In this section
@article{Goncalves:2016:10.1039/C6MD00531D,
author = {Goncalves, V and Brannigan, JA and Laporte, A and Bell, AS and Roberts, SM and Wilkinson, AJ and Leatherbarrow, RJ and Tate, EW},
doi = {10.1039/C6MD00531D},
journal = {MedChemComm},
pages = {191--197},
title = {Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase},
url = {http://dx.doi.org/10.1039/C6MD00531D},
volume = {8},
year = {2016}
}
TY - JOUR
AB - 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).
AU - Goncalves,V
AU - Brannigan,JA
AU - Laporte,A
AU - Bell,AS
AU - Roberts,SM
AU - Wilkinson,AJ
AU - Leatherbarrow,RJ
AU - Tate,EW
DO - 10.1039/C6MD00531D
EP - 197
PY - 2016///
SN - 2040-2511
SP - 191
TI - Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
T2 - MedChemComm
UR - http://dx.doi.org/10.1039/C6MD00531D
UR - http://hdl.handle.net/10044/1/43036
VL - 8
ER -
