title: Chemical tagging strategies for mass spectrometry-based phospho-proteomics.
abstract: The study of protein phosphorylation in combination with chemical methods may serve several purposes. The removal of the phosphate group from phosphoserine and -threonine residues by beta-elimination has been employed to improve sensitivity for mass spectrometric detection and to attach affinity tags for phosphopeptide enrichment. More recently, phosphoramidate chemistry has been shown to be another promising tool for enriching phosphorylated peptides, and other phosphate-directed reactions may also be applicable to the study of the phosphoproteome in the future. In recent years, the combination of large-scale phospho-proteomics studies with stable isotope labeling for quantification purposes has become of growing importance, frequently involving the introduction of chemical tags such as iTRAQ. In this chapter, we will highlight several key strategies that involve chemical tagging reactions.
authors.affiliation: Department of Analytical Chemistry and Food Chemistry, University of Vienna, Vienna, Austria.
authors.forename: Alexander
authors.initials: A
authors.lastname: Leitner
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lindner
mesh_terms: D000465:Algorithms; D000818:Animals; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D008954:Models, Biological; D010750:Phosphoproteins / Q000032:analysis* / Q000737:chemistry; D040901:Proteomics / Q000379:methods*; D013194:Staining and Labeling / Q000379:methods*
chemical_list: D010750:Phosphoproteins