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Proceedings of the National Academy of Sciences of the United States of America|August 22, 2002
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicityHideki Sakahira, Peter Breuer, Manajit K Hayer-Hartl, et al.Nature|February 4, 2026
Single-molecule dynamics of the TRiC chaperonin system in vivoRongqin Li, Niko Dalheimer, Martin B D Müller, et al.Biological Chemistry|November 30, 2006
Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1pZdravko Dragovic, Yasuhito Shomura, Nikolay Tzvetkov, et al.Journal of Molecular Biology|April 27, 2010
Physicochemical determinants of chaperone requirementsGian Gaetano Tartaglia, Christopher M Dobson, F Ulrich Hartl, et al.Molecular Cell|August 28, 2010
The three-dimensional organization of polyribosomes in intact human cellsFlorian Brandt, Lars-Anders Carlson, F Ulrich Hartl, et al.Cell|November 7, 2017
Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular HomeostasisToshiaki Izawa, Sae-Hun Park, Liang Zhao, et al.Frontiers in Molecular Biosciences|April 27, 2017
Rubisco Activases: AAA+ Chaperones Adapted to Enzyme RepairJavaid Y Bhat, Gabriel Thieulin-Pardo, F Ulrich Hartl, et al.The EMBO Journal|May 12, 2006
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70sZdravko Dragovic, Sarah A Broadley, Yasuhito Shomura, et al.Nature Communications|February 18, 2015
Action of the Hsp70 chaperone system observed with single proteinsJoão M Nunes, Manajit Mayer-Hartl, F Ulrich Hartl, et al.Journal of Molecular Biology|September 21, 2005
De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteriaHung-Chun Chang, Christian M Kaiser, F Ulrich Hartl, et al.Pageof 21