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Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1016/0003-2697(89)90602-7openalex-snapshot
Calculation of protein extinction coefficients from amino acid sequence data
inferredcites →https://doi.org/10.1016/0003-9861(59)90090-6openalex-snapshot
Tissue sulfhydryl groups
inferredcites →https://doi.org/10.1016/0959-440x(95)80013-qopenalex-snapshot
The formation of protein disulphide bonds
inferredcites →https://doi.org/10.1016/j.bbamcr.2007.12.011openalex-snapshot
Ero1 and redox homeostasis in the endoplasmic reticulum
inferredcites →https://doi.org/10.1016/j.cell.2007.02.039openalex-snapshot
Modulation of Cellular Disulfide-Bond Formation and the ER Redox Environment by Feedback Regulation of Ero1
inferredcites →https://doi.org/10.1016/s0021-9258(20)64285-5openalex-snapshot
Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
inferredcites →https://doi.org/10.1016/s0092-8674(04)00418-0openalex-snapshot
Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
inferredcites →https://doi.org/10.1016/s1097-2765(00)80017-9openalex-snapshot
The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1016/s1097-2765(00)80018-0openalex-snapshot
Ero1p: A Novel and Ubiquitous Protein with an Essential Role in Oxidative Protein Folding in the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1021/bi00051a027openalex-snapshot
Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase
inferredcites →https://doi.org/10.1021/bi00077a018openalex-snapshot
Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
inferredcites →https://doi.org/10.1021/bi00444a023openalex-snapshot
Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction
inferredcites →https://doi.org/10.1038/11047openalex-snapshot
Competition between glutathione and protein thiols for disulphide-bond formation
inferredcites →https://doi.org/10.1038/emboj.2008.202openalex-snapshot
A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells
inferredcites →https://doi.org/10.1038/nrm954openalex-snapshot
Formation and transfer of disulphide bonds in living cells
inferredcites →https://doi.org/10.1038/sj.emboj.7601505openalex-snapshot
ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
inferredcites →https://doi.org/10.1038/sj.embor.7400311openalex-snapshot
The human protein disulphide isomerase family: substrate interactions and functional properties
inferredcites →https://doi.org/10.1038/sj.embor.7400645openalex-snapshot
The role of glutathione in disulphide bond formation and endoplasmic‐reticulum‐generated oxidative stress
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03590.xopenalex-snapshot
The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1‐Lα
inferredcites →https://doi.org/10.1073/pnas.0506448103openalex-snapshot
Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
inferredcites →https://doi.org/10.1074/jbc.275.7.4827openalex-snapshot
ERO1-L, a Human Protein That Favors Disulfide Bond Formation in the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1074/jbc.m003061200openalex-snapshot
Endoplasmic Reticulum Oxidoreductin 1-Lβ (ERO1-Lβ), a Human Gene Induced in the Course of the Unfolded Protein Response
inferredcites →https://doi.org/10.1074/jbc.m403192200openalex-snapshot
Two Conserved Cysteine Triads in Human Ero1α Cooperate for Efficient Disulfide Bond Formation in the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1074/jbc.m406912200openalex-snapshot
Glutathione Is Required to Regulate the Formation of Native Disulfide Bonds within Proteins Entering the Secretory Pathway
inferredcites →https://doi.org/10.1074/jbc.m409210200openalex-snapshot
The Contributions of Protein Disulfide Isomerase and Its Homologues to Oxidative Protein Folding in the Yeast Endoplasmic Reticulum
inferredcites →https://doi.org/10.1074/jbc.m411409200openalex-snapshot
Glutathione Directly Reduces an Oxidoreductase in the Endoplasmic Reticulum of Mammalian Cells
inferredcites →https://doi.org/10.1074/jbc.m505023200openalex-snapshot
Tissue-specific Expression and Dimerization of the Endoplasmic Reticulum Oxidoreductase Ero1β
inferredcites →https://doi.org/10.1074/jbc.m511764200openalex-snapshot
Domain Architecture of Protein-disulfide Isomerase Facilitates Its Dual Role as an Oxidase and an Isomerase in Ero1p-mediated Disulfide Formation
inferredcites →https://doi.org/10.1074/jbc.r600037200openalex-snapshot
Generating Disulfides in Multicellular Organisms: Emerging Roles for a New Flavoprotein Family
inferredcites →https://doi.org/10.1089/ars.2007.1837openalex-snapshot
In Vivo Reduction-Oxidation State of Protein Disulfide Isomerase: The Two Active Sites Independently Occur in the Reduced and Oxidized Forms
inferredcites →https://doi.org/10.1091/mbc.e05-05-0417openalex-snapshot
Disulfide Transfer between Two Conserved Cysteine Pairs Imparts Selectivity to Protein Oxidation by Ero1
inferredcites →https://doi.org/10.1093/emboj/19.17.4493openalex-snapshot
The CXXCXXC motif determines the folding, structure and stability of human Ero1‐Lα
inferredcites →https://doi.org/10.1093/emboj/20.22.6288openalex-snapshot
Manipulation of oxidative protein folding and PDI redox state in mammalian cells
inferredcites →https://doi.org/10.1126/science.1078376openalex-snapshot
Coordinated Nonvectorial Folding in a Newly Synthesized Multidomain Protein
inferredcites →https://doi.org/10.1126/science.290.5496.1571openalex-snapshot
Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.3869890openalex-extracted
Reductive Stress in the Endoplasmic Reticulum Caused by Ero1α S-Nitrosation Accelerates Senescence
inferred← citeshttps://doi.org/10.1002/9780470015902.a0024169openalex-snapshot
Structural Basis of Disulfide Bond Formation in the Bacterial Periplasm and Mammalian ER
inferred← citeshttps://doi.org/10.1002/pro.473openalex-snapshot
Steps in reductive activation of the disulfide‐generating enzyme Ero1p
inferred← citeshttps://doi.org/10.1007/s00441-016-2488-5openalex-snapshot
Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space
inferred← citeshttps://doi.org/10.1007/s00709-012-0463-xopenalex-snapshot
The oxidative protein folding machinery in plant cells
inferred← citeshttps://doi.org/10.1007/s11626-011-9461-0openalex-snapshot
Quiescin sulfhydryl oxidase (QSOX) is expressed in the human atheroma core: possible role in apoptosis
inferred← citeshttps://doi.org/10.1007/s12035-018-1028-6openalex-snapshot
The Endoplasmic Reticulum Stress Response in Neuroprogressive Diseases: Emerging Pathophysiological Role and Translational Implications
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.02.007openalex-snapshot
Forming disulfides in the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1016/j.bbamem.2010.06.003openalex-snapshot
Oxidation-driven protein import into mitochondria: Insights and blind spots
inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.02.004openalex-snapshot
Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation
inferred← citeshttps://doi.org/10.1016/j.bbrc.2009.09.045openalex-snapshot
Structure–function analysis of human protein Ero1-Lα
inferred← citeshttps://doi.org/10.1016/j.bcp.2009.12.009openalex-snapshot
Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells
inferred← citeshttps://doi.org/10.1016/j.cbpa.2021.110959openalex-snapshot
Suppressed expression of oxidoreductin-like protein, Oxidor, increases follicle degeneration and decreases survival during the overwintering diapause of the mosquito Culex pipiens
inferred← citeshttps://doi.org/10.1016/j.celrep.2023.112742openalex-snapshot
The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER
inferred← citeshttps://doi.org/10.1016/j.foodchem.2018.02.080openalex-snapshot
Characterization of wheat endoplasmic reticulum oxidoreductin 1 and its application in Chinese steamed bread
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2012.02.037openalex-snapshot
Protein disulfide isomerase in redox cell signaling and homeostasis
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2014.07.037openalex-snapshot
Oxidative protein folding: From thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.01.032openalex-snapshot
Composition of the redox environment of the endoplasmic reticulum and sources of hydrogen peroxide
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.02.007openalex-snapshot
