| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1193551 | International Journal of Mass Spectrometry | 2012 | 8 Pages |
The use of tandem mass spectrometry to identify and characterize sites of protein adenosine diphosphate (ADP) ribosylation will be reviewed. Specifically, we will focus on data acquisition schemes and fragmentation techniques that provide peptide sequence and modification site information. Also discussed are uses of synthetic standards to aid characterization, and an enzymatic method that converts ADP-ribosylated peptides into ribosyl mono phosphorylated peptides making identification amenable to traditional phosphopeptide characterization methods. Finally the potential uses of these techniques to characterize poly ADP-ribosylation sites, and inherent challenges, are addressed.
Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (118 K)Download as PowerPoint slideHighlights► We review current tandem MS methods for identification of ADP-ribosylated peptides. ► ADP-ribosylated peptide identification is complicated by ADP-ribose fragmentation. ► A systematic nomenclature for ADP-ribosylated peptide fragments is proposed. ► Extensions from mono to poly ADP-ribosylation MS identification methods are discussed.
