@article{Luscher2021ADPri-54458,
  year={2021},
  doi={10.1111/febs.16142},
  title={ADP‐ribosyltransferases, an update on function and nomenclature},
  issn={1742-464X},
  journal={The FEBS Journal},
  author={Lüscher, Bernhard and Ahel, Ivan and Altmeyer, Matthias and Ashworth, Alan and Bai, Peter and Chang, Paul and Cohen, Michael and Corda, Daniela and Dantzer, Françoise and Mangerich, Aswin}
}

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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-07-29T14:19:32Z</dc:date>
    <dc:contributor>Altmeyer, Matthias</dc:contributor>
    <dc:creator>Lüscher, Bernhard</dc:creator>
    <dc:language>eng</dc:language>
    <dc:creator>Dantzer, Françoise</dc:creator>
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    <dc:contributor>Ashworth, Alan</dc:contributor>
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    <dc:creator>Altmeyer, Matthias</dc:creator>
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    <dc:creator>Bai, Peter</dc:creator>
    <dc:creator>Corda, Daniela</dc:creator>
    <dcterms:abstract xml:lang="eng">ADP-ribosylation, a modification of proteins, nucleic acids and metabolites, confers broad functions, including roles in stress responses elicited for example by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases, which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ADP-ribosyltransferases are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as anti-viral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ADP-ribosyltransferases and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ADP-ribosyltransferases that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ADP-ribosyltransferases to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.</dcterms:abstract>
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    <dcterms:title>ADP‐ribosyltransferases, an update on function and nomenclature</dcterms:title>
    <dc:contributor>Chang, Paul</dc:contributor>
    <dc:contributor>Lüscher, Bernhard</dc:contributor>
    <dc:contributor>Mangerich, Aswin</dc:contributor>
    <dc:creator>Mangerich, Aswin</dc:creator>
    <dc:creator>Ashworth, Alan</dc:creator>
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    <dcterms:issued>2021</dcterms:issued>
    <dc:contributor>Bai, Peter</dc:contributor>
    <dc:contributor>Corda, Daniela</dc:contributor>
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    <dc:creator>Chang, Paul</dc:creator>
    <dc:creator>Ahel, Ivan</dc:creator>
    <dc:contributor>Ahel, Ivan</dc:contributor>
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    <dc:contributor>Cohen, Michael</dc:contributor>
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