Characterization of a Carbon-Carbon Hydrolase from Mycobacterium tuberculosis Involved in Cholesterol Metabolism
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Pathogen roid rage: cholesterol utilization by Mycobacterium tuberculosisA flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolismActivity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosisCharacterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatisThe Lid Domain of the MCP Hydrolase DxnB2 Contributes to the Reactivity toward Recalcitrant PCB MetabolitesA Substrate-Assisted Mechanism of Nucleophile Activation in a Ser–His–Asp Containing C–C Bond HydrolaseStructure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversityShrinking the FadE proteome of Mycobacterium tuberculosis: insights into cholesterol metabolism through identification of an α2β2 heterotetrameric acyl coenzyme A dehydrogenase familyPathway profiling in Mycobacterium tuberculosis: elucidation of cholesterol-derived catabolite and enzymes that catalyze its metabolismNovel inhibitors of cholesterol degradation in Mycobacterium tuberculosis reveal how the bacterium's metabolism is constrained by the intracellular environmentPathogenic mycobacteria achieve cellular persistence by inhibiting the Niemann-Pick Type C disease cellular pathwayIdentification of arylamine N-acetyltransferase inhibitors as an approach towards novel anti-tubercularsCatabolism and biotechnological applications of cholesterol degrading bacteria.Accurate macromolecular crystallographic refinement: incorporation of the linear scaling, semiempirical quantum-mechanics program DivCon into the PHENIX refinement packageInhibition of the M. tuberculosis 3β-hydroxysteroid dehydrogenase by azasteroids.Cholesterol catabolism as a therapeutic target in Mycobacterium tuberculosis.The tuberculosis drug discovery and development pipeline and emerging drug targets.Investigation of the mycobacterial enzyme HsaD as a potential novel target for anti-tubercular agents using a fragment-based drug design approach.The Minimal Unit of Infection: Mycobacterium tuberculosis in the Macrophage.Bacterial degradation of bile salts.Adventures in Rhodococcus - from steroids to explosives.The Mycobacterium tuberculosis cytochromes P450: physiology, biochemistry & molecular intervention.Updating and curating metabolic pathways of TB.3-Ketosteroid 9α-hydroxylase enzymes: Rieske non-heme monooxygenases essential for bacterial steroid degradation.Tuberculosis drug discovery and emerging targets.Genome-wide bioinformatics analysis of steroid metabolism-associated genes in Nocardioides simplex VKM Ac-2033D.Cholesterol metabolism: a potential therapeutic target in Mycobacteria.Deciphering the transcriptional regulation of cholesterol catabolic pathway in mycobacteria: identification of the inducer of KstR repressor.Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site.Characterization of the KstR2 regulator responsible of the lower cholesterol degradative pathway in Mycobacterium smegmatis.Cyclipostins and Cyclophostin analogs as promising compounds in the fight against tuberculosis.The essential function of genes for a hydratase and an aldehyde dehydrogenase for growth of Pseudomonas sp. strain Chol1 with the steroid compound cholate indicates an aldolytic reaction step for deacetylation of the side chainDetection of Delta-like 1 ligand for the diagnosis of tuberculous meningitis: An effective and rapid diagnostic method.Characterisation of a putative AraC transcriptional regulator from Mycobacterium smegmatis.TB Summit 2014: prevention, diagnosis, and treatment of tuberculosis-a meeting report of a Euroscicon conference.Degradation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1 proceeds via an aldehyde intermediate.Regulation of the KstR2 regulon of Mycobacterium tuberculosis by a cholesterol catabolite.Tuning the substrate selectivity of meta-cleavage product hydrolase by domain swapping.
P2860
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P2860
Characterization of a Carbon-Carbon Hydrolase from Mycobacterium tuberculosis Involved in Cholesterol Metabolism
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին 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
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@ast
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@en
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@nl
type
label
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@ast
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@en
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@nl
prefLabel
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@ast
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@en
Characterization of a Carbon-C ...... lved in Cholesterol Metabolism
@nl
P2093
P2860
P50
P3181
P356
P1476
Characterization of a carbon-c ...... lved in cholesterol metabolism
@en
P2093
Edward D Lowe
Katherine C Yam
Nathan A Lack
Robin L Owen
P2860
P304
P3181
P356
10.1074/JBC.M109.058081
P407
P577
2009-10-29T00:00:00Z