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 …

Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

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

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 …

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 …

Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …

The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …

Hsp70s comprise a deeply conserved chaperone family that has a central role in
maintaining protein homeostasis. In humans, Hsp70 client specificity is provided by 49 …

Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the
generation of misfolded proteins exceeds the cellular refolding and degradative capacity …

The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …