A study of the structure-activity relationship for diazaborine inhibition of Escherichia coli enoyl-ACP reductase
- 1 May 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 309 (1) , 171-180
- https://doi.org/10.1006/jmbi.2001.4643
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Crystallographic analysis of triclosan bound to enoyl reductaseJournal of Molecular Biology, 1999
- Crystal Structure of the Mycobacterium tuberculosis Enoyl-ACP Reductase, InhA, in Complex with NAD+ and a C16 Fatty Acyl SubstrateJournal of Biological Chemistry, 1999
- Molecular basis of triclosan activityNature, 1999
- Genetic Evidence that InhA of Mycobacterium smegmatis Is a Target for TriclosanAntimicrobial Agents and Chemotherapy, 1999
- A Mechanism of Drug Action Revealed by Structural Studies of Enoyl ReductaseScience, 1996
- The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexesPlant Molecular Biology, 1994
- inhA , a Gene Encoding a Target for Isoniazid and Ethionamide in Mycobacterium tuberculosisScience, 1994
- Preparation and antibacterial activities of new 1,2,3-diazaborine derivatives and analogsJournal of Medicinal Chemistry, 1984
- Fatty acid synthase — an example of protein evolution by gene fusionTrends in Biochemical Sciences, 1984
- A diazaborine derivative inhibits lipopolysaccharide biosynthesisNature, 1981