The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein.

@article{Zhou2006TheOS,
  title={The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein.},
  author={Wenbo Zhou and Min Zhu and Mark A. Wilson and Gregory A. Petsko and Anthony L. Fink},
  journal={Journal of molecular biology},
  year={2006},
  volume={356 4},
  pages={1036-48}
}
DJ-1 has been reported to have chaperone activity by preventing the aggregation of some proteins, and by structural analogy to Hsp31. The L166P mutation has been linked to a familial early onset form of Parkinson's disease (PD). Since the aggregation of alpha-synuclein is believed to be a critical step in the etiology of PD, we have investigated the interaction of wild-type DJ-1 and its oxidized forms with alpha-synuclein. Native (unoxidized) DJ-1 did not inhibit alpha-synuclein fibrillation… CONTINUE READING
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