ERp29, an unusual redox-inactive member of the thioredoxin family.

  title={ERp29, an unusual redox-inactive member of the thioredoxin family.},
  author={Souren Mkrtchian and Tatyana Sandalova},
  journal={Antioxidants & redox signaling},
  volume={8 3-4},
Oxidative folding in the endoplasmic reticulum is accomplished by a group of oxidoreductases where the protein disulfide isomerase (PDI) plays a key role. Structurally, redox-active PDI domains, like many other enzymes utilizing cysteine chemistry, adopt characteristic thioredoxin folds. However, this structural unit is not necessarily associated with the redox function and the current review focuses on the interesting example of a loss-of-function PDI-like protein from the endoplasmic… CONTINUE READING


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