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Issue 8, 2016
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Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry

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Abstract

Phosphorylation is a post-translational modification (PTM) fundamental for processes such as signal transduction and enzyme activity. We propose to apply data-independent acquisition (DIA) using mass spectrometry (MS) to determine unexplored phosphorylation events on isobarically modified peptides. Such peptides are commonly not quantitatively discriminated in phosphoproteomics due to their identical mass.

Graphical abstract: Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry

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Publication details

The article was received on 16 May 2016, accepted on 08 Jun 2016 and first published on 09 Jun 2016


Article type: Communication
DOI: 10.1039/C6MB00385K
Citation: Mol. BioSyst., 2016,12, 2385-2388

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    Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry

    S. Sidoli, R. Fujiwara, K. Kulej and B. A. Garcia, Mol. BioSyst., 2016, 12, 2385
    DOI: 10.1039/C6MB00385K

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