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Omics score: 1005

Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development.

ABSTRACT: Data from ProteomeXchange, PXD ID: PXD001863. File: HEK_HeLa_MCF_ PEAKS7.mgf. Published as part of Angew Chem Int Ed Engl. 2015 Mar 25 . From the Abstract: {{i}} 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.{{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Homo_sapiens_viruses, Human

DISEASE(S): Not Available

SUBMITTER: Broncel M, et al.

PROVIDER: GPM32320014414 | GPMDB |

REPOSITORIES: GPMDB

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Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.

Broncel Malgorzata M Serwa Remigiusz A RA Ciepla Paulina P Krause Eberhard E Dallman Margaret J MJ Magee Anthony I AI Tate Edward W EW

Angewandte Chemie (International ed. in English) 20150325 20

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. ...[more]

PMID: 25807930

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