Article
Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.
Open biology - 1 Jun 2024
McAlary Luke, Nan Jeremy R, Shyu Clay, Sher Mine, Plotkin Steven S, Cashman Neil R
Abstract excerpt
Mutations in the protein superoxide dismutase-1 (SOD1) promote its misfolding and aggregation, ultimately causing familial forms of the debilitating neurodegenerative disease amyotrophic lateral sclerosis (ALS). Currently, over 220 (mostly missense) ALS-causing mutations in the SOD1 protein have been identified, indicating that common structural features are responsible for aggregation and toxicity. Using in...
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