{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T00:10:41Z","timestamp":1793146241473,"version":"4.5.0"},"reference-count":82,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,10,22]],"date-time":"2024-10-22T00:00:00Z","timestamp":1729555200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018007","name":"Ulla Carin Lindquist Foundation for ALS Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100018007","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003792","name":"Brain Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003792","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006129","name":"King Gustaf V and Queen Victoria's Masonic Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006129","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008084","name":"Neuroscience Association","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008084","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.fr","clinicalkey.jp","clinicalkey.es","clinicalkey.com.au","clinicalkey.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neurobiology of Disease"],"published-print":{"date-parts":[[2024,11]]},"DOI":"10.1016\/j.nbd.2024.106718","type":"journal-article","created":{"date-parts":[[2024,10,28]],"date-time":"2024-10-28T01:47:13Z","timestamp":1730080033000},"page":"106718","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"special_numbering":"C","title":["Specific analysis of SOD1 enzymatic activity in CSF from ALS patients with and without SOD1 mutations"],"prefix":"10.1016","volume":"202","author":[{"given":"Laura","family":"Leykam","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin M.E.","family":"Forsberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrika","family":"Nordstr\u00f6m","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin","family":"Hjertkvist","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agneta","family":"\u00d6berg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eva","family":"Jonsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter M.","family":"Andersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan L.","family":"Marklund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Per","family":"Zetterstr\u00f6m","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0005","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."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0010","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."},{"issue":"Pt 10","key":"10.1016\/j.nbd.2024.106718_bb0015","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1093\/brain\/120.10.1723","article-title":"Phenotypic heterogeneity in motor neuron disease patients with CuZn-superoxide dismutase mutations in Scandinavia","volume":"120","author":"Andersen","year":"1997","journal-title":"Brain"},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0020","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1046\/j.1471-4159.1998.70020715.x","article-title":"CuZn-superoxide dismutase, extracellular superoxide dismutase, and glutathione peroxidase in blood from individuals homozygous for Asp90Ala CuZu-superoxide dismutase mutation","volume":"70","author":"Andersen","year":"1998","journal-title":"J. Neurochem."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0025","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1111\/j.1468-1331.2011.03501.x","article-title":"EFNS guidelines on the clinical management of amyotrophic lateral sclerosis (MALS)\u2013revised report of an EFNS task force","volume":"19","author":"Andersen","year":"2012","journal-title":"Eur. J. Neurol."},{"issue":"5","key":"10.1016\/j.nbd.2024.106718_bb0030","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1056\/NEJMc1905039","article-title":"Phenotype in an infant with SOD1 homozygous truncating mutation","volume":"381","author":"Andersen","year":"2019","journal-title":"N. Engl. J. Med."},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0035","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.jmb.2009.03.026","article-title":"The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding","volume":"388","author":"Antonyuk","year":"2009","journal-title":"J. Mol. Biol."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0040","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."},{"issue":"10","key":"10.1016\/j.nbd.2024.106718_bb0045","first-page":"2293","article-title":"Superoxide dismutase isoenzymes in the normal and diseased human cornea","volume":"42","author":"Behndig","year":"2001","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"issue":"4","key":"10.1016\/j.nbd.2024.106718_bb0050","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1007\/s13311-022-01237-4","article-title":"Design of a randomized, placebo-controlled, phase 3 trial of tofersen initiated in clinically presymptomatic SOD1 variant carriers: the ATLAS study","volume":"19","author":"Benatar","year":"2022","journal-title":"Neurotherapeutics"},{"issue":"14","key":"10.1016\/j.nbd.2024.106718_bb0055","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."