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@article{Olaleye:2014:10.1039/c4ob01669f,
author = {Olaleye, TO and Brannigan, JA and Roberts, SM and Leatherbarrow, RJ and Wilkinson, AJ and Tate, EW},
doi = {10.1039/c4ob01669f},
journal = {Organic & Biomolecular Chemistry},
pages = {8132--8137},
title = {Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites},
url = {http://dx.doi.org/10.1039/c4ob01669f},
volume = {12},
year = {2014}
}
TY - JOUR
AB - N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex.
AU - Olaleye,TO
AU - Brannigan,JA
AU - Roberts,SM
AU - Leatherbarrow,RJ
AU - Wilkinson,AJ
AU - Tate,EW
DO - 10.1039/c4ob01669f
EP - 8137
PY - 2014///
SN - 1477-0539
SP - 8132
TI - Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites
T2 - Organic & Biomolecular Chemistry
UR - http://dx.doi.org/10.1039/c4ob01669f
UR - http://hdl.handle.net/10044/1/26871
VL - 12
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821