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Plos Biology|May 5, 2011
Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSZhihui Sun, Zamia Diaz, Xiaodong Fang, 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.Cell|April 21, 2018
Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like DomainsLin Guo, Hong Joo Kim, Hejia Wang, 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.Molecular Cell|August 14, 2018
Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule LocalizationLeeanne McGurk, Edward Gomes, Lin Guo, 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.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.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.Pageof 20