Identification and quantitation of signal molecule-dependent protein phosphorylation
Type
ArticleKAUST Department
Bioscience Core LabBiological and Environmental Sciences and Engineering (BESE) Division
Core Labs
Date
2013-09-03Permanent link to this record
http://hdl.handle.net/10754/562969
Metadata
Show full item recordAbstract
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 PressJournal
Methods in Molecular BiologyISBN
9781627034401PubMed ID
23681576ae974a485f413a2113503eed53cd6c53
10.1007/978-1-62703-441-8-9
Scopus Count
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