Protein disulfide–isomerase, a folding catalyst and a redox-regulated chaperone
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.02.011openalex-snapshot
A PDI-catalyzed thiol–disulfide switch regulates the production of hydrogen peroxide by human Ero1
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.02.019openalex-snapshot
The antioxidant machinery of the endoplasmic reticulum: Protection and signaling
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.06.021openalex-snapshot
Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2022.01.006openalex-snapshot
ER reductive stress caused by Ero1α S-nitrosation accelerates senescence
inferred← citeshttps://doi.org/10.1016/j.isci.2024.111189openalex-snapshot
Development of luciferase-based highly sensitive reporters that detect ER-associated protein biogenesis abnormalities
inferred← citeshttps://doi.org/10.1016/j.jmb.2010.12.039openalex-snapshot
Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation
inferred← citeshttps://doi.org/10.1016/j.jtha.2024.03.008openalex-snapshot
Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis
inferred← citeshttps://doi.org/10.1016/j.molcel.2010.11.010openalex-snapshot
Oxidative Protein Folding by an Endoplasmic Reticulum-Localized Peroxiredoxin
inferred← citeshttps://doi.org/10.1016/j.redox.2015.11.004openalex-snapshot
Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover
inferred← citeshttps://doi.org/10.1016/j.redox.2018.11.005openalex-snapshot
Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
inferred← citeshttps://doi.org/10.1016/j.redox.2022.102244openalex-snapshot
The extracellular Ero1α/PDI electron transport system regulates platelet function by increasing glutathione reduction potential
inferred← citeshttps://doi.org/10.1016/j.redox.2026.104427openalex-snapshot
Targeting the Ero1α-PDI oxidative protein folding pathway as a broad-spectrum strategy against coronavirus
inferred← citeshttps://doi.org/10.1016/j.tibs.2011.05.004openalex-snapshot
Multiple ways to make disulfides
inferred← citeshttps://doi.org/10.1016/j.tibs.2022.06.011openalex-snapshot
Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00527openalex-snapshot
Endoplasmic Reticulum Redoxome: Protein Folding and Beyond
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00123openalex-snapshot
Chemistry and Enzymology of Disulfide Cross-Linking in Proteins
inferred← citeshttps://doi.org/10.1021/acs.jafc.6b05192openalex-snapshot
Recombinant Wheat Endoplasmic Reticulum Oxidoreductin 1 Improved Wheat Dough Properties and Bread Quality
inferred← citeshttps://doi.org/10.1021/bi400052uopenalex-snapshot
Increased Redox-Sensitive Green Fluorescent Protein Reduction Potential in the Endoplasmic Reticulum following Glutathione-Mediated Dimerization
inferred← citeshttps://doi.org/10.1021/bi900241kopenalex-snapshot
Enzyme Activity of Phosphatase of Regenerating Liver Is Controlled by the Redox Environment and Its C-Terminal Residues
inferred← citeshttps://doi.org/10.1021/bi902222sopenalex-snapshot
Quiescin Sulfhydryl Oxidase from Trypanosoma brucei: Catalytic Activity and Mechanism of a QSOX Family Member with a Single Thioredoxin Domain
inferred← citeshttps://doi.org/10.1038/emboj.2008.293openalex-snapshot
A non‐catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway
inferred← citeshttps://doi.org/10.1038/emboj.2010.203openalex-snapshot
Disulphide production by Ero1α–PDI relay is rapid and effectively regulated
inferred← citeshttps://doi.org/10.1038/emboj.2010.222openalex-snapshot
Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI
inferred← citeshttps://doi.org/10.1038/emboj.2010.273openalex-snapshot
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1038/s41467-023-39078-0openalex-snapshot
FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions
inferred← citeshttps://doi.org/10.1038/s41598-021-87944-yopenalex-snapshot
Homeostasis of the ER redox state subsequent to proteasome inhibition
inferred← citeshttps://doi.org/10.1038/s41598-023-41375-zopenalex-snapshot
Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast
inferred← citeshttps://doi.org/10.1038/srep02456openalex-snapshot
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
inferred← citeshttps://doi.org/10.1042/bj20091878openalex-snapshot
Disulfide formation in plant storage vacuoles permits assembly of a multimeric lectin
inferred← citeshttps://doi.org/10.1042/bj20101357openalex-snapshot
The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation
inferred← citeshttps://doi.org/10.1042/bj20130360openalex-snapshot
Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst
inferred← citeshttps://doi.org/10.1042/bj20140234openalex-snapshot
Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases
inferred← citeshttps://doi.org/10.1042/bj20141423openalex-snapshot
Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme
inferred← citeshttps://doi.org/10.1042/bsr20130124openalex-snapshot
Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262
inferred← citeshttps://doi.org/10.1042/bst20130168openalex-snapshot
Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV
inferred← citeshttps://doi.org/10.1073/pnas.1618985114openalex-snapshot
Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase
inferred← citeshttps://doi.org/10.1074/jbc.m109.021113openalex-snapshot
Deciphering Structural and Functional Roles of Individual Disulfide Bonds of the Mitochondrial Sulfhydryl Oxidase Erv1p
inferred← citeshttps://doi.org/10.1074/jbc.m110.156596openalex-snapshot
The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α
inferred← citeshttps://doi.org/10.1074/jbc.m111.227181openalex-snapshot
Functional in Vitro Analysis of the ERO1 Protein and Protein-disulfide Isomerase Pathway
inferred← citeshttps://doi.org/10.1074/jbc.m111.231357openalex-snapshot
Molecular Bases of Cyclic and Specific Disulfide Interchange between Human ERO1α Protein and Protein-disulfide Isomerase (PDI)
inferred← citeshttps://doi.org/10.1074/jbc.m111.298810openalex-snapshot
Crystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic Cycle
inferred← citeshttps://doi.org/10.1074/jbc.m112.405050openalex-snapshot
Hyperactivity of the Ero1α Oxidase Elicits Endoplasmic Reticulum Stress but No Broad Antioxidant Response
inferred← citeshttps://doi.org/10.1074/jbc.m113.510065openalex-snapshot
Endoplasmic Reticulum Oxidoreductin-1α (Ero1α) Improves Folding and Secretion of Mutant Proinsulin and Limits Mutant Proinsulin-induced Endoplasmic Reticulum Stress
inferred← citeshttps://doi.org/10.1074/jbc.m113.529305openalex-snapshot
Lack of an Efficient Endoplasmic Reticulum-localized Recycling System Protects Peroxiredoxin IV from Hyperoxidation
inferred← citeshttps://doi.org/10.1074/jbc.m114.602961openalex-snapshot
Different Interaction Modes for Protein-disulfide Isomerase (PDI) as an Efficient Regulator and a Specific Substrate of Endoplasmic Reticulum Oxidoreductin-1α (Ero1α)
inferred← citeshttps://doi.org/10.1074/jbc.m115.694257openalex-snapshot
Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1
inferred← citeshttps://doi.org/10.1074/jbc.m115.694810openalex-snapshot
Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative Stress
inferred← citeshttps://doi.org/10.1074/jbc.m116.735662openalex-snapshot
Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase
inferred← citeshttps://doi.org/10.1074/jbc.ra119.010917openalex-snapshot
Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding
inferred← citeshttps://doi.org/10.1074/jbc.ra119.011766openalex-snapshot
Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)–protein disulfide-isomerase relay when protein folding capacity is exceeded
inferred← citeshttps://doi.org/10.1074/mcp.m800580-mcp200openalex-snapshot
Elucidation of Thioredoxin Target Protein Networks in Mouse
inferred← citeshttps://doi.org/10.1080/21624054.2016.1170273openalex-snapshot
Interplay between redox and protein homeostasis
inferred← citeshttps://doi.org/10.1083/jcb.200911086openalex-snapshot
ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
inferred← citeshttps://doi.org/10.1083/jcb.201110090openalex-snapshot
Balanced Ero1 activation and inactivation establishes ER redox homeostasis
inferred← citeshttps://doi.org/10.1083/jcb.201211155openalex-snapshot
Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox
inferred← citeshttps://doi.org/10.1083/jcb.201303027openalex-snapshot
Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases
inferred← citeshttps://doi.org/10.1089/ars.2008.2326openalex-snapshot
Efficient Peroxide-Mediated Oxidative Refolding of a Protein at Physiological pH and Implications for Oxidative Folding in the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1089/ars.2009.2466openalex-snapshot
Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation
inferred← citeshttps://doi.org/10.1089/ars.2009.2529openalex-snapshot
Redox Control of Endoplasmic Reticulum Function
inferred← citeshttps://doi.org/10.1089/ars.2010.3098openalex-snapshot
Oxidative Protein Folding and the Quiescin–Sulfhydryl Oxidase Family of Flavoproteins
inferred← citeshttps://doi.org/10.1089/ars.2010.3157openalex-snapshot
Oxidative Protein Folding in the Mitochondrial Intermembrane Space
inferred← citeshttps://doi.org/10.1089/ars.2010.3230openalex-snapshot
Molecular Mechanisms Regulating Oxidative Activity of the Ero1 Family in the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1089/ars.2010.3575openalex-snapshot
How Proteins Form Disulfide Bonds
inferred← citeshttps://doi.org/10.1089/ars.2011.4418openalex-snapshot
Structure, Mechanism, and Evolution of Ero1 Family Enzymes
inferred← citeshttps://doi.org/10.1089/ars.2011.4475openalex-snapshot
The Physiological Functions of Mammalian Endoplasmic Oxidoreductin 1: On Disulfides and More
inferred← citeshttps://doi.org/10.1089/ars.2011.4481openalex-snapshot
Low-Molecular-Weight Oxidants Involved in Disulfide Bond Formation
inferred← citeshttps://doi.org/10.1089/ars.2012.4651openalex-snapshot
Expression of the Endoplasmic Reticulum Oxidoreductase Ero1α in Gastro-Intestinal Cancer Reveals a Link Between Homocysteine and Oxidative Protein Folding
inferred← citeshttps://doi.org/10.1089/ars.2013.5236openalex-snapshot
Glutathione Peroxidase 7 Utilizes Hydrogen Peroxide Generated by Ero1α to Promote Oxidative Protein Folding
inferred← citeshttps://doi.org/10.1089/ars.2014.5841openalex-snapshot
Three Approaches to One Problem: Protein Folding in the Periplasm, the Endoplasmic Reticulum, and the Intermembrane Space
inferred← citeshttps://doi.org/10.1089/ars.2014.5849openalex-snapshot
The Thioredoxin Superfamily in Oxidative Protein Folding
inferred← citeshttps://doi.org/10.1089/ars.2017.7148openalex-snapshot
Reexamining the Function of Glutathione in Oxidative Protein Folding and Secretion
inferred← citeshttps://doi.org/10.1089/ars.2018.7615openalex-snapshot
Quantitative Analyses of the Yeast Oxidative Protein Folding Pathway In Vitro and In Vivo
inferred← citeshttps://doi.org/10.1089/ars.2021.0018openalex-snapshot
ERO1-PDI Redox Signaling in Health and Disease
inferred← citeshttps://doi.org/10.1091/mbc.e12-02-0102openalex-snapshot
Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1091/mbc.e14-10-1422openalex-snapshot
Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space
inferred← citeshttps://doi.org/10.1093/plcell/koac202openalex-snapshot
Endoplasmic reticulum oxidoreductin provides resilience against reductive stress and hypoxic conditions by mediating luminal redox dynamics
inferred← citeshttps://doi.org/10.1093/plphys/kiab457openalex-snapshot
Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding
inferred← citeshttps://doi.org/10.1098/rstb.2011.0403openalex-snapshot
Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
inferred← citeshttps://doi.org/10.1101/cshperspect.a013219openalex-snapshot
Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1101/cshperspect.a033910openalex-snapshot
Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis
inferred← citeshttps://doi.org/10.1104/pp.19.00020openalex-snapshot
AtERO1 and AtERO2 Exhibit Differences in Catalyzing Oxidative Protein Folding in the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1111/j.1365-2443.2010.01434.xopenalex-snapshot
MBSJ MCC Young Scientist Award 2009 REVIEW: Structural basis of protein disulfide bond generation in the cell
inferred← citeshttps://doi.org/10.1111/j.1600-0854.2010.01108.xopenalex-snapshot
Oxidative Protein Folding in the Secretory Pathway and Redox Signaling Across Compartments and Cells
