The HSP70 family of heat shock proteins consists of molecular chaperones of approximately
70kDa in size that serve critical roles in protein homeostasis. These adenosine …

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 …

Small-molecule chemical probes or tools have become progressively more important in
recent years as valuable reagents to investigate fundamental biological mechanisms and …

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their
expression is induced in response to a wide variety of physiological and environmental …

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 …

Stress or heat shock proteins (HSPs) 70 and 90 are powerful chaperones whose expression
is induced in response to a wide variety of physiological and environmental insults. These …

The inhibition of heat shock protein 70 (HSP70) is an emerging strategy in cancer therapy.
Unfortunately, no specific inhibitors are clinically available. By yeast two-hybrid screening …

The evolutionarily conserved stress-inducible HSP70 molecular chaperone plays a central
role in maintaining protein quality control in response to various forms of stress …

Abstract Heat shock protein 70 (Hsp70) is a powerful chaperone whose expression is
induced in response to a wide variety of physiological and environmental insults, including …

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 …