Affinage

ERO1A

ERO1-like protein alpha · UniProt Q96HE7

Length
468 aa
Mass
54.4 kDa
Annotated
2026-06-09
100 papers in source corpus 47 papers cited in narrative 47 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 10/10 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ERO1A (Ero1α) is a FAD-dependent, ER-resident type II membrane sulfhydryl oxidase that serves as a primary engine of oxidative protein folding by feeding oxidizing equivalents into protein disulfide isomerase (PDI) (PMID:10671517, PMID:20802462). It catalyzes disulfide bond formation through a cyclic relay involving two conserved cysteine triads (the Cys85-Cys94-Cys99 active site and the Cys391-Cys394-Cys397 outer site), with Cys94 forming the mixed disulfide that transfers oxidizing power to PDI; mutation of Cys394 or Cys397 abolishes activity (PMID:10671517, PMID:15136577). Specific targeting of PDI is achieved through a protruding β-hairpin that docks into the hydrophobic pocket of the PDI b'-domain, directing preferential oxidation of the PDI a' active site (PMID:20834232, PMID:21398518). Ero1α activity is tightly self-limiting: regulatory disulfides in a flexible loop (involving Cys104/Cys131 and Cys208/Cys241) toggle the enzyme between active and inactive states, and reduced PDI activates while oxidized PDI inactivates the oxidase, creating a feedback loop that matches output to substrate demand (PMID:18833192, PMID:18971943, PMID:20834232, PMID:24758166, PMID:27703014). Because the catalytic cycle consumes O2 and generates H2O2, Ero1α is a major source of luminal ER H2O2, which is productively re-used by peroxidases such as GPx7 to drive further PDI oxidation (PMID:20095866, PMID:23919619). The enzyme is dynamically retained in the early secretory pathway through covalent binding to ERp44 and non-covalent association with PDI, which also chaperones it against aggregation (PMID:16677073, PMID:23979138). Layered post-translational controls tune its activity and abundance: Fam20C phosphorylation at Ser145 activates the oxidase, FBXO6-directed ubiquitination drives its proteasomal degradation, ERp44 SUMOylation governs its ER retention versus secretion, iNOS-mediated S-nitrosation inactivates it, and SIRT5-reversed Lys396 succinylation modulates its pro-apoptotic activity (PMID:29858230, PMID:27855403, PMID:36427672, PMID:35033630, PMID:40243486). Functionally, Ero1α supports secretion and folding of disulfide-rich clients including adiponectin, VEGF, MHC class I, PD-L1 and Notch (PMID:17452443, PMID:15592500, PMID:25870246, PMID:28160557, PMID:18809725), and it is enriched at the mitochondria-associated ER membrane where it shapes Ca2+ fluxes toward mitochondria and is wired into ER-stress apoptosis via CHOP-dependent induction and IP3R1 stimulation (PMID:20186508, PMID:21854214, PMID:19752026). On the platelet surface and dense tubular system, extracellular Ero1α oxidizes PDI and modifies allosteric disulfides in STIM1 (Cys49-Cys56) and SERCA2 (Cys875-Cys887) to promote Ca2+ mobilization and aggregation (PMID:20562109, PMID:35077997, PMID:37132383). In cancer and hypoxia, HIF-1α- and CHOP-driven Ero1α supports tumor secretion and pro-tumorigenic signaling, including an mTORC1→Ero1α→IL-6/STAT3/SLC7A11 axis conferring ferroptosis resistance, in a manner dependent on its catalytic activity (PMID:15592500, PMID:38610018, PMID:32724477).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2000 High

    Established that the human ERO1 ortholog is a functional ER oxidoreductase, answering whether the yeast oxidative-folding machinery is conserved in mammals.

    Evidence Yeast ero1-1 complementation, microsome fractionation, Endo-H glycan analysis and cysteine mutagenesis

    PMID:10671517

    Open questions at the time
    • Did not define the full disulfide relay to PDI
    • Cofactor and partner enzymes not yet mapped
  2. 2004 High

    Defined the dual cysteine-triad electron-transfer architecture and identified PDI and ERp44 as mixed-disulfide partners, establishing how oxidizing equivalents move through the enzyme.

    Evidence Yeast complementation, mutagenesis and mixed-disulfide trapping with PDI/ERp44

    PMID:15136577

    Open questions at the time
    • Atomic-level interface with PDI not resolved
    • Regulatory disulfide switch not yet defined
  3. 2005 High

    Connected Ero1α to physiological hypoxic adaptation by showing HIF-1-dependent induction supports secretion of disulfide-rich VEGF, framing it as the adaptive oxidoreductase under low oxygen.

    Evidence HIF-1-deficient cell epistasis, siRNA knockdown and VEGF secretion assay under hypoxia

    PMID:15592500

    Open questions at the time
    • Did not address other hypoxic clients
    • Mechanism of catalysis under low O2 not addressed
  4. 2006 High

    Resolved how a soluble-pathway oxidase is kept in the ER, showing competing covalent ERp44 and non-covalent PDI interactions retain and chaperone Ero1α.

    Evidence Secretion/retention assays and co-IP in HeLa with dominant-negative PDI mutants

    PMID:16677073

    Open questions at the time
    • Quantitative affinities not determined
    • How retention is dynamically modulated not addressed
  5. 2008 High

    Uncovered the intramolecular disulfide switch and substrate-feedback logic that prevents hyperoxidation, answering how the enzyme avoids runaway activity.

    Evidence MS identification of a Cys94-Cys131 regulatory disulfide, cell-based oxidation assays, mutants, isoform comparison, plus in vitro redox potential measurements; and in vivo demonstration that CHOP induces Ero1α to stimulate IP3R1-mediated Ca2+ apoptosis and that Ero1α oxidizes Notch LNR disulfides in Drosophila

    PMID:18809725 PMID:18833192 PMID:18971943 PMID:19752026

    Open questions at the time
    • Structural basis of loop rearrangement not yet visualized
    • Full roster of regulatory cysteines incomplete
  6. 2010 High

    Provided atomic and quantitative mechanism: crystal structures in two redox states plus kinetic assays showed PDI reduction potential and loop disulfides set the rate of catalysis, and localization/imaging tied Ero1α to the MAM, luminal H2O2 production, and ER-mitochondria Ca2+ fluxes.

