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 …

Free radical-induced macromolecular damage has been studied extensively as a
mechanism of oxidative stress, but large-scale intervention trials with free radical …

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 …

Triacylglycerols (TAGs) are the main source of stored energy in the body, providing an
important substrate pool for mitochondrial beta-oxidation. Imbalances in the amount of TAGs …

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 thioredoxin system—formed by thioredoxin reductase and its characteristic substrate
thioredoxin—is an important constituent of the intracellular redox milieu. Interactions with …

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 endoplasmic reticulum (ER) is the largest organelle of the cell and participates in
multiple essential functions, including the production of secretory proteins, lipid synthesis …

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 …