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@article{Hassan:2025:10.1016/bs.mie.2025.06.012,
author = {Hassan, S and Zhang, J and Kallemeijn, W and Tate, EW},
doi = {10.1016/bs.mie.2025.06.012},
journal = {Methods Enzymol},
pages = {299--316},
title = {Chemical proteomic approaches to investigate S-prenylation.},
url = {http://dx.doi.org/10.1016/bs.mie.2025.06.012},
volume = {719},
year = {2025}
}
TY - JOUR
AB - Protein S-prenylation is a post-translational lipid modification that occurs at C-terminal cysteines. While S-prenylation has been widely studied in the context of disease biology and drug discovery, only in the last decade have robust proteomic techniques emerged to study the complex dynamics between different classes of protein prenyltransferases, significantly aiding the development and application of tools and inhibitors. Herein, we describe the use of S-prenylation probes as a chemical proteomic technique to interrogate S-geranylgeranylation and S-farnesylation, the two classes of protein prenylation, from sample preparation to mass spectrometry analysis.
AU - Hassan,S
AU - Zhang,J
AU - Kallemeijn,W
AU - Tate,EW
DO - 10.1016/bs.mie.2025.06.012
EP - 316
PY - 2025///
SP - 299
TI - Chemical proteomic approaches to investigate S-prenylation.
T2 - Methods Enzymol
UR - http://dx.doi.org/10.1016/bs.mie.2025.06.012
UR - https://www.ncbi.nlm.nih.gov/pubmed/40992845
VL - 719
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