Max Planck Institute for Multidisciplinary Sciences

Publications

Journal Article (294)

1.

Journal Article

Putko, P.; Romero, J. A.; Pantoja, C. F.; Zweckstetter, M.; Kazimierczuk, K.; Zawadzka-Kazimierczuk, A.: Using temperature coefficients to support resonance assignment of intrinsically disordered proteins. Journal of Biomolecular NMR 79, pp. 59 - 65 (2025)

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2.

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Chakraborty, P.; Zweckstetter, M.: Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation. Nature Communications 16, 669 (2025)

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3.

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Kulvicius, T.; Zhang, D.; Poustka, L.; Bölte, S.; Jahn, L.; Flügge, S.; Kraft, M.; Zweckstetter, M.; Nielsen-Saines, K.; Wörgötter, F. et al.; Marschik, P. B.: Deep learning empowered sensor fusion boosts infant movement classification. Communications Medicine 5, 16 (2025)

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4.

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Marvian, A.T.; Strauss, T.; Tang, Q.; Tuck, B.J.; Keeling, S.; Rüdiger, D.; Mirzazadeh Dizaji, N.; Mohammad-Beigi, H.; Nuscher, B.; Chakraborty, P. et al.; Sutherland, D.S.; McEwan, W.A.; Köglsperger, T.; Zahler, S.; Zweckstetter, M.; Lichtenthaler, S.F.; Wurst, W.; Schwarz, S.; Höglinger, G.: Distinct regulation of Tau Monomer and aggregate uptake and intracellular accumulation in human neurons. Molecular Neurodegeneration 19, 100 (2024)

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5.

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Chakraborty, P.; Ibáñez de Opakua, A.; Purslow, J. A.; Fromm, S. A.; Chatterjee, D.; Zachrdla, M.; Zhuang, S.; Puri, S.; Wolozin, B.; Zweckstetter, M.: 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 (2024)

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6.

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Ukmar‐Godec, T.; Yu, T.; de Opakua, A. I.; Pantoja, C. F.; Munari, F.; Zweckstetter, M.: Conformational diversity of human HP1α. Protein Science 33 (7), e5079 (2024)

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7.

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Ibáñez de Opakua, A.; Pantoja, C. F.; Cima-Omori, M.-S.; Dienemann, C.; Zweckstetter, M.: Impact of distinct FG nucleoporin repeats on Nup98 self-association. Nature Communications 15, 3797 (2024)

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8.

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Antón, R.; Treviño, M.Á.; Pantoja-Uceda, D.; Félix, S.; Babu, M.; Cabrita, E.J.; Zweckstetter, M.; Tinnefeld, P.; Vera, A.M.; Oroz, J.: Alternative low-populated conformations prompt phase transitions in polyalanine repeat expansions. Nature Communications 15 (1), 1925 (2024)

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9.

Journal Article

Zhuang, S.; Chakraborty, P.; Zweckstetter, M.: Regulation of tau by peptidyl-prolyl isomerases. Current Opinion in Structural Biology 84, 102739 (2024)

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10.

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Ukmar-Godec, T.; Cima-Omori, M.-S.; Yerkesh, Z.; Eswara, K.; Yu, T.; Ramesh, R.; Riviere, G.; de Opakua, A.I.; Fischle, W.; Zweckstetter, M.: Multimodal interactions drive chromatin phase separation and compaction. Proceedings of the National Academy of Sciences of the United States of America 120 (50), e2308858120 (2023)

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11.

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Shen, Z.; Sun, D.; Savastano, A.; Varga, S. J.; Cima-Omori, M.-S.; Becker, S.; Honigmann, A.; Zweckstetter, M.: Multivalent Tau/PSD-95 interactions arrest in vitro condensates and clusters mimicking the postsynaptic density. Nature Communications 14, 6839 (2023)

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12.

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Chakraborty, P.; Zweckstetter, M.: Role of aberrant phase separation in pathological protein aggregation. Current Opinion in Structural Biology 82, 102678 (2023)

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13.

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Huang, Y.; Wen, J.; Ramirez, L.-M.; Gümüşdil, E.; Pokhrel, P.; Man, V. H.; Ye, H.; Han, Y.; Liu, Y.; Li, P. et al.; Su, Z.; Wang, J.; Mao, H.; Zweckstetter, M.; Perrett, S.; Wu, S.; Gao, M.: Methylene blue accelerates liquid-to-gel transition of tau condensates impacting tau function and pathology. Nature Communications 14, 5444 (2023)

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14.

