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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Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Mitochondrial peptide methionine sulfoxide reductaseQ9UJ68Details
cAMP-dependent protein kinase catalytic subunit alphaP17612Details
ADP-ribosylation factor 1P84077Details