Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry. Issue 8 (15th June 2016)

• Record Type: Journal Article
• Authors: Sidoli, Simone; Fujiwara, Rina; Kulej, Katarzyna; Garcia, Benjamin A.
• Is Part Of: Molecular bioSystems. Volume 12:Issue 8(2016:Aug.)
• Page Start: 2385
• Page End: 2388
• Publication Date: 2016-06-15
• Subjects: Molecular biology -- Periodicals; Biochemistry -- Periodicals; 571.7405
• DOI: 10.1039/c6mb00385k
• Languages: English
• ISSNs: 1742-206X

Abstract

Abstract : Data-independent acquisition (DIA) is here applied to determine unexplored phosphorylation events on isobarically modified peptides. 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.