Issue 8, 2016

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

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

Supplementary files

Article information

Article type
Communication
Submitted
16 May 2016
Accepted
08 Jun 2016
First published
09 Jun 2016

Mol. BioSyst., 2016,12, 2385-2388

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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