Researcher Portfolio
Kraus, Michael
Numerical Methods in Plasma Physics (NMPP), Max Planck Institute for Plasma Physics, Max Planck Society, Tokamak Theory (TOK), Max Planck Institute for Plasma Physics, Max Planck Society
Researcher Profile
Position: Tokamak Theory (TOK), Max Planck Institute for Plasma Physics, Max Planck Society
Position: Numerical Methods in Plasma Physics (NMPP), Max Planck Institute for Plasma Physics, Max Planck Society
Additional IDs: ORCID:
https://orcid.org/0000-0001-7637-3979
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons109696
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]