Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS.

@article{Yamashita2007HeatshockP1,
  title={Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS.},
  author={Hirofumi Yamashita and Jun Kawamata and Katsuya Okawa and Rie Kanki and Tomoki Nakamizo and Takumi Hatayama and Koji Yamanaka and Ryosuke Takahashi and Shun Shimohama},
  journal={Journal of neurochemistry},
  year={2007},
  volume={102 5},
  pages={1497-1505}
}
A dominant mutation in the gene for copper-zinc superoxide dismutase (SOD1) is the most frequent cause of the inherited form of amyotrophic lateral sclerosis. Mutant SOD1 provokes progressive degeneration of motor neurons by an unidentified acquired toxicity. Exploiting both affinity purification and mass spectrometry, we identified a novel interaction between heat-shock protein 105 (Hsp105) and mutant SOD1. We detected this interaction both in spinal cord extracts of mutant SOD1(G93A… CONTINUE READING

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