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@article{Thinon:2014:10.1038/ncomms5919,
author = {Thinon, E and Serwa, RA and Broncel, M and Brannigan, JA and Brassat, U and Wright, MH and Heal, WP and Wilkinson, AJ and Mann, DJ and Tate, EW},
doi = {10.1038/ncomms5919},
journal = {Nature Communications},
pages = {1--13},
title = {Global profiling of co- and post-translationally N-myristoylated proteomes in human cells},
url = {http://dx.doi.org/10.1038/ncomms5919},
volume = {5},
year = {2014}
}
TY - JOUR
AB - Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.
AU - Thinon,E
AU - Serwa,RA
AU - Broncel,M
AU - Brannigan,JA
AU - Brassat,U
AU - Wright,MH
AU - Heal,WP
AU - Wilkinson,AJ
AU - Mann,DJ
AU - Tate,EW
DO - 10.1038/ncomms5919
EP - 13
PY - 2014///
SN - 2041-1723
SP - 1
TI - Global profiling of co- and post-translationally N-myristoylated proteomes in human cells
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/ncomms5919
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000342984100015&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://www.nature.com/articles/ncomms5919
UR - http://hdl.handle.net/10044/1/18701
VL - 5
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