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Issue 1, 2017
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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

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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).

Graphical abstract: Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

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Publication details

The article was received on 20 Sep 2016, accepted on 09 Nov 2016 and first published on 11 Nov 2016


Article type: Research Article
DOI: 10.1039/C6MD00531D
Med. Chem. Commun., 2017,8, 191-197
  • Open access: Creative Commons BY license
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    Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

    V. Goncalves, J. A. Brannigan, A. Laporte, A. S. Bell, S. M. Roberts, A. J. Wilkinson, R. J. Leatherbarrow and E. W. Tate, Med. Chem. Commun., 2017, 8, 191
    DOI: 10.1039/C6MD00531D

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