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@article{Rackham:2015:10.1039/c5md00241a,
author = {Rackham, MD and Yu, Z and Brannigan, JA and Heal, WP and Paape, D and Barker, KV and Wilkinson, AJ and Smith, DF and Leatherbarrow, RJ and Tate, EW},
doi = {10.1039/c5md00241a},
journal = {MedChemComm},
pages = {1761--1766},
title = {Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase},
url = {http://dx.doi.org/10.1039/c5md00241a},
volume = {6},
year = {2015}
}
TY - JOUR
AB - N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.
AU - Rackham,MD
AU - Yu,Z
AU - Brannigan,JA
AU - Heal,WP
AU - Paape,D
AU - Barker,KV
AU - Wilkinson,AJ
AU - Smith,DF
AU - Leatherbarrow,RJ
AU - Tate,EW
DO - 10.1039/c5md00241a
EP - 1766
PY - 2015///
SN - 2040-2511
SP - 1761
TI - Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
T2 - MedChemComm
UR - http://dx.doi.org/10.1039/c5md00241a
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000364153700004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/29875
VL - 6
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