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SOD1 aggregation and ALS: Role of metallation states and disulfide status

Title
SOD1 aggregation and ALS: Role of metallation states and disulfide status
Authors
Sheng Y.Chattopadhyay M.Whitelegge J.Valentine J.S.
Ewha Authors
Joan S. Valentine
SCOPUS Author ID
Joan S. Valentinescopus
Issue Date
2012
Journal Title
Current Topics in Medicinal Chemistry
ISSN
1568-0266JCR Link
Citation
vol. 12, no. 22, pp. 2560 - 2572
Indexed
SCIE; SCOPUS WOS scopus
Abstract
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the death of motor neurons. About 10% of ALS cases are inherited (familial), and a large subset of them are caused by mutations in the gene encoding the copper-zinc superoxide dismutase (SOD1). The detection of SOD1-positive inclusions in familial ALS patients suggests the role of SOD1 aggregation underlying the pathology of familial ALS. Although SOD1 mutant proteins are different in structure, stability and activity, they all exhibit a higher aggregation propensity than wild-type SOD1. We here review the recent studies on the role of metallation states and disulfide status in the unfolding, misfolding, and aggregation of SOD1. Investigations of the mechanism of SOD1 aggregation enhance our understanding of onset and progression of ALS and have implications for therapeutic approaches for treating ALS. © 2012 Bentham Science Publishers.
DOI
10.2174/1568026611212220010
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일반대학원 > 바이오융합과학과 > Journal papers
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