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New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP.

作者信息

Argyrou Argyrides, Vetting Matthew W, Blanchard John S

机构信息

Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.

出版信息

J Am Chem Soc. 2007 Aug 8;129(31):9582-3. doi: 10.1021/ja073160k. Epub 2007 Jul 18.

Abstract
摘要

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本文引用的文献

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Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis.
Biochemistry. 2006 Nov 28;45(47):13947-53. doi: 10.1021/bi061874m.
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Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
Nat Struct Mol Biol. 2006 May;13(5):408-13. doi: 10.1038/nsmb1089. Epub 2006 Apr 30.
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The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance.
Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13881-6. doi: 10.1073/pnas.2235848100. Epub 2003 Nov 17.
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A fast and efficient metal-mediated oxidation of isoniazid and identification of isoniazid-NAD(H) adducts.
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Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Science. 1998 Jan 2;279(5347):98-102. doi: 10.1126/science.279.5347.98.
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inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis.
Science. 1994 Jan 14;263(5144):227-30. doi: 10.1126/science.8284673.

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