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 …

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 …

Cancer cells are commonly subjected to endoplasmic reticulum (ER) stress. To gain survival
advantage, cancer cells exploit the adaptive aspects of the unfolded protein response such …

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 …

Within the last two decades, there has been increasing evidence that heat-shock proteins
can have a differential influence on the immune system. They can either provoke or …

Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential
protein refolding and triage decisions to maintain protein homeostasis. Numerous co …

The Hsp90 molecular chaperone, along with a set of approximately 50 cochaperones,
mediates the folding and activation of hundreds of cellular proteins in an ATP-dependent …

Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their
function in the cytosol has been well studied. Notably, chaperones are also present in the …

Cells are exposed to several environmental or chemical stressors that may cause DNA
damage. DNA damage alters the normal functioning of the cell and contributes to several …

The epichaperome, a dynamic and integrated network of chaperone proteins, extends its
roles beyond basic protein folding to protein stabilization and intracellular signal …