scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.274.12.7784 |
P698 | PubMed publication ID | 10075670 |
P2093 | author name string | G Georgiou | |
H F Gilbert | |||
P H Bessette | |||
J J Cotto | |||
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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 | ||
Protein folding in the bacterial periplasm | Q35621918 | ||
Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation | Q35970767 | ||
In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. | Q36157575 | ||
Chromosomal transformation of Escherichia coli recD strains with linearized plasmids. | Q36177080 | ||
Mutation of conserved residues in Escherichia coli thioredoxin: Effects on stability and function | Q36277627 | ||
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 | ||
Leaderless polypeptides efficiently extracted from whole cells by osmotic shock | Q39846925 | ||
Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature | Q39948895 | ||
Protein folding in the periplasm of Escherichia coli | Q40683971 | ||
Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure | Q41230313 | ||
Protein misfolding in the cell envelope of Escherichia coli: new signaling pathways | Q41361800 | ||
Making and breaking disulfide bonds | Q41620623 | ||
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase | Q42156942 | ||
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli | Q42843291 | ||
Kinetic analysis of the folding and unfolding of a mutant form of bovine pancreatic trypsin inhibitor lacking the cysteine-14 and -38 thiols | Q44379877 | ||
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
Protein folding activities of Escherichia coli protein disulfide isomerase | Q46312417 | ||
Paracoccus denitrificans CcmG is a periplasmic protein-disulphide oxidoreductase required for c- and aa3-type cytochrome biogenesis; evidence for a reductase role in vivo | Q48049000 | ||
Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. | Q52524766 | ||
Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. | Q54588808 | ||
Redox states of DsbA in the periplasm of Escherichia coli. | Q54612842 | ||
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes. | Q54787854 | ||
Protein folding | Q68539600 | ||
Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes | Q73039144 | ||
Disulfide bond catalysts in Escherichia coli | Q74420339 | ||
Reconstitution of a protein disulfide catalytic system | Q74465528 | ||
P433 | issue | 12 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 7784-7792 | |
P577 | publication date | 1999-03-01 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | |
P478 | volume | 274 |
Q57889876 | 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD |
Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
Q39145574 | A new role for Escherichia coli DsbC protein in protection against oxidative stress |
Q28484215 | A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein |
Q27673179 | Atomic Resolution Insights into Curli Fiber Biogenesis |
Q90592392 | C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning |
Q34545621 | Catalysis of disulfide bond formation and isomerization in Escherichia coli |
Q33996659 | Computation-directed identification of OxyR DNA binding sites in Escherichia coli |
Q42086336 | Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase |
Q39492391 | Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins |
Q27641276 | Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1) |
Q34828345 | Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. |
Q43244316 | De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC. |
Q30332482 | Dehydration converts DsbG crystal diffraction from low to high resolution. |
Q44559355 | Dimerization by domain hybridization bestows chaperone and isomerase activities |
Q41787799 | Disulfide bond formation and cysteine exclusion in gram-positive bacteria |
Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
Q80877153 | Disulfide bond isomerization in prokaryotes |
Q30416941 | Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity |
Q73897313 | Disulfide bonds are generated by quinone reduction |
Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
Q30376017 | Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems. |
Q39501974 | DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa |
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. |
Q73731229 | DsbG, a protein disulfide isomerase with chaperone activity |
Q30981412 | Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli |
Q35970728 | Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways |
Q39647812 | Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. |
Q40702083 | F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues |
Q42097551 | Genetic analysis of activation of the Vibrio cholerae Cpx pathway |
Q40469171 | Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing |
Q27642487 | Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis |
Q34490362 | Identification of disulfide bond isomerase substrates reveals bacterial virulence factors. |
Q43792245 | Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. |
Q44730682 | In vivo substrate specificity of periplasmic disulfide oxidoreductases |
Q31613031 | Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA. |
Q30362756 | Laboratory evolution of one disulfide isomerase to resemble another |
Q27007462 | Many roles of the bacterial envelope reducing pathways |
Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
Q39678300 | Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells |
Q38361490 | Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli |
Q78066764 | Oxidative protein folding is driven by the electron transport system |
Q30369955 | Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomics analysis. |
Q27653607 | Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue |
Q34680350 | Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin |
Q30832013 | Purification, characterization and biosynthesis of parabutoxin 3, a component of Parabuthus transvaalicus venom |
Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
Q27677973 | Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium |
Q27680391 | Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis |
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 |
Q41882010 | Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant |
Q26738760 | Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents |
Q90253526 | The Chaperone Activities of DsbG and Spy Restore Peptidoglycan Biosynthesis in the elyC Mutant by Preventing Envelope Protein Aggregation |
Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
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 |
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 |
Q36539649 | The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis. |
Q33537167 | The thioredoxin superfamily: redundancy, specificity, and gray-area genomics |
Q33843037 | Thioredoxin A Is Essential for Motility and Contributes to Host Infection of Listeria monocytogenes via Redox Interactions |
Q37094827 | Thioredoxin-like proteins in F and other plasmid systems |
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. |
Q59001298 | Where do the electrons go? |
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