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

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

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 - Jan 1 2016
Externally publishedYes

Fingerprint

Phosphopeptides
Mass Spectrometry
Phosphorylation
Peptides
Post Translational Protein Processing
Signal Transduction
Enzymes

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

Cite this

Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry. / Sidoli, Simone; Fujiwara, Rina; Kulej, Katarzyna; Garcia, Benjamin A.

In: Molecular BioSystems, Vol. 12, No. 8, 01.01.2016, p. 2385-2388.

Research output: Contribution to journalArticle

Sidoli, Simone ; Fujiwara, Rina ; Kulej, Katarzyna ; Garcia, Benjamin A. / Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry. In: Molecular BioSystems. 2016 ; Vol. 12, No. 8. pp. 2385-2388.
@article{3daa0b0ea5524e7fa8fc6ebbfdc07430,
title = "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.",
author = "Simone Sidoli and Rina Fujiwara and Katarzyna Kulej and Garcia, {Benjamin A.}",
year = "2016",
month = "1",
day = "1",
doi = "10.1039/c6mb00385k",
language = "English (US)",
volume = "12",
pages = "2385--2388",
journal = "Molecular BioSystems",
issn = "1742-206X",
publisher = "Royal Society of Chemistry",
number = "8",

}

TY - JOUR

T1 - Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry

AU - Sidoli, Simone

AU - Fujiwara, Rina

AU - Kulej, Katarzyna

AU - Garcia, Benjamin A.

PY - 2016/1/1

Y1 - 2016/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84979255274&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84979255274&partnerID=8YFLogxK

U2 - 10.1039/c6mb00385k

DO - 10.1039/c6mb00385k

M3 - Article

C2 - 27301801

AN - SCOPUS:84979255274

VL - 12

SP - 2385

EP - 2388

JO - Molecular BioSystems

JF - Molecular BioSystems

SN - 1742-206X

IS - 8

ER -