| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2004Sci...303..534K |
| P356 | DOI | 10.1126/SCIENCE.1091724 |
| P698 | PubMed publication ID | 14739460 |
| P5875 | ResearchGate publication ID | 8907099 |
| P2093 | author name string | Hiroshi Kadokura | |
| James C A Bardwell | |||
| Jon Beckwith | |||
| Thomas Zander | |||
| Hongping Tian | |||
| P433 | issue | 5657 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | protein folding | Q847556 |
| P304 | page(s) | 534-537 | |
| P577 | publication date | 2004-01-01 | |
| P1433 | published in | Science | Q192864 |
| P1476 | title | Snapshots of DsbA in action: detection of proteins in the process of oxidative folding | |
| P478 | volume | 303 |
| Q27667445 | A Disulfide Bridge Network within the Soluble Periplasmic Domain Determines Structure and Function of the Outer Membrane Protein RCSF |
| Q27657179 | A cis-Proline in -Hemoglobin Stabilizing Protein Directs the Structural Reorganization of -Hemoglobin |
| Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
| Q43228884 | A periplasmic reducing system protects single cysteine residues from oxidation |
| 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. |
| Q36954475 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. |
| Q33599927 | Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies |
| Q48160549 | Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay |
| Q35587095 | Characterization of protein cross-links via mass spectrometry and an open-modification search strategy. |
| Q41997244 | Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae |
| Q30277068 | Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein |
| Q38634845 | Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions. |
| Q41456212 | Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. |
| 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. |
| Q27656012 | Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE |
| Q27667359 | Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC |
| Q34828345 | Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. |
| Q37386934 | DSB proteins and bacterial pathogenicity. |
| Q35004080 | Detecting folding intermediates of a protein as it passes through the bacterial translocation channel |
| Q27644275 | Discovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked Chains |
| Q27680864 | Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa |
| Q41787799 | Disulfide bond formation and cysteine exclusion in gram-positive bacteria |
| Q37083585 | Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm |
| Q49788752 | Disulfide bond formation in prokaryotes |
| Q26823827 | Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead |
| Q30416941 | Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity |
| Q30155243 | Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export |
| Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
| Q34627585 | Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay |
| Q30376017 | Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems. |
| Q30427170 | DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system |
| Q24336855 | ERp57 is essential for efficient folding of glycoproteins sharing common structural domains |
| Q41912356 | Engineered pathways for correct disulfide bond oxidation |
| Q41891646 | Engineering Escherichia coli BL21(DE3) derivative strains to minimize E. coli protein contamination after purification by immobilized metal affinity chromatography |
| Q92945212 | Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli |
| Q89550640 | Escherichia coli Extract-Based Cell-Free Expression System as an Alternative for Difficult-to-Obtain Protein Biosynthesis |
| Q40702083 | F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues |
| Q30406080 | FipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation |
| Q42144045 | Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii |
| Q35236867 | Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA. |
| 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. |
| Q27675610 | Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′ |
| Q40447079 | Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms |
| Q34490362 | Identification of disulfide bond isomerase substrates reveals bacterial virulence factors. |
| Q27311872 | Identification of novel nuclear targets of human thioredoxin 1 |
| Q57471356 | Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family member |
| Q52314279 | Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase. |
| Q29616477 | Importing mitochondrial proteins: machineries and mechanisms |
| Q35933165 | Key players involved in bacterial disulfide-bond formation |
| Q30362756 | Laboratory evolution of one disulfide isomerase to resemble another |
| Q30301079 | Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization |
| Q59281484 | Ligand Binding Rapidly Induces Disulfide-dependent Dimerization of Glycoprotein VI on the Platelet Plasma Membrane |
| Q30152829 | Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane |
| Q24324109 | MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria |
| Q41460551 | Mapping native disulfide bonds at a proteome scale |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q57811254 | Methods to identify the substrates of thiol-disulfide oxidoreductases |
| Q36938873 | Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase |
| Q58003554 | Molecular Basis for Specificity of the Extracytoplasmic Thioredoxin ResA |
| Q35860792 | Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA |
| Q66680689 | Mutagenesis of DsbAss is Crucial for the Signal Recognition Particle Mechanism in : Insights from Molecular Dynamics Simulations |
| Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
| Q40943090 | Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily |
| Q33982252 | Nonconsecutive disulfide bond formation in an essential integral outer membrane protein |
| Q36195204 | Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. |
| Q36685039 | Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbA |
| Q27667688 | Oxidation State-dependent Protein-Protein Interactions in Disulfide Cascades |
| Q37194302 | Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis. |
| Q37406754 | Physical and functional interaction of transmembrane thioredoxin-related protein with major histocompatibility complex class I heavy chain: redox-based protein quality control and its potential relevance to immune responses |
| Q46945576 | Predicting disulfide connectivity from protein sequence using multiple sequence feature vectors and secondary structure. |
| Q27653607 | Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue |
| Q30153518 | Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli |
| Q42353700 | Protein folding drives disulfide formation |
| Q24791434 | Protein quality control in the bacterial periplasm |
| Q24797314 | Protein thiol modifications visualized in vivo |
| Q37895211 | Proteomic methods unravel the protein quality control in Escherichia coli |
| Q36751426 | Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. |
| Q34697369 | RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli |
| Q24630110 | Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase |
| 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 |
| Q34077220 | Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli |
| Q27680167 | Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases |
| Q34976588 | Severe zinc depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins |
| Q27649310 | Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding |
| Q27651712 | Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis |
| Q27684516 | Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori |
| Q27675432 | Structural and functional characterization of Helicobacter pylori DsbG |
| Q27678934 | Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c |
| Q34692501 | Substrate recognition by the protein disulfide isomerases |
| Q42208779 | Tailoring protein nanomechanics with chemical reactivity. |
| Q38956970 | The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites. |
| Q50301904 | The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli |
| Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
| 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 |
| Q47727168 | The TPR domain of BepA is required for productive interaction with substrate proteins and the β-barrel assembly machinery complex |
| Q39760295 | The active-site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilis |
| 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 |
| Q38189243 | The lipopolysaccharide export pathway in Escherichia coli: structure, organization and regulated assembly of the Lpt machinery |
| 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. |
| Q34172330 | The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin. |
| Q43018224 | The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme |
| Q44856945 | Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili |
| Q57751771 | Two pKM101-encoded proteins, the pilus-tip protein TraC and Pep, assemble on the Escherichia coli cell surface as adhesins required for efficient conjugative DNA transfer |
| Q51602297 | Use of the SHuffle Strains in Production of Proteins. |
| Q36242585 | Versatility of the endoplasmic reticulum protein folding factory |
| Q41481673 | YajL, prokaryotic homolog of parkinsonism-associated protein DJ-1, functions as a covalent chaperone for thiol proteome. |
| Q58112051 | cis-Proline Mutants of Quiescin Sulfhydryl Oxidase 1 With Altered Redox Properties Undermine ECM Integrity and Cell Adhesion in Fibroblast Cultures |
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