Researcher Portfolio

Zweckstetter, Markus

Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, Research Group of Protein Structure Determination using NMR, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society

Researcher Profile

Position: Research Group of Protein Structure Determination using NMR, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society

Position: Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society

Researcher ID: https://pure.mpg.de/cone/persons/resource/persons16093

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Publications

(1 - 25 of 298)

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: Putko, P., Romero, J. A., Pantoja, C. F., Zweckstetter, M., Kazimierczuk, K., & Zawadzka-Kazimierczuk, A. (2025). Using temperature coefficients to support resonance assignment of intrinsically disordered proteins. Journal of Biomolecular NMR, 79, 59-65. doi:10.1007/s10858-024-00452-9. [PubMan] : Brücke, C., Al-Azzani, M., Ramalingam, N., Ramón, M., Sousa, R. L., Buratti, F., Zech, M., Sicking, K., Amaral, L., Gelpi, E., Chandran, A., Agarwal, A., Chaves, S. R., Fernández, C. O., Dettmer, U., Lautenschläger, J., Zweckstetter, M., Fernandez Busnadiego, R., Zimprich, A., & Outeiro, T. F. (2025). A novel alpha-synuclein G14R missense variant is associated with atypical neuropathological features. medRxiv. doi:10.1101/2024.09.23.24313864. [PubMan] : Chakraborty, P., & Zweckstetter, M. (2025). Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation. Nature Communications, 16: 669. doi:10.1038/s41467-025-56028-0. [PubMan] : Kulvicius, T., Zhang, D., Poustka, L., Bölte, S., Jahn, L., Flügge, S., Kraft, M., Zweckstetter, M., Nielsen-Saines, K., Wörgötter, F., & Marschik, P. B. (2025). Deep learning empowered sensor fusion boosts infant movement classification. Communications Medicine, 5: 16. doi:10.1038/s43856-024-00701-w. [PubMan] : Marvian, A., Strauss, T., Tang, Q., Tuck, B., Keeling, S., Rüdiger, D., Mirzazadeh Dizaji, N., Mohammad-Beigi, H., Nuscher, B., Chakraborty, P., Sutherland, D., McEwan, W., Köglsperger, T., Zahler, S., Zweckstetter, M., Lichtenthaler, S., Wurst, W., Schwarz, S., & Höglinger, G. (2024). Distinct regulation of Tau Monomer and aggregate uptake and intracellular accumulation in human neurons. Molecular Neurodegeneration, 19: 100. doi:10.1186/s13024-024-00786-w. [PubMan] : Chakraborty, P., Ibáñez de Opakua, A., Purslow, J. A., Fromm, S. A., Chatterjee, D., Zachrdla, M., Zhuang, S., Puri, S., Wolozin, B., & Zweckstetter, M. (2024). GSK3β phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments. Proceedings of the National Academy of Sciences of the United States of America, 121(52): e2414176121. doi:10.1073/pnas.2414176121. [PubMan] : Ukmar‐Godec, T., Yu, T., de Opakua, A. I., Pantoja, C. F., Munari, F., & Zweckstetter, M. (2024). Conformational diversity of human HP1α. Protein Science, 33(7): e5079. doi:10.1002/pro.5079. [PubMan] : Ibáñez de Opakua, A., Pantoja, C. F., Cima-Omori, M.-S., Dienemann, C., & Zweckstetter, M. (2024). Impact of distinct FG nucleoporin repeats on Nup98 self-association. Nature Communications, 15: 3797. doi:10.1038/s41467-024-48194-4. [PubMan] : Antón, R., Treviño, M., Pantoja-Uceda, D., Félix, S., Babu, M., Cabrita, E., Zweckstetter, M., Tinnefeld, P., Vera, A., & Oroz, J. (2024). Alternative low-populated conformations prompt phase transitions in polyalanine repeat expansions. Nature Communications, 15(1): 1925. doi:10.1038/s41467-024-46236-5. [PubMan] : Zhuang, S., Chakraborty, P., & Zweckstetter, M. (2024). Regulation of tau by peptidyl-prolyl isomerases. Current Opinion in Structural Biology, 84: 102739. doi:10.1016/j.sbi.2023.102739. [PubMan] : Ukmar-Godec, T., Cima-Omori, M.-S., Yerkesh, Z., Eswara, K., Yu, T., Ramesh, R., Riviere, G., de Opakua, A., Fischle, W., & Zweckstetter, M. (2023). Multimodal interactions drive chromatin phase separation and compaction. Proceedings of the National Academy of Sciences of the United States of America, 120(50): e2308858120. doi:10.1073/pnas.2308858120. [PubMan] : Shen, Z., Sun, D., Savastano, A., Varga, S. J., Cima-Omori, M.