SpringerProtocols: Abstract: Protein ADP-Ribosylation

Protein ADP-Ribosylation

By: Keith D. Philibert², Henk Zwiers²

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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.

Affiliation(s): (2) Endocrine Research Group, Departments of Medical Physiology and MedicaI Biochemistry, Faculty of Medicine, The University Of Calgary, Alberta, Canada

Book Title: Regulatory Protein Modification: Techniques and Protocols

Series: Neuromethods | Volume: 30 | Pub. Date: Dec-01-1996 | Page Range: 365-394 | DOI: 10.1385/0-89603-415-1:365

Subject: Neuroscience

References

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