Identification of a protein required for disulfide bond formation in vivo.
about
Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)Salmonella typhimurium encodes an SdiA homolog, a putative quorum sensor of the LuxR family, that regulates genes on the virulence plasmid.Active cytotoxic necrotizing factor 1 associated with outer membrane vesicles from uropathogenic Escherichia coli.Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumA pathway for disulfide bond formation in vivoTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaPlants and animals share functionally common bacterial virulence factorsEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmThe zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPaseUse of model plant hosts to identify Pseudomonas aeruginosa virulence factorsYeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulumOxidative protein folding in eukaryotes: mechanisms and consequencesProtein thiol modifications visualized in vivoTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaDisulfide bond formation in the bacterial periplasm: major achievements and challenges aheadMany roles of the bacterial envelope reducing pathwaysOrchestration of secretory protein folding by ER chaperonesReducing systems protecting the bacterial cell envelope from oxidative damageShedding light on disulfide bond formation: engineering a redox switch in green fluorescent proteinThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosisThe oxidase DsbA folds a protein with a nonconsecutive disulfideStructural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidisPreparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBNMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.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 EnzymesCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEIntramolecular amide bonds stabilize pili on the surface of bacilliAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisStructural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumCrystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbCDisarming Burkholderia pseudomallei : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In VivoStructural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosisComparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct ClassesThe Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide IsomeraseDissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosaAn Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold
P2860
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P2860
Identification of a protein required for disulfide bond formation in vivo.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Identification of a protein required for disulfide bond formation in vivo.
@en
Identification of a protein required for disulfide bond formation in vivo.
@nl
type
label
Identification of a protein required for disulfide bond formation in vivo.
@en
Identification of a protein required for disulfide bond formation in vivo.
@nl
prefLabel
Identification of a protein required for disulfide bond formation in vivo.
@en
Identification of a protein required for disulfide bond formation in vivo.
@nl
P2093
P1433
P1476
Identification of a protein required for disulfide bond formation in vivo.
@en
P2093
Bardwell JC
Beckwith J
McGovern K
P304
P356
10.1016/0092-8674(91)90532-4
P407
P577
1991-11-01T00:00:00Z