Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sites. by Matic, I, Ahel, I, Hay, RT

Specificity of reversible ADP-ribosylation and regulation of cellular processes by Crawford, K, Bonfiglio, J, Mikoč, A, Matic, I, Ahel, I

Serine ADP-ribosylation reversal by the hydrolase ARH3 by Fontana, P, Bonfiglio, J, Palazzo, L, Bartlett, E, Matic, I, Ahel, I

Serine is the major residue for ADP-ribosylation upon DNA damage by Palazzo, L, Leidecker, O, Prokhorova, E, Dauben, H, Matic, I, Ahel, I

Interplay of histone marks with serine ADP-ribosylation by Bartlett, E, Bonfiglio, J, Prokhorova, E, Colby, T, Zobel, F, Ahel, I, Matic, I

Serine is a new target residue for endogenous ADP-ribosylation on histones by Leidecker, O, Bonfiglio, J, Colby, T, Zhang, Q, Atanassov, I, Zaja, R, Palazzo, L, Stockum, A, Ahel, I, Matic, I

Regulation of translesion synthesis DNA polymerase eta by monoubiquitination. by Bienko, M, Green, C, Sabbioneda, S, Crosetto, N, Matic, I, Hibbert, R, Begovic, T, Niimi, A, Mann, M, Lehmann, A, Dikic, I

Serine ADP-Ribosylation Depends on HPF1 by Bonfiglio, J, Fontana, P, Zhang, Q, Colby, T, Gibbs-Seymour, I, Atanassov, I, Bartlett, E, Zaja, R, Ahel, I, Matic, I

Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens by Rack, J, Morra, R, Barkauskaite, E, Kraehenbuehl, R, Ariza, A, Qu, Y, Ortmayer, M, Leidecker, O, Cameron, D, Matic, I, Peleg, A, Leys, D, Traven, A, Ahel, I

Disruption of macrodomain protein SCO6735 increases antibiotic production in Streptomyces coelicolor by Lalić, J, Posavec Marjanović, M, Palazzo, L, Perina, D, Sabljić, I, Žaja, R, Colby, T, Pleše, B, Halasz, M, Jankevicius, G, Bucca, G, Ahel, M, Matić, I, Ćetković, H, Luić, M, Mikoč, A, Ahel, I