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 molecular chaperone family (which comprises, among other proteins, the 90-
kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major …

▪ Abstract Major histocompatibility complex (MHC) class I molecules display on the cell
surface 8-to 10-residue peptides derived from the spectrum of proteins expressed in the …

▪ Abstract Classical class I molecules assemble in the endoplasmic reticulum (ER) with
peptides mostly generated from cytosolic proteins by the proteasome. The activity of the …

Increased synthesis of heat shock proteins (hsp) occurs in prokaryotic and eukaryotic cells
when they are exposed to stress. By increasing their hsp content, cells protect themselves …

Heat shock protein (HSP) preparations derived from cancer cells and virus-infected cells
have been shown previously to elicit cancer-specific or virus-specific immunity. The …

While expression of HSPs may be induced by heat tive immunity to cancer challenges, ie, by
the very shock, glucose deprivation, and other stresses, most HSPs are present in abundant …

Abstract Drew Pardoll (Johns Hopkins Oncology Center) examines prospects for therapeutic
cancer vaccines. Considering how it is that the immune system fails to recognize and …

Heat-shock proteins chaperone antigenic peptides that are generated within cells. Such
chaperoning is a part of the endogenous pathway of antigen presentation by MHC class I …

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