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Mutations in superoxide dismutase 1 (SOD1) associated with familial amyotrophic lateral sclerosis induce misfolding and aggregation of the protein with the inherent propensity of mutant SOD1 to aggregate generally correlating, with a few exceptions, to the duration of illness in patients with the same mutation. One notable exception was the D101N variant, which has been described as wild‐type‐like...
J. Neurochem. (2012) 121, 475–485.
AbstractMutations in superoxide dismutase 1 (SOD1) cause familial amyotrophic lateral sclerosis. The Cu‐binding capacity of SOD1 has spawned hypotheses that implicate metal‐mediated production of reactive species as a potential mechanism of toxicity. In past experiments, we have tested such hypotheses by mutating residues in SOD1 that normally coordinate the binding...
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