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• W1998275064 endingPage "487" @default.
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• W1998275064 abstract "Mutations to the ubiquitous antioxidant enzyme Cu/Zn superoxide dismutase (SOD1) were the first established genetic cause of the fatal, adult-onset neurodegenerative disease amyotrophic lateral sclerosis (ALS). It is widely accepted that these mutations do not cause ALS via a loss of antioxidant function, but elucidating the alternate toxic gain of function has proven to be elusive. Under physiological conditions, SOD1 binds one copper ion and one zinc ion per monomer to form a highly stable and functional homodimer, but there is now ample evidence to indicate aberrant persistence of SOD1 in an intermediate metal-deficient state may contribute to the protein’s involvement in ALS. This review briefly discusses some of the data to support a role for metal-deficient SOD1 in the development of ALS and some of the outcomes from drug development studies that have aimed to modify the symptoms of ALS by targeting the metal state of SOD1. The implications for the metal state of SOD1 in cases of sporadic ALS that do not involve mutant SOD1 are also discussed." @default.
• W1998275064 created "2016-06-24" @default.
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• W1998275064 creator A5026838566 @default.
• W1998275064 creator A5045915090 @default.
• W1998275064 date "2015-03-11" @default.
• W1998275064 modified "2023-10-01" @default.
• W1998275064 title "Metal-deficient SOD1 in amyotrophic lateral sclerosis" @default.
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• W1998275064 doi "https://doi.org/10.1007/s00109-015-1273-3" @default.
• W1998275064 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4408375" @default.
• W1998275064 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25754173" @default.
• W1998275064 hasPublicationYear "2015" @default.
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