Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance
about
Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatisStructure of RdxA--an oxygen-insensitive nitroreductase essential for metronidazole activation in Helicobacter pyloriCrystal Structure of Reduced MsAcg, a Putative Nitroreductase from Mycobacterium smegmatis and a Close Homologue of Mycobacterium tuberculosis AcgStructural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitorsTowards a new combination therapy for tuberculosis with next generation benzothiazinonesMolecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanismDecaprenylphosphoryl-β-D-ribose 2'-epimerase, the target of benzothiazinones and dinitrobenzamides, is an essential enzyme in Mycobacterium smegmatisNew Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in MycobacteriaComputational databases, pathway and cheminformatics tools for tuberculosis drug discovery.Comparative genomics of the dormancy regulons in mycobacteriaCrystal structure of the fungal nitroreductase Frm2 from Saccharomyces cerevisiae.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.Arabinogalactan and lipoarabinomannan biosynthesis: structure, biogenesis and their potential as drug targets.Antituberculars which target decaprenylphosphoryl-β-D-ribofuranose 2'-oxidase DprE1: state of art.Antimycobacterial drugs currently in Phase II clinical trials and preclinical phase for tuberculosis treatment.The DprE1 enzyme, one of the most vulnerable targets of Mycobacterium tuberculosis.Drug Resistance Mechanisms in Mycobacterium tuberculosis.Synthesis of 2-(2,4-dihydroxyphenyl)thieno-1,3-thiazin-4-ones, their lipophilicity and anticancer activity in vitro.Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis.Nitroarenes as Antitubercular Agents: Stereoelectronic Modulation to Mitigate Mutagenicity.Understanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism.Benzothiazinones mediate killing of Corynebacterineae by blocking decaprenyl phosphate recycling involved in cell wall biosynthesis.Evolutionary and molecular foundations of multiple contemporary functions of the nitroreductase superfamily.A Novel Mechanism of Inactivating Antibacterial Nitro Compounds in the Human Pathogen Staphylococcus aureus by Overexpression of a NADH-Dependent Flavin Nitroreductase.Molecular Targets Related Drug Resistance Mechanisms in MDR-, XDR-, and TDR-Mycobacterium tuberculosis Strains.Decaprenyl-phosphoryl-ribose 2'-epimerase (DprE1): challenging target for antitubercular drug discovery.Challenging the Drug-Likeness Dogma for New Drug Discovery in Tuberculosis
P2860
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
P2860
Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Biological and structural char ...... in benzothiazinone resistance
@ast
Biological and structural char ...... in benzothiazinone resistance
@en
Biological and structural char ...... in benzothiazinone resistance
@nl
type
label
Biological and structural char ...... in benzothiazinone resistance
@ast
Biological and structural char ...... in benzothiazinone resistance
@en
Biological and structural char ...... in benzothiazinone resistance
@nl
prefLabel
Biological and structural char ...... in benzothiazinone resistance
@ast
Biological and structural char ...... in benzothiazinone resistance
@en
Biological and structural char ...... in benzothiazinone resistance
@nl
P2093
P50
P1476
Biological and structural char ...... in benzothiazinone resistance
@en
P2093
Ana Luisa De Jesus Lopes Ribeiro
Anna Milano
Anna Paola Lucarelli
Aurora Piazza
David Giganti
Edda De Rossi
Elena Salina
Giulia Degiacomi
Giulia Manina
Henrieta Skovierová
P2860
P304
P356
10.1111/J.1365-2958.2010.07277.X
P407
P50
P577
2010-09-01T00:00:00Z