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 …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

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 …

The aggregation of specific proteins is hypothesized to underlie several degenerative
diseases, which are collectively known as amyloid disorders. However, the mechanistic …

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

The HSP70 family of heat shock proteins consists of molecular chaperones of approximately
70kDa in size that serve critical roles in protein homeostasis. These adenosine …

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 …

The toxic accumulation of misfolded proteins as inclusions, fibrils, or aggregates is a
hallmark of many neurodegenerative diseases. However, how molecular chaperones, such …

Hsp70 proteins are central components of the cellular network of molecular chaperones and
folding catalysts. They assist a large variety of protein folding processes in the cell by …