Background: Protein aggregation is a hallmark of neurodegenerative diseases. Results: Oxidation of the hSOD1-Trp 32 residue promotes enzyme covalent dimerization, oligomerization, and aggregation. Conclusion: A novel pathway for hSOD1 aggregation is revealed. Significance: The uniqueness of the Trp 32 residue makes its oxidation potentially relevant to ALS pathogenesis.
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