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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.

SUBMITTER: Sidoli S

PROVIDER: S-EPMC5091076 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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

Sidoli Simone S Fujiwara Rina R Kulej Katarzyna K Garcia Benjamin A BA

Molecular bioSystems 20160701 8

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. ...[more]

PMID: 27301801

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