Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin. - Wikidata - awgldk - TriplyDB

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

http://www.wikidata.org/entity/Q33591624

about

Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead Structure of a bacterial homologue of vitamin K epoxide reductase Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c 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 Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis The 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production Simultaneous analysis of multiple Mycobacterium tuberculosis knockdown mutants in vitro and in vivo Structural basis for catalysis at the membrane-water interface.New pieces to an old puzzle: identifying the warfarin-binding site that prevents clotting.Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.Evolutionary biochemistry: revealing the historical and physical causes of protein properties.Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria.Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells.Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis.Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis.Mechanisms of oxidative protein folding in the bacterial cell envelope.Integrating protein homeostasis strategies in prokaryotes.Coumarin-based drugs: a patent review (2008 -- present).Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1.Reoxidation of the Thiol-Disulfide Oxidoreductase MdbA by a Bacterial Vitamin K Epoxide Reductase in the Biofilm-Forming Actinobacterium Actinomyces oris.Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis.A new dihydrofuranocoumarin from Opopanax hispidus (Friv.) Griseb.The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain.Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB.Bioenergetics of Mycobacterium: An Emerging Landscape for Drug Discovery.

P2860

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P2860

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

http://www.wikidata.org/entity/Q33591624

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@ast

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@en

type

label

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@ast

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@en

prefLabel

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@ast

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@en

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

@en

P2093

April Wayman

http://www.w3.org/2001/XMLSchema#string

Dana Boyd

http://www.w3.org/2001/XMLSchema#string

Jon Beckwith

http://www.w3.org/2001/XMLSchema#string

Jun-Rong Wei

http://www.w3.org/2001/XMLSchema#string

Rachel J Dutton

http://www.w3.org/2001/XMLSchema#string

P2860

Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin

Controlling gene expression in mycobacteria with anhydrotetracycline and Tet repressor

Clustal W and Clustal X version 2.0

Genes required for mycobacterial growth defined by high density mutagenesis

Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2

Identification of the gene for vitamin K epoxide reductase

Vitamin K epoxide reductase: homology, active site and catalytic mechanism

VKORC1 and the vitamin K cycle

Rapid, low-technology MIC determination with clinical Mycobacterium tuberculosis isolates by using the microplate Alamar Blue assay

The genetic basis of resistance to anticoagulants in rodents

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anticoagulation

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