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The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the ra...
ORGANISM(S): Escherichia coli 
2020-01-15 | PXD016509 | Pride
Elimination of misfolded proteins is crucial for proteostasis and to prevent proteinopathies. Nedd4/Rsp5 emerged as a major E3 ligase involved in multiple quality control pathways that target misfolded plasma membrane proteins, aggregated polypeptides, and cytosolic heat-induced misfolded proteins f...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-03-01 | PXD004747 | Pride
Endoplasmic reticulum (ER)-associated degradation (ERAD) and ER-phagy are two principal degradative mechanisms in the ER; however, the crosstalk between these two pathways and its physiological significance remain unexplored. Here we report that SEL1L-HRD1 ERAD limits autophagy and that, when ERAD i...
ORGANISM(S): Mus musculus (Mouse) 
2023-04-25 | PXD040899 | Pride
Several mechanisms are known to cause monomeric protein misfolding. Coarse-grained simulations have predicted an additional mechanism exists involving off-pathway, non-covalent lasso entanglements, which are long-lived kinetic traps and structurally resemble the native state. Here, we examine whethe...
ORGANISM(S): Escherichia coli 
2025-08-11 | PXD066083 | Pride
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