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    Identification and quantitation of signal molecule-dependent protein phosphorylation

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    Type
    Article
    Authors
    Groen, Arnoud J.
    Thomas, Ludivine
    Lilley, Kathryn S.
    Marondedze, Claudius cc
    KAUST Department
    Bioscience Core Lab
    Biological and Environmental Sciences and Engineering (BESE) Division
    Core Labs
    Date
    2013-09-03
    Permanent link to this record
    http://hdl.handle.net/10754/562969
    
    Metadata
    Show full item record
    Abstract
    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.
    Publisher
    Humana Press
    Journal
    Methods in Molecular Biology
    ISBN
    9781627034401
    DOI
    10.1007/978-1-62703-441-8-9
    10.1007/978-1-62703-441-8_9
    PubMed ID
    23681576
    ae974a485f413a2113503eed53cd6c53
    10.1007/978-1-62703-441-8-9
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Core Lab

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