Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological
processes through their facilitation of protein folding, disaggregation, and remodeling. The …

Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

Hsp70s and J-proteins, which constitute one of the most ubiquitous types of molecular
chaperone machineries, function in a wide variety of cellular processes. J-proteins play a …

The defining feature of the Hsp40 chaperone family is a∼ 70-amino-acid-residue signature,
termed the J domain, that is necessary for orchestrating interactions with its Hsp70 …

Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone
partnerships that are key components of cellular chaperone networks involved in facilitating …

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 …

Heat shock proteins of 40 kDa (Hsp40s), also called J proteins, are obligate partners of
Hsp70s. Via their highly conserved and functionally critical J domain, J proteins interact and …

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms
and in nearly all intracellular compartments. They function in many fundamental processes …

J proteins are obligate cochaperones of Hsp70s, stimulating their ATPase activity and thus
allowing them to function in multiple cellular processes. In most cellular compartments, an …

Hsp70 participates in a broad spectrum of protein folding processes extending from nascent
chain folding to protein disaggregation. This versatility in function is achieved through a …