Heat shock proteins (HSPs) are a large family of chaperones that are involved in protein
folding and maturation of a variety of “client” proteins protecting them from degradation …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …

The 70-kDa heat shock protein (HSP70) family of molecular chaperones represents one of
the most ubiquitous classes of chaperones and is highly conserved in all organisms …

Protein–protein interactions (PPIs) control the assembly of multi-protein complexes and,
thus, these contacts have enormous potential as drug targets. However, the field has …

Mechanistic studies from cell culture and animal models have revealed critical roles for the
heat shock protein Hsp70 in cancer initiation and progression. Surprisingly, many effects of …

The allosteric mechanism of Hsp70 molecular chaperones enables ATP binding to the N-
terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal …

A network of molecular chaperones is known to bind proteins ('clients') and balance their
folding, function and turnover. However, it is often unclear which chaperones are critical for …

Bag3, a nucleotide exchange factor of the heat shock protein Hsp70, has been implicated in
cell signaling. Here, we report that Bag3 interacts with the SH3 domain of Src, thereby …

Following sequencing and assembly of the human genome, the preferred methods for
identification of new drug targets have changed dramatically. Modern tactics such as …

Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this
task, they employ a large number of cochaperones and adapter proteins. Here, we review …