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Article Dans Une Revue MedChemComm Année : 2017

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

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Résumé

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).

Dates et versions

hal-01496799 , version 1 (27-03-2017)

Identifiants

Citer

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, 2017, 8 (1), pp.191 - 197. ⟨10.1039/C6MD00531D⟩. ⟨hal-01496799⟩
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