A pathological link between dysregulated copper binding in Cu/Zn-superoxide dismutase and amyotrophic lateral sclerosis
Author:
Affiliation:
1. Department of Chemistry, Keio University
Publisher
The Society for Free Radical Research Japan
Subject
Clinical Biochemistry,Nutrition and Dietetics,Medicine (miscellaneous)
Link
https://www.jstage.jst.go.jp/article/jcbn/71/2/71_22-42/_pdf
Reference63 articles.
1. 1 McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 244: 6049–6055.
2. 2 Miller AF. Superoxide dismutases: ancient enzymes and new insights. FEBS Lett 2012; 586: 585–595.
3. 3 Gralla EB, Valentine JS. Null mutants of Saccharomyces cerevisiae Cu,Zn superoxide dismutase: characterization and spontaneous mutation rates. J Bacteriol 1991; 173: 5918–5920.
4. 4 Phillips JP, Campbell SD, Michaud D, Charbonneau M, Hilliker AJ. Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity. Proc Natl Acad Sci U S A 1989; 86: 2761–2765.
5. 5 Saccon RA, Bunton-Stasyshyn RK, Fisher EM, Fratta P. Is SOD1 loss of function involved in amyotrophic lateral sclerosis? Brain 2013; 136 (Pt 8): 2342–2358.
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