Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824
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Development of a Bioluminescent Nitroreductase Probe for Preclinical ImagingRv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosisPentacyclic nitrofurans with in vivo efficacy and activity against nonreplicating Mycobacterium tuberculosisActivation of Bicyclic Nitro-drugs by a Novel Nitroreductase (NTR2) in LeishmaniaMolecular insights into the binding of coenzyme F420 to the conserved protein Rv1155 from Mycobacterium tuberculosis.Mycobacterial F420H2-Dependent Reductases Promiscuously Reduce Diverse Compounds through a Common Mechanism.Bactericidal activity of PA-824 against Mycobacterium tuberculosis under anaerobic conditions and computational analysis of its novel analogues against mutant Ddn receptorMutations in genes for the F420 biosynthetic pathway and a nitroreductase enzyme are the primary resistance determinants in spontaneous in vitro-selected PA-824-resistant mutants of Mycobacterium tuberculosisA novel F(420) -dependent anti-oxidant mechanism protects Mycobacterium tuberculosis against oxidative stress and bactericidal agentsPhysiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Thiolates chemically induce redox activation of BTZ043 and related potent nitroaromatic anti-tuberculosis agentsThe redox cofactor F420 protects mycobacteria from diverse antimicrobial compounds and mediates a reductive detoxification system.Oxidative Phosphorylation as a Target Space for Tuberculosis: Success, Caution, and Future Directions.Antimycobacterial Metabolism: Illuminating Mycobacterium tuberculosis Biology and Drug Discovery.Nitroarenes as Antitubercular Agents: Stereoelectronic Modulation to Mitigate Mutagenicity.Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases3D-QSAR and cell wall permeability of antitubercular nitroimidazoles against Mycobacterium tuberculosis.Update of Antitubercular Prodrugs from a Molecular Perspective: Mechanisms of Action, Bioactivation Pathways, and Associated Resistance.Design of 2-Nitroimidazooxazine Derivatives as Deazaflavin-Dependent Nitroreductase (Ddn) Activators as Anti-Mycobacterial Agents Based on 3D QSAR, HQSAR, and Docking Study with In Silico Prediction of Activity and Toxicity.Untargeted metabolomics reveals a new mode of action of pretomanid (PA-824).Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis
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P2860
Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@ast
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@en
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@nl
type
label
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@ast
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@en
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@nl
prefLabel
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@ast
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@en
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@nl
P2093
P2860
P50
P921
P3181
P1433
P1476
Structure of Ddn, the Deazafla ...... reductive Activation of PA-824
@en
P2093
Amit Nayyar
Badry Bursulaya
Bernhard H Geierstanger
David H Jones
Helena I Boshoff
Inhee Choi
Jennifer Shaffer
Meera Gurumurthy
Pornwaratt Niyomrattanakit
Susan E Cellitti
P2860
P304
P3181
P356
10.1016/J.STR.2011.11.001
P577
2012-01-11T00:00:00Z