{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T13:13:02Z","timestamp":1790341982746,"version":"4.1.0"},"reference-count":62,"publisher":"Oxford University Press (OUP)","issue":"8","license":[{"start":{"date-parts":[[2019,7,23]],"date-time":"2019-07-23T00:00:00Z","timestamp":1563840000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R01 CA182804"],"award-info":[{"award-number":["R01 CA182804"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Superoxide dismutase 1 (SOD1) is the principal cytoplasmic superoxide dismutase in humans and plays a major role in redox potential regulation. It catalyses the transformation of the superoxide anion (O2\u2022\u2212) into hydrogen peroxide. Heterozygous variants in SOD1 are a common cause of familial amyotrophic lateral sclerosis. In this study we describe the homozygous truncating variant c.335dupG (p.C112Wfs*11) in SOD1 that leads to total absence of enzyme activity. The resulting phenotype is severe and marked by progressive loss of motor abilities, tetraspasticity with predominance in the lower extremities, mild cerebellar atrophy, and hyperekplexia-like symptoms. Heterozygous carriers have a markedly reduced enzyme activity when compared to wild-type controls but show no overt neurologic phenotype. These results are in contrast with the previously proposed theory that a loss of function is the underlying mechanism in SOD1-related motor neuron disease and should be considered before application of previously proposed SOD1 silencing as a treatment option for amyotrophic lateral sclerosis.<\/jats:p>","DOI":"10.1093\/brain\/awz182","type":"journal-article","created":{"date-parts":[[2019,6,5]],"date-time":"2019-06-05T07:14:00Z","timestamp":1559718840000},"page":"2230-2237","source":"Crossref","is-referenced-by-count":92,"title":["SOD1 deficiency: a novel syndrome distinct from amyotrophic lateral sclerosis"],"prefix":"10.1093","volume":"142","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2305-9948","authenticated-orcid":false,"given":"Julien H","family":"Park","sequence":"first","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christiane","family":"Elpers","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janine","family":"Reunert","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael L","family":"McCormick","sequence":"additional","affiliation":[{"name":"Free Radical and Radiation Biology Program, Department of Radiation Oncology, Holden Comprehensive Cancer Center, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julia","family":"Mohr","sequence":"additional","affiliation":[{"name":"CeGaT GmbH und Praxis f\u00fcr Humangenetik T\u00fcbingen, T\u00fcbingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saskia","family":"Biskup","sequence":"additional","affiliation":[{"name":"CeGaT GmbH und Praxis f\u00fcr Humangenetik T\u00fcbingen, T\u00fcbingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oliver","family":"Schwartz","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephan","family":"Rust","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marianne","family":"Gr\u00fcneberg","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"Seelh\u00f6fer","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrike","family":"Schara","sequence":"additional","affiliation":[{"name":"Department of Paediatric Neurology, University Hospital Essen, Essen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugen","family":"Boltshauser","sequence":"additional","affiliation":[{"name":"Department of Paediatric Neurology, University Children\u2019s Hospital, Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1254-8765","authenticated-orcid":false,"given":"Douglas R","family":"Spitz","sequence":"additional","affiliation":[{"name":"Free Radical and Radiation Biology Program, Department of Radiation Oncology, Holden Comprehensive Cancer Center, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thorsten","family":"Marquardt","sequence":"additional","affiliation":[{"name":"Department of General Paediatrics, University of M\u00fcnster, M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2019,7,25]]},"reference":[{"key":"2019080505443204000_awz182-B1","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1038\/nmeth0410-248","article-title":"A method and server for predicting