scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M311391200 |
P698 | PubMed publication ID | 14726535 |
P2093 | author name string | Annie Hiniker | |
James C A Bardwell | |||
P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
Crystal structure of a plant ribonuclease, RNase LE | Q27622398 | ||
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine | Q27638626 | ||
Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins | Q27731293 | ||
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor | Q27732204 | ||
PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization | Q28139371 | ||
Reassessment of Ellman's reagent | Q28274979 | ||
Structure and function of bacterial outer membrane proteins: barrels in a nutshell | Q30168847 | ||
The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm | Q33551316 | ||
Osmoregulated periplasmic glucans in Proteobacteria | Q33898313 | ||
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade | Q33927908 | ||
Osmoregulated periplasmic glucan synthesis is required for Erwinia chrysanthemi pathogenicity | Q33996196 | ||
Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar typhimurium and Escherichia coli | Q34010272 | ||
Oxidative protein folding in bacteria | Q34124799 | ||
Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells | Q34275598 | ||
Disulfide bond isomerization in prokaryotes | Q35058901 | ||
PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA | Q35922206 | ||
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli | Q36087470 | ||
osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli | Q36112059 | ||
Osmotic regulation of PhoE porin synthesis in Escherichia coli | Q36254181 | ||
Prediction of membrane-spanning beta-strands and its application to maltoporin | Q36278128 | ||
Structural and functional analysis of cloned DNA containing genes responsible for branched-chain amino acid transport in Escherichia coli | Q36359746 | ||
Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo | Q36450266 | ||
An in vivo pathway for disulfide bond isomerization in Escherichia coli | Q36687328 | ||
Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly | Q38361694 | ||
Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. | Q39714839 | ||
Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease | Q39840351 | ||
Human carbonic anhydrase IV: in vitro activation and purification of disulfide-bonded enzyme following expression in Escherichia coli | Q41125352 | ||
Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands | Q41743298 | ||
Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family | Q43614343 | ||
Dimerization by domain hybridization bestows chaperone and isomerase activities | Q44559355 | ||
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. | Q47348771 | ||
Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling pathogenicity of Pseudomonas syringae | Q48100281 | ||
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 | ||
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
The Effect of Folding Catalysts on the In Vivo Folding Process of Different Antibody Fragments Expressed in Escherichia coli | Q57840157 | ||
Disulfide bonds are generated by quinone reduction | Q73897313 | ||
In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | Q74602402 | ||
Influence of the yihE gene of Shigella flexneri on global gene expression: on analysis using DNA arrays | Q74607675 | ||
Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
P433 | issue | 13 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 12967-12973 | |
P577 | publication date | 2004-01-15 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | In vivo substrate specificity of periplasmic disulfide oxidoreductases | |
P478 | volume | 279 |
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 |
Q39145574 | A new role for Escherichia coli DsbC protein in protection against oxidative stress |
Q33570139 | A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity. |
Q40454159 | Activation of A431 human carcinoma cell motility by extracellular high-mobility group box 1 protein and epidermal growth factor stimuli. |
Q39244663 | An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding |
Q35074321 | Analysis of the isomerase and chaperone-like activities of an amebic PDI (EhPDI). |
Q53507814 | Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System. |
Q33892804 | Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. |
Q49597995 | Bacterial periplasmic oxido-reductases are essential for the activity of oxidized human antimicrobial β-defensin 1. |
Q33599927 | Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies |
Q90592392 | C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning |
Q39665863 | Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens. |
Q54275279 | Characterization of Helicobacter pylori HP0231 (DsbK): role in disulfide bond formation, redox homeostasis and production of Helicobacter cystein-rich protein HcpE. |
Q36644629 | Characterization of VCC-1, a Novel Ambler Class A Carbapenemase from Vibrio cholerae Isolated from Imported Retail Shrimp Sold in Canada |
Q41997244 | Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae |
Q30157308 | Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics |
Q27680624 | Comparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes |
Q30277068 | Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein |
Q42086336 | Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase |
Q46640858 | Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. |
Q34828345 | Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. |
Q37386934 | DSB proteins and bacterial pathogenicity. |
Q42236528 | Deciphering the genetic basis of Moraxella catarrhalis complement resistance: a critical role for the disulphide bond formation system. |
Q35004080 | Detecting folding intermediates of a protein as it passes through the bacterial translocation channel |
Q27679294 | Disarming Burkholderia pseudomallei : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In Vivo |
Q27680864 | Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa |
Q49788752 | Disulfide bond formation in prokaryotes |
Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
Q80877153 | Disulfide bond isomerization in prokaryotes |
Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
Q30376017 | Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems. |
Q40452562 | DsbA plays a critical and multifaceted role in the production of secreted virulence factors by the phytopathogen Erwinia carotovora subsp. atroseptica. |
Q64098761 | Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis |
Q37713231 | Enhanced interaction of Vibrio cholerae virulence regulators TcpP and ToxR under oxygen-limiting conditions |
Q41046825 | Evolution of Escherichia coli for growth at high temperatures |
Q42009573 | Folding Optimization In Vivo Uncovers New Chaperones. |
Q36019079 | Genetic analysis of 15 protein folding factors and proteases of the Escherichia coli cell envelope |
Q27666964 | Genetic selection designed to stabilize proteins uncovers a chaperone called Spy |
Q37335942 | Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN |
Q38020872 | Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies |
Q35933165 | Key players involved in bacterial disulfide-bond formation |
Q30362756 | Laboratory evolution of one disulfide isomerase to resemble another |
Q27007462 | Many roles of the bacterial envelope reducing pathways |
Q41460551 | Mapping native disulfide bonds at a proteome scale |
Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
Q50072414 | Mode of Salmonella and Escherichia coli O157:H7 inactivation by a stabilized oxychloro-based sanitizer |
Q35860792 | Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA |
Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
Q33982252 | Nonconsecutive disulfide bond formation in an essential integral outer membrane protein |
Q36969531 | Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli. |
Q36685039 | Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbA |
Q90178754 | Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development |
Q24797314 | Protein thiol modifications visualized in vivo |
Q34635044 | Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb). |
Q37895211 | Proteomic methods unravel the protein quality control in Escherichia coli |
Q27681723 | Quality control of disulfide bond formation in pilus subunits by the chaperone FimC |
Q27015968 | Reducing systems protecting the bacterial cell envelope from oxidative damage |
Q41670252 | Role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli |
Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
Q26738760 | Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents |
Q41711501 | The CpxR/CpxA two-component regulatory system up-regulates the multidrug resistance cascade to facilitate Escherichia coli resistance to a model antimicrobial peptide |
Q37035909 | The MerR-like regulator BrlR confers biofilm tolerance by activating multidrug efflux pumps in Pseudomonas aeruginosa biofilms |
Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
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 |
Q36606739 | The origami of thioredoxin-like folds |
Q27647336 | The oxidase DsbA folds a protein with a nonconsecutive disulfide |
Q36539649 | The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis. |
Q30156116 | The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD. |
Q36909442 | The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis. |
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Q54457239 | The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases. |
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 |
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. |
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