    Evidence X-ray crystallography, dual active-site PDI redox kinetics, ER-targeted H2O2 sensor, MAM fractionation and Ca2+ imaging, plus platelet-surface co-IP and aggregation assays

    PMID:20095866 PMID:20130085 PMID:20186508 PMID:20562109 PMID:20657012 PMID:20802462 PMID:20834232 PMID:21854214

    Open questions at the time
    • In vivo significance of MAM enrichment not fully tested
    • Identity of all MAM Ca2+ effectors incomplete
  7. 2013 High

    Expanded the oxidoreductase network and refined how PDI both regulates and is a substrate, showing Ero1α partners with multiple PDI-family members and forms a peroxidase relay with GPx7 that reuses H2O2.

    Evidence Proteomic co-IP, SPR, in vitro folding assays with GPx7 cysteine mutants and domain mapping

    PMID:23919619 PMID:24043701

    Open questions at the time
    • Relative flux through PDI vs GPx7/GSH routes in vivo unquantified
    • Selectivity among PDI-family partners not fully resolved
  8. 2014 High

    Dissected the asymmetric dual role of PDI as both regulator and substrate and identified small-molecule (BPA) interference, clarifying the feedback inactivation logic.

    Evidence In vitro oxidase assays with PDI domain mutants, regulatory disulfide formation under controlled O2, and structural/cell-based analysis of BPA inhibition

    PMID:24758166 PMID:25122773 PMID:25258311

    Open questions at the time
    • Cellular concentrations driving regulator vs substrate modes unknown
    • Physiological relevance of BPA exposure not established
  9. 2015 Medium

    Refined the regulatory cysteine map by assigning a positive catalytic and PDI-interaction role to Cys208/Cys241, and extended client/disease scope to MHC class I folding and CHOP-driven liver injury.

    Evidence Mutagenesis with in vitro oxidase assays and GPx8 co-IP; co-IP/knockdown for MHC class I; CHOP-KO mouse with Ero1α rescue in acute liver failure

    PMID:25387528 PMID:25870246 PMID:26609561

    Open questions at the time
    • Structural impact of Cys208/Cys241 minimal but functional role mechanism partial
    • MHC class I and liver findings from single labs
  10. 2018 Medium

    Identified post-translational activation by Fam20C phosphorylation and degradation by FBXO6, establishing kinase- and ubiquitin-based control over Ero1α levels and activity.

    Evidence In vitro kinase assay with MS site mapping and phospho-mutants; in vivo ubiquitination and half-life assays; plus TAM/CCL2-induced upregulation driving invasion

    PMID:27855403 PMID:29858230 PMID:30165193

    Open questions at the time
    • Crosstalk between phosphorylation, degradation and redox switches unresolved
    • Upstream signals coordinating these PTMs incomplete
  11. 2022 High

    Established Ero1α as a redox node controlling Ca2+ handling in distinct tissues and as a target of multiple PTMs, by identifying its substrate cysteines on RyR2 and its inactivation by S-nitrosation and its ERp44-SUMO-controlled retention.

    Evidence RyR2-Cys4806 mutagenesis with SR redox biosensor and animal model; iNOS S-nitrosation with constitutively active Ero1α rescue; ERp44 SUMOylation co-IP with Ubc9-KO mice; platelet GSH redox assays; ERO1-KO interactomics linking it to N-glycosylation via MAGT1

    PMID:35033630 PMID:35077997 PMID:35086342 PMID:36063727 PMID:36427672

    Open questions at the time
    • Integration of these PTMs into a single regulatory hierarchy unclear
    • Tissue specificity of substrate disulfide modification not generalized
  12. 2023 Medium

    Connected Ero1α to UPR balance and tumor immunity, showing its ablation skews IRE1α/PERK signaling toward immunogenic cell death and enhances anti-PD-1 efficacy.

    Evidence Genetic ablation in tumor cells with scRNA-seq, UPR analysis and anti-PD-1 therapeutic models

    PMID:37769655

    Open questions at the time
    • Direct molecular link between Ero1α loss and UPR branch imbalance not mapped
    • Single-lab tumor models
  13. 2024 Medium

    Placed Ero1α downstream of mTORC1 in cancer metabolism and within MAM/muscle physiology, defining an IL-6/STAT3/SLC7A11 ferroptosis-resistance axis and a SEPN1 interaction governing ER redox and bioenergetics.

    Evidence mTORC1 cell models with ChIP and luciferase reporter plus xenografts; ERO1A-SEPN1 co-IP with double-KO mouse rescue; isoform-specific KO in palmitate-stressed β-cells

    PMID:38402623 PMID:38610018 PMID:38692092

    Open questions at the time
    • Mechanism by which mTORC1 elevates Ero1α not fully defined
    • Single-lab disease models
  14. 2025 Medium

    Extended PTM regulation to SIRT5-reversed Lys396 succinylation and m6A-based mRNA control, linking Ero1α to endothelial apoptosis and trophoblast invasion.

    Evidence Quantitative succinylome/MS with SIRT5 gain/loss in HUVECs; MeRIP-qPCR with METTL3 manipulation and ERO1A rescue in trophoblasts

    PMID:40243486 PMID:40652673

    Open questions at the time
    • Effect of Lys396 succinylation on catalytic mechanism not biochemically resolved
    • Single-lab, context-specific findings

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the many layers of regulation (intramolecular disulfide switches, phosphorylation, ubiquitination, S-nitrosation, succinylation, SUMO-controlled retention, m6A) are integrated to set Ero1α activity in specific cell types and disease states remains unresolved.
  • No unified model linking PTM hierarchy to redox switching
  • In vivo flux balance between Ero1α, GPx7/8, Prx4 and glutathione routes unquantified
  • Therapeutic consequences of selective Ero1α inhibition across tissues untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016491 oxidoreductase activity 4 GO:0140096 catalytic activity, acting on a protein 3 GO:0016740 transferase activity 2
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005886 plasma membrane 3
Pathway
R-HSA-109582 Hemostasis 3 R-HSA-392499 Metabolism of proteins 3 R-HSA-8953897 Cellular responses to stimuli 3
Partners
ATP2A2ERP44ERP46ERP57GPX7GPX8P4HBSTIM1

