Endoplasmic reticulum oxidoreductin 1
Short name | Ero1 |
Overlapping homologous superfamilies |
Description
References
1.Pathways for protein disulphide bond formation. Frand AR, Cuozzo JW, Kaiser CA. Trends Cell Biol. 10, 203-10, (2000). View articlePMID: 10754564
2.Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Frand AR, Kaiser CA. Mol. Biol. Cell 11, 2833-43, (2000). View articlePMID: 10982384
3.Balanced Ero1 activation and inactivation establishes ER redox homeostasis. Kim S, Sideris DP, Sevier CS, Kaiser CA. J. Cell Biol. 196, 713-25, (2012). View articlePMID: 22412017
4.Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H, Bulleid NJ. EMBO J. 27, 2988-97, (2008). View articlePMID: 18971943
5.Role of the ERO1-PDI interaction in oxidative protein folding and disease. Shergalis AG, Hu S, Bankhead A 3rd, Neamati N. Pharmacol Ther 210, 107525, (2020). PMID: 32201313
6.Structure, mechanism, and evolution of Ero1 family enzymes. Araki K, Inaba K. Antioxid Redox Signal 16, 790-9, (2012). PMID: 22145624
GO terms
biological process
molecular function
cellular component
Cross References
ENZYME
Contributing Member Database Entries
- PIRSF:PIRSF017205
- PANTHER:PTHR12613
- Pfam:PF04137