The publication feed below is often incomplete and out of date; for an up to date summary of our publications please see Google Scholar or Pub Med

Citation

BibTex format

@article{Masumoto:2015:10.1042/BST20150018,
author = {Masumoto, N and Lanyon-Hogg, T and Rodgers, UR and Konitsiotis, AD and Magee, AI and Tate, EW},
doi = {10.1042/BST20150018},
journal = {Biochemical Society Transactions},
pages = {246--252},
title = {Membrane bound O-acyltransferases and their inhibitors},
url = {http://dx.doi.org/10.1042/BST20150018},
volume = {43},
year = {2015}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Since the identification of the membrane-bound O-acyltransferase (MBOATs) protein family in the early2000s, three distinct members [porcupine (PORCN), hedgehog (Hh) acyltransferase (HHAT) and ghrelin Oacyltransferase(GOAT)] have been shown to acylate specific proteins or peptides. In this review, topologydetermination, development of assays to measure enzymatic activities and discovery of small moleculeinhibitors are compared and discussed for each of these enzymes.
AU  - Masumoto,N
AU  - Lanyon-Hogg,T
AU  - Rodgers,UR
AU  - Konitsiotis,AD
AU  - Magee,AI
AU  - Tate,EW
DO  - 10.1042/BST20150018
EP  - 252
PY  - 2015///
SN  - 1470-8752
SP  - 246
TI  - Membrane bound O-acyltransferases and their inhibitors
T2  - Biochemical Society Transactions
UR  - http://dx.doi.org/10.1042/BST20150018
UR  - http://hdl.handle.net/10044/1/26873
VL  - 43
ER  -
Download

Contact

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