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Citation

BibTex format

@article{Storck:2019:10.1038/s41557-019-0237-6,
author = {Storck, Saha E and Morales, Sanfrutos J and Serwa, R and Panyain, N and Lanyon-Hogg, T and Tolmachova, T and Ventimiglia, L and Martin-Serrano, J and Seabra, M and Wojciak-Stothard, B and Tate, E},
doi = {10.1038/s41557-019-0237-6},
journal = {Nature Chemistry},
pages = {552--561},
title = {Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics},
url = {http://dx.doi.org/10.1038/s41557-019-0237-6},
volume = {11},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Post-translational farnesylation or geranylgeranylation at a C-terminal cysteine residue regulates the localization and function of over 100 proteins, including the Ras isoforms, and is a therapeutic target in diseases including cancer and infection. Here, we report global and selective profiling of prenylated proteins in living cells enabled by the development of isoprenoid analogues YnF and YnGG in combination with quantitative chemical proteomics. Eighty prenylated proteins were identified in a single human cell line, 64 for the first time at endogenous abundance without metabolic perturbation. We further demonstrate that YnF and YnGG enable direct identification of post-translationally processed prenylated peptides, proteome-wide quantitative analysis of prenylation dynamics and alternative prenylation in response to four different prenyltransferase inhibitors, and quantification of defective Rab prenylation in a model of the retinal degenerative disease choroideremia.
AU  - Storck,Saha E
AU  - Morales,Sanfrutos J
AU  - Serwa,R
AU  - Panyain,N
AU  - Lanyon-Hogg,T
AU  - Tolmachova,T
AU  - Ventimiglia,L
AU  - Martin-Serrano,J
AU  - Seabra,M
AU  - Wojciak-Stothard,B
AU  - Tate,E
DO  - 10.1038/s41557-019-0237-6
EP  - 561
PY  - 2019///
SN  - 1755-4330
SP  - 552
TI  - Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics
T2  - Nature Chemistry
UR  - http://dx.doi.org/10.1038/s41557-019-0237-6
UR  - https://www.nature.com/articles/s41557-019-0237-6
UR  - http://hdl.handle.net/10044/1/69030
VL  - 11
ER  -
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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