Identification and quantitation of signal molecule-dependent protein phosphorylation

Arnoud J. Groen, Ludivine Thomas, Kathryn S. Lilley, Claudius Marondedze

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Phosphoproteomics is a fast-growing field that aims at characterizing phosphorylated proteins in a cell or a tissue at a given time. Phosphorylation of proteins is an important regulatory mechanism in many cellular processes. Gel-free phosphoproteome technique involving enrichment of phosphopeptide coupled with mass spectrometry has proven to be invaluable to detect and characterize phosphorylated proteins. In this chapter, a gel-free quantitative approach involving 15N metabolic labelling in combination with phosphopeptide enrichment by titanium dioxide (TiO2) and their identification by MS is described. This workflow can be used to gain insights into the role of signalling molecules such as cyclic nucleotides on regulatory networks through the identification and quantification of responsive phospho(proteins). © Springer Science+Business Media New York 2013.
Original languageEnglish (US)
Pages (from-to)121-137
Number of pages17
JournalMethods in Molecular Biology
StatePublished - Sep 3 2013

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology


Dive into the research topics of 'Identification and quantitation of signal molecule-dependent protein phosphorylation'. Together they form a unique fingerprint.

Cite this