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Protein ADP-Ribosylation

  • Protocol
Regulatory Protein Modification

Part of the book series: Neuromethods ((NM,volume 30))

Abstract

ADP-ribosylation of proteins was originally discovered in 1966 by Chambon et al. (1966), who detected polymers of ADP-ribose attached to protein substrates. Since that time, protein ADP-ribosylation has been identified in a diverse range of species, from bacteria to human, as well as within virtually every cellular compartment (Hilz et al., 1984; Ueda and Hayaishi, 1985; Ogura et al, 1990; Williamson and Moss, 1990; Aktories and Wegner, 1992). In general, ADP-ribosylation is a posttranslational modification in which one or more ADP-ribose moieties are transferred from a nicotinamide adenine dinucleotide (NAD+) donor to an amino acid acceptor. It is important to note that NAD+ is a substrate in this process rather than a cofactor as it is in many enzyme reactions.

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Authors and Affiliations

  1. Endocrine Research Group, Departments of Medical Physiology and MedicaI Biochemistry, Faculty of Medicine, The University Of Calgary, Alberta, Canada

    Keith D. Philibert & Henk Zwiers

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  1. Keith D. Philibert
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  1. Cornell University Medical College, New York, NY

    Hugh C. Hemmings Jr. (MD,PhD) (MD,PhD)

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Philibert, K.D., Zwiers, H. (1997). Protein ADP-Ribosylation. In: Hemmings, H.C. (eds) Regulatory Protein Modification. Neuromethods, vol 30. Humana Press. https://doi.org/10.1385/0-89603-415-1:365

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  • DOI: https://doi.org/10.1385/0-89603-415-1:365

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-415-0

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