Goncalves, Victor, Brannigan, James A., Laporte, Alice et al. (5 more authors) (2017) Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MedChemComm. pp. 191-197. ISSN 2040-2511
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).
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017, The Royal Society of Chemistry. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 09 Feb 2017 11:40 |
Last Modified: | 21 Jan 2025 17:24 |
Published Version: | https://doi.org/10.1039/c6md00531d |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1039/c6md00531d |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:112169 |