Researcher Portfolio

 
   

Kostrhon, Sebastian

Department of Biochemistry, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria, Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society  

 

Researcher Profile

 
Position: Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society
Position: Department of Biochemistry, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons213734

External references

 
WorldCat Search for Kostrhon, Sebastian
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Publications

 
 
 : Horn-Ghetko, D., Hopf, L. V. M., Tripathi-Giesgen, I., Du, J., Kostrhon, S., Tung Vu, D., Beier, V., Steigenberger, B., Prabu, J. R., Stier, L., Bruss, E. M., Mann, M., Xiong, Y., & Schulman, B. A. (2024). Noncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex. Nature Structural & Molecular Biology, 31(7), 1083-1094. doi:10.1038/s41594-024-01257-y. [PubMan] : Berrocal, D. A. P. A., Vishwanatha, T. M., Horn-Ghetko, D., Botsch, J. J., Hehl, L. A., Kostrhon, S., Misra, M., Dikic, I., Geurink, P. P., van Dam, H., Schulman, B. A., & Mulder, M. P. C. (2023). A Pro-Fluorescent Ubiquitin-Based Probe to Monitor Cysteine-Based E3 Ligase Activity. Angewandte Chemie International Edition, 62(32): e202303319. doi:10.1002/anie.202303319. [PubMan] : Kostrhon, S. (2022). Cryo-EM structure of CUL5-ARIH2 E3-E3 Ligase complex reveals novel allosteric NEDD8 mechanism. PhD Thesis, TUM, Fakultät für Chemie, München. [PubMan] : Kostrhon, S., Prabu, J. R., Baek, K., Horn-Ghetko, D., Gronau, S. v., Klügel, M., Basquin, J., Alpi, A. F., & Schulman, B. A. (2021). CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation. Nature Chemical Biology, 17(10), 1075-1083. doi:10.1038/s41589-021-00858-8. [PubMan]