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Updated: Mar 19, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry
Simone Sidoli1, Rina Fujiwara1, Katarzyna Kulej2
1Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Room 9-124, 3400 Civic Center Blvd, Bldg 421, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu.
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.
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