Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.

@article{Rodrguez2002FamilialAL,
  title={Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.},
  author={Jorge A. Rodr{\'i}guez and Joan Selverstone Valentine and Daryl K. Eggers and James A. Roe and Ashutosh Tiwari and R. H. Brown and Lawrence J. Hayward},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 18},
  pages={15932-7}
}
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc superoxide dismutase (SOD1) associated with familial amyotrophic lateral sclerosis (FALS). Multiple endothermic unfolding transitions were observed by differential scanning calorimetry for partially metallated SOD1 enzymes isolated from a baculovirus system. We correlated the metal ion contents of SOD1 variants with the occurrence of distinct melting transitions. Altered thermal stability upon… CONTINUE READING
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Stability of FALS-associated Mutant SOD1 Enzymes

  • B. A. Hosler, G. A. Nicholson, +14 authors Jr.
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