Cited by 104Advanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and ApplicationsProtein Tyrosine Phosphatases

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Catch me if you can: Mass spectrometry‐based phosphoproteomics and quantification strategies

Eyrich, Beate, Sickmann, Albert, Zahedi, René Peiman·2011·PROTEOMICS

DOI 10.1002/pmic.201000489

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Abstract

Phosphorylation of proteins is one of the most prominent PTMs and for instance a key regulator of signal transduction. In order to improve our understanding of cellular phosphorylation events, considerable effort has been devoted to improving the analysis of phosphorylation by MS‐based proteomics. Different enrichment strategies for phosphorylated peptides/proteins, such as immunoaffinity chromatography (IMAC) or titanium dioxide, have been established and constantly optimized for subsequent MS analysis. Concurrently, specific MS techniques were developed for more confident identification and phosphorylation site localization. In addition, more attention is paid to the LC‐MS instrumentation to avoid premature loss of phosphorylated peptides within the analytical system. Despite major advances in all of these fields, the analysis of phosphopeptides still remains far from being routine in proteomics. However, to reveal cellular regulation by phosphorylation events, not only qualitative information about the phosphorylation status of proteins but also, in particular, quantitative information about distinct changes in phosphorylation patterns upon specific stimulation is mandatory. Thus, yielded insights are of outstanding importance for the emerging field of systems biology. In this review, we will give an insight into the historical development of phosphoproteome analysis and discuss its recent progress particularly regarding phosphopeptide quantification and assessment of phosphorylation stoichiometry.

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Phosphorylation
Veenstra, T. D. (2019) · doi:10.1002/9781119081661.ch11

Authors: Eyrich, B., Sickmann, A., & Zahedi, R. P.
Affiliations: Leibniz Institute for Analytical Sciences - ISAS (DE)
Corresponding author: Zahedi, René Peiman
ORCID: Sickmann, Albert
Zahedi, René Peiman
Venue: PROTEOMICS
Publisher: Wiley
Published: 2011-01-11
Volume: 11
Issue: 4
Pages: 554-570
ISSN: 1615-9853 (ISSN-L)
1615-9861
DOI: 10.1002/pmic.201000489
OpenAlex: W2109482992
Cited by: 104
References: 178
Citations by year: 2026: 2 · 2025: 2 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 7 · 2015: 12 · 2014: 10 · 2013: 18 · 2012: 21
FWCI: 1.62
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: PROTEOMICS (publishedVersion)
PubMed (publishedVersion)
Funders: Ministerium für Innovation, Wissenschaft, Forschung und Technologie des Landes Nordrhein-Westfalen
Bundesministerium für Bildung und Forschung (31P5800)
Topics: Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: phosphoproteomics, protein phosphorylation, phosphopeptide quantification, phosphorylation stoichiometry, phosphopeptide enrichment, immunoaffinity chromatography, titanium dioxide enrichment, phosphorylation site localization, signal transduction, systems biology
MeSH terms: Phosphoproteins, Mass Spectrometry, Proteomics

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Catch me if you can: Mass spectrometry‐based phosphoproteomics and quantification strategies

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