A Limited Role for Disulfide Cross-linking in the Aggregation of Mutant SOD1 Linked to Familial Amyotrophic Lateral Sclerosis

One of the mechanisms by which mutations in superoxide dismutase 1 (SOD1) cause familial amyotrophic lateral sclerosis (fALS) is proposed to involve the accumulation of detergent-insoluble, disulfide-cross-linked, mutant protein. Recent studies have implicated cysteine residues at positions 6 and 11...

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Bibliographic Details
Main Authors: Karch, Celeste M., Borchelt, David R.
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2008
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2376231/
https://ncbi.nlm.nih.gov/pubmed/18316367
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M800564200
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