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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. et al.; Liesche-Starnecker, F.; Zweckstetter, M.; Lingor, P.: 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 (2023)

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15.

Journal Article

Buratti, F. A.; Fernández, C. O.; Zweckstetter, M.: Parkinson's disease-linked V15A mutation facilitates α-synuclein aggregation by reducing membrane affinity. Protein Science 32 (8), e4693 (2023)

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16.

Journal Article

Yu, T.; Flores-Solis, D.; Eastep, G.N.; Becker, S.; Zweckstetter, M.: Phosphatidylserine-dependent structure of synaptogyrin remodels the synaptic vesicle membrane. Nature Structural and Molecular Biology 30, pp. 926 - 934 (2023)

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17.

Journal Article

Ramirez, L.M.; Zweckstetter, M.: Molecular-level interplay between intrinsically disordered clients and Hsp90. Current Opinion in Chemical Biology 74, 102304 (2023)

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18.

Journal Article

Edkins, A. L. L.; Zweckstetter, M.; Sawarkar, R.: Tenth International Symposium on the Hsp90 chaperone machine. Cell Stress and Chaperones 28, pp. 231 - 237 (2023)

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19.

Journal Article

Pantoja, C.F.; Ibáñez de Opakua, A.; Cima-Omori, M.-S.; Zweckstetter, M.: Determining the Physico-Chemical Composition of Biomolecular Condensates from Spatially-Resolved NMR. Angewandte Chemie International Edition 62 (17), e202218078 (2023)

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20.

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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. et al.; de Opakua, A. I.; Zweckstetter, M.; Seabra, M. C.; Mendes, C. S.; Outeiro, T. F.; Domingos, P. M.; Santos, C. N.: Genipin prevents alpha-synuclein aggregation and toxicity by affecting endocytosis, metabolism and lipid storage. Nature Communications 14, 1918 (2023)

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21.

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Abyzov, A.; Mandelkow, E.; Zweckstetter, M.; Rezaei-Ghaleh, N.: Fast Motions Dominate Dynamics of Intrinsically Disordered Tau Protein at High Temperatures. Chemistry – A European Journal 29 (17), e202203493 (2023)

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22.

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Boeynaems, S.; Chong, S.; Gsponer, J.; Holt, L.; Milovanovic, D.; Mitrea, D. M.; Mueller-Cajar, O.; Portz, B.; Reilly, J. F.; Reinkemeier, C. D. et al.; 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.: Phase Separation in Biology and Disease; Current Perspectives and Open Questions. Journal of Molecular Biology 435 (5), 167971 (2023)

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23.

Journal Article

Jiang, L.; Chakraborty, P.; Zhang, L.; Wong, M.; Hill, S. E.; Webber, C. J.; Libera, J.; Blair, L. J.; Wolozin, B.; Zweckstetter, M.: Chaperoning of specific tau structure by immunophilin FKBP12 regulates the neuronal resilience to extracellular stress. Science Advances 9 (5), eadd9789 (2023)

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24.

Journal Article

Chakraborty, P.; Rivière, G.; Hebestreit, A.; de Opakua, A.I.; Vorberg, I.M.; Andreas, L. B.; Zweckstetter, M.: Acetylation discriminates disease-specific tau deposition. Nature Communications 14 (1), 5919 (2023)

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25.

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Flores-Solis, D.; Lushpinskaia, I.P.; Polyansky, A.A.; Changiarath, A.; Boehning, M.; Mirkovic, M.; Walshe, J.; Pietrek, L.M.; Cramer, P.; Stelzl, L.S. et al.; Zagrovic, B.; Zweckstetter, M.: Driving forces behind phase separation of the carboxy-terminal domain of RNA polymerase II. Nature Communications 14 (1), 5979 (2023)

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26.

Journal Article

Lushpinskaia, I. P. P.; Flores-Solis, D.; Zweckstetter, M.: Structure and phase separation of the C-terminal domain of RNA polymerase II. Biological Chemistry 404 (8-9), pp. 839 - 844 (2023)

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27.

