Recombinant Human ERO1-like protein alpha (ERO1L)

1. High expression of ERO1L is associated with poor prognosis of patients with gastric cancer. These results indicate that ERO1L expression may be a clinically promising therapeutic target for prevention of gastric cancer. PMID: 26987398
2. ERO1alpha plays a crucial role in HSC proliferation via posttranslational modification of collagen and MT1-MMP PMID: 28774960
3. Study shows that ERO1L and NARS expression level are up-regulated in primary lung adenocarcinoma and identifies them with a potential to promote tumor metastasis and growth of cancer cells. PMID: 27161446
4. a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines. PMID: 27703014
5. Expression of ERO1-alpha in MDA-MB-231 cells promotes tumour growth via promoting angiogenesis. Knockdown of ERO1-alpha inhibits secretion of VEGF by inhibition of oxidative protein folding. In triple-negative breast cancer cases, the expression of ERO1-alpha was upregulated and related to the number of the blood vessels. ERO1-alpha was a poor prognosis factor in triple-negative breast cancer. PMID: 27100727
6. Data indicate a new mechanism of Ero1alpha regulation in which thiol-disulfide exchange at Cys208-Cys241 affects the stability of the Cys94-Cys131 inhibitory disulfide through allosteric and/or inter-molecular communication. PMID: 26609561
7. the cancer-associated ERO1-alpha regulates the expression of the MHC class I molecule via oxidative folding PMID: 25870246
8. Data suggest that expression of ERO1alpha (oxidoreductin-1-L-alpha) and CHOP (c/EBP-homologous protein) is up-regulated in liver of patients with acute liver failure. PMID: 25387528
9. These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells PMID: 25595776
10. PDI has a role as a competent regulator and a specific substrate of Ero1alpha govern efficient and faithful oxidative protein folding and maintain the ER redox homeostasis PMID: 25258311
11. These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation. PMID: 25122773
12. The high expression of Ero1alpha in cancers of the esophagus and stomach demonstrates the importance of ER redox regulation in the gastro-intestinal (GI) tract in health and disease. PMID: 23373818
13. GPx7 promotes oxidative protein folding, directly utilizing Ero1alpha-generated hydrogen peroxide in the early secretory compartment. PMID: 23919619
14. A simple feedback mechanism of regulation of Ero1alpha was identified involving its primary substrate. PMID: 24758166
15. The expression of hERO1-alpha in cancer cells is associated with poorer prognosis. PMID: 23578220
16. Report on the establishment of an engineered CHOS cell line that has been engineered to express both XBP-1S) and ERO1-Lalpha and has been named CHOS-XE. CHOS-XE cells produced increased antibody (MAb) yields (5.3- 6.2 fold) in comparison to CHOS cells. PMID: 23335490
17. ER stress induced by misfolded proinsulin was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin may be a viable therapeutic strategy in the treatment of type 2 diabetes. PMID: 24022479
18. This paper reported the interactions of Ero1 with protein disulfide isomerase family proteins and chaperones, highlighting the effect that redox flux has on Ero1 partnerships. PMID: 23530257
19. hyperoxidation generated by Ero1alpha-C104A/C131A is addressed in the ER lumen and is unlikely to exert oxidative injury throughout the cell. PMID: 23027870
20. the levels, subcellular localization, and activity of Ero1alpha coordinately regulate Ca(2+) and redox homeostasis and signaling in the early secretory compartment. PMID: 21854214
21. the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha. PMID: 21757736
22. Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI). PMID: 21398518
23. Results show that within the ER, Ero1alpha is almost exclusively found on the mitochondria-associated membrane (MAM). PMID: 20186508
24. A dynamic equilibrium between Ero1- and glutathione disulphide-mediated oxidation of protein disulphide isomerases constitutes an important element of endoplasmic reticulum redox homeostasis. PMID: 20802462
25. Ero1alpha limits its oxidative activity using four regulatory cysteines properly positioned within a critical loop that transfers electrons from protein disulphide isomerase to the FAD-containing active site. PMID: 20834232
26. proving that the activity of Ero1-Lalpha results in H(2)O(2) formation in the endoplasmic reticulum PMID: 20095866
27. Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. PMID: 20562109
28. The results demonstrate that the specificity of Ero1alpha toward the active sites of PDI requires the presence of the regulatory disulfides. PMID: 20657012
29. an appropriate Ero1alpha-PDI ratio is critical for regulating the binding-release cycle of CTA1 by PDI during retro-translocation, and PDI's redox state has a role in targeting it to the retro-translocon PMID: 20130085
30. oxygen regulation of ERO1-Lalpha expression likely is to maintain the transfer rate of oxidizing equivalents to PDI in situations of an altered cellular redox state induced by changes of the cellular oxygen tension PMID: 12752442
31. two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum PMID: 15136577
32. glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum PMID: 15161913
33. Hypoxic induction of Ero1-L alpha is key adaptive response in a previously unrecognized HIF-1-mediated pathway that operates to improve protein secretion under hypoxia and might be used for inhibiting tumor growth via inhibiting VEGF-driven angiogenesis. PMID: 15592500
34. Results determine the redox-driven shutdown mechanism of Ero1alpha from the formation of a disulphide bond between the active-site Cys(94) and Cys(131). PMID: 18833192
35. Data suggest that partial regulatory disulfide reduction may be a mechanism for preventing excessive Ero1alpha activity and oxidation of PDI or that additional factors are required for Ero1alpha activation within the mammalian ER. PMID: 18971943
36. In this report, the structural model of human Ero1-L alpha was built at first. PMID: 19766098

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HGNC: 13280

OMIM: 615435

KEGG: hsa:30001

STRING: 9606.ENSP00000379042

UniGene: Hs.525339