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 endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins
that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is …

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 flux of Ca2+ from the endoplasmic reticulum (ER) to mitochondria regulates
mitochondria metabolism. Within tumor tissue, mitochondria metabolism is frequently …

In recent years, it has become clear that balanced regulation of reactive oxygen species is of
critical significance for cell-fate determination as well as for stem cell development, function …

Studies on thioredoxin (Trx) and its related molecules have expanded dramatically recently.
Proteins that share the similar active-site sequence,-Cys-Xxx-Yyy-Cys-, are called the Trx …

The folding of secretory proteins is a well-understood mechanism, based on decades of
research on endoplasmic reticulum (ER) chaperones. These chaperones interact with newly …

Vitamin K epoxide reductase (VKOR) sustains blood coagulation by reducing vitamin K
epoxide to the hydroquinone, an essential cofactor for the γ-glutamyl carboxylation of many …

Oxidative stresses are largely mediated by intracellular protein oxidations by reactive
oxygen species (ROS). Host cells are equipped with antioxidants that scavenge ROS. The …

Human thioredoxin (TRX) was first identified in human T-cell leukemia virus type I (HTLV-I)-
positive T-cell lines and is associated with the pathophysiology of retroviral infections. TRX …