Abstract
Background: Cu, Zn-superoxide dismutase (SOD1) possesses a highly conserved intramolecular disulfide bond. Results: Structural destabilization of SOD1 scrambles the intramolecular disulfide to form cross-linked oligomers with an intermolecular disulfide bond. Conclusion: Disulfide scrambling is a key to understand the folding/misfolding process of SOD1. Significance: A disulfide-scrambling model provides a molecular pathomechanism describing the formation of disulfide-linked SOD1 oligomers in amyotrophic lateral sclerosis.
Original language | English |
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Pages (from-to) | 4970-4980 |
Number of pages | 11 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2013 Feb 15 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology