeostasis is common to transgenic mice expressing human mutant superoxide dismutase-1s regardless of their copper-binding abilities","volume":"54","author":"Tokuda","year":"2013","journal-title":"Neurobiol Dis"}],"container-title":["Human Molecular Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/hmg\/article-pdf\/34\/16\/1380\/63413604\/ddaf088.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/hmg\/article-pdf\/34\/16\/1380\/63413604\/ddaf088.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,8,19]],"date-time":"2025-08-19T05:16:44Z","timestamp":1755580604000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/hmg\/article\/34\/16\/1380\/8154642"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6,1]]},"references-count":59,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2025,6,1]]},"published-print":{"date-parts":[[2025,8,16]]}},"URL":"https:\/\/doi.org\/10.1093\/hmg\/ddaf088","relation":{},"ISSN":["0964-6906","1460-2083"],"issn-type":[{"value":"0964-6906","type":"print"},{"value":"1460-2083","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2025,8,15]]},"published":{"date-parts":[[2025,6,1]]}}}