Article
A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.
Structure (London, England : 1993) - 1 Nov 2016
Fay James M, Zhu Cheng, Proctor Elizabeth A, Tao Yazhong, Cui Wenjun, Ke Hengming, Dokholyan Nikolay V
Abstract excerpt
The majority of amyotrophic lateral sclerosis (ALS)-related mutations in the enzyme Cu,Zn superoxide dismutase (SOD1), as well as a post-translational modification, glutathionylation, destabilize the protein and lead to a misfolded oligomer that is toxic to motor neurons. The biophysical role of another physiological SOD1 modification, T2-phosphorylation, has remained a mystery. Here, we find that a...
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