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

Simone Sidoli, Rina Fujiwara, Katarzyna Kulej, Benjamin A. Garcia

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2385-2388
Number of pages4
JournalMolecular BioSystems
Volume12
Issue number8
DOIs
StatePublished - 2016

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry'. Together they form a unique fingerprint.

Cite this