Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to
limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of …

Exposure to acute physical and/or psychological stressors induces a cascade of
physiological changes collectively termed the stress response. The stress response is …

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 …

Amongst the families of intracellular molecules that chaperone and assist with the trafficking
of other proteins, notably during conditions of cellular stress, heat shock protein (hsp) 70 is …

Extracellular heat-shock proteins (eHsp) such as those belonging to the 70-kDa family of
Hsp (eg, Hsp72) have been hypothesized to act as a “danger signal” to immune cells …

The heat shock proteins are a family of highly conserved proteins with critical roles in
maintaining cellular homeostasis and in protecting the cell from stressful conditions. While …

Heat shock proteins (HSPs) were initially discovered as participants in the cellular response
to stress. It is now clear, however, that self and microbial HSPs also play an important role in …

Human heat shock protein 60 (Hsp60) exhibits immunoregulatory properties, primarily by
inducing pro-inflammatory responses in innate immune cells. Extensive analyses identified …

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 …

Abstract Background Heat shock protein 70 (Hsp70) is an intracellular chaperone protein
with regulatory and cytoprotective functions. Hsp70 can also be found in the extracellular …