Imperial College London
Portrait Picture

Prof Ed Tate

Faculty of Natural Sciences, Department of Chemistry

GSK Chair in Chemical Biology
 
 
 
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Contact

 

+44 (0)20 7594 3752e.tate Website CV

 
 
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Assistant

 

Ms Agnes Lee +44 (0)20 7594 9852

 
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Location

 

301BMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Benns:2020:10.1016/j.cbpa.2020.06.011,
author = {Benns, HJ and Wincott, CJ and Tate, EW and Child, MA},
doi = {10.1016/j.cbpa.2020.06.011},
journal = {Current Opinion in Chemical Biology},
pages = {20--29},
title = {Activity- and reactivity-based proteomics: Recent technological advances and applications in drug discovery.},
url = {http://dx.doi.org/10.1016/j.cbpa.2020.06.011},
volume = {60},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Activity-based protein profiling (ABPP) is recognized as a powerful and versatile chemoproteomic technology in drug discovery. Central to ABPP is the use of activity-based probes to report the activity of specific enzymes or reactivity of amino acid types in complex biological systems. Over the last two decades, ABPP has facilitated the identification of new drug targets and discovery of lead compounds in human and infectious disease. Furthermore, as part of a sustained global effort to illuminate the druggable proteome, the repertoire of target classes addressable with activity-based probes has vastly expanded in recent years. Here, we provide an overview of ABPP and summarise the major technological advances with an emphasis on probe development.
AU  - Benns,HJ
AU  - Wincott,CJ
AU  - Tate,EW
AU  - Child,MA
DO  - 10.1016/j.cbpa.2020.06.011
EP  - 29
PY  - 2020///
SN  - 1367-5931
SP  - 20
TI  - Activity- and reactivity-based proteomics: Recent technological advances and applications in drug discovery.
T2  - Current Opinion in Chemical Biology
UR  - http://dx.doi.org/10.1016/j.cbpa.2020.06.011
UR  - https://www.ncbi.nlm.nih.gov/pubmed/32768892
UR  - https://www.sciencedirect.com/science/article/pii/S1367593120300946?via%3Dihub
UR  - http://hdl.handle.net/10044/1/81705
VL  - 60
ER  -
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