Analysis of the human genome reveals that approximately a third of all open reading frames
code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of …

The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER
quality control (ERQC) system. The ERQC facilitates folding and modification of secretory …

The endoplasmic reticulum (ER) is an organelle of nucleated cells that produces proteins,
lipids and oligosaccharides. ER volume and activity are increased upon induction of …

The response to endoplasmic reticulum (ER) stress relies on activation of unfolded protein
response (UPR) sensors, and the outcome of the UPR depends on the duration and strength …

Disulfide bond formation in the endoplasmic reticulum by the sulfhydryl oxidase Ero1 family
is thought to be accompanied by the concomitant formation of hydrogen peroxide. Since …

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 …

Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative protein folding in the
endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of …

Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-
third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol …

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 …

Thyroglobulin (Tg) is a vertebrate secretory protein synthesized in the thyrocyte endoplasmic
reticulum (ER), where it acquires N-linked glycosylation and conformational maturation …