Researcher Portfolio
Nusseck, Manfred
Department Human Perception, Cognition and Action, Max Planck Institute for Biological Cybernetics, Max Planck Society, Max Planck Institute for Biological Cybernetics, Max Planck Society
Researcher Profile
Position: Max Planck Institute for Biological Cybernetics, Max Planck Society
Position: Department Human Perception, Cognition and Action, Max Planck Institute for Biological Cybernetics, Max Planck Society
Additional IDs: MPIKYB: manfred
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons84115
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]