Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis
about
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolismRegulating the Intersection of Metabolism and Pathogenesis in Gram-positive BacteriaStructure-Guided Discovery of Phenyl-diketo Acids as Potent Inhibitors of M. tuberculosis Malate SynthasePhylogenetic analysis of vitamin B12-related metabolism in Mycobacterium tuberculosis.Potential inhibitors for isocitrate lyase of Mycobacterium tuberculosis and non-M. tuberculosis: a summaryNew insights into TB physiology suggest untapped therapeutic opportunitiesSimultaneous analysis of multiple Mycobacterium tuberculosis knockdown mutants in vitro and in vivoRole of the transcriptional regulator RamB (Rv0465c) in the control of the glyoxylate cycle in Mycobacterium tuberculosisRegulation of central metabolism genes of Mycobacterium tuberculosis by parallel feed-forward loops controlled by sigma factor E (σ(E))Cholesterol catabolism by Mycobacterium tuberculosis requires transcriptional and metabolic adaptationsFunctional characterization of a vitamin B12-dependent methylmalonyl pathway in Mycobacterium tuberculosis: implications for propionate metabolism during growth on fatty acidsA novel role of the PrpR as a transcription factor involved in the regulation of methylcitrate pathway in Mycobacterium tuberculosisNovel inhibitors of cholesterol degradation in Mycobacterium tuberculosis reveal how the bacterium's metabolism is constrained by the intracellular environmentGenomic versatility and functional variation between two dominant heterotrophic symbionts of deep-sea Osedax wormsMetabolic Perspectives on PersistenceRedundancy control in pathway databases (ReCiPa): an application for improving gene-set enrichment analysis in Omics studies and "Big data" biology.A systems biology framework for modeling metabolic enzyme inhibition of Mycobacterium tuberculosis.The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin.The growth and survival of Mycobacterium smegmatis is enhanced by co-metabolism of atmospheric H2.Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infectionPathway-selective sensitization of Mycobacterium tuberculosis for target-based whole-cell screeningCarbon flux rerouting during Mycobacterium tuberculosis growth arrest.The Sculpting of the Mycobacterium tuberculosis Genome by Host Cell-Derived PressuresTrans-species communication in the Mycobacterium tuberculosis-infected macrophageA chemical genetic screen in Mycobacterium tuberculosis identifies carbon-source-dependent growth inhibitors devoid of in vivo efficacy.The tuberculosis drug discovery and development pipeline and emerging drug targets.Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.Role of Alanine Dehydrogenase of Mycobacterium tuberculosis during Recovery from Hypoxic Nonreplicating Persistence.Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial PhosphataseNonsteroidal anti-inflammatory drug sensitizes Mycobacterium tuberculosis to endogenous and exogenous antimicrobialsOverexpression of the Rv0805 phosphodiesterase elicits a cAMP-independent transcriptional responseTranscriptional Profiling of Mycobacterium tuberculosis Exposed to In Vitro Lysosomal Stress.Roles of the glyoxylate and methylcitrate cycles in sexual development and virulence in the cereal pathogen Gibberella zeae.The Minimal Unit of Infection: Mycobacterium tuberculosis in the Macrophage.Methylcitrate cycle defines the bactericidal essentiality of isocitrate lyase for survival of Mycobacterium tuberculosis on fatty acidsModulation of Central Carbon Metabolism by Acetylation of Isocitrate Lyase in Mycobacterium tuberculosis.Recent advances in antituberculous drug development and novel drug targets.Protein targets for structure-based anti-Mycobacterium tuberculosis drug discovery.Genes and regulatory networks involved in persistence of Mycobacterium tuberculosis.Hijacking and Use of Host Lipids by Intracellular Pathogens.
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P2860
Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis
description
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im August 2006 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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vedecký článok (publikovaný 2006/08/01)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/08/01)
@nl
наукова стаття, опублікована в серпні 2006
@uk
مقالة علمية (نشرت في أغسطس 2006)
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name
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@ast
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@en
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@nl
type
label
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@ast
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@en
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@nl
prefLabel
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@ast
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@en
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@nl
P2093
P2860
P3181
P1476
Dual role of isocitrate lyase ...... in Mycobacterium tuberculosis
@en
P2093
Ernesto J. Muñoz-Elías
Helmus van de Langemheen
James C. Sacchettini
John D. McKinney
Ty A. Gould
P2860
P304
P3181
P356
10.1111/J.1365-2958.2006.05297.X
P407
P577
2006-08-01T00:00:00Z