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0060","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."},{"issue":"11","key":"10.1016\/j.nbd.2024.106718_bb0065","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1007\/s40265-023-01904-6","article-title":"Tofersen: first approval","volume":"83","author":"Blair","year":"2023","journal-title":"Drugs"},{"issue":"17","key":"10.1016\/j.nbd.2024.106718_bb0070","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"},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0075","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1089\/hum.2015.122","article-title":"Therapeutic rAAVrh10 mediated SOD1 silencing in adult SOD1 G93A mice and nonhuman primates","volume":"27","author":"Borel","year":"2016","journal-title":"Hum. Gene Ther."},{"issue":"5","key":"10.1016\/j.nbd.2024.106718_bb0080","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":"Bowling","year":"1995","journal-title":"J. Neurochem."},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0085","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1056\/NEJMra1603471","article-title":"Amyotrophic lateral sclerosis","volume":"377","author":"Brown","year":"2017","journal-title":"N. Engl. J. Med."},{"issue":"5384","key":"10.1016\/j.nbd.2024.106718_bb0090","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"},{"issue":"5\u20136","key":"10.1016\/j.nbd.2024.106718_bb0095","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1080\/21678421.2023.2189925","article-title":"A novel homozygous loss-of-function variant in SOD1 causing progressive spastic tetraplegia and axial hypotonia","volume":"24","author":"\u00c7akar","year":"2023","journal-title":"Amyotroph. Lateral Scler. Frontotemporal Degener."},{"issue":"14","key":"10.1016\/j.nbd.2024.106718_bb0100","doi-asserted-by":"crossref","first-page":"6264","DOI":"10.1073\/pnas.92.14.6264","article-title":"Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia","volume":"92","author":"Carlsson","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"10","key":"10.1016\/j.nbd.2024.106718_bb0105","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1016\/S0891-5849(00)00280-X","article-title":"Overexpression of copper\/zinc superoxide dismutase does not prevent neonatal lethality in mutant mice that lack manganese superoxide dismutase","volume":"28","author":"Copin","year":"2000","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.nbd.2024.106718_bb0110","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.semcdb.2018.02.021","article-title":"Unconventional protein secretion triggered by nutrient starvation","volume":"83","author":"Cruz-Garcia","year":"2018","journal-title":"Semin. Cell Dev. Biol."},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0115","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1002\/ana.410410212","article-title":"Epidemiology of mutations in superoxide dismutase in amyotrophic lateal sclerosis","volume":"41","author":"Cudkowicz","year":"1997","journal-title":"Ann. Neurol."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0120","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1080\/146608202760834111","article-title":"SOD1 activity and protective factors in familial ALS patients with L84F SOD1 mutation","volume":"3","author":"Curti","year":"2002","journal-title":"Amyotroph. Lateral Scler. Other Motor Neuron Disord."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0125","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1186\/s13023-021-01993-0","article-title":"Progressive spastic tetraplegia and axial hypotonia (STAHP) due to SOD1 deficiency: is it really a new entity?","volume":"16","author":"de Souza","year":"2021","journal-title":"Orphanet J. Rare Dis."},{"issue":"5124","key":"10.1016\/j.nbd.2024.106718_bb0130","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1126\/science.8351519","article-title":"Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase","volume":"261","author":"Deng","year":"1993","journal-title":"Science"},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0135","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1007\/s11033-024-09513-6","article-title":"Discovery of a novel homozygous SOD1 truncating variant bolsters infantile SOD1 deficiency syndrome","volume":"51","author":"Dogan","year":"2024","journal-title":"Mol. Biol. Rep."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0140","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."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0145","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1093\/brain\/awab416","article-title":"Infantile SOD1 deficiency syndrome caused by a homozygous SOD1 variant with absence of enzyme activity","volume":"145","author":"Ezer","year":"2022","journal-title":"Brain"},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0150","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.mayocp.2022.10.012","article-title":"Population-based evaluation of total protein in cerebrospinal fluid","volume":"98","author":"Fautsch","year":"2023","journal-title":"Mayo Clin. Proc."