about
targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysisGlutamine synthetase sequence evolution in the mycobacteria and their use as molecular markers for Actinobacteria speciationComprehensive identification of conditionally essential genes in mycobacteriaCharacterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug developmentThe structure of Mycobacteria 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase, an essential enzyme, provides a platform for drug discoveryCharacterization of Active Site Structure in CYP121: A CYTOCHROME P450 ESSENTIAL FOR VIABILITY OF MYCOBACTERIUM TUBERCULOSIS H37RvPrioritizing genomic drug targets in pathogens: application to Mycobacterium tuberculosisFunctional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosisProtection elicited by two glutamine auxotrophs of Mycobacterium tuberculosis and in vivo growth phenotypes of the four unique glutamine synthetase mutants in a murine modelAll four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasisThe role of GlnD in ammonia assimilation in Mycobacterium tuberculosisideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress responseAdenylylation of mycobacterial Glnk (PII) protein is induced by nitrogen limitationMycothiol is essential for growth of Mycobacterium tuberculosis ErdmanProbing host pathogen cross-talk by transcriptional profiling of both Mycobacterium tuberculosis and infected human dendritic cells and macrophages.Nitrogen control in Mycobacterium smegmatis: nitrogen-dependent expression of ammonium transport and assimilation proteins depends on the OmpR-type regulator GlnRGlutamate dehydrogenase and glutamine synthetase are regulated in response to nitrogen availability in Myocbacterium smegmatisPoly-L-glutamate/glutamine synthesis in the cell wall of Mycobacterium bovis is regulated in response to nitrogen availability.The role of glutamine oxoglutarate aminotransferase and glutamate dehydrogenase in nitrogen metabolism in Mycobacterium bovis BCG.New targets and inhibitors of mycobacterial sulfur metabolism.The Transcriptional Repressor, MtrR, of the mtrCDE Efflux Pump Operon of Neisseria gonorrhoeae Can Also Serve as an Activator of "off Target" Gene (glnE) ExpressionPhylogenomic exploration of the relationships between strains of Mycobacterium avium subspecies paratuberculosisThe Mycobacterium tuberculosis MEP (2C-methyl-d-erythritol 4-phosphate) pathway as a new drug target.P(II) signal transduction proteins: nitrogen regulation and beyond.Ammonia assimilation in rumen bacteria: a review.Nitrogen metabolism in Mycobacterium tuberculosis physiology and virulence.Methionine sulfoximine resistance in Mycobacterium tuberculosis is due to a single nucleotide deletion resulting in increased expression of the major glutamine synthetase, GlnA1.Development of new antituberculous agents based on new drug targets and structure-activity relationship.Targeted gene knockout and essentiality testing by homologous recombination.Inhibition of the sole type I signal peptidase of Mycobacterium tuberculosis is bactericidal under replicating and nonreplicating conditions.Essentiality of succinate dehydrogenase in Mycobacterium smegmatis and its role in the generation of the membrane potential under hypoxia.Use of a tetracycline-inducible system for conditional expression in Mycobacterium tuberculosis and Mycobacterium smegmatis.Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus mycobacteria.
P2860
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P2860
description
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im Oktober 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/10/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/10/01)
@nl
наукова стаття, опублікована в жовтні 2000
@uk
مقالة علمية (نشرت في أكتوبر 2000)
@ar
name
glnE is an essential gene in Mycobacterium tuberculosis
@ast
glnE is an essential gene in Mycobacterium tuberculosis
@en
glnE is an essential gene in Mycobacterium tuberculosis
@nl
type
label
glnE is an essential gene in Mycobacterium tuberculosis
@ast
glnE is an essential gene in Mycobacterium tuberculosis
@en
glnE is an essential gene in Mycobacterium tuberculosis
@nl
prefLabel
glnE is an essential gene in Mycobacterium tuberculosis
@ast
glnE is an essential gene in Mycobacterium tuberculosis
@en
glnE is an essential gene in Mycobacterium tuberculosis
@nl
P2860
P1476
glnE is an essential gene in Mycobacterium tuberculosis
@en
P2093
N. G. Stoker
P2860
P304
P356
10.1128/JB.182.20.5715-5720.2000
P407
P577
2000-10-01T00:00:00Z