Heat shock proteins (HSPs) of eukaryotes are evolutionarily conserved molecules present in
all the major intracellular organelles. They mainly function as molecular chaperones and …

Heat shock proteins (Hsps) hold a dual role depending on their location. Inside cells, they
fulfill essential survival functions as molecular chaperones forming complexes with …

Recently, growing evidences that extracellular heat shock protein (HSP) functions as
endogenous immunomodulator for innate and adaptive immune responses have been …

Heat shock proteins (Hsp) are a diverse group of constitutive and/or stress-induced
molecules that are categorized into several classes on the basis of their molecular weight …

Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as
molecular chaperones, and play a critical role in maintaining cellular proteostasis by …

Heat shock proteins exert their beneficial effects via basically two modes of action
depending on their relative location within the host. Intracellular heat shock proteins found …

The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Heat shock proteins are molecular chaperones which support tumor development by
regulating various cellular processes including unfolded protein response, mitochondrial …

Heat shock proteins (HSPs) are highly conserved stress proteins known as molecular
chaperones, which are considered to be cytoplasmic proteins with functions restricted to the …

As molecular chaperones, heat-shock proteins (HSPs) function to limit protein aggregation,
facilitate protein refolding and chaperone other proteins. Under conditions of cellular stress …