},{"issue":"7","key":"10.1016\/j.nbd.2024.106718_bb0155","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0011552","article-title":"Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients","volume":"5","author":"Forsberg","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2024.106718_bb0160","article-title":"Precisionsmedicinsk genterapi har bromsat utveckling av ALS","volume":"121","author":"Forsberg","year":"2024","journal-title":"L\u00e4kartidningen"},{"issue":"4","key":"10.1016\/j.nbd.2024.106718_bb0165","doi-asserted-by":"crossref","first-page":"915","DOI":"10.2353\/ajpath.2008.080119","article-title":"Loss of extracellular superoxide dismutase leads to acute lung damage in the presence of ambient air: a potential mechanism underlying adult respiratory distress syndrome","volume":"173","author":"Gongora","year":"2008","journal-title":"Am. J. Pathol."},{"issue":"5166","key":"10.1016\/j.nbd.2024.106718_bb0170","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"},{"issue":"8","key":"10.1016\/j.nbd.2024.106718_bb0175","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1016\/S1474-4422(24)00259-X","article-title":"Tofersen for SOD-1-associated amyotrophic lateral sclerosis","volume":"23","author":"Haberkamp","year":"2024","journal-title":"Lancet Neurol."},{"issue":"18","key":"10.1016\/j.nbd.2024.106718_bb0180","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."},{"issue":"18","key":"10.1016\/j.nbd.2024.106718_bb0185","doi-asserted-by":"crossref","first-page":"6340","DOI":"10.1073\/pnas.84.18.6340","article-title":"Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase","volume":"84","author":"Hjalmarsson","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.nbd.2024.106718_bb0190","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bbrc.2023.05.022","article-title":"Human SOD1 is secreted via a conventional secretion pathway in Saccharomyces cerevisiae","volume":"666","author":"Hosomi","year":"2023","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"Pt 7","key":"10.1016\/j.nbd.2024.106718_bb0195","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":"Jacobsson","year":"2001","journal-title":"Brain"},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0200","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1006\/nbdi.2002.0508","article-title":"CuZn-superoxide dismutase in D90A heterozygotes from recessive and dominant ALS pedigrees","volume":"10","author":"Jonsson","year":"2002","journal-title":"Neurobiol. Dis."},{"issue":"Pt 1","key":"10.1016\/j.nbd.2024.106718_bb0205","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"},{"issue":"12","key":"10.1016\/j.nbd.2024.106718_bb0210","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."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0215","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":"Jonsson","year":"2009","journal-title":"Neurobiol. Dis."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0220","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."},{"issue":"5\u20136","key":"10.1016\/j.nbd.2024.106718_bb0225","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1080\/21678421.2017.1301481","article-title":"Comprehensive analysis to explain reduced or increased SOD1 enzymatic activity in ALS patients and their relatives","volume":"18","author":"Keskin","year":"2017","journal-title":"Amyotroph. Lateral Scler. Frontotemporal Degener."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0230","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1002\/ana.24950","article-title":"Pyrimethamine significantly lowers cerebrospinal fluid Cu\/Zn superoxide dismutase in amyotrophic lateral sclerosis patients with SOD1 mutations","volume":"81","author":"Lange","year":"2017","journal-title":"Ann. Neurol."},{"issue":"23","key":"10.1016\/j.nbd.2024.106718_bb0235","doi-asserted-by":"crossref","first-page":"7504","DOI":"10.1016\/S0021-9258(17)32878-8","article-title":"Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase","volume":"251","author":"Marklund","year":"1976","journal-title":"J. Biol. Chem."},{"issue":"24","key":"10.1016\/j.nbd.2024.106718_bb0240","doi-asserted-by":"crossref","first-page":"7634","DOI":"10.1073\/pnas.79.24.7634","article-title":"Human copper-containing superoxide dismutase of high molecular weight","volume":"79","author":"Marklund","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0245","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/bj2200269","article-title":"Properties of extracellular superoxide dismutase from human lung","volume":"220","author":"Marklund","year":"1984","journal-title":"Biochem. J."},{"key":"10.1016\/j.nbd.2024.106718_bb0250","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/S0076-6879(02)49322-6","article-title":"Extracellular superoxide dismutase","volume":"349","author":"Marklund","year":"2002","journal-title":"Methods Enzymol."},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0255","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1111\/j.1432-1033.1974.tb03714.x","article-title":"Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase","volume":"47","author":"Marklund","year":"1974","journal-title":"Eur. J. Biochem."