The endoplasmic reticulum (ER) plays a major role in regulating synthesis, folding, and
orderly transport of proteins. It is also essentially involved in various cellular signaling …

The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells
was one of the first mechanisms of catalysed protein folding to be discovered. Protein …

The ERp57/PDIA3 protein is a pleiotropic member of the PDIs family and, although
predominantly located in the endoplasmic reticulum (ER), has indeed been found in other …

Calnexin and calreticulin are related proteins that comprise an ER chaperone system that
ensures the proper folding and quality control of newly synthesized glycoproteins. The …

The endoplasmic reticulum (ER) is a highly versatile protein factory that is equipped with
chaperones and folding enzymes essential for protein folding. ER quality control guided by …

The exposure of calreticulin (CRT) on the plasma membrane can precede anthracycline-
induced apoptosis and is required for cell death to be perceived as immunogenic. Mass …

The conventional treatment of cancer relies upon radiotherapy and chemotherapy. Such
treatments supposedly mediate their effects via the direct elimination of tumor cells …

Peptide binding to MHC class I molecules is a component of a folding and assembly process
that occurs in the endoplasmic reticulum (ER) and uses both cellular chaperones and …

Disturbance of endoplasmic reticulum (ER) proteostasis is a common feature of amyotrophic
lateral sclerosis (ALS). Protein disulfide isomerases (PDI s) are ER foldases identified as …

The protein ERp57/GRP58 is a stress-responsive protein and a component of the protein
disulfide isomerase family. Its functions in the endoplasmic reticulum are well known …