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

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

doi:10.1039/c6mb00385k

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

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

Research output: Contribution to journal › Article › peer-review

10 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 language	English
Pages (from-to)	2385-2388
Number of pages	4
Journal	Molecular BioSystems
Volume	12
Issue number	8
DOIs	https://doi.org/10.1039/c6mb00385k
State	Published - 2016

Access to Document

10.1039/c6mb00385k

Cite this

@article{08dda3ce4321492695fcaa8a79deb766,

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.}",

note = "Publisher Copyright: {\textcopyright} 2016 The Royal Society of Chemistry.",

year = "2016",

doi = "10.1039/c6mb00385k",

language = "English",

volume = "12",

pages = "2385--2388",

journal = "Molecular BioSystems",

issn = "1742-206X",

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

Y1 - 2016

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

U2 - 10.1039/c6mb00385k

DO - 10.1039/c6mb00385k

M3 - Article

C2 - 27301801

AN - SCOPUS:84979255274

SN - 1742-206X

VL - 12

SP - 2385

EP - 2388

JO - Molecular BioSystems

JF - Molecular BioSystems

IS - 8

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this