Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment.

@article{Maynard2009AccumulationOU,
  title={Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment.},
  author={Christa J. Maynard and Claudia B{\"o}ttcher and Zaira Ortega and Ruben Smith and Bogdan I Florea and Miguel D{\'i}az-Hern{\'a}ndez and Patrik Brundin and Herman S Overkleeft and Jia-yi Li and Jos{\'e} J Lucas and Nico P Dantuma},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 33},
  pages={13986-91}
}
Aggregation-prone proteins have been suggested to overwhelm and impair the ubiquitin/proteasome system (UPS) in polyglutamine (polyQ) disorders, such as Huntington's disease (HD). Overexpression of an N-terminal fragment of mutant huntingtin (N-mutHtt), an aggregation-prone polyQ protein responsible for HD, obstructs the UPS in cellular models. Furthermore, based on the accumulation of polyubiquitin conjugates in brains of R6/2 mice, which express human N-mutHtt and are one of the most severe… CONTINUE READING

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