are a family of enzymes that play a crucial role in the formation and rearrangement of disulfide bonds in proteins, which is essential for proper protein folding and function. Recent research has ...

A newly developed luciferase-based reporter can detect problems in protein translocation and disulfide bond formation in the endoplasmic reticulum (ER), as reported by researchers at Science Tokyo.

This method imitates the natural enzyme that mediates the disulfide bond formation, by creating a highly reactive environment to greatly speed up the formation and rearrangement of these bonds.

The high-resolution structure of an oxidoreductase from the archaeon Pyrococcus furiosus shows that it comprises two adjacent domains each with the thioredoxin (trx/grx) fold. Its functional ...