title: Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.
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.
authors: Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ (UK).
authors: Malgorzata
authors: M
authors: Broncel
authors: Remigiusz A
authors: RA
authors: Serwa
authors: Paulina
authors: P
authors: Ciepla
authors: Eberhard
authors: E
authors: Krause
authors: Margaret J
authors: MJ
authors: Dallman
authors: Anthony I
authors: AI
authors: Magee
authors: Edward W
authors: EW
authors: Tate
mesh_terms: D047108:Embryonic Development; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D007202:Indicators and Reagents / Q000737:chemistry; D008055:Lipids / Q000737:chemistry*; D061986:MCF-7 Cells; D013058:Mass Spectrometry; D015394:Molecular Structure; D020543:Proteome / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D007202:Indicators and Reagents; D008055:Lipids; D020543:Proteome
keywords: capture reagents; lipidation; mass spectrometry; post-translational modification; proteomics