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

Goncalves, V, Brannigan, JA, Laporte, A, Bell, AS, Roberts, SM, Wilkinson, AJ, Leatherbarrow, RJ and Tate, EW (2017) Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MEDCHEMCOMM, 8 (1). pp. 191-197. ISSN 2040-2503

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Open Access URL: http://dx.doi.org/10.1039/C6MD00531D (Published version)


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).

Item Type: Article
Uncontrolled Keywords: 0304 Medicinal And Biomolecular Chemistry, 0305 Organic Chemistry, 1115 Pharmacology And Pharmaceutical Sciences
Subjects: R Medicine > RM Therapeutics. Pharmacology
Divisions: Vice-Chancellor's Office
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Date Deposited: 26 Jul 2017 09:38
Last Modified: 20 Apr 2022 09:09
DOI or ID number: 10.1039/c6md00531d
URI: https://researchonline.ljmu.ac.uk/id/eprint/6860
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