Researcher Portfolio
Schulman, Brenda
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
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons213292
Publications
(1 - 25 of 83)
: Muhar, M. F., Farnung, J., Cernakova, M., Hofmann, R., Henneberg, L. T., Pfleiderer, M. M., Denoth-Lippuner, A., Kalčic, F., Nievergelt, A. S., Peters Al-Bayati, M., Sidiropoulos, N. D., Beier, V., Mann, M., Jessberger, S., Jinek, M., Schulman, B., Bode, J. W., & Corn, J. E. (2025). C-terminal amides mark proteins for degradation via SCF–FBXO31. Nature, 638, 519-527. doi:10.1038/s41586-024-08475-w. [PubMan] : Kraus, F., He, Y., Swarup, S., Overmyer, K. A., Jiang, Y., Brenner, J., Capitanio, C., Bieber, A., Jen, A., Nightingale, N. M., Anderson, B. J., Lee, C., Paulo, J. A., Smith, I. R., Plitzko, J. M., Gygi, S. P., Schulman, B. A., Wilfling, F., Coon, J. J., & Harper, J. W. (2025). Global cellular proteo-lipidomic profiling of diverse lysosomal storage disease mutants using nMOST. Science Advances, 11(4): eadu5787. doi:10.1126/sciadv.adu5787. [PubMan] : Alkhalaf, L. M., Arrowsmith, C., Balskus, E. P., Bergamini, G., Bhandari, R., Chang, C. J., Chen, P., Chen, X., Ciulli, A., Cricco, J. A., Davis, B. G., Delbianco, M., Dudareva, N., Dueber, E., Ferguson, F., de Giuseppe, P. O., Hamachi, I., Hammond, M. C., Hatzios, S. K., Do Heo, W., Janet, J. P., Kamat, S. S., Knapp, S., Krishnan, Y., Lang, K., Laraia, L., Leveson-Gower, R. B., Li, X. D., Liu, D. R., Liu, M.-F., London, N., Mahanta, N., Mayor-Ruiz, C., Muir, T., Murakami, M. T., Rhee, H.-W., Robers, M., Satz, A., Schulman, B. A., Shen, B., Shoichet, B., Strauss, E., Suzuki, T., Tiwary, P., Waldmann, H., Ward, T. R., Weeks, A., Weerapana, E., & Winter, G. (2025). Thoughts for the future. Nature Chemical Biology, 21, 6-15. doi:10.1038/s41589-024-01802-2. [PubMan] : Scott, D. C., Chittori, S., Purser, N., King, M. T., Maiwald, S. A., Churion, K., Nourse, A., Lee, C., Paulo, J. A., Miller, D. J., Elledge, S. J., Harper, J. W., Kleiger, G., & Schulman, B. A. (2024). Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases. Nature Communications, 15(1): 9899. doi:10.1038/s41467-024-54126-z. [PubMan] : Farnung, J., & Schulman, B. A. (2024). Ubiquitin is a chemist's playground. Nature Chemistry, 16(11): 1918. doi:10.1038/s41557-024-01660-4. [PubMan] : Adolf, F., Du, J., Goodall, E. A., Walsh Jr, R. M., Rawson, S., Gronau, S. v., Harper, J. W., Hanna, J., & Schulman, B. A. (2024). Visualizing chaperone-mediated multistep assembly of the human 20S proteasome. Nature Structural & Molecular Biology, 31(8), 1176-1188. doi:10.1038/s41594-024-01268-9. [PubMan] : 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] : Kagiou, C., Cisneros, J. A., Farnung, J., Liwocha, J., Offensperger, F., Dong, K., Yang, K., Tin, G., Horstmann, C. S., Hinterndorfer, M., Paulo, J. A., Scholes, N. S., Sanchez Avila, J., Fellner, M., Andersch, F., Hannich, J. T., Zuber, J., Kubicek, S., Gygi, S. P., Schulman, B. A., & Winter, G. E. (2024). Alkylamine-tethered molecules recruit FBXO22 for targeted protein degradation. Nature Communications, 15(1): 5409. doi:10.1038/s41467-024-49739-3. [PubMan] : Yi, S. A., Sepic, S., Schulman, B. A., Ordureau, A., & An, H. (2024). mTORC1-CTLH E3 ligase regulates the degradation of HMG-CoA synthase 1 through the Pro/N-degron