Zweckstetter, Markus

Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 782

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology

Alzheimer's disease research and treatmentsAdvanced NMR Techniques and Applications

Cited by 652

Structure of the human voltage-dependent anion channel

Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., & Zeth, K. (2008) · Proceedings of the National Academy of Sciences

Mitochondrial Function and PathologyProtein Structure and Dynamics

Cited by 588

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamics

Cited by 524

Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2005) · Journal of Biological Chemistry

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 324

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 318

Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry

Abyzov, A., Blackledge, M., & Zweckstetter, M. (2022) · Chemical Reviews

Protein Structure and DynamicsRNA Research and Splicing

Cited by 215

N-truncated amyloid β (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits

Bouter, Y., Dietrich, K., Wittnam, J. L., Rezaei-Ghaleh, N., Pillot, T., Papot-Couturier, S., Lefebvre, T., Sprenger, F., Wirths, O., Zweckstetter, M., et al. (2013) · Acta Neuropathologica

Alzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

Cited by 175

Fasudil attenuates aggregation of α-synuclein in models of Parkinson’s disease

Tatenhorst, L., Eckermann, K., Dambeck, V., Fonseca-Ornelas, L., Walle, H., Lopes da Fonseca, T., Koch, J. C., Becker, S., Tönges, L., Bähr, M., et al. (2016) · Acta Neuropathologica Communications

Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and Signaling

Cited by 158

Folding of the Tau Protein on Microtubules

Kadavath, H., Jaremko, M., Jaremko, Ł., Biernat, J., Mandelkow, E., & Zweckstetter, M. (2015) · Angewandte Chemie International Edition

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 153

Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules

Fischer, D., Mukrasch, M. D., Biernat, J., Bibow, S., Blackledge, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · Biochemistry

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 149

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications

Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamics

Cited by 148

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications

Heat shock proteins researchAlzheimer's disease research and treatments

Cited by 100

GSK3β phosphorylation catalyzes the aggregation of tau into Alzheimer’s disease-like filaments

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) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

Cited by 96

Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2

Schwalbe, M., Biernat, J., Bibow, S., Ozenne, V., Jensen, M. R., Kadavath, H., Blackledge, M., Mandelkow, E., & Zweckstetter, M. (2013) · Biochemistry

Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamics

Cited by 78

NMR hawk‐eyed view of AlphaFold2 structures

Zweckstetter, M. (2021) · Protein Science

Protein Structure and DynamicsAdvanced NMR Techniques and Applications

Cited by 47

The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure

Cario, A., Savastano, A., Wood, N. B., Liu, Z., Previs, M. J., Hendricks, A. G., Zweckstetter, M., & Berger, C. L. (2022) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamics

Cited by 19