Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events

@article{Jackrel2014PotentiatedHV,
  title={Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events},
  author={Meredith E Jackrel and Morgan E DeSantis and Bryan A. Martinez and Laura M. Castellano and Rachel M. Stewart and Kim A. Caldwell and Guy A Caldwell and James Shorter},
  journal={Cell},
  year={2014},
  volume={156},
  pages={170-182}
}
There are no therapies that reverse the proteotoxic misfolding events that underpin fatal neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD). Hsp104, a conserved hexameric AAA+ protein from yeast, solubilizes disordered aggregates and amyloid but has no metazoan homolog and only limited activity against human neurodegenerative disease proteins. Here, we reprogram Hsp104 to rescue TDP-43, FUS, and α-synuclein proteotoxicity by mutating single… CONTINUE READING
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