damaging missense mutations","volume":"7","author":"Adzhubei","year":"2010","journal-title":"Nat Methods"},{"key":"2019080505443204000_awz182-B2","doi-asserted-by":"crossref","first-page":"13541","DOI":"10.1074\/jbc.R111.312181","article-title":"Battles with iron: manganese in oxidative stress protection","volume":"287","author":"Aguirre","year":"2012","journal-title":"J Biol Chem"},{"key":"2019080505443204000_awz182-B3","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1002\/ana.10369","article-title":"\u201cTrue\u201d sporadic ALS associated with a novel SOD-1 mutation","volume":"52","author":"Alexander","year":"2002","journal-title":"Ann Neurol"},{"key":"2019080505443204000_awz182-B4","doi-asserted-by":"crossref","first-page":"6371","DOI":"10.1074\/jbc.M209915200","article-title":"Analysis of the cytosolic proteome in a cell culture model of familial amyotrophic lateral sclerosis reveals alterations to the proteasome, antioxidant defenses, and nitric oxide synthetic pathways","volume":"278","author":"Allen","year":"2003","journal-title":"J Biol Chem"},{"issue":"Pt 4","key":"2019080505443204000_awz182-B5","first-page":"1153","article-title":"Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation","volume":"119","author":"Andersen","year":"1996","journal-title":"A clinical and genealogical study of 36 patients. Brain"},{"key":"2019080505443204000_awz182-B6","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":"2019080505443204000_awz182-B7","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"},{"key":"2019080505443204000_awz182-B8","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.ijrobp.2017.10.019","article-title":"Phase 1b\/2a trial of the superoxide dismutase mimetic GC4419 to reduce chemoradiotherapy-induced oral mucositis in patients with oral cavity or oropharyngeal carcinoma","volume":"100","author":"Anderson","year":"2018","journal-title":"Int J Radiat Oncol Biol Phys"},{"key":"2019080505443204000_awz182-B9","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1203\/PDR.0b013e3181a9eafb","article-title":"Oxygen toxicity and reactive oxygen species: the devil is in the details","volume":"66","author":"Auten","year":"2009","journal-title":"Pediatr Res"},{"key":"2019080505443204000_awz182-B10","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1136\/jnnp-2016-313521","article-title":"Defining SOD1 ALS natural history to guide therapeutic clinical trial design","volume":"88","author":"Bali","year":"2017","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"2019080505443204000_awz182-B11","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.neuron.2006.09.018","article-title":"ALS: a disease of motor neurons and their nonneuronal neighbors","volume":"52","author":"Boillee","year":"2006","journal-title":"Neuron"},{"key":"2019080505443204000_awz182-B12","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":"2019080505443204000_awz182-B13","doi-asserted-by":"crossref","first-page":"eaau6414","DOI":"10.1126\/scitranslmed.aau6414","article-title":"Safe and effective superoxide dismutase 1 silencing using artificial microRNA in macaques","volume":"10","author":"Borel","year":"2018","journal-title":"Sci Transl Med"},{"key":"2019080505443204000_awz182-B14","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":"2019080505443204000_awz182-B15","doi-asserted-by":"crossref","first-page":"2745","DOI":"10.1093\/bioinformatics\/btv195","article-title":"PROVEAN web server: a tool to predict the functional effect of amino acid substitutions and indels","volume":"31","author":"Choi","year":"2015","journal-title":"Bioinformatics"},{"key":"2019080505443204000_awz182-B16","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s12275-017-6647-5","article-title":"Unraveling new functions of superoxide dismutase using yeast model system: beyond its conventional role in superoxide radical scavenging","volume":"55","author":"Chung","year":"2017","journal-title":"J Microbiol"},{"key":"2019080505443204000_awz182-B17","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1038\/378342a0","article-title":"Toxic mutants in Charcot's sclerosis","volume":"378","author":"Cleveland","year":"1995","journal-title":"Nature"},{"key":"2019080505443204000_awz182-B18","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/0003-9861(92)90282-2","article-title":"Antioxidant