title: Quantitation of protein post-translational modifications using isobaric tandem mass tags.
abstract: Post-translational modifications (PTMs) of proteins are known to modulate many cellular processes and their qualitative and quantitative evaluation is fundamental for understanding the mechanisms of biological events. Over the past decade, improvements in sample preparation techniques and enrichment strategies, the development of quantitative labeling strategies, the launch of a new generation of mass spectrometers and the creation of bioinformatics tools for the interrogation of ever larger datasets has established MS-based quantitative proteomics as a powerful workflow for global proteomics, PTM analysis and the elucidation of key biological mechanisms. With the advantage of their multiplexing capacity and the flexibility of an ever-growing family of different peptide-reactive groups, isobaric tandem mass tags facilitate quantitative proteomics and PTM experiments and enable higher sample throughput. In this review, we focus on the technical concept and utility of the isobaric tandem mass tag labeling approach to PTM analysis, including phosphorylation, glycosylation and S-nitrosylation.
authors.affiliation: Proteome Sciences plc, Coveham House, Downside Bridge Road, Cobham, KT11 3EP, UK.
authors.forename: Hui-Chung
authors.initials: HC
authors.lastname: Liang
authors.forename: Emma
authors.initials: E
authors.lastname: Lahert
authors.forename: Ian
authors.initials: I
authors.lastname: Pike
authors.forename: Malcolm
authors.initials: M
authors.lastname: Ward
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013194:Staining and Labeling / Q000379:methods*
chemical_list: D011506:Proteins