The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that ensures cellular
proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 …

Heat shock proteins (HSPs), also known as stress proteins and extrinsic chaperones, are a
suite of highly conserved proteins of varying molecular weight (c. 16–100 kDa) produced in …

Heat shock proteins (hsp) have been found to play a fundamental role in the recovery from
multiple stress conditions and to offer protection from subsequent insults. The function of hsp …

Malaria parasite infection is initiated by the mosquito-transmitted sporozoite stage, a highly
motile invasive cell that targets hepatocytes in the liver for infection. A promising approach to …

Endoplasmic reticulum (ER) chaperones (eg, calreticulin, heat shock proteins, and
isomerases) perform a multitude of functions within the ER. However, many of these …

Heat shock proteins (hsps) are among the most abundant intracellular proteins. Their
synthesis is rapidly up-regulated by various 'stressors' including temperature, glucose …

Little is known about the composition and functional differences between extracellular
vesicle (EV) subsets, such as microvesicles (MVs) and exosomes (EXOs), nor to what extent …

During tumor development and progression, intrinsic and extrinsic factors trigger
endoplasmic reticulum (ER) stress and the unfolded protein response, resulting in the …

Lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) has been identified as a
major receptor for oxidized low-density lipoprotein (ox-LDL) in endothelial cells, monocytes …