effect of manganese","volume":"299","author":"Coassin","year":"1992","journal-title":"Arch Biochem Biophys"},{"key":"2019080505443204000_awz182-B19","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0006-8993(95)00063-V","article-title":"Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS)","volume":"676","author":"Dal Canto","year":"1995","journal-title":"Brain Res"},{"key":"2019080505443204000_awz182-B20","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1093\/hmg\/ddm226","article-title":"Familial amyotrophic lateral sclerosis-linked SOD1 mutants perturb fast axonal transport to reduce axonal mitochondria content","volume":"16","author":"De Vos","year":"2007","journal-title":"Hum Mol Genet"},{"key":"2019080505443204000_awz182-B21","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"},{"key":"2019080505443204000_awz182-B22","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/sj.onc.1208207","article-title":"CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life","volume":"24","author":"Elchuri","year":"2005","journal-title":"Oncogene"},{"key":"2019080505443204000_awz182-B23","first-page":"2","article-title":"Antimicrobial actions of reactive oxygen species","author":"Fang","year":"2011","journal-title":"mBio"},{"key":"2019080505443204000_awz182-B24","doi-asserted-by":"crossref","first-page":"9257","DOI":"10.1074\/jbc.M115.708057","article-title":"Superoxide dismutase (SOD)-mimetic M40403 is protective in cell and fly models of paraquat toxicity: IMPLICATIONS FOR PARKINSON DISEASE","volume":"291","author":"Filograna","year":"2016","journal-title":"J Biol Chem"},{"key":"2019080505443204000_awz182-B25","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.expneurol.2011.09.020","article-title":"Absence of SOD1 leads to oxidative stress in peripheral nerve and causes a progressive distal motor axonopathy","volume":"233","author":"Fischer","year":"2012","journal-title":"Exp Neurol"},{"key":"2019080505443204000_awz182-B26","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1021\/bi9020378","article-title":"Signaling functions of reactive oxygen species","volume":"49","author":"Forman","year":"2010","journal-title":"Biochemistry"},{"key":"2019080505443204000_awz182-B27","doi-asserted-by":"crossref","first-page":"2534","DOI":"10.1523\/JNEUROSCI.20-07-02534.2000","article-title":"Early and selective loss of neuromuscular synapse subtypes with low sprouting competence in motoneuron diseases","volume":"20","author":"Frey","year":"2000","journal-title":"J Neurosci"},{"key":"2019080505443204000_awz182-B28","doi-asserted-by":"crossref","first-page":"18515","DOI":"10.1074\/jbc.272.30.18515","article-title":"Superoxide anion radical (O2-.), superoxide dismutases, and related matters","volume":"272","author":"Fridovich","year":"1997","journal-title":"J Biol Chem"},{"key":"2019080505443204000_awz182-B29","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1089\/ars.2011.3999","article-title":"Superoxide dismutases: role in redox signaling, vascular function, and diseases","volume":"15","author":"Fukai","year":"2011","journal-title":"Antioxid Redox Signal"},{"key":"2019080505443204000_awz182-B30","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":"2019080505443204000_awz182-B31","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.nbd.2007.07.003","article-title":"Time course of preferential motor unit loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis","volume":"28","author":"Hegedus","year":"2007","journal-title":"Neurobiol Dis"},{"key":"2019080505443204000_awz182-B32","doi-asserted-by":"crossref","first-page":"Rc215","DOI":"10.1523\/JNEUROSCI.22-06-j0001.2002","article-title":"Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS","volume":"22","author":"Higgins","year":"2002","journal-title":"J Neurosci"},{"key":"2019080505443204000_awz182-B33","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1042\/BJ20061386","article-title":"Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production","volume":"402","author":"Iuchi","year":"2007","journal-title":"Biochem J"},{"key":"2019080505443204000_awz182-B34","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/ana.21356","article-title":"Inclusions of amyotrophic lateral sclerosis-linked superoxide dismutase in ventral horns, liver, and