In this section
@article{Ward:2016:10.1021/acschembio.6b00766,
author = {Ward, JA and McLellan, L and Stockley, M and Gibson, KR and Whitlock, GA and Knights, C and Harrigan, JA and Jacq, X and Tate, EW},
doi = {10.1021/acschembio.6b00766},
journal = {ACS Chemical Biology},
pages = {3268--3272},
title = {Quantitative Chemical Proteomic Profiling of Ubiquitin Specific Proteases in Intact Cancer Cells},
url = {http://dx.doi.org/10.1021/acschembio.6b00766},
volume = {11},
year = {2016}
}
TY - JOUR
AB - Deubiquitinating enzymes play an important role in a plethora of therapeutically relevant processes and are emerging as pioneering drug targets. Herein, we present a novel probe, Ubiquitin Specific Protease (USP) inhibitor, alongside an alkyne-tagged activity-based probe analogue. Activity-based proteome profiling identified 12 USPs, including USP4, USP16, and USP33, as inhibitor targets using submicromolar probe concentrations. This represents the first intact cell activity-based profiling of deubiquitinating enzymes. Further analysis demonstrated functional inhibition of USP33 and identified a synergistic relationship in combination with ATR inhibition, consistent with USP4 inhibition.
AU - Ward,JA
AU - McLellan,L
AU - Stockley,M
AU - Gibson,KR
AU - Whitlock,GA
AU - Knights,C
AU - Harrigan,JA
AU - Jacq,X
AU - Tate,EW
DO - 10.1021/acschembio.6b00766
EP - 3272
PY - 2016///
SN - 1554-8937
SP - 3268
TI - Quantitative Chemical Proteomic Profiling of Ubiquitin Specific Proteases in Intact Cancer Cells
T2 - ACS Chemical Biology
UR - http://dx.doi.org/10.1021/acschembio.6b00766
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000390179700006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/43848
VL - 11
ER -
