Researcher Portfolio
Sherpa, Dawafuti
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/persons238966
Publications
: 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] : 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] : Sherpa, D. (2022). Structural and functional characterization of GID/CTLH E3 ubiquitin ligases. PhD Thesis, Technische Universität, Fakultät für Chemie, München. [PubMan] : Sherpa, D., Mueller, J., Karayel, Ö., Xu, P., Yao, Y., Chrustowicz, J., Gottemukkala, K. V., Baumann, C. A., Gross, A., Czarnecki, O., Zhang, W., Gu, J., Nilvebrant, J., Sidhu, S. S., Murray, P. J., Mann, M., Weiss, M. J., Schulman, B. A., & Alpi, A. F. (2022). Modular UBE2H-CTLH E2-E3 complexes regulate erythroid maturation. eLife, 11: e77937. doi:10.7554/eLife.77937. [PubMan] : Langlois, C. R., Beier, V., Karayel, O., Chrustowicz, J., Sherpa, D., Mann, M., & Schulman, B. A. (2022). A GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters. EMBO Reports, 23(6): e53835. doi:10.15252/embr.202153835. [PubMan] : Qiao, S., Lee, C.-W., Sherpa, D., Chrustowicz, J., Cheng, J. D., Duennebacke, M., Steigenberger, B., Karayel, O., Tung Vu, D., Gronau, S. v., Mann, M., Wilfling, F., & Schulman, B. (2022). Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation. Nature Communications, 13(1): 3041. doi:10.1038/s41467-022-30803-9. [PubMan] : Sherpa, D., Chrustowicz, J., & Schulman, B. (2022). How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini. Molecular Cell, 82(8), 1424-1438. doi:10.1016/j.molcel.2022.02.004. [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] : 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] : Langlois, C. R., Qiao, S., Sherpa, D., Chrustowicz, J., Beier, V., Karayel, O., & Schulman, B. (2020). The GID E3 Ubiquitin Ligase Converts Between Anticipatory and Active States Through the Incorporation of Swappable Substrate Receptors. The FASEB Journal, 34, 1-1. [PubMan] : Wilfling, F., Lee, C.-W., Erdmann, P. S., Zheng, Y., Sherpa, D., Jentsch, S., Pfander, B., Schulman, B. A., & Baumeister, W. (2020). A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits. Molecular Cell, 80(5), 764-778.e7. doi:10.1016/j.molcel.2020.10.030. [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] : Sherpa, D. (2018). Structural and functional characterization of novel E3 ubiquitin ligase, focusing on Proline/N-end rule pathway. Master Thesis, Ludwig-Maximilians Universität, Dep. of Cell and Developmental Biology, München. [PubMan]