| scholarly article | Q13442814 |
| review article | Q7318358 |
| P356 | DOI | 10.1016/S0065-3233(01)59009-9 |
| P698 | PubMed publication ID | 11868275 |
| P2093 | author name string | Bardwell JC | |
| Bader MW | |||
| P2860 | cites work | Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli | Q27621623 |
| Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B | Q27730283 | ||
| 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 | ||
| 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 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| Thioredoxin--a fold for all reasons | Q29618984 | ||
| The reductive cleavage of disulfide bonds and its application to problems of protein structure. | Q30334068 | ||
| Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex. | Q31387729 | ||
| Principles of protein folding in the cellular environment | Q33536619 | ||
| The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo | Q33728264 | ||
| Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade | Q33927908 | ||
| On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily | Q33993677 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain | Q36688584 | ||
| 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 | ||
| Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli | Q37620314 | ||
| Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli | Q39845433 | ||
| Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA− menA− double quinone mutant | Q40082859 | ||
| Building bridges: disulphide bond formation in the cell | Q40576198 | ||
| Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability--a review. | Q41532663 | ||
| Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. | Q41846532 | ||
| 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 | ||
| 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 | ||
| Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli | Q42843291 | ||
| Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. | Q52524766 | ||
| Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+. | Q54096984 | ||
| The CcmE protein from Escherichia coli is a haem-binding protein | Q60584830 | ||
| Contributions of substrate binding to the catalytic activity of DsbC. | Q64974634 | ||
| DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA | Q71891832 | ||
| Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo | Q72413394 | ||
| Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH | Q72551904 | ||
| Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase | Q72638394 | ||
| Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
| Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm | Q73537525 | ||
| DsbG, a protein disulfide isomerase with chaperone activity | Q73731229 | ||
| Disulfide bonds are generated by quinone reduction | Q73897313 | ||
| The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC | Q74127474 | ||
| Reconstitution of a protein disulfide catalytic system | Q74465528 | ||
| In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | Q74602402 | ||
| Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation | Q77892269 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Chaperone activity of DsbC | Q77955138 | ||
| Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
| P921 | main subject | Escherichia coli | Q25419 |
| P304 | page(s) | 283-301 | |
| P577 | publication date | 2001-01-01 | |
| P1433 | published in | Advances in Protein Chemistry | Q15756442 |
| P1476 | title | Catalysis of disulfide bond formation and isomerization in Escherichia coli | |
| P478 | volume | 59 |
| Q30362750 | Analyzing transmembrane chemoreceptors using in vivo disulfide formation between introduced cysteines. |
| Q30155144 | Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation |
| Q83275101 | Conformational isomers of denatured and unfolded proteins: methods of production and applications |
| Q42126977 | Oxidative folding of hirudin in human serum |
| Q83370024 | Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or hirudin model |
| Q37895211 | Proteomic methods unravel the protein quality control in Escherichia coli |
| Q34046537 | The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. |
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