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Disulfide Bonds Are Generated by Quinone Reduction

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06471.xopenalex-snapshot

The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.

inferredcites →https://doi.org/10.1002/j.1460-2075.1995.tb07347.xopenalex-snapshot

Identification and characterization of a new disulfide isomerase‐like protein (DsbD) in Escherichia coli.

inferredcites →https://doi.org/10.1016/0005-2728(77)90071-8openalex-snapshot

Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA− menA− double quinone mutant

inferredcites →https://doi.org/10.1016/0076-6879(67)10071-2openalex-snapshot

[68] Isolation and determination of ubiquinone

inferredcites →https://doi.org/10.1016/0092-8674(91)90532-4openalex-snapshot

Identification of a protein required for disulfide bond formation in vivo

inferredcites →https://doi.org/10.1016/0092-8674(95)90210-4openalex-snapshot

Why is DsbA such an oxidizing disulfide catalyst?

inferredcites →https://doi.org/10.1016/0968-0004(94)90072-8openalex-snapshot

Protein disulphide isomerase: building bridges in protein folding

inferredcites →https://doi.org/10.1016/s0021-9258(18)41691-2openalex-snapshot

In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.

inferredcites →https://doi.org/10.1016/s0021-9258(20)65115-8openalex-snapshot

Specific interaction between protein and ubiquinone in succinate-ubiquinone reductase.

inferredcites →https://doi.org/10.1016/s0076-6879(83)91010-8openalex-snapshot

[8] Reassessment of Ellman's reagent

inferredcites →https://doi.org/10.1016/s0092-8674(00)81016-8openalex-snapshot

Oxidative Protein Folding Is Driven by the Electron Transport System

inferredcites →https://doi.org/10.1016/s0092-8674(00)81642-6openalex-snapshot

Electron Avenue

inferredcites →https://doi.org/10.1016/s0969-2126(98)00077-xopenalex-snapshot

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

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/10.1016/s1097-2765(00)80198-7openalex-snapshot

Ero1p Oxidizes Protein Disulfide Isomerase in a Pathway for Disulfide Bond Formation in the Endoplasmic Reticulum

inferredcites →https://doi.org/10.1021/bi00015a019openalex-snapshot

Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli

inferredcites →https://doi.org/10.1021/bi00070a016openalex-snapshot

The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo

inferredcites →https://doi.org/10.1021/bi00217a004openalex-snapshot

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

inferredcites →https://doi.org/10.1021/bi960335mopenalex-snapshot

Structure Determination of the N-Terminal Thioredoxin-like Domain of Protein Disulfide Isomerase Using Multidimensional Heteronuclear 13C/15N NMR Spectroscopy

inferredcites →https://doi.org/10.1021/bi971888fopenalex-snapshot

Contributions of Substrate Binding to the Catalytic Activity of DsbC

inferredcites →https://doi.org/10.1038/365464a0openalex-snapshot

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

inferredcites →https://doi.org/10.1038/43344openalex-snapshot

Where do the electrons go?

inferredcites →https://doi.org/10.1038/73295openalex-snapshot

Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.

inferredcites →https://doi.org/10.1046/j.1365-2958.1997.5581925.xopenalex-snapshot

A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins

inferredcites →https://doi.org/10.1073/pnas.90.3.1038openalex-snapshot

A pathway for disulfide bond formation in vivo.

inferredcites →https://doi.org/10.1073/pnas.93.23.13048openalex-snapshot

An in vivo pathway for disulfide bond isomerization in Escherichia coli

inferredcites →https://doi.org/10.1073/pnas.94.22.11857openalex-snapshot

Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

inferredcites →https://doi.org/10.1074/jbc.273.17.10302openalex-snapshot

Reconstitution of a Protein Disulfide Catalytic System

inferredcites →https://doi.org/10.1074/jbc.274.12.7784openalex-snapshot

In Vivo and in Vitro Function of theEscherichia coli Periplasmic Cysteine Oxidoreductase DsbG

inferredcites →https://doi.org/10.1074/jbc.274.13.8717openalex-snapshot

Identification of Quinone-binding and Heme-ligating Residues of the Smallest Membrane-anchoring Subunit (QPs3) of Bovine Heart Mitochondrial Succinate:Ubiquinone Reductase

inferredcites →https://doi.org/10.1074/jbc.275.18.13349openalex-snapshot

DsbG, a Protein Disulfide Isomerase with Chaperone Activity

inferredcites →https://doi.org/10.1093/emboj/18.12.3271openalex-snapshot

Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm

inferredcites →https://doi.org/10.1093/emboj/18.21.5963openalex-snapshot

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli

inferredcites →https://doi.org/10.1093/emboj/18.5.1192openalex-snapshot

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway

inferredcites →https://doi.org/10.1128/jb.179.21.6602-6608.1997openalex-snapshot

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin

inferredcites →https://doi.org/10.1146/annurev.genet.32.1.163openalex-snapshot

THE GENETICS OF DISULFIDE BOND METABOLISM

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Roles of methionine and cysteine residues of the Escherichia coli sensor kinase HprS in reactive chlorine species sensing

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Disulfide Bond Formation in Prokaryotes

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The Catalysis of Disulfide Bond Formation in Prokaryotes

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Selective Dealkylation of Alkyl Aryl Ethers

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Key Players Involved in Bacterial Disulfide‐Bond Formation

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Crystallization and Initial Crystallographic Analysis of the Disulfide Bond Isomerase DsbC in Complex with the α Domain of the Electron Transporter DsbD

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Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?

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NMR-Spectroscopic Investigation of Disulfide Dynamics in Unfolded States of Proteins

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A Half-Century of Oxidative Folding and Protein Disulphide Formation

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The Problem of Expression of Multidisulfide Bonded Recombinant Proteins in E. coli

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The Production of Coenzyme Q10 in Microorganisms

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Expression and Fermentation Strategies for Recombinant Protein Production in Escherichia Coli

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nDsbD: a redox interaction hub in the Escherichia coli periplasm

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Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology

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Enhancement of NADPH availability for coproduction of coenzyme Q10 and farnesol from Rhodobacter sphaeroides

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Human Coenzyme Q10 Deficiency

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CoQ10 a super-vitamin: review on application and biosynthesis

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Disulfide bond formation in Escherichia coli

inferred← citeshttps://doi.org/10.1016/b978-012200731-6.50009-4openalex-snapshot

Disulfide Bond Formation in Prokaryotes and Eukaryotes

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The role of UbiX in Escherichia coli coenzyme Q biosynthesis

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The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited

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Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm

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Disulfide bond isomerization in prokaryotes

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Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation

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Enhanced production of CoQ10 by constitutive overexpression of 3-demethyl ubiquinone-9 3-methyltransferase under tac promoter in Rhodobacter sphaeroides

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Pathways of disulfide bond formation in Escherichia coli

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Application of Fragment-Based Drug Discovery to Membrane Proteins: Identification of Ligands of the Integral Membrane Enzyme DsbB

inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.12.001openalex-snapshot

A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone

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Preparation and structure of the charge‐transfer intermediate of the transmembrane redox catalyst DsbB

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Structural and functional characterization of Helicobacter pylori DsbG

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Reducing systems protecting the bacterial cell envelope from oxidative damage

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Antioxidant efficiency and mechanisms of green tea, rosemary or maté extracts in porcine Longissimus dorsi subjected to iron-induced oxidative stress

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Reaction of quinones with proteins: Kinetics of adduct formation, effects on enzymatic activity and protein structure, and potential reversibility of modifications

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High-resolution Structures of Escherichia coli cDsbD in Different Redox States: A Combined Crystallographic, Biochemical and Computational Study

inferred← citeshttps://doi.org/10.1016/j.jmb.2008.05.050openalex-snapshot

Thermodynamic Aspects of DsbD-Mediated Electron Transport

inferred← citeshttps://doi.org/10.1016/j.jmb.2008.07.061openalex-snapshot

Evidence for Proton Shuffling in a Thioredoxin-Like Protein during Catalysis

inferred← citeshttps://doi.org/10.1016/j.jmb.2013.02.009openalex-snapshot

Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer

inferred← citeshttps://doi.org/10.1016/j.jmb.2013.04.034openalex-snapshot

Topological Plasticity of Enzymes Involved in Disulfide Bond Formation Allows Catalysis in Either the Periplasm Or the Cytoplasm

inferred← citeshttps://doi.org/10.1016/j.jmb.2019.05.049openalex-snapshot

The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features

inferred← citeshttps://doi.org/10.1016/j.jmb.2020.04.008openalex-snapshot

Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA

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Cellular redox poise modulation; the role of coenzyme Q10, gene and metabolic regulation

