Researcher Portfolio
Dr. Theobalt, Christian
Computer Graphics, MPI for Informatics, Max Planck Society, Programming Logics, MPI for Informatics, Max Planck Society, Visual Computing and Artificial Intelligence, MPI for Informatics, Max Planck Society
Researcher Profile
Position: Visual Computing and Artificial Intelligence, MPI for Informatics, Max Planck Society
Position: Computer Graphics, MPI for Informatics, Max Planck Society
Position: Programming Logics, MPI for Informatics, Max Planck Society
Additional IDs: ORCID:
https://orcid.org/0000-0001-6104-6625
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons45610
External references
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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] : Li, J., Purser, N., Liwocha, J., Scott, D. C., Byers, H. A., Steigenberger, B., Hill, S., Tripathi-Giesgen, I., Hinkle, T., Hansen, F. M., Prabu, J. R., Radhakrishnan, S. K., Kirkpatrick, D. S., Reichermeier, K. M., Schulman, B. A., & Kleiger, G. (2024). Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting. Molecular Cell, 84(7), 1304-1320. doi:10.1016/j.molcel.2024.01.022. [PubMan] : Liwocha, J., Li, J., Purser, N., Rattanasopa, C., Maiwald, S., Krist, D. T., Scott, D. C., Steigenberger, B., Prabu, J. R., Schulman, B. A., & Kleiger, G. (2024). Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases. Nature Structural & Molecular Biology, 31(2), 378-389. doi:10.1038/s41594-023-01206-1. [PubMan] : Hehl, L. A., Horn-Ghetko, D., Prabu, J. R., Vollrath, R., Tung Vu, D., Pérez Berrocal, D. A., Mulder, M. P. C., van der Heden van Noort, G. J., & Schulman, B. A. (2024). Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5. Nature Chemical Biology, 20, 190-200. doi:10.1038/s41589-023-01414-2. [PubMan] : Chrustowicz, J., Sherpa, D., Li, J., Langlois, C. R., Papadopoulou, E. C., Tung Vu, D., Hehl, L. A., Karayel, Ö., Beier, V., Gronau, S. v., Müller, J., Prabu, J. R., Mann, M., Kleiger, G., Alpi, A. F., & Schulman, B. A. (2024). Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies. Molecular Cell, 84(2), 293-308. doi:10.1016/j.molcel.2023.11.027. [PubMan] : Wallace, I., Baek, K., Prabu, J. R., Vollrath, R., von Gronau, S., Schulman, B. A., & Swatek, K. N. (2023). Insights into the ISG15 transfer cascade by the UBE1L activating enzyme. Nature Communications, 14(1): 7970. doi:10.1038/s41467-023-43711-3. [PubMan] : Chrustowicz, J., Sherpa, D., Teyra, J., Loke, M. S., Popowicz, G. M., Basquin, J., Sattler, M., Prabu, J. R., Sidhu, S. S., & Schulman, B. (2022). Multifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases. Journal of Molecular Biology, 434(2): 167347. doi:10.1016/j.jmb.2021.167347. [PubMan] : Ferguson, C. J., Urso, O., Bodrug, T., Gassaway, B. M., Watson, E. R., Prabu, J. R., Lara-Gonzalez, P., Martinez-Chacin, R. C., Wu, D. Y., Brigatti, K. W., Puffenberger, E. G., Taylor, C. M., Haas-Givler, B., Jinks, R. N., Strauss, K. A., Desai, A., Gabel, H. W., Gygi, S. P., Schulman, B. A., Brown, N. G., & Bonni, A. (2022). APC7 mediates ubiquitin signaling in constitutive heterochromatin in the developing mammalian brain. Molecular Cell, 82(1), 90-105. doi:10.1016/j.molcel.2021.11.031. [PubMan] : Horn-Ghetko, D., Krist, D. T., Prabu, J. R., Baek, K., Mulder, M. P. C., Kluegel, M., Scott, D. C., Ovaa, H., Kleiger, G., & Schulman, B. (2021). Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly. Nature, 590(7847), 671-676. doi:10.1038/s41586-021-03197-9. [PubMan] : Sherpa, D., Chrustowicz, J., Qiao, S., Langlois, C. R., Hehl, L. A., Gottemukkala, K. V., Hansen, F. M., Karayel, O., von Gronau, S., Prabu, J. R., Mann, M., Alpi, A. F., & Schulman, B. A. (2021). GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme. Molecular Cell, 81(11), 2445-2459.e13. doi:10.1016/j.molcel.2021.03.025. [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] : Miller-Vedam, L. E., Bräuning, B., Popova, K. D., Oakdale, N. T. S., Bonnar, J. L., Prabu, J. R., Boydston, E. A., Sevillano, N., Shurtleff, M. J., Stroud, R. M., Craik, C. S., Schulman, B. A., Frost, A., & Weissman, J. S. (2020). Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. eLife, 9: e62611. doi:10.7554/eLife.62611. [PubMan] : Oh, E., Mark, K. G., Mocciaro, A., Watson, E. R., Prabu, J. R., Cha, D. D., Kampmann, M., Gamarra, N., Zhou, C. Y., & Rape, M. (2020). Gene expression and cell identity controlled by anaphase-promoting complex. Nature, 579, 136-140. doi:10.1038/s41586-020-2034-1. [PubMan] : Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020). NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly. Nature, 578, 461-466. doi:10.1038/s41586-020-2000-y. [PubMan] : Schuller, S. K., Schuller, J. M., Prabu, J. R., Baumgärtner, M., Bonneau, F., Basquin, J., & Conti, E. (2020). Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex. eLife, 9: e61467. doi:10.7554/eLife.61467. [PubMan] : Qiao, S., Langlois, C. R., Chrustowicz, J., Sherpa, D., Karayel, O., Hansen, F. M., Beier, V., von Gronau, S., Bollschweiler, D., Schäfer, T., Alpi, A. F., Mann, M., Prabu, J. R., & Schulman, B. (2020). Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. MOLECULAR CELL, 77(1), 150-163.e9. doi:10.1016/j.molcel.2019.10.009. [PubMan] : Watson, E. R., Grace, C. R. R., Zhang, W., Miller, D. J., Davidson, I. F., Prabu, J. R., Yu, S., Bolhuis, D. L., Kulko, E. T., Vollrath, R., Haselbach, D., Stark, H., Peters, J.-M., Brown, N. G., Sidhu, S. S., & Schulman, B. A. (2019). Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site. Proceedings of the National Academy of Sciences of the United States of America, 116(35), 17280-17289. doi:10.1073/pnas.1902889116. [PubMan] : Ozgur, S., Buchwald, G., Falk, S., Chakrabarti, S., Prabu, J. R., & Conti, E. (2015). The conformational plasticity of eukaryotic RNA-dependent ATPases. The FEBS Journal, 282(5), 850-863. doi:10.1111/febs.13198. [PubMan] : Prabu, J. R., Müller, M., Thomae, A. W., Schüssler, S., Bonneau, F., Becker, P. B., & Conti, E. (2015). Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. MOLECULAR CELL, 60(3), 487-499. doi:10.1016/j.molcel.2015.10.011. [PubMan] : Schmalen, I., Reischl, S., Wallach, T., Klemz, R., Grudziecki, A., Prabu, J. R., Benda, C., Kramer, A., & Wolf, E. (2014). Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation. CELL, 157(5), 1203-1215. doi:10.1016/j.cell.2014.03.057. [PubMan]