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Medicinal Research Reviews|February 12, 2020
The clinical trial landscape in amyotrophic lateral sclerosis-Past, present, and futureHeike J Wobst, Korrie L Mack, Dean G Brown, et al.
Nature Structural & Molecular Biology|January 30, 2007
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activityShannon M Doyle, James Shorter, Michal Zolkiewski, et al.
Cell|December 28, 2007
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104Petra Wendler, James Shorter, Celia Plisson, et al.
ACS Chemical Neuroscience|May 13, 2022
Sequestration of TDP-43<sup>216-414</sup> Aggregates by Cytoplasmic Expression of the proSAAS ChaperoneJuan R Peinado, Kriti Chaplot, Timothy S Jarvela, et al.
The Journal of Clinical Investigation|August 16, 2008
Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson diseaseChristophe Lo Bianco, James Shorter, Etienne Régulier, et al.
Plos One|March 13, 2008
Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activitiesHeather Sadlish, Heike Rampelt, James Shorter, et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience|October 16, 2015
Chaperones in NeurodegenerationIris Lindberg, James Shorter, R Luke Wiseman, et al.
The Journal of Biological Chemistry|January 10, 2016
Mechanistic Insights into Hsp104 PotentiationMariana P Torrente, Edward Chuang, Megan M Noll, et al.
Plos Genetics|October 3, 2024
The middle domain of Hsp104 can ensure substrates are functional after processingHannah E Buchholz, Jane E Dorweiler, Sam Guereca, et al.
The Journal of Biological Chemistry|May 26, 2009
TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicityBrian S Johnson, David Snead, Jonathan J Lee, et al.
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