pathway. Molecular Cell, 84(11), 2166-2184. doi:10.1016/j.molcel.2024.04.026. [PubMan] : Gottemukkala, K. V., Chrustowicz, J., Sherpa, D., Sepic, S., Tung Vu, D., Karayel, O., Papadopoulou, E. C., Gross, A., Schorpp, K., von Gronau, S., Hadian, K., Murray, P. J., Mann, M., Schulman, B. A., & Alpi, A. F. (2024). Non-canonical substrate recognition by the human WDR26-CTLH E3 ligase regulates prodrug metabolism. Molecular Cell, 84(10), 1948-1963.e11. doi:10.1016/j.molcel.2024.04.014. [PubMan] : Gross, A., Müller, J., Chrustowicz, J., Strasser, A., Gottemukkala, K. V., Sherpa, D., Schulman, B. A., Murray, P. J., & Alpi, A. F. (2024). Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly. FEBS Letters, 598(9), 978-994. doi:10.1002/1873-3468.14866. [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] : Hoyer, M. J., Capitanio, C., Smith, I. R., Paoli, J. C., Bieber, A., Jiang, Y., Paulo, J. A., Gonzalez-Lozano, M. A., Baumeister, W., Wilfling, F., Schulman, B. A., & Harper, J. W. (2024). Combinatorial selective ER-phagy remodels the ER during neurogenesis. Nature Cell Biology, 26, 378-392. doi:10.1038/s41556-024-01356-4. [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] : Botsch, J. J., Junker, R., Sorgenfrei, M., Ogger, P. P., Stier, L., von Gronau, S., Murray, P. J., Seeger, M. A., Schulman, B. A., & Bräuning, B. (2024). Doa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE. Nature Communications, 15(1): 410. doi:10.1038/s41467-023-44670-5. [PubMan] : Lewis, S. C., Jourdain, A. A., Schulman, B. A., Vousden, K. H., Fabius, J. M., & Liu, H. (2024). Recovering from the stress of the COVID-19 pandemic. Molecular Cell, 84(1), 8-11. doi:10.1016/j.molcel.2023.11.013. [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] : Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., & Schulman, B. A. (2023). Activity-based profiling of cullin-RING E3 networks by conformation-specific probes. Nature Chemical Biology, 19, 1513-1523. doi:10.1038/s41589-023-01392-5. [PubMan] : Purser, N., Tripathi-Giesgen, I., Li, J., Scott, D. C., Horn-Ghetko, D., Baek, K., Schulman, B. A., Alpi, A. F., & Kleiger, G. (2023). Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase. Biochemical Journal, 480(22), 1817-1831. doi:10.1042/BCJ20230373. [PubMan] : Hehl, L. A., & Schulman, B. A. (2023). To be (in a transcriptional complex) or not to be (promoting UBR5 ubiquitylation): That is an answer to how degradation controls gene expression. Molecular Cell, 83(15), 2616-2618. doi:10.1016/j.molcel.2023.07.010. [PubMan] : Kraus, F., Goodall, E. A., Smith, I. R., Jiang, Y., Paoli, J. C., Adolf, F., Zhang, J., Paulo, J. A., Schulman, B. A., & Harper, J. W. (2023). PARK15/FBXO7 is dispensable for PINK1/Parkin mitophagy in iNeurons and HeLa cell systems. EMBO Reports, 24(8): e56399. doi:10.15252/embr.202256399. [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] : Gonzalez, A., Covarrubias-Pinto, A., Bhaskara, R. M., Glogger, M., Kuncha, S. K., Xavier, A., Seemann, E., Misra, M., Hoffmann, M. E., Bräuning, B., Balakrishnan, A., Qualmann, B., Doetsch, V., Schulman, B. A., Kessels, M. M., Huebner, C. A., Heilemann, M., Hummer, G., & Dikic, I. (2023). Ubiquitination regulates ER-phagy and remodelling of endoplasmic reticulum. Nature, 618(7964), 394-401. doi:10.1038/s41586-023-06089-2. [PubMan]