| scholarly article | Q13442814 |
| P819 | ADS bibcode | 1993PNAS...90.1038B |
| P356 | DOI | 10.1073/PNAS.90.3.1038 |
| P932 | PMC publication ID | 45806 |
| P698 | PubMed publication ID | 8430071 |
| P5875 | ResearchGate publication ID | 14769381 |
| P2093 | author name string | G Jander | |
| J Beckwith | |||
| J C Bardwell | |||
| N Martin | |||
| J O Lee | |||
| D Belin | |||
| P2860 | cites work | Principles that govern the folding of protein chains | Q28236872 |
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| Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae | Q33613621 | ||
| Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme | Q33937247 | ||
| Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli | Q34235769 | ||
| Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli | Q36087470 | ||
| Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator | Q36423135 | ||
| 7 Uses of transposons with emphasis on Tn10 | Q36439570 | ||
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| Protein folding: local structures, domains, subunits, and assemblies | Q37679302 | ||
| A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae | Q42599846 | ||
| Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme | Q44682382 | ||
| Western and dot immunoblotting analysis of viral antigens and antibodies: Application to murine hepatitis virus | Q45804216 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
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| Is the hydrophobic effect stabilizing or destabilizing in proteins? | Q57909124 | ||
| Isolation and characterization of sulfhydryl oxidase from bovine milk | Q66919559 | ||
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| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 1038-42 | |
| P577 | publication date | 1993-02-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | A pathway for disulfide bond formation in vivo | |
| P478 | volume | 90 |
| Q38289494 | A Bacterial Thioredoxin-like Protein That Is Exposed to the Periplasm Has Redox Properties Comparable with Those of Cytoplasmic Thioredoxins |
| Q36065069 | A Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces oris |
| Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
| Q35692775 | A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery |
| Q39835331 | A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli |
| 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 |
| Q50515989 | A protein oxidase catalysing disulfide bond formation is localized to the chloroplast thylakoids. |
| Q74486160 | A single dipeptide sequence modulates the redox properties of a whole enzyme family |
| Q37168806 | A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence |
| Q46261151 | Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments |
| Q56967363 | An essential role for DsbA in cytochromec synthesis and formate-dependent nitrite reduction byEscherichia coli K-12 |
| Q36687328 | An in vivo pathway for disulfide bond isomerization in Escherichia coli |
| Q30411815 | Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB |
| Q58091963 | Bacillus megaterium adapts to acid stress condition through a network of genes: Insight from a genome-wide transcriptome analysis |
| Q44362222 | Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. |
| Q63359921 | Chapter 32 Translocation of proteins across the bacterial cytoplasmic membrane |
| Q37631345 | Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity |
| Q30452970 | Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae |
| Q45044166 | Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. |
| Q37232482 | Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073. |
| Q48052369 | Cloning and expression of the gene for a protein disulfide oxidoreductase from Azotobacter vinelandii: complementation of an Escherichia coli dsbA mutant strain |
| Q42271387 | 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 |
| Q90494637 | Complex Oxidation of Apocytochromes c during Bacterial Cytochrome c Maturation |
| Q42565094 | Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP |
| Q27656012 | Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE |
| Q27732066 | Crystal structure of the DsbA protein required for disulphide bond formation in vivo |
| Q34828345 | Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. |
| Q38361694 | Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly |
| Q39459725 | Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space |
| Q39845716 | Defective export in Escherichia coli caused by DsbA'-PhoA hybrid proteins whose DsbA' domain cannot fold into a conformation resistant to periplasmic proteases |
| Q30332482 | Dehydration converts DsbG crystal diffraction from low to high resolution. |
| Q38270038 | Description of the topographical changes associated to the different stages of the DsbA catalytic cycle. |
| Q52524766 | Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. |
| Q24600389 | Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli |
| Q27680864 | Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa |
| Q36353781 | Disulfide bond formation and ToxR activity in Vibrio cholerae |
| Q39837913 | Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II |
| Q37083585 | Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm |
| Q49788752 | Disulfide bond formation in prokaryotes |
| Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
| Q26823827 | Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead |
| Q33712972 | Disulfide bond formation involves a quinhydrone-type charge–transfer complex |
| Q73897313 | Disulfide bonds are generated by quinone reduction |
| Q34275598 | Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells |
| Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
| Q73513823 | Domains within the Vibrio cholerae toxin coregulated pilin subunit that mediate bacterial colonization |
| Q39842062 | Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA. |
| Q39501974 | DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa |
| Q39654926 | DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis |
| Q44260052 | DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo |
| Q44366662 | DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. |
| Q33932871 | DsbC activation by the N-terminal domain of DsbD. |