Evidence

Reading pass · 47 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 Human ERO1-L (ERO1A) is a type II integral membrane protein of the endoplasmic reticulum that favors disulfide bond formation in secretory proteins; it complements the yeast ero1-1 thermosensitive mutant, and its activity requires conserved cysteines Cys-394 and Cys-397 (mutation of either abolishes function). Yeast complementation assay, subcellular fractionation (microsome), Endo-H glycan sensitivity, site-directed mutagenesis of conserved cysteines The Journal of biological chemistry High 10671517
2004 Two conserved cysteine triads in human Ero1α (Cys85-Cys94-Cys99 and Cys391-Cys394-Cys397) cooperate in electron transfer; Cys94 likely forms the mixed disulfide with PDI; dominant-negative phenotypes arise from mutations in Cys394, Cys397, or Cys99; Ero1α forms mixed disulfides with both PDI and ERp44. Yeast complementation, site-directed mutagenesis, mixed-disulfide trapping with PDI and ERp44, redox-dependent conformational analysis The Journal of biological chemistry High 15136577
2006 Ero1α (and Ero1β) are dynamically retained in the ER via covalent interactions with ERp44 and non-covalent interactions with PDI; PDI and ERp44 compete for Ero1 binding; PDI also prevents Ero1 aggregation/dimerization, chaperoning its own oxidase; retention is KDEL/RDEL-dependent. Co-expression/secretion assay in HeLa cells, co-immunoprecipitation, dominant-negative PDI mutants lacking active-site cysteines Antioxidants & redox signaling High 16677073
2007 Ero1-Lα is required for secretion of high-molecular-weight adiponectin complexes from adipocytes; siRNA knockdown of Ero1-Lα reduces adiponectin secretion, and ectopic Ero1-Lα expression in Ero1-Lα-deficient fibroblasts stimulates adiponectin secretion after adipogenic conversion. siRNA knockdown, ectopic overexpression in Ero1-Lα-deficient cells, adiponectin secretion ELISA, adipocyte differentiation model (3T3-L1) Molecular and cellular biology Medium 17452443
2008 A disulfide switch regulates Ero1α activity: formation of a disulfide between active-site Cys94 (normally paired with Cys99) and regulatory Cys131 silences the enzyme; PDI (reduced) competes with Cys131 for Cys94, creating a feedback loop linking Ero1α activation to availability of its substrate reduced PDI. The isoform Ero1β lacks an equivalent switch. Mass spectrometry identification of regulatory disulfide, cell-based ER oxidation assay, Ero1α-C131A overexpression, comparison with Ero1β The EMBO journal High 18833192
2008 In Drosophila, Ero1L is specifically required for disulfide bond formation in the three Lin12-Notch repeats (LNRs) of the Notch extracellular domain; loss of Ero1L causes Notch accumulation in the ER, ER stress, and specific defects in lateral inhibition and inductive signaling. Mosaic genetic screen, biochemical disulfide bond assay of LNR domains, immunofluorescence of Notch localization, UPR reporter assay The Journal of cell biology High 18809725
2008 Recombinant human Ero1α has oxidase activity toward thioredoxin and PDI (requiring glutathione for sustained PDI oxidation); non-catalytic regulatory disulfides have a midpoint reduction potential of approximately −275 mV, making them stable in ER redox conditions and only partially reducible by PDI (E°' ≈ −180 mV), limiting excessive Ero1α activity. In vitro oxidase assay with recombinant Ero1α, site-directed mutagenesis of regulatory cysteines, redox potential measurement The EMBO journal High 18971943
2009 CHOP transcriptionally induces Ero1α during ER stress; Ero1α then stimulates the inositol 1,4,5-trisphosphate receptor (IP3R1) to increase IP3-induced calcium release (IICR), promoting calcium-dependent apoptosis. siRNA knockdown of Ero1α or IP3R1 blocks ER stress–induced apoptosis; reconstitution of Ero1α in Chop−/− macrophages restores IICR and apoptosis. siRNA knockdown (Ero1α, IP3R1), genetic loss-of-function (Ero1a, Chop mouse mutants), ectopic reconstitution in Chop−/− macrophages, live-cell calcium imaging, in vivo tunicamycin model The Journal of cell biology High 19752026
2005 Ero1-Lα is transcriptionally induced by hypoxia and hypoglycemia via the HIF-1 transcription factor (independently of p53); siRNA-mediated reduction of Ero1-Lα inhibits VEGF secretion under hypoxia, implicating it as the key adaptive oxidoreductase for disulfide-dependent protein secretion under low-oxygen conditions. HIF-1 genetic epistasis (HIF-1-deficient cells), siRNA knockdown, VEGF secretion assay, diamide rescue experiment, northern/western blotting under hypoxia Oncogene High 15592500
2010 Crystal structures of human Ero1α in hyperactive and inactive forms reveal that regulatory cysteines are positioned in a flexible loop; disulfide rearrangements within this loop modulate oxidative activity. Specific targeting of PDI is mediated by electrostatic and hydrophobic interactions between the Ero1α protruding β-hairpin and the PDI b'-domain substrate-binding pocket. X-ray crystallography of human Ero1α in two redox states, structural analysis of PDI-interaction interface The EMBO journal High 20834232
2010 Ero1α is almost exclusively localized to the mitochondria-associated ER membrane (MAM); this localization requires oxidizing ER conditions. Chemical reduction of the ER—but not ER stress per se—releases Ero1α from the MAM; normoxic conditions are also required. Subcellular fractionation, confocal immunofluorescence, chemical reduction of ER (DTT), hypoxia experiments Cell stress & chaperones Medium 20186508
2010 Ero1α oxidase activity generates H2O2 within the ER lumen in live cells; manipulation of Ero1-Lα levels by overexpression or siRNA causes parallel changes in luminal H2O2. Calcium mobilization from intracellular stores decreases ER H2O2, indicating crosstalk between ER redox and calcium signaling. Live-cell ER-targeted fluorescent H2O2 sensor, Ero1-Lα overexpression and siRNA, calcium mobilization experiments Antioxidants & redox signaling High 20095866
2010 The Ero1α-PDI redox cycle regulates retro-translocation of cholera toxin CTA1: reduced PDI binds and unfolds CTA1, then Ero1α oxidizes PDI to enable toxin release. Ero1α knockdown increases reduced PDI, blocks toxin release, and increases PDI–Derlin-1 interaction; Ero1α overexpression also blocks retro-translocation by preventing PDI engagement of the toxin. siRNA knockdown, Ero1α overexpression, retro-translocation assay, co-immunoprecipitation of PDI–Derlin-1 Molecular biology of the cell Medium 20130085
2010 Ero1α is expressed on blood platelets in association with PDI and αIIbβ3; it is recruited to the platelet surface upon agonist stimulation. Surface Ero1α physically associates with PDI and αIIbβ3 (confirmed by co-immunoprecipitation and confocal colocalization). Blocking surface Ero1α with antibodies decreases platelet aggregation and fibrinogen/PAC-1 binding; Ero1α transfection into MEG01 cells increases αIIbβ3 receptor activity. Co-immunoprecipitation, confocal microscopy, antibody-blocking platelet aggregation assay, PAC-1/fibrinogen binding, Ero1α transfection in MEG01 cells The Journal of biological chemistry Medium 20562109
2010 Wild-type Ero1α oxidizes only one PDI active site at a slow rate; a deregulated Ero1α mutant lacking regulatory disulfides oxidizes both PDI active sites equivalently and faster. When PDI active-site cysteines are mutated to lower their reduction potential, wild-type Ero1α oxidizes both sites with a 12-fold increase in rate, demonstrating that PDI reduction potential limits the rate of Ero1α-catalyzed PDI oxidation. Novel dual active-site PDI redox assay, site-directed mutagenesis of Ero1α regulatory cysteines and PDI active sites, in vitro oxidation kinetics The Journal of biological chemistry High 20657012
2010 After reductive challenge, ER disulfide content recovers within seconds; PDI is the main substrate of Ero1α; Ero1α mixed-disulfide complexes form primarily with PDI and to a lesser extent ERp57 and ERp72, but not with TMX3. PDI oxidation level is precisely regulated, not through ER import/export of thiols but via dynamic equilibrium between Ero1α and glutathione disulfide-mediated oxidation. Kinetics of ER redox recovery (ERO1-deficient cells), mixed-disulfide trapping, redox western blotting of PDI family members, thiol transport experiments The EMBO journal High 20802462
2011 Ero1α is enriched in MAM and regulates Ca2+ fluxes at the ER-mitochondria interface: Ero1α knockdown inhibits mitochondrial Ca2+ fluxes; overexpression of redox-active Ero1α increases passive Ca2+ efflux from the ER, lowering ER Ca2+ content and mitochondrial Ca2+ responses to IP3 agonists. RNA interference, Ero1α overexpression, mitochondrial Ca2+ uniporter activity measurement, live-cell Ca2+ imaging, MAM fractionation Antioxidants & redox signaling High 21854214
2011 ERO1α specifically interacts with PDI via its protruding β-hairpin engaging the hydrophobic pocket of the PDI b'-domain, leading to preferential oxidation of the C-terminal PDI a'-domain. ERO1α associates preferentially with reduced PDI. ERp44 inhibits ERO1α-dependent PDI oxidation when an ERp44 mutant lacking the C-terminal tail is used. Docking simulations, systematic biochemical analysis, mixed-disulfide trapping, domain-specific oxidation assays, ERp44 interaction analysis The Journal of biological chemistry High 21398518
2012 Hyperactive Ero1α (C104A/C131A mutant) leads to hyperoxidation of ERp57 and induces UPR targets BiP and HERP; these effects are mediated through oxidative perturbation of the ER glutathione redox buffer (reversed by NAC, aggravated by BSO). No broad cytosolic antioxidant response is triggered; oxidative challenge is addressed within the ER lumen. Ero1α hyperactive mutant overexpression, microarray transcriptomics, NAC/BSO pharmacological manipulation, cell viability assay The Journal of biological chemistry Medium 23027870
2013 Ero1α is identified as interacting with ERp46, ERp57, and P5 (in addition to PDI) by proteomic analysis and surface plasmon resonance; PDI induces conformational flexibility in Ero1α shuttle cysteine Cys99 facilitating intramolecular electron transfer to the active site. PDI preferentially oxidizes other oxidoreductases via its a' domain (bypassing the a domain which accepts electrons from reduced glutathione). Proteomic co-immunoprecipitation of Ero1α-associated proteins, surface plasmon resonance, kinetic measurements, redox equilibrium analysis The Journal of cell biology High 24043701
2013 GPx7 utilizes Ero1α-produced H2O2 to promote oxidative protein folding via PDI; H2O2 oxidizes GPx7 Cys57 to sulfenic acid, resolved by Cys86 to form an intramolecular disulfide; both sulfenic acid and disulfide forms of GPx7 can oxidize PDI. GPx7 preferentially interacts with PDI a domain. This Ero1α/GPx7/PDI triad generates two disulfide bonds per O2 consumed. In vitro oxidative folding assay, mutagenesis of GPx7 cysteines, in vivo (cell-based) complementation, interaction domain mapping Antioxidants & redox signaling High 23919619
2013 Ero1α and peroxiredoxin 4 (Prx4) share similar intracellular localization mechanisms in the early secretory compartment: sequential interactions with PDI (preferentially for Ero1α) and ERp44 (equally for both) prevent their secretion in a KDEL/RDEL-dependent manner. Co-immunoprecipitation, secretion assays, ER retention competition assays with PDI and ERp44 The Journal of biological chemistry Medium 23979138
2014 PDI serves dual roles with Ero1α: either catalytic domain (a or a') rapidly facilitates formation of Ero1α regulatory disulfides (PDI as regulator, independent of substrate-binding domain), while activated Ero1α specifically binds PDI via hydrophobic interactions and preferentially oxidizes domain a' (PDI as substrate). Several PDI family members are potent regulators of Ero1α activity. In vitro oxidase assay, PDI domain mutants, biochemical interaction assays, redox equilibrium analysis The Journal of biological chemistry High 25258311
2014 Specific PDI family members (PDI and ERp46) catalyze the formation of regulatory disulfides in Ero1α to inactivate it; molecular oxygen and H2O2 are inefficient at forming the correct regulatory disulfides. Both active sites of PDI contribute to regulatory disulfide formation in Ero1α, and PDI's substrate-binding domain is required for efficient electron transfer. In vitro regulatory disulfide formation assay under controlled O2, site-directed mutagenesis of PDI active sites, PDI substrate-binding domain mutants The Biochemical journal High 24758166
2014 Bisphenol A (BPA) inhibits Ero1α-catalyzed PDI oxidation by blocking the interaction between the PDI b'-domain and the Ero1α β-hairpin; the phenol groups of BPA compete with the conserved tryptophan in Ero1α's protruding β-hairpin for binding to PDI. BPA slows PDI reoxidation and causes PDI reduction in HeLa cells. BPA does not affect the PDI-Prx4 interaction. In vitro Ero1α-PDI oxidation assay with BPA, structural analysis (crystallography of PDI-BPA complex), cell-based PDI redox assay The Journal of biological chemistry High 25122773
2015 CHOP promotes hepatocellular injury in acute liver failure through upregulation of ERO1α; CHOP-deficient mice show decreased ERO1α expression and reduced ROS-induced cell death; ERO1α overexpression restores injury in CHOP-deficient mice, demonstrating epistasis: CHOP→ERO1α→ROS. CHOP knockout mouse model, ERO1α overexpression rescue experiment, in vivo ALF model (GalN/LPS), in vitro siRNA The Biochemical journal Medium 25387528
2015 ERO1-α is required for oxidative folding of MHC class I heavy chains; it associates with PDI, calnexin, and immature MHC class I before peptide-loading complex assembly. ERO1-α regulates the redox state and cell-surface expression of MHC class I, altering susceptibility to CD8+ T cell killing. Co-immunoprecipitation (ERO1α with PDI, calnexin, MHC class I), ERO1α siRNA knockdown, flow cytometry of surface MHC class I, CTL killing assay Journal of immunology Medium 25870246
2015 Cysteines 208 and 241 in Ero1α function beyond negative regulation; their mutation lowers the turnover rate under reducing conditions, identifying a positive catalytic role. A reciprocal crosstalk exists between the stability of the Cys208-Cys241 disulfide and the inhibitory disulfides involving Cys104/Cys131; GPx8 recruitment to Ero1α is controlled by the Cys208/Cys241 redox state. Site-directed mutagenesis, in vitro oxidase activity assays, reductive stimulation experiments, GPx8 co-immunoprecipitation Redox biology Medium 26609561
2016 The Cys208-Cys241 disulfide in Ero1α is reduced by PDI and other PDI family members during PDI oxidation; this disulfide pair provides a platform for functional interaction with PDI that enhances Ero1α oxidative activity. Mutation of Cys208/Cys241 does not affect overall Ero1α structure (confirmed by DSC and SAXS), establishing a purely functional regulatory role for this pair. In vitro PDI oxidation assay, differential scanning calorimetry (DSC), small-angle X-ray scattering (SAXS), site-directed mutagenesis The Journal of biological chemistry High 27703014
2016 ERO1-α promotes production of PD-L1 in breast cancer cells via two mechanisms: facilitating oxidative folding of PD-L1 protein and increasing HIF-1α protein expression, which in turn elevates PD-L1 mRNA; ERO1-α depletion reduces tumor PD-L1 and inhibits Jurkat T cell apoptosis induced by tumor PD-L1. ERO1-α siRNA/overexpression, PD-L1 flow cytometry, HIF-1α western blotting, Jurkat co-culture apoptosis assay Oncotarget Medium 28160557
2017 ERO1α KO by CRISPR/Cas9 in HCT116 colorectal cancer cells changes integrin-β1 glycosylation, reduces cell-surface integrin-β1 expression specifically under hypoxia, and results in contact-inhibited morphology and diminished cell motility. This establishes a link between ERO1α expression and integrin-β1 activation under hypoxic conditions. CRISPR/Cas9 knockout, glycosylation analysis, flow cytometry of surface integrin-β1, cell motility and proliferation assays under normoxia/hypoxia Scientific reports Medium 28839225
2018 TAM-secreted CCL2 induces ERO1-α upregulation in non-neoplastic MCF10A breast epithelial cells; ERO1-α is required for TAM-induced MMP-9 upregulation and invasive phenotype involving transcription factors c-Fos and c-Jun. Indirect co-culture system, comparative proteomics, ERO1-α siRNA, cytokine array, MMP-9 assay, invasion assay Cancer letters Medium 30165193
2018 Fam20C (Golgi casein kinase) phosphorylates Ero1α at Ser145, greatly enhancing its oxidase activity. This phosphorylation occurs in the Golgi and Ero1α is then retrograde-transported to the ER via ERp44. Fam20C depletion results in a more reduced ER; phosphorylation is induced under hypoxia, reductive stress, and lactation. Co-immunoprecipitation of Fam20C with ER luminal proteins, in vitro kinase assay, Ser145 phospho-mutants, ER redox assay, MS phosphorylation site identification, ERp44 dependence assay The EMBO journal High 29858230
2016 FBXO6, a substrate recognition component of the SCF E3 ubiquitin ligase, mediates polyubiquitination and proteasomal degradation of the N-glycoprotein Ero1L; FBXO6 overexpression increases Ero1L polyubiquitination and decreases its stability, while FBXO6 inhibition prolongs Ero1L half-life. Co-immunoprecipitation, in vivo ubiquitination assay, Ero1L stability/half-life assay, FBXO6 overexpression/knockdown Cellular physiology and biochemistry Medium 27855403
2022 Ero1α-mediated SR oxidation causes dissociation of intraluminal ERp44 from the RyR2 Ca2+ channel via a redox-sensitive interaction involving RyR2 Cys4806; Ero1α inhibition (EN460) or genetic knockdown normalizes SR redox, restores ERp44-RyR2 association, increases Ca2+ transient amplitude, and reduces proarrhythmic spontaneous Ca2+ waves in hypertrophic cardiomyocytes. Pharmacological inhibition (EN460), Ero1α overexpression, site-directed mutagenesis of RyR2-Cys4806, molecular dynamics simulation, Ca2+ imaging, ERroGFP SR redox biosensor, animal model (TAB) Circulation research High 35086342
2022 Ero1α S-nitrosation by inducible nitric oxide synthase (iNOS) decreases its oxidase activity, causing ER reductive stress during replicative senescence. Inhibition of iNOS decreases Ero1α S-nitrosation and senescence; expression of constitutively active Ero1α restores ER oxidizing state and rescues senescent phenotypes. ER-specific fluorescent redox probes (glutathione and H2O2 sensors), ER-specific catalase model, Ero1α S-nitrosation detection, iNOS inhibition, constitutively active Ero1α overexpression Free radical biology & medicine Medium 35033630
2022 On the platelet surface, Ero1α constitutively oxidizes PDI and further regulates platelet aggregation in a glutathione-dependent manner; the Ero1α/PDI system oxidizes GSH and establishes the reduction potential optimal for platelet aggregation. Oxidized (not reduced) PDI promotes platelet aggregation. Platelet redox assay, Ero1α inhibitor (EN460), PDI redox state measurement, glutathione manipulation, platelet aggregation assay Redox biology Medium 35077997
2022 ERO1 deficiency retards disulfide bond formation in VEGF121 and increases utilization of its single N-glycosylation sequon; ERO1-KO cells show increased interaction of VEGF121 with N-glycosylation pathway proteins, particularly MAGT1 (a thioredoxin-containing component of the post-translational OST complex). ERO1 is thus a physiologic regulator of protein N-glycosylation. ERO1-KO cells, mass spectrometry (unbiased interaction proteomics), N-glycosylation assay, VEGF121 secretion assay Redox biology Medium 36063727
2022 SUMOylation of ERp44 at Lys76 by Ubc9 enhances its covalent binding to Ero1α and ER retention; loss of ERp44 SUMOylation promotes ERp44 degradation and Ero1α secretion, thereby reducing ER stress. Adipocyte-specific Ubc9 KO mice, LC-MS identification of SUMOylated ERp44, K76 mutation, ERp44-Ero1α co-immunoprecipitation, Ero1α secretion assay Metabolism: clinical and experimental Medium 36427672
2023 ERO1A ablation in tumor cells impairs the balance between IRE1α and PERK signaling, induces lethal unfolded protein responses, and promotes immunogenic cell death, enhancing anti-tumor T cell immunity and the efficacy of anti-PD-1 therapy. ERO1A genetic ablation in tumor cells, single-cell RNA-sequencing of tumor microenvironment, UPR pathway analysis, immunogenic cell death assay, anti-PD-1 therapeutic models Cell reports. Medicine Medium 37769655
2023 Platelet ERO1α localizes exclusively in the dense tubular system and promotes Ca2+ mobilization, platelet activation, and aggregation by directly interacting with STIM1 and SERCA2, modifying an allosteric Cys49-Cys56 disulfide in STIM1 and a Cys875-Cys887 disulfide in SERCA2. Mutant STIM1-Cys49/56Ser and SERCA2-Cys875/887Ser show impaired ERO1α interactions. Megakaryocyte-specific and global Ero1α KO mice, intravital microscopy, mass spectrometry, electron microscopy, site-directed mutagenesis of STIM1 and SERCA2 cysteines, Ca2+ mobilization assay, biochemical co-IP Circulation research High 37132383
2024 ERO1A is a functional downstream target of mTORC1; elevated ERO1α promotes ferroptosis resistance via upregulation of SLC7A11 through activation of the IL-6/STAT3 signaling pathway; ERO1α stimulates SLC7A11 transcription via IL-6/STAT3-mediated promoter activation. mTORC1-activated cell models, RNA-seq, cytokine array, ELISA, luciferase reporter assay, chromatin immunoprecipitation, in vivo xenograft and patient-derived xenograft models Journal of experimental & clinical cancer research Medium 38610018
2024 ERO1A interacts with SEPN1 (selenoprotein N) at the MAM; ERO1A depletion in SEPN1 KO cells restores ER redox, re-equilibrates MAM contacts, and rescues mitochondrial bioenergetics and diaphragmatic weakness. ERO1A KO in a SEPN1-loss mouse background blunts ER stress and improves MAM Ca2+ levels and bioenergetics. Co-immunoprecipitation (ERO1A-SEPN1), ERO1A KO in SEPN1-KO mouse model, ER redox assay, MAM fractionation, Ca2+ measurements, respiratory chain assay, diaphragm contractility assay Cell reports. Medicine High 38402623
2024 Specific deletion of ERO1-1α (but not ERO-1β) significantly attenuates palmitate-induced oxidative ER stress, ER Ca2+ dysregulation, mitochondrial H2O2 accumulation, and β-cell death; overexpression of redox-active ERO-1α has the opposite proapoptotic effect. ERO-1α-specific knockout (CRISPR), ERO-1α overexpression, ER-targeted H2O2 and redox sensors, mitochondrial membrane potential assay, Ca2+ imaging, insulin secretion assay Redox biology Medium 38692092
2025 SIRT5 desuccinylates ERO1A at Lys396; under simulated microgravity, SIRT5 is downregulated and ERO1A Lys396 succinylation increases, promoting vascular endothelial cell apoptosis. SIRT5 overexpression protects HUVECs from apoptosis and knockdown of SIRT5 induces apoptosis through ERO1A Lys396 succinylation. LC-MS/MS quantitative succinylome, immunoprecipitation-western blot for Lys396 succinylation, SIRT5 overexpression/knockdown, HUVEC apoptosis assay International journal of molecular sciences Medium 40243486
2025 METTL3-mediated m6A modification of ERO1A mRNA negatively regulates its expression in trophoblasts; METTL3 knockdown elevates ERO1A expression via m6A-dependent mechanism and promotes trophoblast migration and invasion; ERO1A inhibition diminishes the pro-migratory effect of METTL3 depletion. MeRIP-qPCR (m6A-IP), METTL3 knockdown/overexpression, ERO1A functional rescue, trophoblast migration/invasion assays Placenta Medium 40652673
2020 ERO1L-mediated ROS generation is essential for its oncogenic activities in pancreatic cancer; an inactive mutant (ERO1-C394A) fails to promote tumor growth, demonstrating catalytic activity requirement. ERO1L regulates the Warburg effect and aerobic glycolysis, with glycolysis inhibition partially abrogating its growth-promoting activity. ERO1L wild-type vs C394A inactive mutant overexpression, EN460 inhibitor, in vitro proliferation and in vivo xenograft assays, glycolysis inhibitor rescue Theranostics Medium 32724477

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. The Journal of cell biology 511 19752026
2000 ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. The Journal of biological chemistry 261 10671517
2007 Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha. Molecular and cellular biology 236 17452443
2011 Ero1α regulates Ca(2+) fluxes at the endoplasmic reticulum-mitochondria interface (MAM). Antioxidants & redox signaling 185 21854214
2010 Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell stress & chaperones 163 20186508
2008 A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells. The EMBO journal 154 18833192
2005 Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer. Oncogene 141 15592500
2008 Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. The EMBO journal 125 18971943
2013 Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases. The Journal of cell biology 122 24043701
2010 Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium. Antioxidants & redox signaling 119 20095866
2010 Disulphide production by Ero1α-PDI relay is rapid and effectively regulated. The EMBO journal 119 20802462
2010 Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. The EMBO journal 116 20834232
2013 Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding. Antioxidants & redox signaling 100 23919619
2006 Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44. Antioxidants & redox signaling 90 16677073
2020 Endoplasmic Reticulum stress-dependent expression of ERO1L promotes aerobic glycolysis in Pancreatic Cancer. Theranostics 89 32724477
2018 Tumor-associated macrophages secrete CCL2 and induce the invasive phenotype of human breast epithelial cells through upregulation of ERO1-α and MMP-9. Cancer letters 74 30165193
2011 Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI). The Journal of biological chemistry 71 21398518
2015 C/EBP homologous protein (CHOP) contributes to hepatocyte death via the promotion of ERO1α signalling in acute liver failure. The Biochemical journal 68 25387528
2010 The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. The Journal of biological chemistry 68 20657012
2008 Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster. The Journal of cell biology 61 18809725
2017 Cancer-associated oxidoreductase ERO1-α promotes immune escape through up-regulation of PD-L1 in human breast cancer. Oncotarget 58 28160557
2014 Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α). The Journal of biological chemistry 57 25258311
2013 Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway. The Journal of biological chemistry 57 23979138
2012 Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. The Journal of biological chemistry 56 23027870
2018 Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α. The EMBO journal 52 29858230
2016 Cancer-associated oxidoreductase ERO1-α drives the production of VEGF via oxidative protein folding and regulating the mRNA level. British journal of cancer 48 27100727
2015 Cancer-associated oxidoreductase ERO1-α drives the production of tumor-promoting myeloid-derived suppressor cells via oxidative protein folding. Journal of immunology (Baltimore, Md. : 1950) 48 25595776
2004 Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum. The Journal of biological chemistry 48 15136577
2023 Ablation of ERO1A induces lethal endoplasmic reticulum stress responses and immunogenic cell death to activate anti-tumor immunity. Cell reports. Medicine 45 37769655
2017 Hypoxia-inducible ERO1α promotes cancer progression through modulation of integrin-β1 modification and signalling in HCT116 colorectal cancer cells. Scientific reports 45 28839225
2014 Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A. The Journal of biological chemistry 44 25122773
2013 ERO1α-dependent endoplasmic reticulum-mitochondrial calcium flux contributes to ER stress and mitochondrial permeabilization by procaspase-activating compound-1 (PAC-1). Cell death & disease 44 24357799
2021 The NFIB-ERO1A axis promotes breast cancer metastatic colonization of disseminated tumour cells. EMBO molecular medicine 42 33751828
2024 Augmented ERO1α upon mTORC1 activation induces ferroptosis resistance and tumor progression via upregulation of SLC7A11. Journal of experimental & clinical cancer research : CR 40 38610018
2015 Cancer-Associated Oxidase ERO1-α Regulates the Expression of MHC Class I Molecule via Oxidative Folding. Journal of immunology (Baltimore, Md. : 1950) 40 25870246
2010 Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. The Journal of biological chemistry 40 20562109
2013 Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress. The Journal of biological chemistry 38 24022479
2020 ERO1L promotes IL6/sIL6R signaling and regulates MUC16 expression to promote CA125 secretion and the metastasis of lung cancer cells. Cell death & disease 36 33056994
2010 The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin. Molecular biology of the cell 34 20130085
2022 Ero1α-Dependent ERp44 Dissociation From RyR2 Contributes to Cardiac Arrhythmia. Circulation research 32 35086342
2021 ERO1L Is a Novel and Potential Biomarker in Lung Adenocarcinoma and Shapes the Immune-Suppressive Tumor Microenvironment. Frontiers in immunology 32 34354701
2023 SIRT6 deficiency in endothelial cells exacerbates oxidative stress by enhancing HIF1α accumulation and H3K9 acetylation at the Ero1α promoter. Clinical and translational medicine 30 37598403
2022 ER reductive stress caused by Ero1α S-nitrosation accelerates senescence. Free radical biology & medicine 28 35033630
2020 Homocysteine promotes hepatic steatosis by activating the adipocyte lipolysis in a HIF1α-ERO1α-dependent oxidative stress manner. Redox biology 28 33045621
2016 FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 27 27855403
2024 SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA. Cell reports. Medicine 26 38402623
2023 Cordycepin reprogramming lipid metabolism to block metastasis and EMT via ERO1A/mTOR/SREBP1 axis in cholangiocarcinoma. Life sciences 26 37080351
2016 Hypoxia augments MHC class I antigen presentation via facilitation of ERO1-α-mediated oxidative folding in murine tumor cells. European journal of immunology 24 27667124
2022 ERO1 alpha deficiency impairs angiogenesis by increasing N-glycosylation of a proangiogenic VEGFA. Redox biology 23 36063727
2021 The regulation of Ero1-alpha in homocysteine-induced macrophage apoptosis and vulnerable plaque formation in atherosclerosis. Atherosclerosis 23 34478920
2018 ERO1L promotes pancreatic cancer cell progression through activating the Wnt/catenin pathway. Journal of cellular biochemistry 23 30076651
2015 The Hypothermic Influence on CHOP and Ero1-α in an Endoplasmic Reticulum Stress Model of Cerebral Ischemia. Brain sciences 23 25989620
2022 SUMOylation of ERp44 enhances Ero1α ER retention contributing to the pathogenesis of obesity and insulin resistance. Metabolism: clinical and experimental 22 36427672
2024 Biological mechanisms and clinical significance of endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) in human cancer. Journal of experimental & clinical cancer research : CR 20 38454454
2022 The extracellular Ero1α/PDI electron transport system regulates platelet function by increasing glutathione reduction potential. Redox biology 20 35077997
2021 Porcine Circovirus 2 Manipulates the PERK-ERO1α Axis of the Endoplasmic Reticulum To Favor Its Replication by Derepressing Viral DNA from HMGB1 Sequestration within Nuclei. Journal of virology 20 34287039
2021 circ-ACACA promotes proliferation, invasion, migration and glycolysis of cervical cancer cells by targeting the miR-582-5p/ERO1A signaling axis. Oncology letters 20 34584570
2020 MicroRNA-144-3p Inhibits Tumorigenesis of Oral Squamous Cell Carcinoma by downregulating ERO1L. Journal of Cancer 20 31942199
2014 Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases. The Biochemical journal 20 24758166
2023 A Critical Role for ERO1α in Arterial Thrombosis and Ischemic Stroke. Circulation research 19 37132383
2019 ERO1α is a novel endogenous marker of hypoxia in human cancer cell lines. BMC cancer 18 31142270
2024 Non-esterified fatty acid palmitate facilitates oxidative endoplasmic reticulum stress and apoptosis of β-cells by upregulating ERO-1α expression. Redox biology 16 38692092
2020 ERO1α inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells. Molecular and cellular endocrinology 16 32376276
2022 Silica nanoparticles induce ovarian granulosa cell apoptosis via activation of the PERK-ATF4-CHOP-ERO1α pathway-mediated IP3R1-dependent calcium mobilization. Cell biology and toxicology 15 36346508
2020 ERO1α promotes testosterone secretion in hCG-stimulated mouse Leydig cells via activation of the PI3K/AKT/mTOR signaling pathway. Journal of cellular physiology 15 31990068
2020 The Role of ERO1α in Modulating Cancer Progression and Immune Escape. Journal of cancer immunology 15 33615311
2016 Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase. The Journal of biological chemistry 15 27703014
2021 ERO1α mediates endoplasmic reticulum stress-induced apoptosis via microRNA-101/EZH2 axis in colon cancer RKO and HT-29 cells. Human cell 14 33559868
2020 ERO1L promotes NSCLC development by modulating cell cycle-related molecules. Cell biology international 14 32841447
2015 Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover. Redox biology 14 26609561
2022 Crosstalk between ERO1α and ryanodine receptor in arsenite-dependent mitochondrial ROS formation. Biochemical pharmacology 13 35189109
2021 ERO1L Promotes Hepatic Metastasis through Activating Epithelial-Mesenchymal Transition (EMT) in Pancreatic Cancer. Journal of immunology research 13 33681386
2013 Expression of the endoplasmic reticulum oxidoreductase Ero1α in gastro-intestinal cancer reveals a link between homocysteine and oxidative protein folding. Antioxidants & redox signaling 13 23373818
2025 Small molecule-mediated inhibition of the oxidoreductase ERO1A restrains aggressive breast cancer by impairing VEGF and PD-L1 in the tumor microenvironment. Cell death & disease 12 39962052
2022 ERO1L promotes the proliferation and metastasis of lung adenocarcinoma via the Wnt2/β-catenin signaling pathway. Molecular carcinogenesis 11 35785492
2022 Identification of Natural Product Sulfuretin Derivatives as Inhibitors for the Endoplasmic Reticulum Redox Protein ERO1α. ACS bio & med chem Au 10 35892127
2022 Porcine circovirus type 2 induces CHOP-ERO1α-ROS-mediated apoptosis in PK-15 cells. Veterinary microbiology 10 36037618
2021 Endophilin A2-mediated alleviation of endoplasmic reticulum stress-induced cardiac injury involves the suppression of ERO1α/IP3R signaling pathway. International journal of biological sciences 10 34512174
2022 Homocysteine facilitates endoplasmic reticulum stress and apoptosis of hepatocytes by suppressing ERO1α expression via cooperation between DNMT1 and G9a. Cell biology international 9 35347798
2003 Ero1-L, an ischemia-inducible gene from rat brain with homology to global ischemia-induced gene 11 (Giig11), is localized to neuronal dendrites by a dispersed identifier (ID) element-dependent mechanism. Journal of neurochemistry 9 12694393
2023 ERO1α promotes the proliferation and inhibits apoptosis of colorectal cancer cells by regulating the PI3K/AKT pathway. Journal of molecular histology 8 37776473
2023 Inhibition of ERO1a and IDO1 improves dendritic cell infiltration into pancreatic ductal adenocarcinoma. Frontiers in immunology 8 38187398
2025 SIRT5 Alleviates Apoptosis of Vascular Endothelial Cells Under Simulated Microgravity via Desuccinylation of ERO1A. International journal of molecular sciences 6 40243486
2022 Role of Ero1α in cognitive impairment induced by chronic hypoxia. Brain research 6 36220374
2021 Knockdown of PPARδ Induces VEGFA-Mediated Angiogenesis via Interaction With ERO1A in Human Colorectal Cancer. Frontiers in oncology 6 34712608
2024 Inhibition of ERO1L induces autophagy and apoptosis via endoplasmic reticulum stress in colorectal cancer. Cellular signalling 5 39657838
2025 M2 macrophage-secreted KYNU promotes stemness remodeling and malignant behavior in endometrial cancer via the SOD2-mtROS-ERO1α-UPRER axis. Journal of experimental & clinical cancer research : CR 4 40616124
2011 Molecular cloning and characterization of the porcine Ero1L and ERp44 genes: potential roles in controlling energy metabolism. General and comparative endocrinology 4 21664357
2025 ERO1A promotes the proliferation, migration and invasion of bladder cancer through ALOX5 mediated activation of JAK-STAT signaling pathway. Journal of translational medicine 3 41449433
2024 Enhancing S-nitrosoglutathione reductase decreases S-nitrosylation of ERO1α and reduces neuronal death in secondary traumatic brain injury. Nitric oxide : biology and chemistry 3 39566653
2023 ERO1α primes the ryanodine receptor to respond to arsenite with concentration dependent Ca2+ release sequentially triggering two different mechanisms of ROS formation. Chemico-biological interactions 3 37659621
2025 METTL3-dependent m6A modification of ERO1A mRNA regulates trophoblast migration and invasion in early-onset severe preeclampsia. Placenta 2 40652673
2025 ERO1A-positive tumor epithelial cells in colorectal cancer progression: a multi-omics perspective. Apoptosis : an international journal on programmed cell death 2 41028408
2023 Arsenite enhances ERO1α expression via ryanodine receptor dependent and independent mechanisms. Environmental toxicology and pharmacology 2 36781116
2023 Knockdown of ERO1L attenuates tumor growth, migration and invasion in lung adenocarcinoma through Wnt/β‑catenin pathway. Biotechnology & genetic engineering reviews 2 37014092
2023 Suppression of Microglial ERO1a Alleviates Inflammation and Enhances the Efficacy of Rehabilitative Training After Ischemic Stroke. Molecular neurobiology 2 37100971
2022 Inhibition of activity/expression, or genetic deletion, of ERO1α blunts arsenite geno- and cyto-toxicity. Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association 2 35964836
2021 Identification of novel small molecule inhibitors for endoplasmic reticulum oxidoreductase 1α (ERO1α) enzyme: structure-based molecular docking and molecular dynamic simulation studies. Journal of biomolecular structure & dynamics 2 34606425
2025 Functional characterization of key protein biomarkers in spontaneous intracerebral hemorrhage pathogenesis: Structure and function of NUAK1 protein and ERO1L protein macromolecules. International journal of biological macromolecules 1 40203915
2025 Ero1a, the most strongly hypoxia-induced protein in PASMCs, promotes the development of hypoxia- and monocrotaline-induced pulmonary hypertension in rats. Life sciences 1 40414553

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