| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M108697200 |
| P8608 | Fatcat ID | release_aaeagjh6knfvbpdqn7urxc4ivq |
| P698 | PubMed publication ID | 11698406 |
| P2093 | author name string | James C A Bardwell | |
| Tong Xie | |||
| Linda Yu | |||
| Chang-An Yu | |||
| Martin W Bader | |||
| P2860 | cites work | Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 |
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| Where do the electrons go? | Q59001298 | ||
| Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase | Q72631629 | ||
| Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
| Disulfide bonds are generated by quinone reduction | Q73897313 | ||
| 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 | ||
| A pathway for disulfide bond formation in vivo | Q24563594 | ||
| Crystal structure of the DsbA protein required for disulphide bond formation in vivo | Q27732066 | ||
| Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization | Q27760300 | ||
| Electron avenue: pathways of disulfide bond formation and isomerization | Q33760255 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| 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 | ||
| Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli | Q37264681 | ||
| The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding | Q38331200 | ||
| Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway | Q42668332 | ||
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 1649-1652 | |
| P577 | publication date | 2001-11-06 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. | |
| P478 | volume | 277 |
| Q34847230 | A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans |
| Q36289818 | Biosynthesis, bioproduction and novel roles of ubiquinone |
| Q45044166 | Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. |
| 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 |
| Q33712972 | Disulfide bond formation involves a quinhydrone-type charge–transfer complex |
| Q44366662 | DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. |
| Q33187670 | Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein |
| Q38289355 | Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. |
| Q35180509 | Hypersensitive response-like lesions 1 codes for AtPPT1 and regulates accumulation of ROS and defense against bacterial pathogen Pseudomonas syringae in Arabidopsis thaliana |
| Q37418585 | Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB |
| Q50706871 | Kinetic characterization of the disulfide bond-forming enzyme DsbB. |
| Q30802800 | Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli |
| Q30350105 | Mutational analysis of the disulfide catalysts DsbA and DsbB. |
| Q39647375 | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. |
| Q34398742 | RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool |
| Q41387936 | Structure formation during translocon-unassisted co-translational membrane protein folding. |
| Q44429242 | The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli |
| Q36606739 | The origami of thioredoxin-like folds |
| Q41884481 | The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases |
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