The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …

The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly
conserved and present in all living organisms and play vital roles in protein fate. The …

The 70 kDa heat shock proteins (HSP70s) are a group of highly conserved and inducible
heat shock proteins. One of the main functions of HSP70s is to act as molecular chaperones …

In all organisms, heat-shock proteins (HSPs) provide an ancient defense system. These
proteins act as molecular chaperones by assisting proper folding and refolding of misfolded …

HSP70 is a chaperone that accumulates in the cells after many different stresses promoting
cell survival in response to the adverse conditions. In contrast to normal cells, most cancer …

Heat shock proteins (HSPs) are evolutionarily conserved molecules synthesised by cells
exposed to sub-lethal stresses. Acting as molecular chaperones, HSPs protect cells from …

Abstract Heat shock protein 70 (Hsp70) is the most ubiquitous stress-inducible chaperone. It
accumulates in the cells in response to a wide variety of physiological and environmental …

Abstract Heat shock protein 90 (HSP90), a highly and unique chaperone, presents as a
double-edged sword. It plays an essential role in many physiological and pathological …

Heat-shock protein 90 (HSP90) is an important molecule chaperone associated with
tumorigenesis and malignancy. HSP90 is involved in the folding and maturation of a wide …

Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70
family of molecular chaperones and plays a central role in protein homeostasis. The main …