kidney","volume":"63","author":"Jonsson","year":"2008","journal-title":"Ann Neurol"},{"key":"2019080505443204000_awz182-B35","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.gene.2015.11.049","article-title":"Mutant SOD1 mediated pathogenesis of Amyotrophic Lateral Sclerosis","volume":"577","author":"Kaur","year":"2016","journal-title":"Gene"},{"key":"2019080505443204000_awz182-B36","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"},{"key":"2019080505443204000_awz182-B37","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0306-9877(92)90121-R","article-title":"The role of reactive oxygen species in the pathogenesis of multiple sclerosis","volume":"39","author":"LeVine","year":"1992","journal-title":"Med Hypotheses"},{"key":"2019080505443204000_awz182-B38","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.cbi.2014.10.016","article-title":"Free radicals, reactive oxygen species, oxidative stress and its classification","volume":"224","author":"Lushchak","year":"2014","journal-title":"Chem Biol Interact"},{"key":"2019080505443204000_awz182-B39","doi-asserted-by":"crossref","first-page":"4552","DOI":"10.1093\/hmg\/ddp421","article-title":"Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities","volume":"18","author":"Magrane","year":"2009","journal-title":"Hum Mol Genet"},{"key":"2019080505443204000_awz182-B40","doi-asserted-by":"crossref","first-page":"4008","DOI":"10.1210\/endo.139.9.6289","article-title":"Ovarian function in superoxide dismutase 1 and 2 knockout mice","volume":"139","author":"Matzuk","year":"1998","journal-title":"Endocrinology"},{"key":"2019080505443204000_awz182-B41","doi-asserted-by":"crossref","first-page":"3558","DOI":"10.1172\/JCI99081","article-title":"Antisense oligonucleotides extend survival and reverse decrement in muscle response in ALS models","volume":"128","author":"McCampbell","year":"2018","journal-title":"J Clin Invest"},{"key":"2019080505443204000_awz182-B42","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"},{"key":"2019080505443204000_awz182-B43","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1016\/j.freeradbiomed.2006.01.036","article-title":"Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy","volume":"40","author":"Muller","year":"2006","journal-title":"Free Radic Biol Med"},{"key":"2019080505443204000_awz182-B44","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1016\/j.ajhg.2015.11.003","article-title":"SLC39A8 deficiency: a disorder of manganese transport and glycosylation","volume":"97","author":"Park","year":"2015","journal-title":"Am J Hum Genet"},{"key":"2019080505443204000_awz182-B45","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.bbapap.2009.11.004","article-title":"The structural biochemistry of the superoxide dismutases","volume":"1804","author":"Perry","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"2019080505443204000_awz182-B46","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1093\/hmg\/8.8.1451","article-title":"Variation in the biochemical\/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds","volume":"8","author":"Ratovitski","year":"1999","journal-title":"Hum Mol Genet"},{"key":"2019080505443204000_awz182-B47","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"},{"key":"2019080505443204000_awz182-B48","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":"2019080505443204000_awz182-B49","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1093\/brain\/awt097","article-title":"Is SOD1 loss of function involved in amyotrophic lateral sclerosis?","volume":"136(Pt 8)","author":"Saccon","year":"2013","journal-title":"Brain"},{"key":"2019080505443204000_awz182-B50","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1089\/ars.2017.7249","article-title":"Comparison of whole body SOD1 knockout with muscle-specific SOD1 knockout mice reveals a role for nerve redox signaling in regulation of degenerative pathways in skeletal muscle","volume":"28","author":"Sakellariou","year":"2018","journal-title":"Antioxid Redox Signal"},{"key":"2019080505443204000_awz182-B51","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1038\/nmeth.2890","article-title":"MutationTaster2: mutation prediction for the deep-sequencing age","volume":"11","author":"Schwarz","year":"2014","journal-title":"Nat