Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease.

@article{Ju2008ImpairedPA,
  title={Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease.},
  author={Jeong-sun Ju and Sara E. Miller and Phyllis I Hanson and Conrad Chris Weihl},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 44},
  pages={30289-99}
}
Mutations in p97/VCP cause the multisystem disease inclusion body myopathy, Paget disease of the bone and frontotemporal dementia (IBMPFD). p97/VCP is a member of the AAA+ (ATPase associated with a variety of activities) protein family and has been implicated in multiple cellular processes. One pathologic feature in IBMPFD is ubiquitinated inclusions, suggesting that mutations in p97/VCP may affect protein degradation. The present study shows that IBMPFD mutant expression increases… CONTINUE READING
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