Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models.

@article{Bergemalm2006OverloadingOS,
  title={Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models.},
  author={Daniel Bergemalm and Per Andreas Jonsson and Karin Sixtensdotter Graffmo and Peter Munch Andersen and Thomas Br{\"a}nnstr{\"o}m and Anna Rehnmark and Stefan L Marklund},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2006},
  volume={26 16},
  pages={4147-54}
}
Mutants of human superoxide dismutase-1 (hSOD1) cause amyotrophic lateral sclerosis (ALS), and mitochondria are thought to be primary targets of the cytotoxic action. The high expression rates of hSOD1s in transgenic ALS models give high levels of the stable mutants G93A and D90A as well as the wild-type human enzyme, significant proportions of which lack Cu and the intrasubunit disulfide bond. The endogenous murine SOD1 (mSOD1) also lacks Cu and is disulfide reduced but is active and oxidized… CONTINUE READING

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