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0260","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0009-8981(82)90360-6","article-title":"Superoxide dismutase in extracellular fluids","volume":"126","author":"Marklund","year":"1982","journal-title":"Clin. Chim. Acta"},{"issue":"5","key":"10.1016\/j.nbd.2024.106718_bb0265","first-page":"1955","article-title":"Copper- and zinc-containing superoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues","volume":"42","author":"Marklund","year":"1982","journal-title":"Cancer Res."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0270","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1042\/cs0710057","article-title":"Superoxide dismutase isoenzymes in cerebrospinal fluid and plasma from patients with neuronal ceroid-lipofuscinoses","volume":"71","author":"Marklund","year":"1986","journal-title":"Clin. Sci. (Lond.)"},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0275","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":"Marklund","year":"1997","journal-title":"J. Neurochem."},{"issue":"10","key":"10.1016\/j.nbd.2024.106718_bb0280","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1111\/ene.14393","article-title":"Amyotrophic lateral sclerosis: a clinical review","volume":"27","author":"Masrori","year":"2020","journal-title":"Eur. J. Neurol."},{"issue":"22","key":"10.1016\/j.nbd.2024.106718_bb0285","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1016\/S0021-9258(18)63504-5","article-title":"Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)","volume":"244","author":"McCord","year":"1969","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0290","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1002\/mus.27818","article-title":"Neurofilament light-chain response during therapy with antisense oligonucleotide tofersen in SOD1-related ALS: treatment experience in clinical practice","volume":"67","author":"Meyer","year":"2023","journal-title":"Muscle Nerve"},{"key":"10.1016\/j.nbd.2024.106718_bb0295","doi-asserted-by":"crossref","DOI":"10.1002\/mus.28182","article-title":"Clinical and patient-reported outcomes and neurofilament response during tofersen treatment in SOD1-related ALS-A multicenter observational study over 18 months","author":"Meyer","year":"2024","journal-title":"Muscle Nerve"},{"issue":"5","key":"10.1016\/j.nbd.2024.106718_bb0300","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S1474-4422(13)70061-9","article-title":"An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study","volume":"12","author":"Miller","year":"2013","journal-title":"Lancet Neurol."},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0305","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1056\/NEJMoa2003715","article-title":"Phase 1-2 trial of antisense oligonucleotide tofersen for SOD1 ALS","volume":"383","author":"Miller","year":"2020","journal-title":"N. Engl. J. Med."},{"issue":"12","key":"10.1016\/j.nbd.2024.106718_bb0310","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1056\/NEJMoa2204705","article-title":"Trial of antisense oligonucleotide tofersen for SOD1 ALS","volume":"387","author":"Miller","year":"2022","journal-title":"N. Engl. J. Med."},{"issue":"21","key":"10.1016\/j.nbd.2024.106718_bb0315","doi-asserted-by":"crossref","first-page":"6960","DOI":"10.1016\/S0021-9258(19)44679-6","article-title":"The generation of superoxide radical during the autoxidation of hemoglobin","volume":"247","author":"Misra","year":"1972","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.nbd.2024.106718_bb0320","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/1357-2725(96)00004-0","article-title":"Evidence for secretion of cytosolic CuZn superoxide dismutase by Hep G2 cells and human fibroblasts","volume":"28","author":"Mondola","year":"1996","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0325","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1136\/jnnp-2021-327520","article-title":"De novo mutations in SOD1 are a cause of ALS","volume":"93","author":"M\u00fcller","year":"2022","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"issue":"6522","key":"10.1016\/j.nbd.2024.106718_bb0330","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/374504a0","article-title":"A novel SOD mutant and ALS","volume":"374","author":"Orrell","year":"1995","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0335","doi-asserted-by":"crossref","DOI":"10.1093\/braincomms\/fcad017","article-title":"The motor system is exceptionally vulnerable to absence of the ubiquitously expressed superoxide dismutase-1","volume":"5","author":"Park","year":"2023","journal-title":"Brain Commun."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0340","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":"Reaume","year":"1996","journal-title":"Nat. Genet."