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Brás, I. C.; Khani, M. H.; Vasili, E.; Möbius, W.; Riedel, D.; Parfentev, I.; Gerhardt, E.; Fahlbusch, C.; Urlaub, H.; Zweckstetter, M. et al.; Gollisch, T.; Outeiro, T. F.: Molecular Mechanisms Mediating the Transfer of Disease-Associated Proteins and Effects on Neuronal Activity. Journal of Parkinson's Disease: JPD 12, pp. 2397 - 2422 (2022)

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28.

Journal Article

Chakraborty, P.; Zweckstetter, M.: Phase separation of the microtubule-associated protein tau. Essays in Biochemistry 66 (7), pp. 1013 - 1021 (2022)

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29.

Journal Article

de Opakua, A. I.; Geraets, J. A.; Frieg, B.; Dienemann, C.; Savastano, A.; Rankovic, M.; Cima-Omori, M.-S.; Schröder, G. F.; Zweckstetter, M.: Molecular interactions of FG nucleoporin repeats at high resolution. Nature Chemistry 14, pp. 1278 - 1285 (2022)

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30.

Journal Article

Sang, D.; Shu, T.; Pantoja, C. F.; de Opakua, A. I.; Zweckstetter, M.; Holt, L. J.: Condensed-phase signaling can expand kinase specificity and respond to macromolecular crowding. Molecular Cell 82 (19), pp. 3693 - 3711.e10 (2022)

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31.

Journal Article

Frieg, B.; Geraets, J. A.; Strohaeker, T.; Dienemann, C.; Mavroeidi, P.; Jung, B. C.; Kim, W. S.; Lee, S.-J.; Xilouri, M.; Zweckstetter, M. et al.; Schroeder, G. F.: Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein. Communications Biology 5 (1), 1040 (2022)

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32.

Journal Article

Babu, M.; Favretto, F.; Rankovic, M.; Zweckstetter, M.: Peptidyl Prolyl Isomerase A Modulates the Liquid–Liquid Phase Separation of Proline-Rich IDPs. Journal of the American Chemical Society 144 (35), pp. 16157 - 16163 (2022)

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33.

Journal Article

Zachrdla, M.; Savastano, A.; de Opakua, A. I.; Cima-Omori, M.-S.; Zweckstetter, M.: Contributions of the N-terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA-induced phase separation. Protein Science 31 (9), e4409 (2022)

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34.

Journal Article

Buratti, F. A.; Boeffinger, N.; Garro, H. A.; Flores, J. S.; Hita, F. J.; Gonçalves, P. d. C.; Copello, F. d. R.; Lizarraga, L.; Rossetti, G.; Carloni, P. et al.; Zweckstetter, M.; Outeiro, T. F.; Eimer, S.; Griesinger, C.; Fernández, C. O.: Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformations. Protein Science 31 (7), e4360 (2022)

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35.

Journal Article

Kumar, S. T.; Mahul-Mellier, A.-L.; Hegde, R. N.; Riviere, G.; Moons, R.; de Opakua, A. I.; Magalhaes, P.; Rostami, I.; Donzelli, S.; Sobott, F. et al.; Zweckstetter, M.; Lashuel, H. A.: A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity. Science Advances 8 (17), eabn0044 (2022)

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36.

Journal Article

Min, J.-O.; Strohäker, T.; Jeong, B.-C.; Zweckstetter, M.; Lee, S.-J.: Chicago sky blue 6B inhibits α-synuclein aggregation and propagation. Molecular Brain 15, 27 (2022)

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37.

Journal Article

Stelzl, L. S.; Pietrek, L. M.; Holla, A.; Oroz, J.; Sikora, M.; Köfinger, J.; Schuler, B.; Zweckstetter, M.; Hummer, G.: Global Structure of the Intrinsically Disordered Protein Tau Emerges from Its Local Structure. JACS Au 2 (3), pp. 673 - 686 (2022)

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38.

Journal Article

Abyzov, A.; Blackledge, M.; Zweckstetter, M.: Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry. Chemical Reviews 122 (6), pp. 6719 - 6748 (2022)

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39.

Journal Article

Diez, L.; Kapinos, L. E.; Hochmair, J.; Huebschmann, S.; Dominguez-Baquero, A.; Vogt, A.; Rankovic, M.; Zweckstetter, M.; Lim, R. Y. H.; Wegmann, S.: Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98. International Journal of Molecular Sciences 23 (7), 3495 (2022)

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40.

