CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo.

@article{Miller2005CHIPSP,
  title={CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo.},
  author={Victor M. Miller and Rick F Nelson and Cynthia M. Gouvion and Aislinn Joanmarie Williams and Edgardo Rodr{\'i}guez-Lebr{\'o}n and Scott Q. Harper and Beverly L. Davidson and Michael R. Rebagliati and Henry L. Paulson},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2005},
  volume={25 40},
  pages={
          9152-61
        }
}
Huntington's disease (HD) and other polyglutamine (polyQ) neurodegenerative diseases are characterized by neuronal accumulation of the disease protein, suggesting that the cellular ability to handle abnormal proteins is compromised. As both a cochaperone and ubiquitin ligase, the C-terminal Hsp70 (heat shock protein 70)-interacting protein (CHIP) links the two major arms of protein quality control, molecular chaperones, and the ubiquitin-proteasome system. Here, we demonstrate that CHIP… CONTINUE READING

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