Heat shock protein 90 (HSP90) is a vital chaperone protein, regulating signaling pathways
and correcting misfolded proteins in cancer cells by interacting with oncogenic client …

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 …

Cells are repeatedly exposed to environmental or endogenous stresses that can alter
normal cell behavior and increase cell vulnerability. In order to ensure tissue integrity and …

Oxidative damage is a critical cause of diabetic wounds. Exosomes from various stem cells
could promote wound repair. Here, we investigated the potential mechanism by which …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include
the deposition of amyloid-β and tau in Alzheimer's disease, and that of α-synuclein in …

In the past few decades, the development of heat shock protein 90 (Hsp90) inhibitors for
cancer treatment has not stopped. About twenty compounds have been evaluated in the …

Abstract Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate
transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key …

Cancer immunotherapies, including immune checkpoint blockade, have the potential to
significantly impact treatments for diverse tumor types. At present, response failures and …

Simple Summary Heat-shock proteins (HSPs) are molecular chaperones overexpressed in
tumor cells and are necessary for their survival. In leukemia and lymphoma, HSPs have …