Researcher Portfolio
Cerdá Doñate, Elisa
Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society
Researcher Profile
Position: Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons255241
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Publications
: Strachan, J., Leidecker, O., Spanos, C., Le Coz, C., Chapman, E., Arsenijevic, A., Zhang, H., Zhao, N., Spoel, S. H., & Bayne, E. H. (2023). SUMOylation regulates Lem2 function in centromere clustering and silencing. Journal of Cell Science. doi:10.1242/jcs.260868. [PubMan] : Ratz, L., Brambillasca, C., Bartke, L., Huetzen, M. A., Goergens, J., Leidecker, O., Jachimowicz, R. D., van de Ven, M., Proost, N., Siteur, B., de Korte-Grimmerink, R., Bouwman, P., Pulver, E. M., de Bruijn, R., Isensee, J., Hucho, T., Pandey, G., van Lohuizen, M., Mallmann, P., Reinhardt, H. C., Jonkers, J., & Puppe, J. (2022). Combined inhibition of EZH2 and ATM is synthetic lethal in BRCA1-deficient breast cancer. Breast Cancer Res, 24(1), 41. doi:10.1186/s13058-022-01534-y. [PubMan] : Bonfiglio, J. J., Leidecker, O., Dauben, H., Longarini, E. J., Colby, T., San Segundo-Acosta, P., Perez, K. A., & Matic, I. (2020). An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell, 183(4), 1086-1102 e23. doi:10.1016/j.cell.2020.09.055. [PubMan] : Palazzo, L., Leidecker, O., Prokhorova, E., Dauben, H., Matić, I., & Ahel, I. (2018). Serine is the major residue for ADP-ribosylation upon DNA damage. Elife, 7. doi:10.7554/eLife.34334. [PubMan] : Leidecker, O., Bonfiglio, J. J., Colby, T., Zhang, Q., Atanassov, I., Zaja, R., Palazzo, L., Stockum, A., Ahel, I., & Matić, I. (2016). Serine is a new target residue for endogenous ADP-ribosylation on histones. Nat Chem Biol, 12(12), 998-1000. doi:10.1038/nchembio.2180. [PubMan] : Rack, J. G., Morra, R., Barkauskaite, E., Kraehenbuehl, R., Ariza, A., Qu, Y., Ortmayer, M., Leidecker, O., Cameron, D. R., Matić, I., Peleg, A. Y., Leys, D., Traven, A., & Ahel, I. (2015). Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Mol Cell, 59(2), 309-20. doi:10.1016/j.molcel.2015.06.013. [PubMan] : Palazzo, L., Thomas, B., Jemth, A. S., Colby, T., Leidecker, O., Feijs, K. L., Zaja, R., Loseva, O., Puigvert, J. C., Matić, I., Helleday, T., & Ahel, I. (2015). Processing of protein ADP-ribosylation by Nudix hydrolases. Biochem J, 468(2), 293-301. doi:10.1042/BJ20141554. [PubMan] : Leidecker, O., Matić, I., Mahata, B., Pion, E., & Xirodimas, D. P. (2012). The ubiquitin E1 enzyme Ube1 mediates NEDD8 activation under diverse stress conditions. Cell Cycle, 11(6), 1142-50. doi:10.4161/cc.11.6.19559. [PubMan]