| Literature DB >> 28869595 |
Yuhua Fu1, Peng Wu1, Yuyin Pan1, Xiaoli Sun1,2, Huiya Yang1, Marian Difiglia3, Boxun Lu1,4.
Abstract
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 toxicity.Entities:
Mesh:
Substances:
Year: 2017 PMID: 28869595 DOI: 10.1038/nchembio.2461
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040