Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.
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Broncel M, Serwa RA, Ciepla P, Krause E, Dallman MJ, Magee AI, Tate EW
Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.
Angew Chem Int Ed Engl. 2015 May 11;54(20):5948-51. doi: 10.1002/anie.201500342. Epub 2015 Mar 25.
- PubMed ID
- 25807930 [ View in PubMed]
- Abstract
Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development.