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 …

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 …

Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …

Organisms must survive a variety of stressful conditions, including sudden temperature
increases that damage important cellular structures and interfere with essential functions. In …

The chaperone functions of heat shock protein (Hsp) 70 involve an allosteric control
mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate …

The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90
molecular chaperone for in vivo function. Although Hsp90 is required for ligand binding in …

When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein
response (UPR) increases ER-protein-folding capacity to restore protein-folding …

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

The physiological consequences of the unfolded protein response (UPR) are mediated by
changes in gene expression. Underlying them are rapid processes involving preexisting …