IMR Press / FBL / Volume 19 / Issue 7 / DOI: 10.2741/4266

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites
Show Less
1 Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Switzerland
2 Life Science Zurich Graduate School, Molecular Life Science Program, University of Zurich, Switzerland
Front. Biosci. (Landmark Ed) 2014, 19(7), 1041–1056;
Published: 1 June 2014

ADP-ribosylation is a post-translational modification of proteins that comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. It is catalyzed by ADP-ribosyltransferases, a family of currently 22 human proteins that all possess an ADP-ribosyltransferase catalytic domain. ADP-ribosylation is a reversible modification that can be hydrolyzed by ADP-ribosylhydrolases. In order to define the functional role of cellular ADP-ribosylation and the functional contribution of distinct ARTD family members, it is necessary to identify all ADP-ribosylated proteins, as well as their modified residues in the context of different cellular conditions and stresses. Here, we summarize the most recent progress in defining the cellular ADP-ribosylome and the efforts to detect ADP-ribose acceptor sites by enzymatic reactions and mass-spectrometry.

Acceptor Side
Mass Spectrometry
Post-Translational Modification
Back to top