Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

Abstract : The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).
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https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01496799
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Soumis le : lundi 27 mars 2017 - 19:09:17
Dernière modification le : lundi 27 mars 2017 - 19:11:34

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Victor Goncalves, James A. Brannigan, Alice Laporte, Andrew S. Bell, Shirley M. Roberts, et al.. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MedChemComm, Royal Society of Chemistry, 2017, 8 (1), pp.191 - 197. 〈http://pubs.rsc.org/en/content/articlelanding/2017/md/c6md00531d#!divAbstract〉. 〈10.1039/C6MD00531D〉. 〈hal-01496799〉

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