| SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA. | SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA.
Germani S, Van Ho AT, Cherubini A, Varone E, Chernorudskiy A, Renna GM, Fumagalli S, Gobbi M, Lucchetti J, Bolis M, Guarrera L, Craparotta I, Rastelli G, Piccoli G, de Napoli C, Nogara L, Poggio E, Brini M, Cattaneo A, Bachi A, Simmen T, Calì T, Quijano-Roy S, Boncompagni S, Blaauw B, Ferreiro A, Zito E., Free PMC Article | 03/25/2024 |
| A Critical Role for ERO1alpha in Arterial Thrombosis and Ischemic Stroke. | A Critical Role for ERO1α in Arterial Thrombosis and Ischemic Stroke.
Jha V, Xiong B, Kumari T, Brown G, Wang J, Kim K, Lee J, Asquith N, Gallagher J, Asherman L, Lambert T, Bai Y, Du X, Min JK, Sah R, Javaheri A, Razani B, Lee JM, Italiano JE, Cho J., Free PMC Article | 06/1/2023 |
| Homocysteine facilitates endoplasmic reticulum stress and apoptosis of hepatocytes by suppressing ERO1alpha expression via cooperation between DNMT1 and G9a. | Homocysteine facilitates endoplasmic reticulum stress and apoptosis of hepatocytes by suppressing ERO1α expression via cooperation between DNMT1 and G9a.
Shen J, Jiao Y, Ding N, Xie L, Ma S, Zhang H, Yang A, Zhang H, Jiang Y., Free PMC Article | 08/6/2022 |
| Endophilin A2-mediated alleviation of endoplasmic reticulum stress-induced cardiac injury involves the suppression of ERO1alpha/IP3R signaling pathway. | Endophilin A2-mediated alleviation of endoplasmic reticulum stress-induced cardiac injury involves the suppression of ERO1α/IP(3)R signaling pathway.
Liu Y, Hu R, Shen H, Mo Q, Wang X, Zhang G, Li S, Liang G, Hou N, Luo J., Free PMC Article | 02/26/2022 |
| ERO1alpha inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells. | ERO1α inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells.
Hu J, Jin J, Qu Y, Liu W, Ma Z, Zhang J, Chen F. | 05/29/2021 |
| ERO1alpha promotes testosterone secretion in hCG-stimulated mouse Leydig cells via activation of the PI3K/AKT/mTOR signaling pathway. | ERO1α promotes testosterone secretion in hCG-stimulated mouse Leydig cells via activation of the PI3K/AKT/mTOR signaling pathway.
Chen F, Wang Y, Liu Q, Hu J, Jin J, Ma Z, Zhang J. | 03/13/2021 |
| this study shows that the hypoxia-inducible ER-resident oxidase ERO1-alpha plays an important role in the hypoxia-induced augmentation of MHC class I-peptide complex expression | Hypoxia augments MHC class I antigen presentation via facilitation of ERO1-α-mediated oxidative folding in murine tumor cells.
Kajiwara T, Tanaka T, Kukita K, Kutomi G, Saito K, Okuya K, Takaya A, Kochin V, Kanaseki T, Tsukahara T, Hirohashi Y, Torigoe T, Hirata K, Sato N, Tamura Y. | 07/8/2017 |
| Data (including data from knockout mice) suggest that up-regulation of expression of ERO1alpha (oxidoreductin-1-L-alpha) and CHOP (c/EBP-homologous protein) is involved in liver apoptosis/necrosis exhibited in acute liver failure. | C/EBP homologous protein (CHOP) contributes to hepatocyte death via the promotion of ERO1α signalling in acute liver failure.
Rao J, Zhang C, Wang P, Lu L, Qian X, Qin J, Pan X, Li G, Wang X, Zhang F. | 04/25/2015 |
| These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells | Cancer-associated oxidoreductase ERO1-α drives the production of tumor-promoting myeloid-derived suppressor cells via oxidative protein folding.
Tanaka T, Kajiwara T, Torigoe T, Okamoto Y, Sato N, Tamura Y. | 04/25/2015 |
| 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. | Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress.
Wright J, Birk J, Haataja L, Liu M, Ramming T, Weiss MA, Appenzeller-Herzog C, Arvan P., Free PMC Article | 01/4/2014 |
| combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta, and PRDX4 compromised the extracellular matrix and interfered with the intracellular maturation of procollagen | Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice.
Zito E, Hansen HG, Yeo GS, Fujii J, Ron D., Free PMC Article | 01/26/2013 |
| The peak amplitude of calcium transients in homozygous Ero1alpha mutant adult cardiomyocytes was reduced to 42.0 +/- 2.2% (n=10, P </= 0.01) of values recorded in wild-type cardiomyocytes. | The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load.
Chin KT, Kang G, Qu J, Gardner LB, Coetzee WA, Zito E, Fishman GI, Ron D., Free PMC Article | 10/15/2011 |
| Describes mouse Ero1-l in addition to the human gene. | ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.
Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R. | 02/8/2011 |
| Oxygen regulation of ERO1-Lalpha expression likely maintains the transfer rate of oxidizing equivalents to PDI in situations of an altered cellular redox state induced by changes in the cellular oxygen tension | The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha.
Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A. | 02/7/2011 |
| Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation. | A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity.
Blais JD, Chin KT, Zito E, Zhang Y, Heldman N, Harding HP, Fass D, Thorpe C, Ron D., Free PMC Article | 08/16/2010 |
| These data shed new light on how the CHOP pathway of apoptosis triggers calcium-dependent apoptosis through an ERO1-alpha-IP3R pathway. | Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis.
Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR, Tabas I., Free PMC Article | 01/21/2010 |
| Data suggest that ERp44 and Ero1-lalpha play a major role in the assembly of higher-order adiponectin complexes, and highlight the importance of posttranslational events controlling adiponectin levels and the release of adiponectin from adipocytes. | Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention.
Wang ZV, Schraw TD, Kim JY, Khan T, Rajala MW, Follenzi A, Scherer PE., Free PMC Article | 01/21/2010 |
| The endoplasmic reticulum (ER) oxidoreductase Ero1-L alpha and effectors modulating peroxisome proliferator-activated receptor gamma (PPAR gamma) and SIRT1 activities regulate secretion of adiponectin from 3T3-L1 adipocytes. | Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha.
Qiang L, Wang H, Farmer SR., Free PMC Article | 01/21/2010 |