The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

The secretory pathway is responsible for the synthesis, folding, and delivery of a diverse
array of cellular proteins. Secretory protein synthesis begins in the endoplasmic reticulum …

During the maturation of extracellular proteins, disulfide bonds that chemically cross-link
specific cysteines are often added to stabilize a protein or to join it covalently to other …

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 …

In eukaryotic cells, oxidative protein folding occurs in the lumen of the endoplasmic
reticulum (ER), catalyzed by ER sulfhydryl oxidase 1 (Ero1) and protein disulfide isomerase …

Protein secretion is an essential process for living organisms. In eukaryotes, this
encompasses numerous steps mediated by several hundred cellular proteins. The core …

Protein disulfide isomerase plays a key role in catalyzing the folding of secretory proteins. It
features two catalytically inactive thioredoxin domains inserted between two catalytically …

Glutathione is the most abundant low molecular weight thiol in the eukaryotic cytosol. The
compartment-specific ratio and absolute concentrations of reduced and oxidized glutathione …