| scholarly article | Q13442814 |
| P50 | author | Laurent Debarbieux | Q42867472 |
| P2093 | author name string | J Beckwith | |
| P2860 | cites work | Identification of a protein required for disulfide bond formation in vivo | Q48201805 |
| Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. | Q54646876 | ||
| Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli. | Q54750197 | ||
| Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages | Q66900225 | ||
| DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA | Q71891832 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
| Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli | Q78177288 | ||
| Structure of reduced DsbA from Escherichia coli in solution | Q27756913 | ||
| Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization | Q27760300 | ||
| Thioredoxin--a fold for all reasons | Q29618984 | ||
| The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm | Q33551316 | ||
| Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA | Q33877973 | ||
| Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins | Q33889552 | ||
| Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
| Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria | Q34743720 | ||
| 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 | ||
| The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation | Q37631360 | ||
| The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding | Q41883518 | ||
| 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 | ||
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 723-727 | |
| P577 | publication date | 2000-02-01 | |
| P1433 | published in | Journal of Bacteriology | Q478419 |
| P1476 | title | On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily | |
| P478 | volume | 182 |
| Q47281972 | A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation |
| Q34245202 | A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo |
| Q46183002 | A small family of chloroplast atypical thioredoxins |
| Q34545621 | Catalysis of disulfide bond formation and isomerization in Escherichia coli |
| Q38634845 | Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions. |
| Q41456212 | Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. |
| Q77745570 | Disulfide bond formation in periplasm of Escherichia coli |
| Q49788752 | Disulfide bond formation in prokaryotes |
| Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
| Q30981412 | Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli |
| Q37124378 | Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231) |
| Q36638705 | Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways |
| Q40331679 | Insights into Trx1, TRP14, and Prx1 homologs of Paralichthys olivaceus: molecular profiles and transcriptional responses to immune stimulations |
| Q34269611 | Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein. |
| Q46899985 | Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. |
| Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q30168451 | Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA |
| Q43105010 | Prediction of pKa and redox properties in the thioredoxin superfamily. |
| Q42353700 | Protein folding drives disulfide formation |
| Q36203533 | Regulation of protein function by glutathionylation |
| Q37264681 | Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli |
| Q39887818 | The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway |
| Q38038631 | The biological roles of glutaredoxins |
| Q33927908 | Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade |
| Q39714839 | Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. |
| Q42723141 | Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation |
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