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NMR Solution Structure of the Integral Membrane Enzyme DsbB: Functional Insights into DsbB-Catalyzed Disulfide Bond Formation

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Similarities and differences in the thioredoxin superfamily

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New convenient synthesis of iridol. An approach to the synthesis of ubiquinones

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Current prospects for the production of coenzyme Q10 in microbes

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Identification of bottlenecks in Escherichia coli engineered for the production of CoQ10

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Catalysis of disulfide bond formation and isomerization in Escherichia coli

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The FAD- and O2-Dependent Reaction Cycle of Ero1-Mediated Oxidative Protein Folding in the Endoplasmic Reticulum

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ArcB: El sensor del estado redox en bacterias

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Disulfide Bond Formation Enzymes

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Catalytic Antioxidant Activity of Two Diterpenoid Polyphenols of Rosemary, Carnosol, and Isorosmanol, against Lipid Oxidation in the Presence of Cysteine Thiol

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Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli

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Disulfide Bond Isomerization in Prokaryotes

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Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB

inferred← citeshttps://doi.org/10.1038/nrm954openalex-snapshot

Formation and transfer of disulphide bonds in living cells

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Disulfides out of thin air

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Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

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Disulfide bond formation in prokaryotes

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Structure formation during translocon-unassisted co-translational membrane protein folding

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Structural basis and kinetics of inter‐ and intramolecular disulfide exchange in the redox catalyst DsbD

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Disulfide-bond Formation and Isomerization in Prokaryotes

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Integration of heterologous 4-hydroxybenzoic acid transport proteins in Rhodobacter sphaeroides for enhancement of coenzyme Q 10 production

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Isolation and functional expression of human COQ2 , a gene encoding a polyprenyl transferase involved in the synthesis of CoQ

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Identification of a segment of DsbB essential for its respiration‐coupled oxidation

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Oxidative protein folding in bacteria

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The N‐terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre

inferred← citeshttps://doi.org/10.1073/pnas.0403003101openalex-snapshot

Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli : Reconciling two competing pathways

inferred← citeshttps://doi.org/10.1073/pnas.0507570103openalex-snapshot

Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB

inferred← citeshttps://doi.org/10.1073/pnas.171315498openalex-snapshot

DsbC activation by the N-terminal domain of DsbD

inferred← citeshttps://doi.org/10.1073/pnas.1935988100openalex-snapshot

Disulfide bond formation involves a quinhydrone-type charge–transfer complex

inferred← citeshttps://doi.org/10.1073/pnas.2610764123openalex-snapshot

Giant viruses encode vitamin K–based redox modules for lipid modification

inferred← citeshttps://doi.org/10.1073/pnas.97.20.10884openalex-snapshot

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

inferred← citeshttps://doi.org/10.1074/jbc.m108697200openalex-snapshot

Identification of the Ubiquinone-binding Domain in the Disulfide Catalyst Disulfide Bond Protein B

inferred← citeshttps://doi.org/10.1074/jbc.m112222200openalex-snapshot

Uptake of Exogenous Coenzyme Q and Transport to Mitochondria Is Required for bc1 Complex Stability in Yeast coq Mutants

inferred← citeshttps://doi.org/10.1074/jbc.m113.487082openalex-snapshot

Plasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate Reductase

inferred← citeshttps://doi.org/10.1074/jbc.m116.770891openalex-snapshot

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions

inferred← citeshttps://doi.org/10.1074/jbc.m201158200openalex-snapshot

Thiol-Disulfide Oxidoreductases Are Essential for the Production of the Lantibiotic Sublancin 168

inferred← citeshttps://doi.org/10.1074/jbc.m205433200openalex-snapshot

DsbB Catalyzes Disulfide Bond Formation de Novo

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The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli

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DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation

inferred← citeshttps://doi.org/10.1074/jbc.m311391200openalex-snapshot

In Vivo Substrate Specificity of Periplasmic Disulfide Oxidoreductases

inferred← citeshttps://doi.org/10.1074/jbc.m402760200openalex-snapshot

Two Periplasmic Disulfide Oxidoreductases, DsbA and SrgA, Target Outer Membrane Protein SpiA, a Component of the Salmonella Pathogenicity Island 2 Type III Secretion System

inferred← citeshttps://doi.org/10.1074/jbc.m407153200openalex-snapshot

Characterization of the Menaquinone-dependent Disulfide Bond Formation Pathway of Escherichia coli

inferred← citeshttps://doi.org/10.1074/jbc.m505742200openalex-snapshot

Copper Stress Causes an in Vivo Requirement for the Escherichia coli Disulfide Isomerase DsbC

inferred← citeshttps://doi.org/10.1074/jbc.m506189200openalex-snapshot

Reactivities of Quinone-free DsbB from Escherichia coli

inferred← citeshttps://doi.org/10.1074/jbc.m509687200openalex-snapshot

Identification of a Ubiquinone-binding Site That Affects Autophosphorylation of the Sensor Kinase RegB

inferred← citeshttps://doi.org/10.1074/jbc.m611541200openalex-snapshot

Kinetic Characterization of the Disulfide Bond-forming Enzyme DsbB

inferred← citeshttps://doi.org/10.1074/jbc.m707838200openalex-snapshot

Staphylococcus aureus DsbA Does Not Have a Destabilizing Disulfide

inferred← citeshttps://doi.org/10.1074/jbc.m804938200openalex-snapshot

Menaquinone as Well as Ubiquinone as a Bound Quinone Crucial for Catalytic Activity and Intramolecular Electron Transfer in Escherichia coli Membrane-bound Glucose Dehydrogenase

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Structural investigation of vitamin K epoxide reductase domain-containing protein in Leptospira species: a potential target for the development of new leptospirosis treatments as an alternative to antibiotics

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Mini-review: The role of redox in Dopa-mediated marine adhesion

inferred← citeshttps://doi.org/10.1080/1040841x.2019.1622509openalex-snapshot

Engineering of the Dsb (disulfide bond) proteins – contribution towards understanding their mechanism of action and their applications in biotechnology and medicine

inferred← citeshttps://doi.org/10.1083/jcb.200311055openalex-snapshot

Oxidative protein folding in eukaryotes

inferred← citeshttps://doi.org/10.1083/jcb.200707123openalex-snapshot

The disulfide relay system of mitochondria is connected to the respiratory chain

inferred← citeshttps://doi.org/10.1089/152308603768295087openalex-snapshot

The Influence of His94 and Pro149 in Modulating the Activity of V. cholerae DsbA

inferred← citeshttps://doi.org/10.1089/152308603768295131openalex-snapshot

Genomics Perspective on Disulfide Bond Formation

inferred← citeshttps://doi.org/10.1089/152308603768295140openalex-snapshot

Functions of Thiol-Disulfide Oxidoreductases in E. coli : Redox Myths, Realities, and Practicalities

inferred← citeshttps://doi.org/10.1089/ars.2006.8.743openalex-snapshot

Role of the Cytosolic Loop of DsbB in Catalytic Turnover of the Ubiquinone–DsbB Complex

inferred← citeshttps://doi.org/10.1089/ars.2006.8.797openalex-snapshot

Conservation and Diversity of the Cellular Disulfide Bond Formation Pathways

inferred← citeshttps://doi.org/10.1089/ars.2008.2420openalex-snapshot

Structural and Functional Characterization of the Oxidoreductase α-DsbA1 from Wolbachia pipientis

inferred← citeshttps://doi.org/10.1089/ars.2010.3344openalex-snapshot

Structure and Function of DsbA, a Key Bacterial Oxidative Folding Catalyst

inferred← citeshttps://doi.org/10.1089/ars.2010.3575openalex-snapshot

How Proteins Form Disulfide Bonds

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/10.1093/emboj/20.7.1555openalex-snapshot

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA

inferred← citeshttps://doi.org/10.1093/emboj/21.10.2354openalex-snapshot

Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA

inferred← citeshttps://doi.org/10.1093/emboj/21.11.2646openalex-snapshot

Paradoxical redox properties of DsbB and DsbA in the protein disulfide‐introducing reaction cascade

inferred← citeshttps://doi.org/10.1093/emboj/cdf489openalex-snapshot

The disulfide bond isomerase DsbC is activated by an immunoglobulin‐fold thiol oxidoreductase: crystal structure of the DsbC–DsbDα complex

inferred← citeshttps://doi.org/10.1093/emboj/cdg356openalex-snapshot

Mechanism of the electron transfer catalyst DsbB from Escherichia coli

inferred← citeshttps://doi.org/10.1099/mic.0.001603openalex-snapshot

Disulphide bond-forming enzymes in clostridial species

inferred← citeshttps://doi.org/10.1101/2025.06.06.658356openalex-snapshot

Student-led experimental evolution reveals novel biofilm regulators of adaptation to multiple niches

inferred← citeshttps://doi.org/10.1107/s0907444912026388openalex-snapshot

The 1.2 Å resolution crystal structure of TcpG, theVibrio choleraeDsbA disulfide-forming protein required for pilus and cholera-toxin production

inferred← citeshttps://doi.org/10.1107/s0907444913017800openalex-snapshot

Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases

inferred← citeshttps://doi.org/10.1110/ps.051355705openalex-snapshot

The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases

inferred← citeshttps://doi.org/10.1110/ps.062268106openalex-snapshot

The origami of thioredoxin‐like folds

inferred← citeshttps://doi.org/10.1111/febs.70272openalex-snapshot

Heterologous plastoquinone production using a newly identified O 2 ‐dependent cyanobacterial hydroxylase

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/mmi.12192openalex-snapshot

Novel regulatory system nemRA – gloA for electrophile reduction in E scherichia coli K ‐12

inferred← citeshttps://doi.org/10.1126/sciadv.abe3717openalex-snapshot

Termini restraining of small membrane proteins enables structure determination at near-atomic resolution

inferred← citeshttps://doi.org/10.1128/9781555815806.ch7openalex-snapshot

Disulfide Bond Formation in the Periplasm

inferred← citeshttps://doi.org/10.1128/aem.02499-25openalex-snapshot

Genetic diversification of Pseudomonas fluorescens maintained by multi-niche selection within biofilms

inferred← citeshttps://doi.org/10.1128/iai.00938-17openalex-snapshot

Virulence of the Melioidosis Pathogen Burkholderia pseudomallei Requires the Oxidoreductase Membrane Protein DsbB

inferred← citeshttps://doi.org/10.1128/iai.71.7.3960-3970.2003openalex-snapshot

Identification ofActinobacillus pleuropneumoniaeGenes Important for Survival during Infection in Its Natural Host

inferred← citeshttps://doi.org/10.1128/jb.00120-17openalex-snapshot

The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli

inferred← citeshttps://doi.org/10.1128/jb.01080-06openalex-snapshot

The Thiol:Disulfide Oxidoreductase DsbB Mediates the Oxidizing Effects of the Toxic Metalloid Tellurite (TeO32−) on the Plasma Membrane Redox System of the Facultative PhototrophRhodobacter capsulatus

inferred← citeshttps://doi.org/10.1128/jb.01205-06openalex-snapshot

Cys303 in the Histidine Kinase PhoR Is Crucial for the Phosphotransfer Reaction in the PhoPR Two-Component System in Bacillus subtilis

inferred← citeshttps://doi.org/10.1128/jb.186.1.68-79.2004openalex-snapshot

RtsA Coordinately Regulates DsbA and theSalmonellaPathogenicity Island 1 Type III Secretion System

inferred← citeshttps://doi.org/10.1128/jb.187.4.1504-1510.2005openalex-snapshot

Mutational Analysis of the Disulfide Catalysts DsbA and DsbB

inferred← citeshttps://doi.org/10.1128/mbio.00272-10openalex-snapshot

RegB Kinase Activity Is Controlled in Part by Monitoring the Ratio of Oxidized to Reduced Ubiquinones in the Ubiquinone Pool

inferred← citeshttps://doi.org/10.1128/mbio.00912-13openalex-snapshot

Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa

inferred← citeshttps://doi.org/10.1139/w01-071openalex-snapshot

Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium

inferred← citeshttps://doi.org/10.1146/annurev.biochem.72.121801.161459openalex-snapshot

