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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.
Molecular Cell|April 14, 2009
Motor mechanism for protein threading through Hsp104Petra Wendler, James Shorter, David Snead, et al.
Molecular Cell|June 3, 2014
A cellular system that degrades misfolded proteins and protects against neurodegenerationLili Guo, Benoit I Giasson, Alex Glavis-Bloom, et al.
Nature|August 19, 2021
DAXX represents a new type of protein-folding enablerLiangqian Huang, Trisha Agrawal, Guixin Zhu, et al.
Biorxiv : the Preprint Server for Biology|November 26, 2025
Nuclear-import receptors remodel the dilute phase to suppress phase transitions of RNA-binding proteins with prion-like domainsMiriam Linsenmeier, Min Kyung Shinn, Thomas R Mumford, et al.
The Journal of Cell Biology|June 19, 2002
Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusionJoyce M M Muller, James Shorter, Richard Newman, et al.
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.
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