Article
Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1.
Protein science : a publication of the Protein Society - 1 Dec 2015
Broom Helen R, Rumfeldt Jessica A O, Vassall Kenrick A, Meiering Elizabeth M
Abstract excerpt
Neurotoxic misfolding of Cu, Zn-superoxide dismutase (SOD1) is implicated in causing amyotrophic lateral sclerosis, a devastating and incurable neurodegenerative disease. Disease-linked mutations in SOD1 have been proposed to promote misfolding and aggregation by decreasing protein stability and increasing the proportion of less folded forms of the protein. Here we report direct measurement of the thermodynamic...
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