ERO1LB
ERO1-like protein beta is a protein that in humans is encoded by the ERO1LB gene.[3][4]
Interactions
ERO1LB has been shown to interact with P4HB.[5][6]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R (Sep 2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". J Biol Chem. 275 (31): 23685–92. PMID 10818100. doi:10.1074/jbc.M003061200.
- ↑ "Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae)".
- ↑ Anelli, Tiziana; Alessio Massimo; Mezghrani Alexandre; Simmen Thomas; Talamo Fabio; Bachi Angela; Sitia Roberto (Feb 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. England. 21 (4): 835–44. ISSN 0261-4189. PMC 125352
. PMID 11847130. doi:10.1093/emboj/21.4.835. - ↑ Mezghrani, A; Fassio A; Benham A; Simmen T; Braakman I; Sitia R (Nov 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. England. 20 (22): 6288–96. ISSN 0261-4189. PMC 125306 . PMID 11707400. doi:10.1093/emboj/20.22.6288.
Further reading
- Mezghrani A, Fassio A, Benham A, et al. (2002). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. 20 (22): 6288–96. PMC 125306 . PMID 11707400. doi:10.1093/emboj/20.22.6288.
- Anelli T, Alessio M, Mezghrani A, et al. (2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. 21 (4): 835–44. PMC 125352 . PMID 11847130. doi:10.1093/emboj/21.4.835.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- Gess B, Hofbauer KH, Wenger RH, et al. (2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha". Eur. J. Biochem. 270 (10): 2228–35. PMID 12752442. doi:10.1046/j.1432-1033.2003.03590.x.
- Molteni SN, Fassio A, Ciriolo MR, et al. (2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum". J. Biol. Chem. 279 (31): 32667–73. PMID 15161913. doi:10.1074/jbc.M404992200.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
- Dias-Gunasekara S, Gubbens J, van Lith M, et al. (2005). "Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta". J. Biol. Chem. 280 (38): 33066–75. PMID 16012172. doi:10.1074/jbc.M505023200.
- Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach". Mol. Cell Proteomics. 5 (2): 226–33. PMID 16263699. doi:10.1074/mcp.M500324-MCP200.
- Otsu M, Bertoli G, Fagioli C, et al. (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82. PMID 16677073. doi:10.1089/ars.2006.8.274.
- Dias-Gunasekara S, van Lith M, Williams JA, et al. (2006). "Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta". J. Biol. Chem. 281 (35): 25018–25. PMID 16822866. doi:10.1074/jbc.M602354200.
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