Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.
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Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant functionDisulphide production by Ero1α-PDI relay is rapid and effectively regulatedNovel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylationConserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regenerationPeptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesinThe Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bondsTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaVKORC1 and VKORC1L1: Why do Vertebrates Have Two Vitamin K 2,3-Epoxide Reductases?Disulfide bond formation in the bacterial periplasm: major achievements and challenges aheadSuperglue from bacteria: unbreakable bridges for protein nanotechnologyReducing systems protecting the bacterial cell envelope from oxidative damageThe 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 SITEStructure of a bacterial homologue of vitamin K epoxide reductaseStructural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumStructural Insight into Serine Protease Rv3671c that Protects M. tuberculosis from Oxidative and Acidic StressAtomic Resolution Insights into Curli Fiber BiogenesisStructural and functional characterization of Helicobacter pylori DsbGStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerStructural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar TyphimuriumStructure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969cDisarming Burkholderia pseudomallei : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In VivoRv2969c, 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 oxidasesStructural 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 ClassesDissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosaStructures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transferThe vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylationIdentification, activity and disulfide connectivity of C-di-GMP regulating proteins in Mycobacterium tuberculosisVirtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbANovel high throughput pooled shRNA screening identifies NQO1 as a potential drug target for host directed therapy for tuberculosisStructural basis for catalysis at the membrane-water interface.Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank.New pieces to an old puzzle: identifying the warfarin-binding site that prevents clotting.Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.Bacterial thiol oxidoreductases - from basic research to new antibacterial strategiesDisulfide bond formation in prokaryotes: history, diversity and designExpression and crystallization of SeDsbA, SeDsbL and SeSrgA from Salmonella enterica serovar Typhimurium.
P2860
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P2860
Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Bacterial species exhibit dive ...... tein disulfide bond formation.
@en
type
label
Bacterial species exhibit dive ...... tein disulfide bond formation.
@en
prefLabel
Bacterial species exhibit dive ...... tein disulfide bond formation.
@en
P2093
P2860
P356
P1476
Bacterial species exhibit dive ...... otein disulfide bond formation
@en
P2093
Jon Beckwith
Rachel J Dutton
P2860
P304
11933-11938
P356
10.1073/PNAS.0804621105
P407
P577
2008-08-11T00:00:00Z