Researcher Portfolio
Schäfer, Tillmann
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society
Researcher Profile
Position: Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society
Position: Cryo-EM Facility (Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society)
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons238712
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Publications
: Hickey, K. L., Panov, A., Whelan, E. M., Schäfer, T., Mizrak, A., Kopito, R. R., Baumeister, W., Fernández-Busnadiego, R., & Harper, J. W. (2024). Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. Proceedings of the National Academy of Sciences of the United States of America, 121(50): e2417390121. doi:10.1073/pnas.2417390121. [PubMan] : Bonneau, F., Basquin, J., Steigenberger, B., Schäfer, T., Schäfer, I. B., & Conti, E. (2023). Nuclear mRNPs are compact particles packaged with a network of proteins promoting RNA–RNA interactions. Genes & Development, 37(11-12), 505-517. doi:10.1101/gad.350630.123. [PubMan] : Riera Tur, I., Schäfer, T., Hornburg, D., Mishra, A., da Silva Padilha, M., Fernandez-Mosquera, L., Feigenbutz, D., Auer, P., Mann, M., Baumeister, W., Klein, R., Meissner, F., Raimundo, N., Fernandez-Busnadiego, R., & Dudanova, I. (2022). Amyloid-like aggregating proteins cause lysosomal defects in neurons via gain-of-function toxicity. Life science alliance, 5(3): e202101185. doi:10.26508/lsa.202101185. [PubMan] : Lee, J.-H., Bollschweiler, D., Schäfer, T., & Huber, R. (2021). Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies. Science Advances, 7(2): eabd4413. doi:10.1126/sciadv.abd4413. [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] : Schäfer, T. (2018). Correlative cryo-electron tomography studies of artificial beta-protein aggregates in mammalian cells. PhD Thesis, TUM, München. [PubMan]