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COPPER-ZINC SUPEROXIDE DISMUTASE AND AMYOTROPHIC LATERAL SCLEROSIS
Abstract
▪ Abstract Copper-zinc superoxide dismutase (CuZnSOD, SOD1 protein) is an abundant copper- and zinc-containing protein that is present in the cytosol, nucleus, peroxisomes, and mitochondrial intermembrane space of human cells. Its primary function is to act as an antioxidant enzyme, lowering the steady-state concentration of superoxide, but when mutated, it can also cause disease. Over 100 different mutations have been identified in the sod1 genes of patients diagnosed with the familial form of amyotrophic lateral sclerosis (fALS). These mutations result in a highly diverse group of mutant proteins, some of them very similar to and others enormously different from wild-type SOD1. Despite their differences in properties, each member of this diverse set of mutant proteins causes the same clinical disease, presenting a challenge in formulating hypotheses as to what causes SOD1-associated fALS. In this review, we draw together and summarize information from many laboratories about the characteristics of the individual mutant SOD1 proteins in vivo and in vitro in the hope that it will aid investigators in their search for the cause(s) of SOD1-associated fALS.
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Metadata
- Authors
- Valentine, J. S., Doucette, P. A., & Zittin Potter, S.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2005-06-01
- Volume
- 74
- Issue
- 1
- Pages
- 563-593
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2105442888
- Cited by
- 785
- References
- 7
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- closed
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