Structural Basis for the Variation in Triclosan Affinity to Enoyl Reductases
- 1 October 2004
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 343 (1) , 147-155
- https://doi.org/10.1016/j.jmb.2004.08.033
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesisPublished by Elsevier ,2003
- Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasitesInternational Journal for Parasitology, 2003
- Paradigm shifts in malaria parasite biochemistry and anti‐malarial chemotherapyBioEssays, 2002
- Lipid biosynthesis as a target for antibacterial agentsProgress in Lipid Research, 2001
- Bacterial fatty-acid biosynthesis: a genomics-driven target for antibacterial drug discoveryDrug Discovery Today, 2001
- Nuclear-encoded proteins target to the plastid inToxoplasma gondiiandPlasmodium falciparumProceedings of the National Academy of Sciences, 1998
- Modification of the NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosisScience, 1998
- Enoyl-Acyl Carrier Protein Reductase (fabI) Plays a Determinant Role in Completing Cycles of Fatty Acid Elongation in Escherichia coliJournal of Biological Chemistry, 1995
- Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosisScience, 1995
- Fatty acid synthase — an example of protein evolution by gene fusionTrends in Biochemical Sciences, 1984