The glucose-regulated proteins (GRPs) are stress-inducible chaperones that mostly reside
in the endoplasmic reticulum or the mitochondria. Recent advances show that the GRPs …

The combination of relative nutrient deprivation and dysregulation of protein synthesis make
malignant cells especially prone to protein misfolding. Endoplasmic reticulum stress, which …

The 78-kDa glucose-regulated protein GRP78, also known as BiP and HSP5a, is a
multifunctional protein with activities far beyond its well-known role in the unfolded protein …

Since their original discovery as regulators of follicle-stimulating hormone (FSH) secretion
and erythropoiesis, the TGF-β family members activin and inhibin have been shown to …

The HSPA5 gene encodes the binding immunoglobulin protein (BiP), an Hsp70 family
chaperone localized in the ER lumen. As a highly conserved molecular chaperone, BiP …

GRP78 (glucose-regulated protein of 78 kDa) is traditionally regarded as a major ER
(endoplasmic reticulum) chaperone facilitating protein folding and assembly, protein quality …

The endoplasmic reticulum (ER) is a cellular organelle where secretory and membrane
proteins, as well as lipids, are synthesized and modified. When cells are subjected to ER …

Cancer constitutes a grave problem nowadays in view of the fact that it has become one of
the main causes of death worldwide. Poor clinical prognosis is presumably due to cancer …

The recent discovery that GRP78/BiP, a typical endoplasmic reticulum (ER) lumenal
chaperone, can be expressed on the cell surface, interacting with an increasing repertoire of …

GRP78 is a major endoplasmic reticulum chaperone as well as a master regulator of the
unfolded protein response. In addition to playing an essential role in early embryonic …