A toxic mutant huntingtin species is resistant to selective autophagy.

@article{Fu2017ATM,
  title={A toxic mutant huntingtin species is resistant to selective autophagy.},
  author={Yuhua Fu and Peng Wu and Yuyin Pan and Xiaoli Sun and Hui-ya Yang and M. DiFiglia and B. Lu},
  journal={Nature chemical biology},
  year={2017},
  volume={13 11},
  pages={
          1152-1154
        }
}
Protein misfolding is a common theme in neurodegenerative disorders including Huntington's disease (HD). The HD-causing mutant huntingtin protein (mHTT) has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, and the most toxic of these is the one recognized by antibody 3B5H10. Here we show that the 3B5H10-recognized mHTT species has a slower degradation rate due to its resistance to selective autophagy in human cells and brains, revealing mechanisms of its higher… Expand
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