About: Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis

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About: Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 1997 (ast) vědecký článek publikovaný v roce 1997 (cs) 1997 թուականի Յունուարին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в січні 1997 (uk) 1997 թվականի հունվարին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1997/01/31) (sk) مقالة علمية (نشرت في 31-1-1997) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) wetenschappelijk artikel (gepubliceerd op 1997/01/31) (nl) scientific journal article (en) im Januar 1997 veröffentlichter wissenschaftlicher Artikel (de) 1997 ജനുവരി 31 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
publication date	wds:Q28486741-E8217AB9-D6DC-410D-99E4-5833826FB591
publication date	1997-01-31 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28486741-8666FEA6-0795-4827-8B44-4AEB827B9ED7
language of work or name	English
cites work	wds:Q28486741-03C57DAD-1952-49AE-AAA2-DBA58ACA3FC0 wds:Q28486741-069F6BE5-F2BD-4EF5-BD54-F56435997D95 wds:Q28486741-14853AAE-6902-4952-9C15-4D2684FB5589 wds:Q28486741-18E545A1-9643-49AE-8325-A1C512B15E86 wds:Q28486741-1928AA53-9454-427F-B214-9A1973CF628A wds:Q28486741-1D86BFDE-6A0F-4D13-8D6A-42C46F2BDFB2 wds:Q28486741-1DD3545E-EFC0-48A8-81C0-7747A70209CB wds:Q28486741-23AC16EE-A958-43F8-BE06-7283FC42D337 wds:Q28486741-25272813-664F-4D46-9CD3-C12BA8BF00EA wds:Q28486741-25929A40-776D-4E30-A90C-FE341C673CBF wds:Q28486741-370D3559-966E-4A02-B342-A8E50C770D34 wds:Q28486741-4259E5A9-5851-404A-B2CB-3E5225643910 wds:Q28486741-4DCD41CE-F85A-4ED5-AA17-5102FE70051E wds:Q28486741-54B2DCC3-16BD-4225-A41D-99E90DDE3EFB wds:Q28486741-5782971B-FB3C-44ED-87F9-E9353A90B4A2 wds:Q28486741-585C569C-61AC-4E81-8706-E4550399F8B0 wds:Q28486741-681E3FF4-558F-43E4-BFF8-E6D6A3DAA398 wds:Q28486741-77FE56C5-CDD3-4803-8BB1-23E6C7EF6233 wds:Q28486741-780960DE-0A08-4F2D-89C7-0CC7835A7847 wds:Q28486741-7BD2B007-3FB4-4FC0-AB28-66CD2BC79F26 wds:Q28486741-88690917-CC31-42E5-8D34-A78650603FE3 wds:Q28486741-8C7526C4-5216-4F6C-BF0F-437364A5F226 wds:Q28486741-93B93F3E-CEE0-4E32-AB6D-31D83E78B0D4 wds:Q28486741-9F84214D-EAD7-4979-921B-38AB74ADAA93 wds:Q28486741-A17F7F12-8BBD-4298-810E-CD3A73F8ED44 wds:Q28486741-A506CAC3-901A-4027-9BEF-17828DCADEE7 wds:Q28486741-AA17C8DC-46DE-42D4-BB86-2B15378414BE wds:Q28486741-B06950C3-D8C5-42FE-90BF-67ECB7B67FA6 wds:Q28486741-B63E9669-8DFD-46B8-AD5C-850DA9B693C3 wds:Q28486741-BC4B3F14-1630-4598-9ECD-3C74DD9B05D8 wds:Q28486741-BF83A507-E21F-4EE4-B093-EA91E7504BCE wds:Q28486741-BFC3DC3F-4B39-4767-B8B6-A3A0821C319F wds:Q28486741-CE6446AE-97C3-45A4-8F91-637E0757A416 wds:Q28486741-D42F2B12-71A9-452C-A2C9-C6B5733C9B7F wds:Q28486741-D95B2EB6-7BB4-48BF-AD28-F6F8638F799D wds:Q28486741-E2841420-1CC1-4A1B-937F-45530CEFADB8 wds:Q28486741-F00F85F6-3C40-47C5-A808-85324D7BFC30 wds:Q28486741-F47C436A-BE71-4FE4-AFFC-18DE6E6EF9C4 wds:Q28486741-F84B684C-1EF7-4050-ADCF-00CEEE601D8B wds:Q28486741-F92973D7-8D18-42A8-A35E-BC8D6A8FA68B wds:Q28486741-FD738C86-A8B6-40EA-8AAD-0646F77E63FD
cites work	The global tuberculosis situation and the new control strategy of the World Health Organization Tuberculosis: commentary on a reemergent killer Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Electron paramagnetic resonance detectable states of cytochrome P-450cam Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH. Tubercolosis: a neglected disease strikes back A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and -susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: restricted array of mutations associated with drug resistance. The purification and properties of peroxidase in Mycobacterium tuberculosis H37Rv and its possible role in the mechanism of action of isonicotinic acid hydrazide Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum Mutations in katG gene sequences in isoniazid-resistant clinical isolates of Mycobacterium tuberculosis are rare Resonance Raman spectra of horseradish peroxidase: evidence for anomalous heme structure Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes Catalase of Neurospora crassa. 1. Induction, purification, and physical properties The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation Molecular cloning, sequence analysis and expression of the gene for catalase-peroxidase (cpeA) from the photosynthetic bacterium Rhodobacter capsulatus B10. Purification and properties of a halophilic catalase-peroxidase from Haloarcula marismortui Thermostable peroxidase from Bacillus stearothermophilus. Rapid identification of a point mutation of the Mycobacterium tuberculosis catalase-peroxidase (katG) gene associated with isoniazid resistance. Purification and characterization of catalase from a facultative alkalophilic Bacillus. Molecular characterization of three mutations in katG affecting the activity of hydroperoxidase I of Escherichia coli A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels Isolation and characterization of catalase produced by Mycobacterium tuberculosis Comparison of isoniazid oxidation catalyzed by bacterial catalase-peroxidases and horseradish peroxidase Progress in the characterization of catalase-peroxidase from Mycobacterium tuberculosis Molecular mechanisms of multiple drug resistance in clinical isolates of Mycobacterium tuberculosis Spectral characterization and chemical modification of catalase-peroxidase from Streptomyces sp Catalase activity at high concentration of hydrogen peroxide Purification and properties of a peroxidase from Halobacterium halobium L-33 Characterization of the katG and inhA genes of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis Tuberculosis. Beating the bacillus The emergence of drug-resistant tuberculosis in New York City
author name string	wds:Q28486741-1F3FA9A4-13D3-425E-9524-EDE3E8AF1EEB

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