Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.

@article{Ferri2006FamilialAD,
  title={Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.},
  author={Alberto Ferri and Mauro Cozzolino and Claudia Crosio and Monica Nencini and Arianna Casciati and Edith Butler Gralla and Giuseppe Rotilio and Joan Selverstone Valentine and Maria Teresa Carr{\`i}},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 37},
  pages={13860-5}
}
Recent studies suggest that the toxicity of familial amyotrophic lateral sclerosis mutant Cu, Zn superoxide dismutase (SOD1) arises from its selective recruitment to mitochondria. Here we demonstrate that each of 12 different familial ALS-mutant SOD1s with widely differing biophysical properties are associated with mitochondria of motoneuronal cells to a much greater extent than wild-type SOD1, and that this effect may depend on the oxidation of Cys residues. We demonstrate further that mutant… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 93 extracted citations

References

Publications referenced by this paper.

Protein Sci 14:1201–1213

  • S Antonyuk, JS Elam, +7 authors SS Hasnain
  • 2005

Similar Papers

Loading similar papers…