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- W2330661672 endingPage "1041" @default.
- W2330661672 startingPage "1041" @default.
- W2330661672 abstract "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." @default.
- W2330661672 created "2016-06-24" @default.
- W2330661672 creator A5010248856 @default.
- W2330661672 date "2014-01-01" @default.
- W2330661672 modified "2023-10-14" @default.
- W2330661672 title "Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites" @default.
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- W2330661672 doi "https://doi.org/10.2741/4266" @default.
- W2330661672 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24896335" @default.