Highly Influenced
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} }
- Published in Cell 2014
DOI:10.1016/j.cell.2013.11.047
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