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J Biol Chem"},{"key":"CIT0086","first-page":"47551","volume":"277","author":"Rakhit R","year":"2002","journal-title":"Oxidation- induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. J Biol Chem"},{"key":"CIT0087","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s004010000312","volume":"101","author":"Sitte HH","year":"2001","journal-title":"Acta Neuropathol"},{"key":"CIT0088","first-page":"819","volume":"44","author":"Pedersen WA","year":"1998","journal-title":"Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. 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