About: Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis

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rdf:type	Item
description	vědecký článek publikovaný v roce 1995 (cs) artículu científicu espublizáu en 1995 (ast) 1995 թվականի հուլիսին հրատարակված գիտական հոդված (hy) 1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в липні 1995 (uk) wetenschappelijk artikel (gepubliceerd op 1995/07/04) (nl) vedecký článok (publikovaný 1995/07/04) (sk) مقالة علمية (نشرت في 4-7-1995) (ar) article scientifique publié en 1995 (fr) scientific journal article (en) im Juli 1995 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q28487275-1429EC17-00C4-46DA-AB2B-E4926438B7E5
publication date	1995-07-04 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28487275-4FA84444-A0C2-4B95-93F1-2BA07CD4FF05
language of work or name	English
author name string	wds:Q28487275-09EFA12A-6EFA-43A6-9EEA-F7B11FFDA4FC wds:Q28487275-1920E200-144E-4FDE-A015-EA33F5028F5E wds:Q28487275-49896FB6-3680-4B0C-BCA7-DE11FB40A9B1 wds:Q28487275-5BE9F597-E090-4AFC-BD45-8B83E7AE59E1 wds:Q28487275-92072838-34EE-4186-AE0F-3A68F55CDAFD wds:Q28487275-AC80A69C-06B6-4CB0-BCBF-1A622F4C6F96 wds:Q28487275-FC8463B5-82C9-4802-8D9B-FDA29DCDCD44
author name string	A. Quémard J. C. Sacchettini W. R. Jacobs R. Bittman A. Dessen C. Vilcheze J. S. Blanchard
rdfs:label	Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (en) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (nl) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (ast)
skos:prefLabel	Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (en) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (nl) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (ast)
name	Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (en) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (nl) Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (ast)
title	wds:Q28487275-C09AEF54-D62C-4F91-9E07-AB11663D7A66
title	Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis (en)
page(s)	wds:Q28487275-338C2857-ECAB-4C67-8374-02D60F4053DF
page(s)	8235–8241
instance of	wds:Q28487275-14F3022F-2AE1-42A8-A7DD-4942FA65A3C9
instance of	scholarly article
main subject	wds:Q28487275-1083C563-0D42-4D30-8B1B-C24780E88A9E wds:Q28487275-5A71034E-42F6-4458-A032-17C29EC676EE wds:Q28487275-6C660791-6632-4BA7-A11E-2705D5187100
main subject	Mycobacterium tuberculosis tuberculosis isoniazid
PubMed ID	wds:Q28487275-8720191C-3AED-41B7-99AB-0E3793DB975F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7599116
PubMed ID	7599116
published in	wds:Q28487275-A2691A12-7B69-48B8-9685-76564B5541CC
published in	Biochemistry
issue	wds:Q28487275-3388EBEE-B769-4082-9884-F101427C5114
volume	wds:Q28487275-EBDBCE50-4130-4B3E-92CD-B3C903A0C7AF
issue	26
volume	34
DOI	wds:Q28487275-D608AB20-876E-4C02-B895-2F4C271318BD
DOI	http://dx.doi.org/10.1021/BI00026A004
DOI	10.1021/BI00026A004
Fatcat ID	wds:Q28487275-721A5030-8097-40F6-B0D8-F1035BD47983
Fatcat ID	release_5ljihn3ktrhsdpgk3fmp4kxzwe
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28487275
is cites work of	Mycobacterium tuberculosis genes induced during infection of human macrophages Redox homeostasis in mycobacteria: the key to tuberculosis control? Mycobacterium tuberculosis WhiB3: a novel iron-sulfur cluster protein that regulates redox homeostasis and virulence. Polyketide versatility in the biosynthesis of complex mycobacterial cell wall lipids Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis Towards a new tuberculosis drug: pyridomycin - nature's isoniazid Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism Metamorphic enzyme assembly in polyketide diversification Antimycobacterial action of thiolactomycin: an inhibitor of fatty acid and mycolic acid synthesis Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis Revisiting the assignment of Rv0241c to fatty acid synthase type II of Mycobacterium tuberculosis Lipid biosynthesis as a target for antibacterial agents AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis Antimycobacterial activities of isoxyl and new derivatives through the inhibition of mycolic acid synthesis Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis The envelope layers of mycobacteria with reference to their pathogenicity. Novel mutations in ndh in isoniazid-resistant Mycobacterium tuberculosis isolates In vitro inhibition of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA by isoniazid Detection of first- and second-line drug resistance in Mycobacterium tuberculosis clinical isolates by pyrosequencing Substrate recognition by β-ketoacyl-ACP synthases. The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis Exploring drug-induced alterations in gene expression in Mycobacterium tuberculosis by microarray hybridization Multidrug-resistant Mycobacterium tuberculosis: molecular perspectives Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan. Mn(III) pyrophosphate as an efficient tool for studying the mode of action of isoniazid on the InhA protein of Mycobacterium tuberculosis Overexpression of inhA, but not kasA, confers resistance to isoniazid and ethionamide in Mycobacterium smegmatis, M. bovis BCG and M. tuberculosis

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