scholarly article | Q13442814 |
review article | Q7318358 |
P356 | DOI | 10.1016/S0092-8674(00)81642-6 |
P698 | PubMed publication ID | 10535729 |
P50 | author | Laurent Debarbieux | Q42867472 |
P2093 | author name string | Beckwith J | |
Debarbieux L | |||
P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain | Q24653700 | ||
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum | Q27936188 | ||
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum | Q27939552 | ||
Thioredoxin--a fold for all reasons | Q29618984 | ||
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics | Q33537167 | ||
The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm | Q33551316 | ||
Making and breaking disulfide bonds | Q41620623 | ||
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 | Q42271387 | ||
Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway | Q42668332 | ||
Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. | Q54593983 | ||
A pleîotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA | Q72697656 | ||
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
Competition between glutathione and protein thiols for disulphide-bond formation | Q73177752 | ||
Scanning and escape during protein-disulfide isomerase-assisted protein folding | Q73182455 | ||
The genetics of disulfide bond metabolism | Q77936221 | ||
Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 117-119 | |
P577 | publication date | 1999-10-01 | |
P1433 | published in | Cell | Q655814 |
P1476 | title | Electron avenue: pathways of disulfide bond formation and isomerization | |
P478 | volume | 99 |
Q43769888 | Amount and redox state of cytoplasmic, membrane and periplasmic proteins in Escherichia coli redox mutants |
Q34637794 | An attractive surface: gram-negative bacterial biofilms |
Q39244663 | An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding |
Q50498506 | AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. |
Q34472653 | Application of the S-pyridylethylation reaction to the elucidation of the structures and functions of proteins |
Q29999427 | Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule Mimics |
Q44533393 | Catalysis of protein folding by an immobilized small-molecule dithiol |
Q41982341 | Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase |
Q34398278 | Clostridium botulinum and its neurotoxins: a metabolic and cellular perspective |
Q34067229 | Complete pathway for protein disulfide bond formation encoded by poxviruses |
Q33996659 | Computation-directed identification of OxyR DNA binding sites in Escherichia coli |
Q28366798 | Coordinate gene regulation by fimbriae-induced signal transduction |
Q34828345 | Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. |
Q90464561 | Disulfide Chaperone Knockouts Enable In Vivo Double Spin Labeling of an Outer Membrane Transporter |
Q73897313 | Disulfide bonds are generated by quinone reduction |
Q82248735 | Disulfide chromophore and its optical activity |
Q39501974 | DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa |
Q31583197 | DsbD-catalyzed transport of electrons across the membrane of Escherichia coli |
Q24292308 | ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family |
Q74273264 | Expression of a TGF-beta superfamily protein, macrophage inhibitory cytokine-1, in the yeast Pichia pastoris |
Q44652130 | FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes |
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. |
Q27631272 | Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a |
Q33904926 | Genes required for cytochrome c synthesis in Bacillus subtilis |
Q35713362 | Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDI |
Q46583622 | Hemextin AB complex, a unique anticoagulant protein complex from Hemachatus haemachatus (African Ringhals cobra) venom that inhibits clot initiation and factor VIIa activity. |
Q43792245 | Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. |
Q48341081 | Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium |
Q39714223 | Just toothpicks and logic: how some labs succeed at solving complex problems |
Q34046362 | Native disulfide bond formation in proteins |
Q39487446 | Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli |
Q28141294 | Pathways for protein disulphide bond formation |
Q33211413 | Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli |
Q34594251 | Redox reactions of regulatory proteins: do kinetics promote specificity? |
Q37264681 | Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli |
Q40739794 | Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function |
Q27635911 | Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein |
Q27639369 | Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment |
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 |
Q35195303 | The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology. |
Q35140826 | The art and design of genetic screens: Escherichia coli |
Q27639655 | The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex |
Q52107363 | The sigmaE regulon and the identification of additional sporulation genes in Bacillus subtilis. |
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 |
Q38775588 | Towards clinical development of a Pfs48/45-based transmission blocking malaria vaccine |
Q39714839 | Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. |
Q24550637 | Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum |
Q84509431 | Vibrational and electronic optical activity of the chiral disulphide group: implications for disulphide bridge conformation |
Search more.