Title : Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis.

Pub. Date : 2003 Nov 28

PMID : 14623191






2 Functional Relationships(s)
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1 To further characterize the folding of SOD1, we study the role of cysteine residues in folding and find that non-native disulfide bond formation may significantly alter SOD1 folding dynamics and aggregation propensity. Disulfides superoxide dismutase 1 Homo sapiens
2 To further characterize the folding of SOD1, we study the role of cysteine residues in folding and find that non-native disulfide bond formation may significantly alter SOD1 folding dynamics and aggregation propensity. Disulfides superoxide dismutase 1 Homo sapiens