Tanigawa Y, Tsuchiya M, Imai Y, Shimoyama M
Biochem Biophys Res Commun. 1983 May 31;113(1):135-41. doi: 10.1016/0006-291x(83)90442-4.
The phosphorylation of nuclear proteins from hen liver nuclei was suppressed under conditions of incubation with NAD. The reconstituted protein kinase assay system containing heat-treated and subsequently ADP-ribosylated nuclei and NI type protein kinase revealed that the ADP-ribosylated nuclear proteins are poor acceptors for the phosphorylation reaction. Therefore, mono(ADP-ribosyl)ation may contribute to the regulation of phosphorylation reaction in nuclei.