},{"issue":"6435","key":"10.1016\/j.nbd.2024.106718_bb0345","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1038\/364362c0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"364","author":"Rosen","year":"1993","journal-title":"Nature"},{"issue":"Pt 8","key":"10.1016\/j.nbd.2024.106718_bb0350","first-page":"2342","article-title":"Is SOD1 loss of function involved in amyotrophic lateral sclerosis?","volume":"136","author":"Saccon","year":"2013","journal-title":"Brain (London, England: 1878)"},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0355","doi-asserted-by":"crossref","DOI":"10.1002\/jev2.12397","article-title":"Recommendations for reproducibility of cerebrospinal fluid extracellular vesicle studies","volume":"13","author":"Sandau","year":"2024","journal-title":"J. Extracell. Vesicles"},{"issue":"12","key":"10.1016\/j.nbd.2024.106718_bb0360","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":"Sato","year":"2005","journal-title":"Neurology"},{"issue":"11","key":"10.1016\/j.nbd.2024.106718_bb0365","doi-asserted-by":"crossref","first-page":"6904","DOI":"10.1074\/jbc.M510764200","article-title":"Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase","volume":"281","author":"Sentman","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.nbd.2024.106718_bb0370","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1161\/01.STR.23.4.515","article-title":"Release of superoxide dismutase into cerebrospinal fluid as a marker of brain lesion in acute cerebral infarction","volume":"23","author":"Strand","year":"1992","journal-title":"Stroke"},{"issue":"3","key":"10.1016\/j.nbd.2024.106718_bb0375","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1093\/clinchem\/34.3.497","article-title":"A simple method for clinical assay of superoxide dismutase","volume":"34","author":"Sun","year":"1988","journal-title":"Clin. Chem."},{"issue":"8","key":"10.1016\/j.nbd.2024.106718_bb0380","doi-asserted-by":"crossref","DOI":"10.3390\/ijms22084155","article-title":"A metal-free, disulfide oxidized form of superoxide dismutase 1 as a primary misfolded species with prion-like properties in the extracellular environments surrounding motor neuron-like cells","volume":"22","author":"Takashima","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0385","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/nn1603","article-title":"Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis","volume":"9","author":"Urushitani","year":"2006","journal-title":"Nat. Neurosci."},{"issue":"10","key":"10.1016\/j.nbd.2024.106718_bb0390","doi-asserted-by":"crossref","first-page":"3582","DOI":"10.1016\/S0021-9258(19)43969-0","article-title":"Superoxide dismutase. Organelle specificity","volume":"248","author":"Weisiger","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.nbd.2024.106718_bb0395","article-title":"A brief overview of the cerebrospinal fluid system and its implications for brain and spinal cord diseases","volume":"15","author":"Wichmann","year":"2021","journal-title":"Front. Hum. Neurosci."},{"key":"10.1016\/j.nbd.2024.106718_bb0400","doi-asserted-by":"crossref","DOI":"10.1016\/j.eclinm.2024.102495","article-title":"Effects of tofersen treatment in patients with SOD1-ALS in a \u201creal-world\u201d setting - a 12-month multicenter cohort study from the German early access program","volume":"69","author":"Wiesenfarth","year":"2024","journal-title":"EClinicalMedicine"},{"issue":"2","key":"10.1016\/j.nbd.2024.106718_bb0405","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1001\/jamaneurol.2013.593","article-title":"SOD1 in cerebral spinal fluid as a pharmacodynamic marker for antisense oligonucleotide therapy","volume":"70","author":"Winer","year":"2013","journal-title":"JAMA Neurol."},{"issue":"1","key":"10.1016\/j.nbd.2024.106718_bb0410","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1471-4159.2011.07177.x","article-title":"Misfolded superoxide dismutase-1 in CSF from amyotrophic lateral sclerosis patients","volume":"117","author":"Zetterstrom","year":"2011","journal-title":"J. Neurochem."}],"container-title":["Neurobiology of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969996124003206?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969996124003206?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,12,2]],"date-time":"2024-12-02T10:28:14Z","timestamp":1733135294000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969996124003206"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11]]},"references-count":82,"alternative-id":["S0969996124003206"],"URL":"https:\/\/doi.org\/10.1016\/j.nbd.2024.106718","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.06.15.599161","asserted-by":"object"}]},"ISSN":["0969-9961"],"issn-type":[{"value":"0969-9961","type":"print"}],"subject":[],"published":{"date-parts":[[2024,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Specific analysis of SOD1 enzymatic activity in CSF from ALS patients with and without SOD1 mutations","name":"articletitle","label":"Article Title"},{"value":"Neurobiology of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.nbd.2024.106718","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"106718"}}