Discovery of a Novel and Potent Class of F. tularensis Enoyl-Reductase (FabI) Inhibitors by Molecular Shape and Electrostatic Matching-Reference-Cited by-同舟云学术

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Discovery of a Novel and Potent Class of F. tularensis Enoyl-Reductase (FabI) Inhibitors by Molecular Shape and Electrostatic Matching

Published:2011-12-05 Issue:1 Volume:55 Page:268-279
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Hevener Kirk E.¹,Mehboob Shahila¹,Su Pin-Chih¹,Truong Kent¹,Boci Teuta¹,Deng Jiangping²,Ghassemi Mahmood²,Cook James L.²,Johnson Michael E.¹

Affiliation:

1. Center for Pharmaceutical Biotechnology, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, Illinois 60607-7173, United States

2. Department of Medicine, University of Illinois College of Medicine, 808 South Wood Street, Chicago, Illinois 60612, United States

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm201168g

Reference56 articles.

1. Inhibiting Bacterial Fatty Acid Synthesis

2. Antibacterial targets in fatty acid biosynthesis

3. The Enoyl-[Acyl-Carrier-Protein] Reductase (FabI) of Escherichia coli, which Catalyzes a Key Regulatory Step in Fatty Acid Biosynthesis, Accepts NADH and NADPH as Cofactors and is Inhibited by Palmitoyl-CoA

4. A triclosan-resistant bacterial enzyme

5. The Enoyl-[acyl-carrier-protein] Reductases FabI and FabL fromBacillus subtilis

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