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Biochim Biophys Acta. 2006 Nov-Dec;1762(11-12):1025-37. Epub 2006 May 22.

Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.

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  • 1Department of Biochemistry, University of Toronto, University Health Network, Toronto Medical Discovery Tower, Medical and Related Sciences (MaRS), 101 College Street, Toronto, ON, Canada, M5G 1L7.

Abstract

Fourteen years after the discovery that mutations in Cu, Zn superoxide dismutase (SOD1) cause a subset of familial amyotrophic lateral sclerosis (fALS), the mechanism by which mutant SOD1 exerts toxicity remains unknown. The two principle hypotheses are (a) oxidative damage stemming from aberrant SOD1 redox chemistry, and (b) misfolding of the mutant protein. Here we review the structure and function of wild-type SOD1, as well as the changes to the structure and function in mutant SOD1. The relative merits of the two hypotheses are compared and a common unifying principle is outlined. Lastly, the potential for therapies targeting SOD1 misfolding is discussed.

PMID:
16814528
[PubMed - indexed for MEDLINE]
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