| Q31583197 | DsbD-catalyzed transport of electrons across the membrane of Escherichia coli |
| Q73731229 | DsbG, a protein disulfide isomerase with chaperone activity |
| Q27653763 | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB |
| Q30981412 | Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli |
| Q42118464 | Effects of oxygen on biofilm formation and the AtlA autolysin of Streptococcus mutans |
| Q33820093 | Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris |
| Q33760255 | Electron avenue: pathways of disulfide bond formation and isomerization |
| Q54559625 | Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties. |
| Q41912356 | Engineered pathways for correct disulfide bond oxidation |
| Q73151253 | Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum |
| Q33877973 | Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA |
| Q39647812 | Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. |
| Q36588505 | Expression and crystallization of DsbA from Staphylococcus aureus |
| Q33830270 | Expression and crystallization of SeDsbA, SeDsbL and SeSrgA from Salmonella enterica serovar Typhimurium |
| Q64449699 | Extracellular DsbA-insensitive folding of Escherichia coli heat-stable enterotoxin STa in vitro |
| Q35601613 | Flagellar assembly in Caulobacter crescentus: a basal body P-ring null mutation affects stability of the L-ring protein |
| Q33187670 | Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein |
| 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. |
| Q78151339 | Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis |
| Q39839133 | Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans |
| Q37364322 | Genetic suppressors and recovery of repressed biochemical memory |
| Q45126644 | Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells |
| Q40583832 | H-NS represses Salmonella enterica serovar Typhimurium dsbA expression during exponential growth |
| Q41331247 | HmsC Controls Yersinia pestis Biofilm Formation in Response to Redox Environment |
| Q40609301 | How proteins cross the bacterial cytoplasmic membrane. |
| Q37620314 | Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli |
| Q36450266 | Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo |
| Q91903544 | Identification of Redox Partners of the Thiol-Disulfide Oxidoreductase SdbA in Streptococcus gordonii |
| Q43792245 | Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. |
| Q38020872 | Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies |
| Q72102596 | In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA) |
| Q74456182 | In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli |
| Q54608202 | In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence |
| Q44730682 | In vivo substrate specificity of periplasmic disulfide oxidoreductases |
| Q39836429 | In vivo sulfhydryl modification of the ligand-binding site of Tsr, the Escherichia coli serine chemoreceptor |
| Q39572517 | Inactivation of DsbA, but not DsbC and DsbD, affects the intracellular survival and virulence of Shigella flexneri. |
| Q54572351 | Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA. |
| Q90577503 | Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes |
| Q36289066 | Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions |
| Q27649041 | Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase |
| Q30155388 | Insights into the structure and assembly of Escherichia coli outer membrane protein A |
| Q37858328 | Integrating protein homeostasis strategies in prokaryotes |
| Q47610685 | Intramembrane Thiol Oxidoreductases: Evolutionary Convergence and Structural Controversy. |
| Q48341081 | Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium |
| Q35933165 | Key players involved in bacterial disulfide-bond formation |
| Q39846925 | Leaderless polypeptides efficiently extracted from whole cells by osmotic shock |
| Q39881687 | Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol-disulfide exchange enzymes |
| Q27007462 | Many roles of the bacterial envelope reducing pathways |
| Q39495963 | Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking |
| Q54376952 | Mapping the folding pathway of the transmembrane protein DsbB by protein engineering |
| Q39931909 | Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation |
| Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q34700221 | Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase |
| Q57811254 | Methods to identify the substrates of thiol-disulfide oxidoreductases |
| Q35230935 | Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain protein STM3615 |
| Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
| Q36087470 | Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli |
| Q40943090 | Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily |
| Q30350105 | Mutational analysis of the disulfide catalysts DsbA and DsbB. |
| Q39678300 | Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells |
| Q35762584 | NlpI-mediated modulation of outer membrane vesicle production through peptidoglycan dynamics in Escherichia coli. |
| Q33982252 | Nonconsecutive disulfide bond formation in an essential integral outer membrane protein |
| Q27617979 | On the role of the cis-proline residue in the active site of DsbA |
| Q38361490 | Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli |
| Q35970767 | Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation |
| Q40370871 | Overexpression of integral membrane proteins for structural studies |
| Q39487446 | Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli |
| Q36195204 | Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. |
| Q43560181 | Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli |
| Q38472604 | Oxidative folding: recent developments |
| Q34540380 | Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space |
| Q34124799 | Oxidative protein folding in bacteria |
| Q24676827 | Oxidative protein folding in eukaryotes: mechanisms and consequences |
| Q78066764 | Oxidative protein folding is driven by the electron transport system |
| Q35922206 | PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA |
| Q39647375 | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. |
| Q28141294 | Pathways for protein disulphide bond formation |
| Q35843643 | Preferential binding of an unfolded protein to DsbA. |
| Q27652023 | Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB |
| Q48159954 | Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. |
| Q29301328 | Protein disulfide isomerase: A multifunctional protein of the endoplasmic reticulum |
| Q35621918 | Protein folding in the bacterial periplasm |
| Q34680350 | Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin |
| Q53230714 | Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli. |
| Q73177773 | Protein oxidation: prime suspect found 'not guilty' |
| Q33277084 | Proteome analysis of virulence factor regulated by autoinducer-2-like activity in Escherichia coli O157:H7. |
| Q37895211 | Proteomic methods unravel the protein quality control in Escherichia coli |
| Q38318518 | Reactivity of the two essential cysteine residues of the periplasmic mercuric ion-binding protein, MerP. |
| Q27015968 | Reducing systems protecting the bacterial cell envelope from oxidative damage |
| Q34444511 | Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. |
| Q43107575 | Reoxidation of the Thiol-Disulfide Oxidoreductase MdbA by a Bacterial Vitamin K Epoxide Reductase in the Biofilm-Forming Actinobacterium Actinomyces oris |
| Q36622135 | Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells |
| Q42668332 | Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway |
| Q41670252 | Role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli |
| Q37264681 | Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli |
| Q73101164 | Roles of disulfide bonds in bacterial alkaline phosphatase |
| Q34555106 | RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system |
| Q41238688 | Secretion of recombinant proteins by Gram-negative bacteria |
| Q27630806 | Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii |
| Q27649310 | Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding |
| Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
| Q41846532 | Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. |
| Q27660252 | Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar Typhimurium |
| Q40788115 | Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. |
| Q47871496 | Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA. |
| Q50027206 | Structural basis of a thiol-disulfide oxidoreductase in the hedgehog-forming actinobacterium Corynebacterium matruchotii |
| Q27659264 | Structure of a bacterial homologue of vitamin K epoxide reductase |
| Q27676407 | Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer |
| Q33212349 | Synthesis of the blood circulating C-terminal fragment of insulin-like growth factor (IGF)-binding protein-4 in its native conformation. Crystallization, heparin and IGF binding, and osteogenic activity |
| Q37125393 | Synthetic effect between envelope stress and lack of outer membrane vesicle production in Escherichia coli. |
| Q26738760 | Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents |
| Q35023691 | Targeting virulence not viability in the search for future antibacterials. |
| Q27682316 | The 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production |
| Q34101630 | The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function |
| Q54436865 | The CXXC motif is more than a redox rheostat. |
| Q41065191 | The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. |
| Q50301904 | The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli |
| Q54649845 | The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains. |
| Q27936188 | The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum |
| Q28360595 | The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly |
| Q37007216 | The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase |
| Q37631360 | The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation |
| Q44230446 | The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum |
| Q34910861 | The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli |
| Q28492915 | The Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB system |
| Q27655136 | The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes |
| Q27639655 | The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex |
| Q34593232 | The disulfide bonding system suppresses CsgD-independent cellulose production in Escherichia coli |
| Q37038829 | The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner |
| Q49331066 | The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain |
| Q47881156 | The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of 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 |
| Q36539649 | The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis. |
| Q41884481 | The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases |
| Q33551316 | The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm |
| Q33537167 | The thioredoxin superfamily: redundancy, specificity, and gray-area genomics |
| Q41883518 | The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding |
| Q30159843 | Thermodynamics of unfolding of an integral membrane protein in mixed micelles |
| Q37094827 | Thioredoxin-like proteins in F and other plasmid systems |
| Q35942715 | Transcriptional regulation of the assT-dsbL-dsbI gene cluster in Salmonella enterica serovar Typhi IMSS-1 depends on LeuO, H-NS, and specific growth conditions. |
| Q35634688 | Transduction of envelope stress in Escherichia coli by the Cpx two-component system |
| Q32060775 | Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli |
| 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. |
| Q24568243 | Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation |
| Q24550637 | Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum |
| 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 |
| Q47374112 | Unraveling solvent-mediated reaction pathways leading to regiospecific mechanochemical cleavage of disulfide bonds in peptides |
| Q39843318 | Use of heme reporters for studies of cytochrome biosynthesis and heme transport |
| Q42723141 | Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation |
| Q50026707 | Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB. |
| Q42743365 | What lies beyond uranus? Preconceptions, ignorance, serendipity and suppressors in the search for biology's secrets |
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