Protein Disulfide Bond Formation in Prokaryotes

inferred← citeshttps://doi.org/10.1146/annurev.cellbio.24.110707.175333openalex-snapshot

Disulfide-Linked Protein Folding Pathways

inferred← citeshttps://doi.org/10.1146/annurev.micro.55.1.21openalex-snapshot

Roles of Thiol-Redox Pathways in Bacteria

inferred← citeshttps://doi.org/10.1186/s12896-020-00615-0openalex-snapshot

Translational regulation of periplasmic folding assistants and proteases as a valuable strategy to improve production of translocated recombinant proteins in Escherichia coli

inferred← citeshttps://doi.org/10.1186/s12934-019-1145-6openalex-snapshot

Co-production of farnesol and coenzyme Q10 from metabolically engineered Rhodobacter sphaeroides

inferred← citeshttps://doi.org/10.1186/s12934-019-1175-0openalex-snapshot

Four thiol-oxidoreductases involved in the formation of disulphide bonds in the Streptomyces lividans TK21 secretory proteins

inferred← citeshttps://doi.org/10.1186/s12934-021-01689-xopenalex-snapshot

Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria

inferred← citeshttps://doi.org/10.1196/annals.1354.008openalex-snapshot

Cellular Redox Regulation and Prooxidant Signaling Systems

inferred← citeshttps://doi.org/10.1371/journal.pone.0081440openalex-snapshot

The α-Proteobacteria Wolbachia pipientis Protein Disulfide Machinery Has a Regulatory Mechanism Absent in γ-Proteobacteria

inferred← citeshttps://doi.org/10.1371/journal.pone.0222595openalex-snapshot

Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development

inferred← citeshttps://doi.org/10.17577/ijertv9is070161openalex-snapshot

Oxidative Protein Folding in Eukaryotes: Consequences and Mechanisms

inferred← citeshttps://doi.org/10.19026/ajfst.5.3080openalex-snapshot

Culture Conditions Affect the Category and Production of Ubiquinones in a Recombinant Escherichia Coli with an Exogenous Decaprenyl Diphosphate Synthase

inferred← citeshttps://doi.org/10.19026/ajfst.5.3156openalex-snapshot

Culture Conditions affect the Category and Production of Ubiquinones in a Recombinant Escherichia Coli with an Exogenous Decaprenyl Diphosphate Synthase

inferred← citeshttps://doi.org/10.3389/fbioe.2022.961776openalex-snapshot

Study of key amino acid residues of GH66 dextranase for producing high-degree polymerized isomaltooligosaccharides and improving of thermostability

inferred← citeshttps://doi.org/10.3390/met12091523openalex-snapshot

Metallic Porphyrazine Networks: Synthesis, as Well as Thermal and Optical Properties for Accelerating the Oxidation of Thiols to Their Disulfides

inferred← citeshttps://doi.org/10.3929/ethz-a-005035470openalex-snapshot

Structural and biophysical characterization of the mechanism of the inner membrane redox catalyst DsbD from Escherichia coli

inferred← citeshttps://doi.org/10.5772/35809openalex-snapshot

Menaquinone as Well as Ubiquinone as a Crucial Component in the Escherichia coli Respiratory Chain

inferred← citeshttps://doi.org/10.5772/63342openalex-snapshot

From Protein Folding to Blood Coagulation: Menaquinone as a Metabolic Link between Bacteria and Mammals

inferred← citeshttps://doi.org/10.5772/67393openalex-snapshot

From Biology to Biotechnology: Disulfide Bond Formation in Escherichia coli

inferred← citeshttps://doi.org/10.6084/m9.figshare.12284831openalex-snapshot

Additional file 1 of Translational regulation of periplasmic folding assistants and proteases as a valuable strategy to improve production of translocated recombinant proteins in Escherichia coli

inferred← citeshttps://doi.org/10.6084/m9.figshare.16816001openalex-snapshot

Additional file 1 of Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria

inferred← citeshttps://doi.org/10.6084/m9.figshare.16816007openalex-snapshot

Additional file 2 of Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria

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