| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M003850200 |
| P698 | PubMed publication ID | 10854438 |
| P2093 | author name string | J C Bardwell | |
| M W Bader | |||
| T Xie | |||
| C A Yu | |||
| P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
| Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli | Q27621623 | ||
| Crystal structure of the DsbA protein required for disulphide bond formation in vivo | Q27732066 | ||
| Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy | Q27732861 | ||
| Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization | Q27760300 | ||
| The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum | Q27936188 | ||
| Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum | Q27939552 | ||
| Reassessment of Ellman's reagent | Q28274979 | ||
| Electron avenue: pathways of disulfide bond formation and isomerization | Q33760255 | ||
| Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer | Q34019971 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
| Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells | Q36622135 | ||
| An in vivo pathway for disulfide bond isomerization in Escherichia coli | Q36687328 | ||
| A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins | Q36893186 | ||
| Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA− menA− double quinone mutant | Q40082859 | ||
| 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 | Q42271387 | ||
| Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway | Q42668332 | ||
| Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli | Q42685653 | ||
| Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase. | Q50519771 | ||
| Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
| Where do the electrons go? | Q59001298 | ||
| Contributions of substrate binding to the catalytic activity of DsbC. | Q64974634 | ||
| Protein disulphide isomerase: building bridges in protein folding | Q72754787 | ||
| Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
| DsbG, a protein disulfide isomerase with chaperone activity | Q73731229 | ||
| Reconstitution of a protein disulfide catalytic system | Q74465528 | ||
| In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | Q74602402 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
| P433 | issue | 34 | |
| P407 | language of work or name | English | Q1860 |
| P1104 | number of pages | 7 | |
| P304 | page(s) | 26082-26088 | |
| P577 | publication date | 2000-08-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Disulfide bonds are generated by quinone reduction | |
| P478 | volume | 275 |
| Q30411815 | Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB |
| Q34545621 | Catalysis of disulfide bond formation and isomerization in Escherichia coli |
| Q64981708 | Co-production of farnesol and coenzyme Q10 from metabolically engineered Rhodobacter sphaeroides. |
| Q88656399 | CoQ10 a super-vitamin: review on application and biosynthesis |
| Q34246180 | Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. |
| Q24675933 | Cys303 in the histidine kinase PhoR is crucial for the phosphotransfer reaction in the PhoPR two-component system in Bacillus subtilis |
| Q27680864 | Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa |
| Q49788752 | Disulfide bond formation in prokaryotes |
| Q33712972 | Disulfide bond formation involves a quinhydrone-type charge–transfer complex |
| Q80877153 | Disulfide bond isomerization in prokaryotes |
| Q33932871 | DsbC activation by the N-terminal domain of DsbD. |
| Q27653763 | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB |
| Q35970728 | Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways |
| Q92945212 | Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli |
| Q34157680 | Formation and transfer of disulphide bonds in living cells |
| Q38289355 | Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. |
| Q92180501 | Four thiol-oxidoreductases involved in the formation of disulphide bonds in the Streptomyces lividans TK21 secretory proteins |
| Q27666964 | Genetic selection designed to stabilize proteins uncovers a chaperone called Spy |
| Q36648798 | Human coenzyme Q10 deficiency |
| Q39776783 | Identification of Actinobacillus pleuropneumoniae genes important for survival during infection in its natural host |
| Q37418585 | Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB |
| Q85069990 | Identification of bottlenecks in Escherichia coli engineered for the production of CoQ(10) |
| Q43792245 | Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. |
| Q44730682 | In vivo substrate specificity of periplasmic disulfide oxidoreductases |
| Q36289066 | Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions |
| Q24293677 | Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ |
| Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
| Q42202168 | Menaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase |
| Q36295043 | Mini-review: the role of redox in Dopa-mediated marine adhesion. |
| Q30350105 | Mutational analysis of the disulfide catalysts DsbA and DsbB. |
| Q24676827 | Oxidative protein folding in eukaryotes: mechanisms and consequences |
| Q90178754 | Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development |
| Q39647375 | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. |
| Q27678990 | Plasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate Reductase |
| Q34398742 | RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool |
| Q37264681 | Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli |
| Q34555106 | RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system |
| Q27680167 | 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 |
| Q40788115 | Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. |
| Q41387936 | Structure formation during translocon-unassisted co-translational membrane protein folding. |
| Q27676407 | Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer |
| Q50301904 | The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli |
| Q44230446 | The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum |
| Q44429242 | The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli |
| Q27639655 | The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex |
| Q36606739 | The origami of thioredoxin-like folds |
| Q41884481 | The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases |
| Q24656248 | The role of UbiX in Escherichia coli coenzyme Q biosynthesis |
| Q42957338 | The thiol:disulfide oxidoreductase DsbB mediates the oxidizing effects of the toxic metalloid tellurite (TeO32-) on the plasma membrane redox system of the facultative phototroph Rhodobacter capsulatus. |
| Q35055321 | The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria. |
| Q39714839 | Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. |
| Q50026707 | Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB. |
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