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2012.08593.xopenalex-snapshot
Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
inferred← citeshttps://doi.org/10.1126/science.1170653openalex-snapshot
Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process
inferred← citeshttps://doi.org/10.1128/mbio.00237-10openalex-snapshot
Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
inferred← citeshttps://doi.org/10.1139/bcb-2018-0189openalex-snapshot
Glutathione: subcellular distribution and membrane transport
inferred← citeshttps://doi.org/10.1161/circresaha.121.320531openalex-snapshot
Ero1α-Dependent ERp44 Dissociation From RyR2 Contributes to Cardiac Arrhythmia
inferred← citeshttps://doi.org/10.1186/1475-2859-10-1openalex-snapshot
Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli
inferred← citeshttps://doi.org/10.1186/s12917-017-1125-1openalex-snapshot
Identification, characterization and purification of porcine Quiescin Q6-Sulfydryl Oxidase 2 protein
inferred← citeshttps://doi.org/10.1186/s13046-024-02990-4openalex-snapshot
Biological mechanisms and clinical significance of endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) in human cancer
inferred← citeshttps://doi.org/10.1242/jcs.059154openalex-snapshot
Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
inferred← citeshttps://doi.org/10.1242/jcs.067843openalex-snapshot
Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation
inferred← citeshttps://doi.org/10.1242/jcs.080895openalex-snapshot
Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1242/jcs.085530openalex-snapshot
Real-time monitoring of redox changes in the mammalian endoplasmic reticulum
inferred← citeshttps://doi.org/10.1242/jcs.240366openalex-snapshot
The pivotal role of ERp44 in patrolling protein secretion
inferred← citeshttps://doi.org/10.1242/jcs.241976openalex-snapshot
The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins
inferred← citeshttps://doi.org/10.1515/hsz-2017-0124openalex-snapshot
Oxidised protein metabolism: recent insights
inferred← citeshttps://doi.org/10.15252/embj.201798699openalex-snapshot
Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α
inferred← citeshttps://doi.org/10.2147/ijn.s75768openalex-snapshot
Oxidative stress and antibacterial properties of a graphene oxide-cystamine nanohybrid
inferred← citeshttps://doi.org/10.26508/lsa.201800090openalex-snapshot
Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding
inferred← citeshttps://doi.org/10.3389/fmolb.2018.00018openalex-snapshot
Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation
inferred← citeshttps://doi.org/10.3390/cells9102314openalex-snapshot
Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.3390/ijms161125977openalex-snapshot
Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori
inferred← citeshttps://doi.org/10.3390/ijms19041219openalex-snapshot
Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology
inferred← citeshttps://doi.org/10.3390/molecules26010171openalex-snapshot
PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
inferred← citeshttps://doi.org/10.3390/molecules27123679openalex-snapshot
The Potential of a Protein Model Synthesized Absent of Methionine
inferred← citeshttps://doi.org/10.3897/phytokeys.70.9053openalex-snapshot
Molecular and morphological evidence for recognition of two species within Harpagonella (Amsinckiinae, Boraginaceae)
inferred← citeshttps://doi.org/10.4049/jimmunol.1303228openalex-snapshot
Cancer-Associated Oxidase ERO1-α Regulates the Expression of MHC Class I Molecule via Oxidative Folding
inferred← citeshttps://doi.org/10.70675/7803cd97zf73cz4061zac78zcd7850387e79openalex-snapshot
Analyse fonctionnelle de protéines métal- ou redox- dépendantes chez les plantes
inferred← citeshttps://doi.org/10.70675/8d12e3efz7530z4798z9984zeef7316b50afopenalex-snapshot
Les glutathion peroxydases et protéine disulfure isomérases de peuplier : potentialités du repliement thiorédoxine pour la catalyse des réactions redox
inferred← citeshttps://doi.org/10.7554/elife.03421openalex-snapshot
Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants
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