Methods"},{"key":"2019080505443204000_awz182-B52","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1212\/WNL.53.6.1239","article-title":"Mice lacking cytosolic copper\/zinc superoxide dismutase display a distinctive motor axonopathy","volume":"53","author":"Shefner","year":"1999","journal-title":"Neurology"},{"key":"2019080505443204000_awz182-B53","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/0003-2697(89)90192-9","article-title":"An assay for superoxide dismutase activity in mammalian tissue homogenates","volume":"179","author":"Spitz","year":"1989","journal-title":"Anal Biochem"},{"issue":"Chapter 7","key":"2019080505443204000_awz182-B54","first-page":"Unit7.5","article-title":"Measurement of MnSOD and CuZnSOD activity in mammalian tissue homogenates","author":"Spitz","year":"2001","journal-title":"Curr Protoc Toxicol"},{"key":"2019080505443204000_awz182-B55","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1002\/ana.24618","article-title":"Adeno-associated virus-delivered artificial microRNA extends survival and delays paralysis in an amyotrophic lateral sclerosis mouse model","volume":"79","author":"Stoica","year":"2016","journal-title":"Ann Neurol"},{"key":"2019080505443204000_awz182-B56","doi-asserted-by":"crossref","first-page":"253","DOI":"10.3109\/10715762.2010.525233","article-title":"Autophagy, reactive oxygen species and the fate of mammalian cells","volume":"45","author":"Szumiel","year":"2011","journal-title":"Free Radic Res"},{"key":"2019080505443204000_awz182-B57","doi-asserted-by":"crossref","first-page":"15587","DOI":"10.1523\/JNEUROSCI.2037-14.2014","article-title":"Delayed disease onset and extended survival in the SOD1G93A rat model of amyotrophic lateral sclerosis after suppression of mutant SOD1 in the motor cortex","volume":"34","author":"Thomsen","year":"2014","journal-title":"J Neurosci"},{"key":"2019080505443204000_awz182-B58","doi-asserted-by":"crossref","first-page":"3155","DOI":"10.1073\/pnas.93.7.3155","article-title":"Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions","volume":"93","author":"Tu","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019080505443204000_awz182-B59","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.neulet.2016.07.059","article-title":"Silencing strategies for therapy of SOD1-mediated ALS","volume":"636","author":"van Zundert","year":"2017","journal-title":"Neurosci Lett"},{"key":"2019080505443204000_awz182-B60","doi-asserted-by":"crossref","first-page":"2463","DOI":"10.1523\/JNEUROSCI.4385-04.2005","article-title":"Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice","volume":"25","author":"Vijayvergiya","year":"2005","journal-title":"J Neurosci"},{"key":"2019080505443204000_awz182-B61","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1016\/j.freeradbiomed.2012.08.570","article-title":"Knockout of SOD1 alters murine hepatic glycolysis, gluconeogenesis, and lipogenesis","volume":"53","author":"Wang","year":"2012","journal-title":"Free Radic Biol Med"},{"key":"2019080505443204000_awz182-B62","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1136\/jnnp-2016-315018","article-title":"Genetic epidemiology of amyotrophic lateral sclerosis: a systematic review and meta-analysis","volume":"88","author":"Zou","year":"2017","journal-title":"J Neurol Neurosurg psychiatry"}],"container-title":["Brain"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/brain\/advance-article-pdf\/doi\/10.1093\/brain\/awz182\/28971195\/awz182.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/brain\/article-pdf\/142\/8\/2230\/29098670\/awz182.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,19]],"date-time":"2019-09-19T22:42:02Z","timestamp":1568932922000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/brain\/article\/142\/8\/2230\/5536868"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7,25]]},"references-count":62,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2019,7,25]]},"published-print":{"date-parts":[[2019,8,1]]}},"URL":"https:\/\/doi.org\/10.1093\/brain\/awz182","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.736245410.793563142","asserted-by":"object"}]},"ISSN":["0006-8950","1460-2156"],"issn-type":[{"value":"0006-8950","type":"print"},{"value":"1460-2156","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2019,8]]},"published":{"date-parts":[[2019,7,25]]}}}