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 …

Heat shock proteins 70 (HSP70s) are steadily gaining more attention in the field of plant
biotic interactions. Though their regulation and activity in plants are much less well …

Molecular chaperones of the Hsp70 family form an important hub in the cellular protein
folding networks in bacteria and eukaryotes, connecting translation with the downstream …

Maintenance of cellular proteostasis is achieved by a multi-layered quality control network,
which counteracts the accumulation of misfolded proteins by refolding and degradation …

Protein aggregation is intimately associated with cellular stress and is accelerated during
aging, disease, and cellular dysfunction. Yeast cells rely on the ATP-consuming chaperone …

During protein quality control, proteotoxic misfolded proteins are recognized by molecular
chaperones, ubiquitylated by dedicated quality control ligases and delivered to the 26S …

Hsp70 is a key cellular system counteracting protein misfolding and aggregation, associated
with stress, ageing, and disease. Hsp70 solubilises aggregates and aids protein refolding …

Abstract Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of
protein homeostasis (proteostasis). Paramount to this role is Hsp70's binding to client …

Molecular chaperones of the Hsp70 family are key components of the cellular protein-folding
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis …

Molecular chaperones of the Hsp70 family are key components of the cellular protein folding
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis …