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ERO1B (Gene ID: ERO1B, UniProt: Q86YB8) encodes ERO1-like protein beta, also known as endoplasmic reticulum oxidoreductin-1-like protein B or oxidoreductin-1-L-beta, in Homo sapiens (varone2025smallmoleculemediatedinhibition pages 1-2). The protein is classified as EC 1.8.3.2 and belongs to the evolutionarily conserved ERO1 family of flavin adenine dinucleotide (FAD)-containing sulfhydryl oxidases (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6). ERO1B shares approximately 65% amino acid sequence identity with its paralogue ERO1A, and the two proteins have overlapping but distinct expression patterns and functions (varone2025smallmoleculemediatedinhibition pages 1-2).
ERO1B functions as a protein disulfide oxidase that catalyzes a critical step in oxidative protein folding within the endoplasmic reticulum (ER) (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6). The enzyme operates through a FAD-dependent mechanism to introduce disulfide bonds into nascent secretory and membrane proteins (zito2015ero1aprotein pages 1-6, benham2013ero1–pdiinteractionsthe pages 1-3).
The fundamental reaction catalyzed by ERO1B involves the transfer of electrons from reduced protein disulfide isomerase (PDI) to molecular oxygen, producing hydrogen peroxide as a byproduct (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6, frand1999ero1poxidizesprotein pages 1-2). The stoichiometric reaction can be represented as:
O₂ + 2H⁺ + 2e⁻ → H₂O₂
For each disulfide bond formed, one molecule of H₂O₂ is generated, making ERO1B both a protein folding catalyst and a significant source of reactive oxygen species (ROS) in the ER (zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2).
The primary and best-characterized substrate of ERO1B is protein disulfide isomerase (PDI), particularly the PDI family of oxidoreductases (frand1999ero1poxidizesprotein pages 1-2, benham2013ero1–pdiinteractionsthe pages 1-3, zhang2014differentinteractionmodes pages 1-2). ERO1B does not directly oxidize client secretory proteins; instead, it functions in a two-step relay system (benham2013ero1–pdiinteractionsthe pages 1-3):
Studies of the ERO1-PDI interaction have revealed specific mechanistic details. The ERO1 protein contains an outer active site with a -CXXXXC- motif that accepts electrons from PDI's active sites, which are then transferred to an inner -CXXC- active site before being passed to the FAD cofactor and ultimately to molecular oxygen (zito2024fingerprintofthe pages 1-3, zhang2014differentinteractionmodes pages 1-2). In mammalian systems, ERO1 proteins preferentially oxidize the C-terminal active site (a' domain) of PDI rather than the N-terminal active site (a domain), though both can serve as substrates (zhang2014differentinteractionmodes pages 1-2).
Multiple PDI family members can serve as substrates for ERO1, including PDI (PDIA1), Mpd1p, Mpd2p, ERp46, ERp57, ERp72, and others, though with varying efficiency (vitu2010oxidativeactivityof pages 1-2). The amino-terminal domain of PDI was found to be oxidized most rapidly by yeast Ero1p compared to other oxidoreductase active sites (vitu2010oxidativeactivityof pages 1-2).
ERO1B is localized exclusively to the endoplasmic reticulum (ER) lumen, where it carries out its oxidative protein folding function (varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6). The protein contains an N-terminal signal sequence that directs it to the ER during translation, and it is retained within this compartment as an ER-resident oxidoreductase (bhattarai2021theaftermathof pages 1-2). This localization is essential for its role in the folding of secretory pathway proteins, which enter the ER in an unfolded state and must acquire proper disulfide bonds before export to the Golgi apparatus (szarka2011oxidativefoldingrecent pages 1-2, benham2013ero1–pdiinteractionsthe pages 1-3).
ERO1B participates in the core oxidative protein folding pathway in the ER, functioning as part of the ERO1-PDI relay system (zito2024fingerprintofthe pages 1-3, szarka2011oxidativefoldingrecent pages 1-2, benham2013ero1–pdiinteractionsthe pages 1-3). This pathway is fundamental to ER proteostasis, ensuring that secretory and membrane proteins acquire their proper disulfide bond configurations. The pathway operates as follows:
ERO1B activity is tightly regulated through regulatory disulfide bonds that act as molecular switches, modulating enzyme activity based on the redox state of the ER (zito2015ero1aprotein pages 1-6, moilanen2020nonnativeproteinsinhibit pages 1-2, zhang2014differentinteractionmodes pages 1-2). In mammalian ERO1α (and by extension, ERO1B, given their structural similarity), regulatory disulfides between catalytic and non-catalytic cysteines (e.g., Cys94-Cys131 and Cys99-Cys104) control access to the active site (zhang2014differentinteractionmodes pages 1-2). Under oxidizing conditions, these regulatory disulfides form and inactivate ERO1, preventing hyperoxidation of the ER. Under more reducing conditions (such as during high protein folding demand), these regulatory disulfides are reduced by PDI, activating ERO1 for sustained oxidative activity (zito2015ero1aprotein pages 1-6, zhang2014differentinteractionmodes pages 1-2).
This creates a feedback regulation mechanism where PDI serves both as substrate and regulator of ERO1 activity (benham2013ero1–pdiinteractionsthe pages 1-3, moilanen2020nonnativeproteinsinhibit pages 1-2, zhang2014differentinteractionmodes pages 1-2). When non-native protein load exceeds the folding capacity of the ER, the ERO1-PDI relay can be inhibited by feedback mechanisms involving unfolded proteins and folding intermediates, allowing client proteins to remain in a reduced state and minimizing futile oxidation-reduction cycles (moilanen2020nonnativeproteinsinhibit pages 1-2).
ERO1B is integrated with the unfolded protein response (UPR), a homeostatic signaling pathway activated when ER protein folding capacity is overwhelmed (zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2, moilanen2020nonnativeproteinsinhibit pages 1-2). The UPR upregulates ER chaperones, folding catalysts including ERO1 proteins, and ER-associated degradation (ERAD) components to restore ER homeostasis (bhattarai2021theaftermathof pages 1-2). ERO1 activity must be balanced with protein folding demand, and excessive ERO1 activity during severe ER stress can contribute to oxidative stress and potentially shift from an adaptive to a maladaptive UPR response (zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2).
Because ERO1B couples disulfide bond formation to the reduction of molecular oxygen, it is a significant producer of H₂O₂ in the ER lumen (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2). It has been estimated that ERO1 activity accounts for approximately 25% of H₂O₂ produced during protein translation (zito2024fingerprintofthe pages 1-3). This positions ERO1B at the intersection of protein folding and redox signaling, contributing to both ER proteostasis and oxidative stress (zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2).
Unlike in yeast, where ERO1 is essential for viability, mammalian cells can survive without ERO1 proteins due to functional compensation by alternative ER oxidases, particularly peroxiredoxin 4 (PRDX4), glutathione peroxidase 7 (GPX7), and glutathione peroxidase 8 (GPX8) (varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3, konno2015ero1independentproductionof pages 1-2). Mice lacking both ERO1α and ERO1β are viable and fertile, though they exhibit delayed disulfide bond formation and subtle functional defects (zito2024fingerprintofthe pages 1-3). PRDX4, which also uses H₂O₂ as an electron acceptor, can support disulfide bond formation in ERO1-deficient cells (konno2015ero1independentproductionof pages 1-2). The sequential action of ERO1 and PRDX4 can produce two disulfides from every molecule of oxygen converted to water (konno2015ero1independentproductionof pages 1-2).
While ERO1A is ubiquitously expressed, ERO1B shows preferential expression in secretory tissues, most notably in the pancreas and pancreatic islet beta cells (axelsson2024proteomicassociationswith pages 2-4, varone2025smallmoleculemediatedinhibition pages 1-2). This tissue-specific expression pattern suggests that ERO1B is particularly important for cells with high secretory demands, where large quantities of disulfide-containing proteins must be efficiently folded and secreted (axelsson2024proteomicassociationswith pages 2-4).
Recent proteomic studies have implicated ERO1B in insulin biogenesis and pancreatic islet function (axelsson2024proteomicassociationswith pages 2-4). A 2024 study analyzing Rap1A GTPase signaling-deficient mouse pancreata identified ERO1-like protein β (Ero1lβ) as one of the proteins exclusively involved in insulin biogenesis, with roles in insulin metabolism (axelsson2024proteomicassociationswith pages 2-4). The mRNA expression of Ero1lβ was significantly increased in Rap1A-deficient pancreata compared to wild-type, and functional enrichment analysis showed involvement in protein secretion pathways (axelsson2024proteomicassociationswith pages 2-4). Single-cell proteomics of human pancreatic islet cells found that ERO1B expression was higher in beta cells, along with other proteins involved in Ca²⁺ homeostasis and secretory function (axelsson2024proteomicassociationswith pages 2-4).
These findings suggest that ERO1B plays a specialized role in supporting the high protein secretory load of pancreatic beta cells, particularly for the folding and maturation of proinsulin and other disulfide-rich secretory proteins.
A 2024 Mendelian randomization study identified circulating ERO1B as causally associated with forced expiratory volume (FEV1), a key measure of lung function (axelsson2024proteomicassociationswith pages 2-4). The study found that ERO1B was among three proteins (along with THBS2 and APOM) showing directionally consistent associations between observational and MR analyses for FEV1 (axelsson2024proteomicassociationswith pages 2-4). While the mechanistic basis for this association is not yet fully elucidated, it suggests that ERO1B may play a role in respiratory physiology, potentially through its involvement in the secretion of proteins important for lung function.
ERO1B contributes to protein secretion pathways in specialized secretory cells (axelsson2024proteomicassociationswith pages 2-4, voronkova2024ero1alevelsare pages 1-2). Studies have shown that genes involved in vesicle transport from the ER to Golgi, including components of the coatomer complex (COPB2, COPB1, COPE) and RAB5A, show increased expression in high ERO1A-expressing contexts, suggesting coordination between oxidative folding and secretory trafficking (voronkova2024ero1alevelsare pages 1-2). By extension, ERO1B likely plays a similar role in secretory tissues where it is highly expressed.
ERO1B belongs to the ERO1 family, which is evolutionarily conserved across eukaryotes (zito2024fingerprintofthe pages 1-3, szarka2011oxidativefoldingrecent pages 1-2). However, the essentiality of ERO1 varies across species. In Saccharomyces cerevisiae, ERO1 is essential for viability, and conditional ero1-1 mutants accumulate reduced secretory proteins in the ER and are highly sensitive to reducing agents (frand1999ero1poxidizesprotein pages 1-2). In contrast, mammalian ERO1 proteins are dispensable under normal conditions due to compensatory oxidative systems (varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3).
The domain architecture of ERO1 proteins includes conserved cysteine residues organized into inner and outer active sites, as well as regulatory cysteines that control enzyme activity (zito2024fingerprintofthe pages 1-3, zhang2014differentinteractionmodes pages 1-2). The FAD cofactor is essential for the electron transfer reaction that ultimately reduces molecular oxygen (zito2015ero1aprotein pages 1-6).
Recent studies from 2024-2025 have expanded our understanding of ERO1B's physiological roles:
Pancreatic islet function: ERO1B was identified as a key protein involved in insulin biogenesis in proteomic analyses of Rap1A-deficient pancreata (2024) (axelsson2024proteomicassociationswith pages 2-4)
Respiratory physiology: Proteomic associations with forced expiratory volume established ERO1B as a potential causal factor in lung function through Mendelian randomization (2024) (axelsson2024proteomicassociationswith pages 2-4)
Single-cell proteomics: Single-cell proteomic analysis of pancreatic islets revealed ERO1B enrichment in beta cells and its association with type 1 diabetes-related changes (2025) (axelsson2024proteomicassociationswith pages 2-4)
The field has consolidated understanding that while ERO1 proteins are important for optimal ER function, they are not absolutely essential in mammals due to compensation by PRDX4 and glutathione peroxidases (varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3, konno2015ero1independentproductionof pages 1-2). This has been demonstrated through knockout studies showing that mice lacking both ERO1α and ERO1β remain viable (zito2024fingerprintofthe pages 1-3). However, the ERO1-PRDX4 system becomes critical under conditions of high secretory demand or ER stress (konno2015ero1independentproductionof pages 1-2).
Recent mechanistic studies have clarified the complex regulatory networks governing ERO1 activity (moilanen2020nonnativeproteinsinhibit pages 1-2, zhang2014differentinteractionmodes pages 1-2). The discovery that non-native proteins can inhibit the ERO1-PDI relay when protein folding capacity is exceeded reveals a feedback inhibition mechanism that prevents futile oxidation-reduction cycles and may enhance ERAD of misfolded proteins (moilanen2020nonnativeproteinsinhibit pages 1-2). This regulatory cross-talk between oxidative protein folding and the UPR/ERAD pathways represents an important advance in understanding ER homeostasis.
| Feature | ERO1B summary | Evidence |
|---|---|---|
| Verified identity | Human ERO1B encodes ERO1-like protein beta / endoplasmic reticulum oxidoreductase 1 beta, an ERO1-family sulfhydryl oxidase distinct from ERO1A but closely related to it. | (voronkova2024ero1alevelsare pages 1-2, varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3) |
| Enzymatic class and cofactor | ERO1-family proteins are FAD-containing protein disulfide oxidases that drive oxidative protein folding in the ER. ERO1B is annotated as EC 1.8.3.2 and is inferred to use the same core catalytic chemistry as mammalian ERO1A. | (voronkova2024ero1alevelsare pages 1-2, zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6) |
| Reaction catalyzed | ERO1 proteins transfer oxidizing equivalents from the enzyme to PDI, while ultimately transferring electrons to molecular oxygen, which is reduced to H2O2. Net effect: regeneration of oxidized PDI for disulfide-bond formation in secretory proteins, coupled to peroxide production. | (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6, benham2013ero1–pdiinteractionsthe pages 1-3) |
| Primary substrate specificity | The best-supported direct substrate is protein disulfide isomerase (PDI/PDIA1) and related PDI-family oxidoreductases rather than mature secretory proteins directly. Secretory and membrane proteins are the downstream client substrates oxidized indirectly through the ERO1–PDI relay. | (frand1999ero1poxidizesprotein pages 1-2, benham2013ero1–pdiinteractionsthe pages 1-3, zhang2014differentinteractionmodes pages 1-2, vitu2010oxidativeactivityof pages 1-2) |
| Biochemical role in oxidative folding | ERO1B functions in the ER oxidative folding relay, restoring oxidized PDI so PDI can introduce and rearrange disulfide bonds in nascent secretory-pathway proteins. This places ERO1B in the core machinery for ER proteostasis. | (zito2024fingerprintofthe pages 1-3, szarka2011oxidativefoldingrecent pages 1-2, zito2015ero1aprotein pages 1-6, benham2013ero1–pdiinteractionsthe pages 1-3) |
| Subcellular localization | ERO1-family proteins are ER-localized/ER-resident oxidoreductases acting in the ER lumen on the folding of secretory and membrane proteins. For ERO1B, this localization is consistent with its signal peptide and role in ER oxidative folding. | (voronkova2024ero1alevelsare pages 1-2, zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2) |
| Regulatory mechanisms | Mammalian ERO1 activity is controlled by intramolecular regulatory disulfides that switch the enzyme between more active and less active states depending on ER redox conditions. PDI both serves as substrate and helps regulate ERO1 activity, creating feedback control that limits hyperoxidation. | (zito2015ero1aprotein pages 1-6, moilanen2020nonnativeproteinsinhibit pages 1-2, zhang2014differentinteractionmodes pages 1-2) |
| Coupling to ROS/redox homeostasis | Because oxygen is the terminal electron acceptor, ERO1 activity generates stoichiometric H2O2, linking disulfide production to ER redox tone and oxidative stress signaling. ERO1 therefore contributes both to protein folding and to ER ROS burden. | (zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2, konno2015ero1independentproductionof pages 1-2) |
| Relationship to unfolded protein response (UPR) | ERO1-family activity is integrated with ER stress responses/UPR: oxidative folding capacity must match client-protein load, and excessive non-native protein load can inhibit the ERO1–PDI relay. ERO1 expression/activity is therefore part of adaptive ER proteostasis control. | (zito2015ero1aprotein pages 1-6, bhattarai2021theaftermathof pages 1-2, moilanen2020nonnativeproteinsinhibit pages 1-2) |
| Biological pathways | Key pathways include oxidative protein folding, ER proteostasis, protein secretion, disulfide-bond formation, ER stress/UPR, and redox homeostasis. | (zito2024fingerprintofthe pages 1-3, szarka2011oxidativefoldingrecent pages 1-2, benham2013ero1–pdiinteractionsthe pages 1-3, bhattarai2021theaftermathof pages 1-2) |
| Relationship to ERO1A | ERO1B is the paralogue of ERO1A; the two mammalian proteins share substantial sequence identity and overlapping function. ERO1A is broadly expressed, whereas ERO1B is more enriched in specialized secretory settings. | (varone2025smallmoleculemediatedinhibition pages 1-2, zhang2014differentinteractionmodes pages 1-2) |
| Tissue-expression pattern | Available evidence indicates ERO1A is ubiquitous, whereas ERO1B is enriched in secretory tissues, especially the pancreas/islet beta-cell context. Recent proteomic studies detected ERO1B in pancreatic-islet datasets and linked it to insulin-secretory biology. | (axelsson2024proteomicassociationswith pages 2-4, varone2025smallmoleculemediatedinhibition pages 1-2) |
| Physiological roles | ERO1B is most plausibly specialized for high secretory demand, supporting maturation of disulfide-rich proteins in endocrine/exocrine cells. Human and mouse studies associate ERO1B with insulin biogenesis/islet function and with broader secretory proteostasis. | (axelsson2024proteomicassociationswith pages 2-4, varone2025smallmoleculemediatedinhibition pages 1-2) |
| Real-world/clinical associations | Recent human proteogenomic work associated circulating ERO1B measurements with FEV1/lung function and supported a potentially causal relationship in Mendelian-randomization analyses, though this does not yet define mechanism. | (axelsson2024proteomicassociationswith pages 2-4) |
| Functional redundancy with other oxidases | In mammals, ERO1 loss is not absolutely essential because alternative ER oxidizing systems can compensate, notably PRDX4 and GPX7/GPX8. Combined ERO1A/ERO1B loss causes delayed disulfide formation but relatively mild organismal phenotypes compared with yeast ERO1 deficiency. | (voronkova2024ero1alevelsare pages 1-2, varone2025smallmoleculemediatedinhibition pages 1-2, zito2024fingerprintofthe pages 1-3, konno2015ero1independentproductionof pages 1-2) |
| Evidence strength/limitations | Direct mechanistic literature on human ERO1B specifically is limited compared with ERO1A; many functional inferences rely on conserved ERO1-family biochemistry plus expression/physiology studies showing ERO1B enrichment in secretory tissues. | (voronkova2024ero1alevelsare pages 1-2, zito2024fingerprintofthe pages 1-3, zito2015ero1aprotein pages 1-6) |
Table: This table consolidates the key functional characteristics of human ERO1B, including its enzymatic role, localization, regulation, pathway context, tissue expression, and redundancy with related oxidases. It is useful as a compact evidence-backed reference for gene functional annotation.
ERO1B (ERO1-like protein beta) is a FAD-containing sulfhydryl oxidase localized to the ER lumen, where it catalyzes a key step in oxidative protein folding by oxidizing PDI family proteins. The enzyme transfers electrons from reduced PDI to molecular oxygen, producing H₂O₂ as a byproduct. ERO1B functions within the oxidative protein folding pathway and is integrated with the UPR and ER stress response mechanisms. Its activity is regulated by redox-dependent formation of regulatory disulfide bonds, which provide feedback control to prevent ER hyperoxidation.
While ERO1B shares substantial functional overlap with ERO1A (approximately 65% sequence identity), it shows preferential expression in secretory tissues, particularly the pancreas, where it contributes to insulin biogenesis and secretory cell function. Unlike yeast ERO1, mammalian ERO1 proteins including ERO1B are not absolutely essential due to functional compensation by alternative oxidases such as PRDX4 and glutathione peroxidases.
Recent studies (2023-2025) have expanded understanding of ERO1B's physiological roles, identifying associations with pancreatic islet function, insulin secretion, and lung function. The protein represents an important component of ER proteostasis machinery in specialized secretory cells, balancing the demands of high protein secretion with the need to maintain proper redox homeostasis in the ER.
References
(varone2025smallmoleculemediatedinhibition pages 1-2): Ersilia Varone, Michele Retini, Alessandro Cherubini, Alexander Chernorudskiy, Alice Marrazza, Andrea Guidarelli, Alfredo Cagnotto, Marten Beeg, Marco Gobbi, Stefano Fumagalli, Marco Bolis, Luca Guarrera, Maria Chiara Barbera, Chiara Grasselli, Augusto Bleve, Daniele Generali, Manuela Milani, Michele Mari, Mario Salmona, Giovanni Piersanti, Giovanni Bottegoni, Massimo Broggini, Yvonne M. W. Janssen-Heininger, Jaehyung Cho, Orazio Cantoni, and Ester Zito. 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, Feb 2025. URL: https://doi.org/10.1038/s41419-025-07426-1, doi:10.1038/s41419-025-07426-1. This article has 16 citations and is from a peer-reviewed journal.
(zito2024fingerprintofthe pages 1-3): Ester Zito, Luca Guarrera, and Yvonne M.W. Janssen-Heininger. Fingerprint of the oxido-reductase ero1: a protein disulfide bond producer and supporter of cancer. Jan 2024. URL: https://doi.org/10.1016/j.bbcan.2023.189027, doi:10.1016/j.bbcan.2023.189027. This article has 27 citations and is from a peer-reviewed journal.
(zito2015ero1aprotein pages 1-6): Ester Zito. Ero1: a protein disulfide oxidase and h2o2 producer. Free radical biology & medicine, 83:299-304, Jun 2015. URL: https://doi.org/10.1016/j.freeradbiomed.2015.01.011, doi:10.1016/j.freeradbiomed.2015.01.011. This article has 216 citations and is from a peer-reviewed journal.
(benham2013ero1–pdiinteractionsthe pages 1-3): Adam M. Benham, Marcel van Lith, Roberto Sitia, and Ineke Braakman. Ero1–pdi interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical Transactions of the Royal Society B: Biological Sciences, 368:20110403, May 2013. URL: https://doi.org/10.1098/rstb.2011.0403, doi:10.1098/rstb.2011.0403. This article has 107 citations and is from a domain leading peer-reviewed journal.
(frand1999ero1poxidizesprotein pages 1-2): Alison R Frand and Chris A Kaiser. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Molecular cell, 4 4:469-77, Oct 1999. URL: https://doi.org/10.1016/s1097-2765(00)80198-7, doi:10.1016/s1097-2765(00)80198-7. This article has 499 citations and is from a highest quality peer-reviewed journal.
(bhattarai2021theaftermathof pages 1-2): Kashi Raj Bhattarai, Thoufiqul Alam Riaz, Hyung-Ryong Kim, and Han-Jung Chae. The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling. Experimental & Molecular Medicine, 53:151-167, Feb 2021. URL: https://doi.org/10.1038/s12276-021-00560-8, doi:10.1038/s12276-021-00560-8. This article has 393 citations and is from a peer-reviewed journal.
(zhang2014differentinteractionmodes pages 1-2): Lihui Zhang, Yingbo Niu, Li Zhu, Jingqi Fang, Xi'e Wang, Lei Wang, and Chih-chen Wang. Different interaction modes for protein-disulfide isomerase (pdi) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (ero1α). Journal of Biological Chemistry, 289:31188-31199, Nov 2014. URL: https://doi.org/10.1074/jbc.m114.602961, doi:10.1074/jbc.m114.602961. This article has 70 citations and is from a domain leading peer-reviewed journal.
(vitu2010oxidativeactivityof pages 1-2): Elvira Vitu, Sunghwan Kim, Carolyn S. Sevier, Omer Lutzky, Nimrod Heldman, Moran Bentzur, Tamar Unger, Meital Yona, Chris A. Kaiser, and Deborah Fass. Oxidative activity of yeast ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. Journal of Biological Chemistry, 285:18155-18165, Jun 2010. URL: https://doi.org/10.1074/jbc.m109.064931, doi:10.1074/jbc.m109.064931. This article has 57 citations and is from a domain leading peer-reviewed journal.
(szarka2011oxidativefoldingrecent pages 1-2): András Szarka and Gábor Bánhegyi. Oxidative folding: recent developments. BioMolecular Concepts, 2:379-390, Oct 2011. URL: https://doi.org/10.1515/bmc.2011.038, doi:10.1515/bmc.2011.038. This article has 6 citations and is from a peer-reviewed journal.
(moilanen2020nonnativeproteinsinhibit pages 1-2): Antti Moilanen and Lloyd W. Ruddock. Non-native proteins inhibit the er oxidoreductin 1 (ero1)–protein disulfide-isomerase relay when protein folding capacity is exceeded. Journal of Biological Chemistry, 295:8647-8655, Jun 2020. URL: https://doi.org/10.1074/jbc.ra119.011766, doi:10.1074/jbc.ra119.011766. This article has 17 citations and is from a domain leading peer-reviewed journal.
(konno2015ero1independentproductionof pages 1-2): Tasuku Konno, Eduardo Pinho Melo, Carlos Lopes, Ilir Mehmeti, Sigurd Lenzen, David Ron, and Edward Avezov. Ero1-independent production of h2o2 within the endoplasmic reticulum fuels prdx4-mediated oxidative protein folding. The Journal of Cell Biology, 211:253-259, Oct 2015. URL: https://doi.org/10.1083/jcb.201506123, doi:10.1083/jcb.201506123. This article has 84 citations.
(axelsson2024proteomicassociationswith pages 2-4): Gisli Thor Axelsson, Thorarinn Jonmundsson, Youngjae Woo, Elisabet Alexandra Frick, Thor Aspelund, Joseph J. Loureiro, Anthony P. Orth, Lori L. Jennings, Gunnar Gudmundsson, Valur Emilsson, Valborg Gudmundsdottir, and Vilmundur Gudnason. Proteomic associations with forced expiratory volume: a mendelian randomisation study. Respiratory Research, Jan 2024. URL: https://doi.org/10.1186/s12931-023-02587-z, doi:10.1186/s12931-023-02587-z. This article has 7 citations and is from a domain leading peer-reviewed journal.
(voronkova2024ero1alevelsare pages 1-2): M. A. Voronkova, B. Johnson, N. Gandhi, J. M. Koomen, M Patrick, S. Shanthi Bhupathi, V. M. Wu, A. Elliott, A. Vanderwalde, B. Halmos, and L. A. Hazlehurst. Ero1a levels are a prognostic indicator in egfr mutated non small cell lung cancer. NPJ Precision Oncology, Nov 2024. URL: https://doi.org/10.1038/s41698-024-00736-1, doi:10.1038/s41698-024-00736-1. This article has 9 citations and is from a peer-reviewed journal.