Journal Article

Pantoja, C. F.; Zweckstetter, M.; Rezaei-Ghaleh, N.: Dynamical component exchange in a model phase separating system: an NMR-based approach. PhysChemChemPhys 24 (10), pp. 6169 - 6175 (2022)

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41.

Journal Article

Nedaei, H.; Rezaei-Ghaleh, N.; Giller, K.; Becker, S.; Karami, L.; Moosavi-Movahedi, A. A.; Griesinger, C.; Saboury, A. A.: The calcium-free form of atorvastatin inhibits amyloid-β(1–42) aggregation in vitro. Journal of Biological Chemistry 298 (3), 101662 (2022)

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42.

Journal Article

Robustelli, P.; Ibanez-de-Opakua, A.; Campbell-Bezat, C.; Giordanetto, F.; Becker, S.; Zweckstetter, M.; Pan, A. C.; Shaw, D. E.: Molecular Basis of Small-Molecule Binding to α-Synuclein. Journal of the American Chemical Society 144 (6), pp. 2501 - 2510 (2022)

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43.

Journal Article

Cario, A.; Savastano, A.; Wood, N. B.; Liu, Z.; Previs, M. J.; Hendricks, A. G.; Zweckstetter, M.; Berger, C. L.: The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure. Proceedings of the National Academy of Sciences of the United States of America 119 (7), e2114215119 (2022)

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44.

Journal Article

Aillaud, I.; Kaniyappan, S.; Chandupatla, R. R.; Ramirez, L. M.; Alkhashrom, S.; Eichler, J.; Horn, A. H. C.; Zweckstetter, M.; Mandelkow, E.-M.; Sticht, H. et al.; Funke, S. A.: A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro. Alzheimer's Research & Therapy 14, 15 (2022)

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45.

Journal Article

Moll, A.; Ramirez, L. M.; Ninov, M.; Schwarz, J.; Urlaub, H.; Zweckstetter, M.: Hsp multichaperone complex buffers pathologically modified Tau. Nature Communications 13, 3668 (2022)

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46.

Journal Article

Dauer née Joppe, K.; Tatenhorst, L.; Caldi Gomes, L.; Zhang, S.; Parvaz, M.; Carboni, E.; Roser, A.-E.; El DeBakey, H.; Bähr, M.; Vogel-Mikuš, K. et al.; Ip, C. W.; Becker, S.; Zweckstetter, M.; Lingor, P.: Brain iron enrichment attenuates α-synuclein spreading after injection of preformed fibrils. Journal of Neurochemistry 159 (3), pp. 554 - 573 (2021)

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47.

Journal Article

Oliveira, L. M. A.; Gasser, T.; Edwards, R.; Zweckstetter, M.; Melki, R.; Stefanis, L.; Lashuel, H. A.; Sulzer, D.; Vekrellis, K.; Halliday, G. M. et al.; Tomlinson, J. J.; Schlossmacher, M.; Jensen, P. H.; Schulze-Hentrich, J.; Riess, O.; Hirst, W.D.; El-Agnaf, O.; Mollenhauer, B.; Lansbury, P.; Outeiro, T. F.: Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease. NPJ Parkinsons Disease 7, 65 (2021)

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48.

Journal Article

Chakraborty, P.; Rivière, G.; Liu, S.; Ibáñez de Opakua, A.; Dervişoğlu, R.; Hebestreit, A.; Andreas, L. B.; Vorberg, I. M.; Zweckstetter, M.: Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils. Nature Communications 12, 4231 (2021)

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49.

Journal Article

Rai, S. K.; Savastano, A.; Singh, P.; Mukhopadhyay, S.; Zweckstetter, M.: Liquid–liquid phase separation of tau: From molecular biophysics to physiology and disease. Protein Science 30 (7), pp. 1294 - 1314 (2021)

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50.

Journal Article

Martinez Hernandez, A.; Silbern, I.; Geffers, I.; Tatenhorst, L.; Becker, S.; Urlaub, H.; Zweckstetter, M.; Griesinger, C.; Eichele, G.: Low-Expressing synucleinopathy mouse models based on oligomer-forming mutations and C-terminal truncation of α-synuclein. Frontiers in Neuroscience 15, 643391 (2021)

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