Abstract 2818 An optimized proteomics workflow for the discovery and validation of acidic ADP-ribose modification sites

The process of ADP–ribosylation is important in the regulation of many critical biochemical pathways. In humans, ADP–ribosylation is regulated by a family of 17 enzymes termed poly–ADP–ribose polymerases (PARPs) while removal is managed through a separate family of glycohydrolases (e.g. macroD1, macroD2, TARG1). Although thousands of potential ADP–ribose (ADPr) modification sites have been identified using high–throughput tandem mass–spectrometry (MS/MS), recent work completed in our lab and others has highlighted the instability of the ester–peptide bond in neutral conditions used for routine proteomics workflows.