Abstract
Polyadenosine diphosphate ribose poly(ADP-ribose) polymerase catalyzes the incorporation of the ADP-ribose moiety of NAD into a homopolymer of repeating ADP-ribose units covalently bound to histones and other nuclear protein acceptors [1, 2]. This DNA-dependent enzyme, highly stimulated by nicks and DNA fragmentation [3, 4], is thought to be involved in several basic functions of the chromatin, especially in DNA repair [5–7].
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De Murcia, G., Huletsky, A., Lamarre, D., Gaudreau, A., Pouyet, J., Poirier, G. (1985). Poly(ADP-Ribose) Glycohydrolase Activity Causes Recondensation of Relaxed Poly(ADP-Ribosyl)ated Polynucleosomes. In: Althaus, F.R., Hilz, H., Shall, S. (eds) ADP-Ribosylation of Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70589-2_25
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DOI: https://doi.org/10.1007/978-3-642-70589-2_25
Publisher Name: Springer, Berlin, Heidelberg
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