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

@article{Mkrtchian2006ERp29AU,
  title={ERp29, an unusual redox-inactive member of the thioredoxin family.},
  author={Souren Mkrtchian and Tatyana Sandalova},
  journal={Antioxidants & redox signaling},
  year={2006},
  volume={8 3-4},
  pages={325-37}
}
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

Citations

Publications citing this paper.
Showing 1-10 of 26 extracted citations

Endoplasmic reticulum protein 29 (ERp29), a protein related to sperm maturation is involved in sperm-oocyte fusion in mouse

Reproductive biology and endocrinology : RB&E • 2010
View 11 Excerpts
Highly Influenced

Comparison of ILK and ERP29 expressions in benign and malignant pancreatic lesions and their clinicopathological significances in pancreatic ductal adenocarcinomas.

Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico • 2016
View 1 Excerpt

Whole-exome sequencing reveals defective CYP3A4 variants predictive of paclitaxel dose-limiting neuropathy.

Clinical cancer research : an official journal of the American Association for Cancer Research • 2015

Similar Papers

Loading similar papers…