Perturbation of endoplasmic reticulum (ER) homeostasis results in a stress condition termed
“ER stress” determining the activation of a finely regulated program defined as unfolded …

Stress induced by the accumulation of unfolded proteins in the endoplasmic reticulum (ER)
is a feature of specialized secretory cells and is also observed in many diseases, including …

Cancer progression is characterized by rapidly proliferating cancer cells that are in need of
increased protein synthesis. Therefore, enhanced endoplasmic reticulum (ER) activity is …

Highlights•PDI is an important oxidase, reductase, isomerase and molecular
chaperone.•PDI expression is up-regulated in select types of cancers.•Silencing PDI results …

Thrombosis, or blood clot formation, and its sequelae remain a leading cause of morbidity
and mortality, and recurrent thrombosis is common despite current optimal therapy. Protein …

The endoplasmic reticulum (ER) is the site of synthesis and folding of secretory and
membrane bound proteins. The capacity of the ER to process proteins is limited and the …

It is evident that regions within tumors are deprived of oxygen, which makes the
microenvironment hypoxic. Cancer cells experiencing hypoxia undergo metabolic …

The protein disulphide isomerase (PDI) gene family is a large, diverse group of enzymes
recognised for their roles in disulphide bond formation within the endoplasmic reticulum …

The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic
reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine …

Protein disulfide isomerase (PDI), an endoplasmic reticulum chaperone protein, catalyzes
disulfide bond breakage, formation, and rearrangement. The effect of PDI inhibition on …