Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.

@article{Vassall2011DecreasedSA,
  title={Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.},
  author={Kenrick A. Vassall and Helen R Stubbs and Heather A. Primmer and Ming Sze Tong and Sarah M Sullivan and Ryan E Sobering and Saipraveen Srinivasan and L K Bri{\`e}re and S. D. Dunn and Wilfredo Col{\'o}n and Elizabeth M. Meiering},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 6},
  pages={2210-5}
}
Protein aggregation is a hallmark of many diseases, including amyotrophic lateral sclerosis (ALS), where aggregation of Cu/Zn superoxide dismutase (SOD1) is implicated in causing neurodegeneration. Recent studies have suggested that destabilization and aggregation of the most immature form of SOD1, the disulfide-reduced, unmetallated (apo) protein is particularly important in causing ALS. We report herein in depth analyses of the effects of chemically and structurally diverse ALS-associated… CONTINUE READING
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Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form

  • A Kerman
  • Acta Neuropathol
  • 2010
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