We study several aspects of protein phosphorylation, a process regulated by protein kinases and phosphatases, frequently altered in cancer and other diseases. The research activities focus on the biochemical and cellular characterization of different kinases and phosphatases, the definition of their structure/function relationship, and the analysis of their signalling pathways in normal and pathological cells. Selective protein kinase inhibitors are developed as potential therapeutic drugs.
5 recent publications
- Salvi M, Trashi E, Cozza G, Franchin C, Arrigoni G, Pinna LA (2012) Investigation on PLK2 and PLK3 substrate recognition. Biochim. Biophys. Acta. 1824:1366-1373.
- Borgo C, Cesaro L, Salizzato V, Ruzzene M, M.L. Massimino, Pinna LA, Donella-Deana A. (2013) Aberrant signaling by protein kinase CK2 in imatinib-resistant chronic myeloid leukaemia cells. Biochemical evidence and therapeutic perspectives. Mol. Oncol. 7:1103-1115
- Cesaro L, Marin O, Venerando A, Donella-Deana A, Pinna LA. (2013) Phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) serine-511 by the combined action of tyrosine kinases and CK2: the implication of tyrosine-512 and phenylalanine-508. Amino Acids. 45:1423-1429
- Costa R, Arrigoni G, Cozza G, Lolli G, Battistutta R, Izpisua Belmonte JC, Pinna LA, Sarno S. (2014) The lysine-specific demethylase 1 is a novel substrate of protein kinase CK2. Biochim. Biophys. Acta 1844:722-729.
- Girardi C, James P, Zanin S, Pinna LA, Ruzzene M. (2014) Differential phosphorylation of Akt1 and Akt2 by protein kinase CK2 may account for isoform specific functions. Biochim. Biophys. Acta, 1843:1865-1874
- University of Padova
- MIUR (Italian Ministry of Education, Universities and Research)
- AIRC (Italian Association for Cancer Research)