-S., Becker, S., Honigmann, A., & Zweckstetter, M. (2023). Multivalent Tau/PSD-95 interactions arrest in vitro condensates and clusters mimicking the postsynaptic density. Nature Communications, 14: 6839. doi:10.1038/s41467-023-42295-2. [PubMan] : Chakraborty, P., & Zweckstetter, M. (2023). Role of aberrant phase separation in pathological protein aggregation. Current Opinion in Structural Biology, 82: 102678. doi:10.1016/j.sbi.2023.102678. [PubMan] : Huang, Y., Wen, J., Ramirez, L.-M., Gümüşdil, E., Pokhrel, P., Man, V. H., Ye, H., Han, Y., Liu, Y., Li, P., Su, Z., Wang, J., Mao, H., Zweckstetter, M., Perrett, S., Wu, S., & Gao, M. (2023). Methylene blue accelerates liquid-to-gel transition of tau condensates impacting tau function and pathology. Nature Communications, 14: 5444. doi:10.1038/s41467-023-41241-6. [PubMan] : Zhang, S., Dauer, K., Strohäker, T., Tatenhorst, L., Gomes, L. C., Mayer, S., Jung, B. C., Kim, W. S. S., Lee, S.-J., Becker, S., Liesche-Starnecker, F., Zweckstetter, M., & Lingor, P. (2023). Alpha-synuclein fibrils amplified from multiple system atrophy and Parkinson's disease patient brain spread after intracerebral injection into mouse brain. Brain Pathology, 33(5): e13196. doi:10.1111/bpa.13196. [PubMan] : Buratti, F. A., Fernández, C. O., & Zweckstetter, M. (2023). Parkinson's disease-linked V15A mutation facilitates α-synuclein aggregation by reducing membrane affinity. Protein Science, 32(8): e4693. doi:10.1002/pro.4693. [PubMan] : Yu, T., Flores-Solis, D., Eastep, G., Becker, S., & Zweckstetter, M. (2023). Phosphatidylserine-dependent structure of synaptogyrin remodels the synaptic vesicle membrane. Nature Structural and Molecular Biology, 30, 926-934. doi:10.1038/s41594-023-01004-9. [PubMan] : Ramirez, L., & Zweckstetter, M. (2023). Molecular-level interplay between intrinsically disordered clients and Hsp90. Current Opinion in Chemical Biology, 74: 102304. doi:10.1016/j.cbpa.2023.102304. [PubMan] : Edkins, A. L. L., Zweckstetter, M., & Sawarkar, R. (2023). Tenth International Symposium on the Hsp90 chaperone machine. Cell Stress and Chaperones, 28, 231-237. doi:10.1007/s12192-023-01342-z. [PubMan] : Pantoja, C., Ibáñez de Opakua, A., Cima-Omori, M.-S., & Zweckstetter, M. (2023). Determining the Physico-Chemical Composition of Biomolecular Condensates from Spatially-Resolved NMR. Angewandte Chemie International Edition, 62(17): e202218078. doi:10.1002/anie.202218078. [PubMan] : Rosado-Ramos, R., Poças, G. M., Marques, D., Foito, A., Sevillano, D. M., Lopes-da-Silva, M., Gonçalves, L. G., Menezes, R., Ottens, M., Stewart, D., de Opakua, A. I., Zweckstetter, M., Seabra, M. C., Mendes, C. S., Outeiro, T. F., Domingos, P. M., & Santos, C. N. (2023). Genipin prevents alpha-synuclein aggregation and toxicity by affecting endocytosis, metabolism and lipid storage. Nature Communications, 14: 1918. doi:10.1038/s41467-023-37561-2. [PubMan] : Abyzov, A., Mandelkow, E., Zweckstetter, M., & Rezaei-Ghaleh, N. (2023). Fast Motions Dominate Dynamics of Intrinsically Disordered Tau Protein at High Temperatures. Chemistry – A European Journal, 29(17): e202203493. doi:10.1002/chem.202203493. [PubMan] : Boeynaems, S., Chong, S., Gsponer, J., Holt, L., Milovanovic, D., Mitrea, D. M., Mueller-Cajar, O., Portz, B., Reilly, J. F., Reinkemeier, C. D., Sabari, B. R., Sanulli, S., Shorter, J., Sontag, E., Strader, L., Stachowiak, J., Weber, S. C., White, M., Zhang, H., Zweckstetter, M., Elbaum-Garfinkle, S., & Kriwacki, R. (2023). Phase Separation in Biology and Disease; Current Perspectives and Open Questions. Journal of Molecular Biology, 435(5): 167971. doi:10.1016/j.jmb.2023.167971. [PubMan] : Jiang, L., Chakraborty, P., Zhang, L., Wong, M., Hill, S. E., Webber, C. J., Libera, J., Blair, L. J., Wolozin, B., & Zweckstetter, M. (2023). Chaperoning of specific tau structure by immunophilin FKBP12 regulates the neuronal resilience to extracellular stress. Science Advances, 9(5): eadd9789. doi:10.1126/sciadv.add9789. [PubMan] : Chakraborty, P., Rivière, G., Hebestreit, A., de Opakua, A., Vorberg, I., Andreas, L. B., & Zweckstetter, M. (2023). Acetylation discriminates disease-specific tau deposition. Nature Communications, 14(1): 5919. doi:10.1038/s41467-023-41672-1. [PubMan]