Heat shock proteins (Hsps) are conserved molecules whose main role is to facilitate folding
of other proteins. Most Hsps are generally stress-inducible as they play a particularly …

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 …

A systemic inflammatory response is observed in patients undergoing hemorrhagic shock
and sepsis. Here we report increased levels of cold-inducible RNA-binding protein (CIRP) in …

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 …

Mycobacterium tuberculosis is the cause of enormous human morbidity and mortality each
year. Although this bacterium can infect and cause disease in many animals, humans are …

Dendritic cells (DCs) are potent antigen-presenting cells that can stimulate resting T cells in
the primary immune response. During the maturation process, immature DCs lose their …

IFN-γ exhibits differential effects depending on the target and can induce cellular activation
and enhance survival or mediate cell death via activation of apoptotic pathways. In this …

Researchers have only just begun to elucidate the relationship between heat shock proteins
(HSP) and Toll-like receptors (TLR). HSP were originally described as an intracellular …

From its original description as solely an intracellular molecular chaperone, heat shock
proteins have now been shown to function as initiators of the host's immune response …

Implicit in the central dogma is the hypothesis that each protein gene product has but one
function. However, over the past decade, it has become clear that many proteins have one …