The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Cell dormancy is a widespread mechanism used by bacteria to evade environmental
threats, including antibiotics. Here we monitored bacterial antibiotic tolerance and regrowth …

Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Hsp70 molecular chaperones are implicated in a wide variety of cellular processes,
including protein biogenesis, protection of the proteome from stress, recovery of proteins …

Proteostasis, the controlled balance of protein synthesis, folding, assembly, trafficking and
degradation, is a paramount necessity for cell homeostasis. Impaired proteostasis is a …

Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …

The molecular chaperone DnaK is essential for viability of Mycobacterium tuberculosis
(Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP …