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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.
Biorxiv : the Preprint Server for Biology|September 21, 2023
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.
Molecular Cell|April 14, 2009
Motor mechanism for protein threading through Hsp104Petra Wendler, James Shorter, David Snead, et al.
Science (New York, N.Y.)|May 7, 2026
Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegenerationKatie E Copley, Jocelyn C Mauna, Helen L Danielson, 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.
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