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dc.contributor.authorGroen, Arnoud J.
dc.contributor.authorThomas, Ludivine
dc.contributor.authorLilley, Kathryn S.
dc.contributor.authorMarondedze, Claudius
dc.date.accessioned2015-08-03T11:17:26Z
dc.date.available2015-08-03T11:17:26Z
dc.date.issued2013-09-03
dc.identifier.isbn9781627034401
dc.identifier.issn10643745
dc.identifier.pmid23681576
dc.identifier.doi10.1007/978-1-62703-441-8-9
dc.identifier.urihttp://hdl.handle.net/10754/562969
dc.description.abstractPhosphoproteomics 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.
dc.publisherHumana Press
dc.subjectGel-free proteomics
dc.subjectMass spectrometry
dc.subjectPhosphoproteomics
dc.subjectQuantitation
dc.subjectTiO2 enrichment
dc.titleIdentification and quantitation of signal molecule-dependent protein phosphorylation
dc.typeArticle
dc.contributor.departmentBioscience Core Lab
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentCore Labs
dc.identifier.journalMethods in Molecular Biology
dc.contributor.institutionDepartment of Biochemistry, Cambridge Centre for Proteomics, University of Cambridge, Cambridge, United Kingdom
kaust.personThomas, Ludivine


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