The chaperone GRP78/Dna K is conserved throughout evolution down to prokaryotes. The
GRP78 inhibitor OSU‐03012 (AR‐12) interacted with sildenafil (Viagra) or tadalafil (Cialis) …

Prior tumor cell studies have shown that the drugs sorafenib (Nexavar) and regorafenib
(Stivarga) reduce expression of the chaperone GRP78. Sorafenib/regorafenib and the multi …

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

GRP78 is a stress-inducible chaperone protein with antiapoptotic properties that is
overexpressed in transformed cells and cells under glucose starvation, acidosis, and …

As one member of 70 kDa heat shock proteins, glucose‐regulated protein 78 (GRP78)
participates in protein folding, transportation and degradation. This sort of capacity can be …

The protein chaperone GRP78 is a master regulator of endoplasmic reticulum (ER) functions
and is frequently over-expressed at the surface of cancer cells where it contributes to chemo …

Cancer cells adapt to chronic stress in the tumor microenvironment by inducing the
expression of GRP78/BiP, a major endoplasmic reticulum chaperone with Ca2+-binding and …

Background Glucose regulating protein 78 (GRP78) is one member of the Heat Shock
Protein family of chaperone proteins (HSPA5) found in eukaryotes. It acts as the master of …

Inhibitors of the molecular chaperone Hsp90 have been shown to enhance tumor cell
radiosensitivity. To begin to address the mechanism responsible, we have determined the …

Chronic hepatitis B (CHB) remains a global health problem, carrying a high risk for
progression into cirrhosis and liver failure. Molecular chaperones are involved in diverse …