Reactive oxygen species (ROS) are products of normal metabolism and xenobiotic
exposure, and depending on their concentration, ROS can be beneficial or harmful to cells …

Cysteine thiols are among the most reactive functional groups in proteins, and their pairing
in disulfide linkages is a common post-translational modification in proteins entering the …

Apoptosis is a conserved homeostatic process critical for organ and tissue morphogenesis,
development, and senescence. This form of programmed cell death also participates in the …

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 …

Glutathione is a ubiquitous molecule found in all parts of the cell where it fulfils a range of
functions from detoxification to protection from oxidative damage. It provides the main redox …

Apoptosis or programmed cell death represents a physiologically conserved mechanism of
cell death that is pivotal in normal development and tissue homeostasis in all organisms. As …

Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is the most abundant intracellular
antioxidant thiol and is central to redox defense during oxidative stress. GSH metabolism is …

The enzymes of the protein disulfide isomerase (PDI) family are thiol–disulfide
oxidoreductases of the endoplasmic reticulum (ER). They contain a CXXC active-site …

The majority of the thiols (SH) 2 and disulfides (SS) in cells are found as the amino acid
cysteine and its disulfide, cystine (Fig. 1 A). The thiolate anion is intrinsically one of the …

Our concept of how disulfides form in proteins entering the secretory pathway has changed
dramatically in recent years. The discovery of endoplasmic reticulum (ER) oxidoreductin 1 …