Article
Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes.
Biophysical chemistry - 1 Sept 2022
Deol Harmeen K, Broom Helen R, Siebeneichler Bruna, Lee Brenda, Leonenko Zoya, Meiering Elizabeth M
Abstract excerpt
Protein misfolding and aggregation are hallmarks of many diseases, including amyotrophic lateral sclerosis (ALS). In familial ALS, aberrant self-association of mutant Cu,Zn-superoxide dismutase (SOD1) is implicated as a key contributor to disease. Mutations have the largest impacts on the stability of the most immature form of SOD1, the unmetallated, disulfide-reduced monomer (apoSH SOD1). Here we demonstrate...
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