| scholarly article | Q13442814 |
| P2093 | author name string | Beckwith J | |
| Katzen F | |||
| P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
| Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization | Q24676777 | ||
| 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 | ||
| Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter | Q27860697 | ||
| Eps1, a novel PDI-related protein involved in ER quality control in yeast | Q27935621 | ||
| Pathways for protein disulphide bond formation | Q28141294 | ||
| Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes | Q30832647 | ||
| The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm | Q33551316 | ||
| 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 | ||
| 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 | ||
| On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily | Q33993677 | ||
| Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
| Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli | Q35627960 | ||
| 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 biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain | Q36688584 | ||
| Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli | Q37620314 | ||
| Identification and characterization of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis | Q39844945 | ||
| Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis | Q42666480 | ||
| 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 | ||
| In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC. | Q50120875 | ||
| Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. | Q52524766 | ||
| Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. | Q54593983 | ||
| Purification and Functional Analysis of the Mycobacterium leprae Thioredoxin/Thioredoxin Reductase Hybrid Protein | Q54601302 | ||
| Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
| Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. | Q54646876 | ||
| Contributions of substrate binding to the catalytic activity of DsbC. | Q64974634 | ||
| DSBC protein: a new member of the thioredoxin fold-containing family | Q71113457 | ||
| Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein | Q72798587 | ||
| Scanning and escape during protein-disulfide isomerase-assisted protein folding | Q73182455 | ||
| 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 | ||
| Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function | Q73665019 | ||
| 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 | ||
| Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
| P433 | issue | 5 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | membrane protein | Q423042 |
| transmembrane protein | Q424204 | ||
| P304 | page(s) | 769-779 | |
| P577 | publication date | 2000-11-01 | |
| P1433 | published in | Cell | Q655814 |
| P1476 | title | Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade | |
| P478 | volume | 103 |
| Q42027426 | 1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| Q57889876 | 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD |
| Q38293884 | A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c. |
| Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
| Q34228037 | A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope |
| Q28484215 | A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein |
| Q37410278 | A periplasmic thioredoxin-like protein plays a role in defense against oxidative stress in Neisseria gonorrhoeae. |
| Q27646618 | A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c |
| Q27639193 | All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade |
| Q27681479 | An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold |
| Q44362222 | Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. |
| Q34695145 | Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes |
| Q34545621 | Catalysis of disulfide bond formation and isomerization in Escherichia coli |
| Q28080871 | Cellular disulfide bond formation in bioactive peptides and proteins |
| Q43244274 | Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation |
| Q36913659 | Comprehensive analysis of transport proteins encoded within the genome of Bdellovibrio bacteriovorus |
| Q42757366 | Control of periplasmic interdomain thiol:disulfide exchange in the transmembrane oxidoreductase DsbD. |
| Q27667359 | Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC |
| Q27641276 | Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1) |
| Q42411902 | Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis |
| Q30331574 | Cysteine regulation of protein function--as exemplified by NMDA-receptor modulation. |
| Q34756436 | Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability |
| Q27680864 | Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa |
| Q77745570 | Disulfide bond formation in periplasm of Escherichia coli |
| Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
| Q26823827 | Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead |
| Q37536471 | Disulfide bond formation system in Escherichia coli. |
| Q34559609 | Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 |
| Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
| Q34627585 | Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay |
| Q44260052 | DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo |
| Q33932871 | DsbC activation by the N-terminal domain of DsbD. |
| Q41912356 | Engineered pathways for correct disulfide bond oxidation |
| Q39109808 | Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues |
| Q39647812 | Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. |
| 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. |
| Q36133918 | Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain |
| Q40469171 | Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing |
| Q37364322 | Genetic suppressors and recovery of repressed biochemical memory |
| Q35682475 | Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231. |
| Q34490362 | Identification of disulfide bond isomerase substrates reveals bacterial virulence factors. |
| Q38020872 | Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies |
| Q44730682 | In vivo substrate specificity of periplasmic disulfide oxidoreductases |
| Q35933165 | Key players involved in bacterial disulfide-bond formation |
| Q30301079 | Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization |
| Q90696168 | Lipase maturation factor 1 affects redox homeostasis in the endoplasmic reticulum |
| Q28754640 | MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress response |
| Q27007462 | Many roles of the bacterial envelope reducing pathways |
| Q34446362 | Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q57811254 | Methods to identify the substrates of thiol-disulfide oxidoreductases |
| Q34543949 | Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli |
| Q46118845 | Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space |
| Q53633026 | Overproduction of CcmABCDEFGH restores cytochrome c maturation in a DsbD deletion strain of E. coli: another route for reductant? |
| Q27667688 | Oxidation State-dependent Protein-Protein Interactions in Disulfide Cascades |
| Q34124799 | Oxidative protein folding in bacteria |
| Q33941860 | Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase |
| Q39249467 | Oxidative stress, protein damage and repair in bacteria. |
| Q39647375 | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. |
| Q48159954 | Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. |
| Q37094594 | Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli |
| Q43988793 | Reconstitution of a disulfide isomerization system |
| Q43920319 | Redox state of cytoplasmic thioredoxin |
| Q35941498 | Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility |
| Q27015968 | Reducing systems protecting the bacterial cell envelope from oxidative damage |
| Q35918506 | Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. |
| Q39504421 | Roles for the Rhodobacter sphaeroides CcmA and CcmG proteins |
| Q48146747 | Solution structure and elevator mechanism of the membrane electron transporter CcdA. |
| Q53666575 | SoxV, an orthologue of the CcdA disulfide transporter, is involved in thiosulfate oxidation in Rhodovulum sulfidophilum and reduces the periplasmic thioredoxin SoxW. |
| Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
| Q43885153 | Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm |
| Q40788115 | Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. |
| Q27702185 | Structure and multistate function of the transmembrane electron transporter CcdA |
| Q27639369 | Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment |
| Q60301186 | Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome Synthetase |
| Q50301904 | The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli |
| Q30932970 | The Dithiol:Disulfide Oxidoreductases DsbA and DsbB of Rhodobacter capsulatus Are Not Directly Involved in Cytochrome c Biogenesis, but Their Inactivation Restores the Cytochrome c Biogenesis Defect of CcdA-Null Mutants |
| Q34351328 | The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli. |
| Q27639655 | The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex |
| Q37038829 | The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner |
| Q28543570 | The effect of tensile stress on the conformational free energy landscape of disulfide bonds |
| Q27641933 | The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction |
| Q77199396 | The expanding world of oxidative protein folding |
| Q41767891 | The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli |
| Q40142869 | The oxidoreductase DsbA plays a key role in the ability of the Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 to resist macrophage killing |
| Q30156116 | The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD. |
| Q34476988 | Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme |
| Q37094827 | Thioredoxin-like proteins in F and other plasmid systems |
| Q39414163 | Topology mapping of insulin-regulated glucose transporter GLUT4 using computational biology. |
| Q35192535 | TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. |
| Q44915305 | Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system |
| Q42046419 | Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD. |
| Q47287209 | Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions |
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