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Chemical proteomics: a powerful tool for exploring protein lipidation
Author(s) -
Elisabeth M. Storck,
Remigiusz A. Serwa,
Edward W. Tate
Publication year - 2013
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20120283
Subject(s) - lipid anchored protein , proteomics , posttranslational modification , computational biology , identification (biology) , prenylation , biology , autophagy , biochemistry , apoptosis , botany , gene , enzyme
The study of post-translational modifications such as protein lipidation is a non-trivial challenge of the post-genomic era. In recent years the field of chemical proteomics has greatly advanced our ability to identify and quantify protein lipidation. In the present review, we give a brief overview of the tools available to study protein acylation, prenylation and cholesterylation, and their application in the identification and quantification of protein lipidation in health and disease.

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