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Nature Structural & Molecular Biology|August 2, 2016
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationAdam L Yokom, Stephanie N Gates, Meredith E Jackrel, et al.
Cell Reports|September 28, 2022
Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3Ryan R Cupo, Alexandrea N Rizo, Gabriel A Braun, et al.
The Journal of Biological Chemistry|November 28, 2013
Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregationMorgan E Desantis, Elizabeth A Sweeny, David Snead, et al.
Nature Chemical Biology|November 17, 2009
A synergistic small-molecule combination directly eradicates diverse prion strain structuresBlake E Roberts, Martin L Duennwald, Huan Wang, et al.
Neuron|March 12, 2019
Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell DeathFatima Gasset-Rosa, Shan Lu, Haiyang Yu, et al.
Molecular Cell|January 9, 2026
Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domainsLin Guo, Jacob R Mann, Jocelyn C Mauna, et al.
FEMS Yeast Research|May 23, 2018
Potentiating Hsp104 activity via phosphomimetic mutations in the middle domainAmber Tariq, JiaBei Lin, Megan M Noll, et al.
The Biochemical Journal|August 22, 2014
Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assemblyKatelyn M Seither, Heather A McMahon, Nikita Singh, et al.
Biochemistry|April 6, 2017
Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 StructuresClarissa L Weaver, Elizabeth C Duran, Korrie L Mack, et al.
Molecular Cell|January 27, 2015
The Hsp104 N-terminal domain enables disaggregase plasticity and potentiationElizabeth A Sweeny, Meredith E Jackrel, Michelle S Go, et al.
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