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@article{Benns:2018:10.1007/82_2018_123,
author = {Benns, HJ and Tate, EW and Child, MA},
doi = {10.1007/82_2018_123},
journal = {Curr Top Microbiol Immunol},
pages = {155--174},
title = {Activity-Based Protein Profiling for the Study of Parasite Biology.},
url = {http://dx.doi.org/10.1007/82_2018_123},
volume = {420},
year = {2018}
}
TY - JOUR
AB - Parasites exist within most ecological niches, often transitioning through biologically and chemically complex host environments over the course of their parasitic life cycles. While the development of technologies for genetic engineering has revolutionised the field of functional genomics, parasites have historically been less amenable to such modification. In light of this, parasitologists have often been at the forefront of adopting new small-molecule technologies, repurposing drugs into biological tools and probes. Over the last decade, activity-based protein profiling (ABPP) has evolved into a powerful and versatile chemical proteomic platform for characterising the function of enzymes. Central to ABPP is the use of activity-based probes (ABPs), which covalently modify the active sites of enzyme classes ranging from serine hydrolases to glycosidases. The application of ABPP to cellular systems has contributed vastly to our knowledge on the fundamental biology of a diverse range of organisms and has facilitated the identification of potential drug targets in many pathogens. In this chapter, we provide a comprehensive review on the different forms of ABPP that have been successfully applied to parasite systems, and highlight key biological insights that have been enabled through their application.
AU - Benns,HJ
AU - Tate,EW
AU - Child,MA
DO - 10.1007/82_2018_123
EP - 174
PY - 2018///
SN - 0070-217X
SP - 155
TI - Activity-Based Protein Profiling for the Study of Parasite Biology.
T2 - Curr Top Microbiol Immunol
UR - http://dx.doi.org/10.1007/82_2018_123
UR - https://www.ncbi.nlm.nih.gov/pubmed/30105424
VL - 420
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