Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works

The Xplor-NIH NMR molecular structure determination package

Schwieters, C. D., Kuszewski, J. J., Tjandra, N., & Clore, G. M. (2003) · Journal of Magnetic Resonance · doi:10.1016/s1090-7807(02)00014-9 · Cited by 2,371 · see citing works

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works

The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data

Wishart, D. S., & Sykes, B. D. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,144 · see citing works

A Century of Alzheimer's Disease

Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,106 · see citing works

Intrinsically unstructured proteins

Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,056 · see citing works

Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

Tjandra, N., & Bax, A. (1997) · Science · doi:10.1126/science.278.5340.1111 · Cited by 1,720 · see citing works

High-Resolution Model of the Microtubule

Nogales, E., Whittaker, M., Milligan, R. A., & Downing, K. H. (1999) · Cell · doi:10.1016/s0092-8674(00)80961-7 · Cited by 1,200 · see citing works

Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

Lange, O. F., Lakomek, N., Farès, C., Schroeder, G. F., Walter, K. F. A., Becker, S., Meiler, J., Grubmüller, H., Griesinger, C., & de Groot, B. L. (2008) · Science · doi:10.1126/science.1157092 · Cited by 1,044 · see citing works

Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.

Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037 · see citing works

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure

von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021 · see citing works

Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques

Wilkins, D. K., Grimshaw, S. B., Receveur‐Brechot, V., Dobson, C. M., Jones, J. A., & Smith, L. J. (1999) · Biochemistry · doi:10.1021/bi991765q · Cited by 1,013 · see citing works

Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR Spectra

Ottiger, M., Delaglio, F., & Bax, A. (1998) · Journal of Magnetic Resonance · doi:10.1006/jmre.1998.1361 · Cited by 967 · see citing works

Function and structure of inherently disordered proteins

Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963 · see citing works

Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress

Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885 · see citing works

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881 · see citing works

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Bertoncini, C. W., Jung, Y., Fernández, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., & Zweckstetter, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407146102 · Cited by 781 · see citing works

Tau protein function in living cells.

Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works

The Primary Structure and Heterogeneity of Tau Protein from Mouse Brain

Lee, G. S., Cowan, N. J., & Kirschner, M. W. (1988) · Science · doi:10.1126/science.3122323 · Cited by 680 · see citing works

Domains of tau Protein and Interactions with Microtubules

Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655 · see citing works

Utilization of Site-Directed Spin Labeling and High-Resolution Heteronuclear Nuclear Magnetic Resonance for Global Fold Determination of Large Proteins with Limited Nuclear Overhauser Effect Data

Battiste, J. L., & Wagner, G. (2000) · Biochemistry · doi:10.1021/bi000060h · Cited by 625 · see citing works

Sequence-Dependent Correction of Random Coil NMR Chemical Shifts

Schwarzinger, S., Kroon, G. J. A., Foss, T. R., Chung, J., Wright, P. E., & Dyson, H. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003760i · Cited by 604 · see citing works

Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons

Chen, J., Kanai, Y., Cowan, N. J., & Hirokawa, N. (1992) · Nature · doi:10.1038/360674a0 · Cited by 601 · see citing works

Structural characterization of the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novák, M., Edwards, P. C., Klug, A., Tichelaar, W., & Crowther, R. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4884 · Cited by 597 · see citing works

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

Schweers, O., Schönbrunn, E., Marx, A., & Mandelkow�, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 569 · see citing works

Proline-directed and non-proline-directed phosphorylation of PHF-tau

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557 · see citing works

Tau protein binds to microtubules through a flexible array of distributed weak sites.

Butner, K. A., & Kirschner, M. W. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.3.717 · Cited by 550 · see citing works

Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.

Wille, H., Drewes, G., Biernat, J., Mandelkow�, E., & Mandelkow�, E. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.118.3.573 · Cited by 477 · see citing works

NMR structures of biomolecules using field oriented media and residual dipolar couplings

Prestegard, J. H., Al‐Hashimi, H. M., & Tolman, J. R. (2000) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500003656 · Cited by 440 · see citing works

Post-translational modifications of tau protein in Alzheimer’s disease

Gong, C.-X., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-004-0221-0 · Cited by 437 · see citing works

Global Hairpin Folding of Tau in Solution

Jeganathan, S., von Bergen, M., Brutlach, H., Steinhoff, H.-J., & Mandelkow, E. (2006) · Biochemistry · doi:10.1021/bi0521543 · Cited by 432 · see citing works

Tau proteins: the molecular structure and mode of binding on microtubules.

Hirokawa, N., Shiomura, Y., & Okabe, S. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.4.1449 · Cited by 389 · see citing works

New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry

Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062465.x · Cited by 378 · see citing works

Ensemble Approach for NMR Structure Refinement against1H Paramagnetic Relaxation Enhancement Data Arising from a Flexible Paramagnetic Group Attached to a Macromolecule

Iwahara, J., Schwieters, C. D., & Clore, G. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031580d · Cited by 328 · see citing works

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 · doi:10.1074/jbc.m501565200 · Cited by 324 · see citing works

Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. paramagnetic relaxation enhancement by nitroxide spin labels

Gillespie, J. R., & Shortle, D. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0954 · Cited by 297 · see citing works

Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly.

Goode, B. L., Denis, P. E., Panda, D., Radeke, M. J., Miller, H. P., Wilson, L., & Feinstein, S. C. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.2.353 · Cited by 296 · see citing works

Coil–globule transition in the denatured state of a small protein

Sherman, E., & Haran, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601395103 · Cited by 294 · see citing works

Structural and Functional Differences between 3-Repeat and 4-Repeat Tau Isoforms

Goode, B. L., Chau, M. F., Denis, P. E., & Feinstein, S. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007489200 · Cited by 241 · see citing works

Going new places using an old MAP: tau, microtubules and human neurodegenerative disease

Garcia, M. L., & Cleveland, D. W. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00172-1 · Cited by 235 · see citing works

Highly Populated Turn Conformations in Natively Unfolded Tau Protein Identified from Residual Dipolar Couplings and Molecular Simulation

Mukrasch, M. D., Markwick, P. R. L., Biernat, J., von Bergen�, M., Bernadó, P., Griesinger, C., Mandelkow�, E., Zweckstetter, M., & Blackledge, M. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0690159 · Cited by 222 · see citing works

Regulation of microtubule-associated proteins

Cassimeris, L., & Spittle, C. S. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)10006-9 · Cited by 220 · see citing works

Domain Conformation of Tau Protein Studied by Solution Small-Angle X-ray Scattering

Mylonas, E., Hascher, A., Bernadó, P., Blackledge, M. J., Mandelkow�, E., & Svergun, D. I. (2008) · Biochemistry · doi:10.1021/bi800900d · Cited by 211 · see citing works

Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: Application to unfolded proteins

Panchal, S. C., Bhavesh, N. S., & Hosur, R. V. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1011239023422 · Cited by 199 · see citing works

The “Jaws” of the Tau-Microtubule Interaction

Mukrasch, M. D., von Bergen�, M., Biernat, J., Fischer, D., Griesinger, C., Mandelkow�, E., & Zweckstetter, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607159200 · Cited by 196 · see citing works

Interaction of tau protein with the dynactin complex

Magnani, E., Fan, J., Gasparini, L., Golding, M., Williams, M., Schiavo, G., Goedert, M., Amos, L., & Spillantini, M. G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601878 · Cited by 186 · see citing works

Kinetic Stabilization of Microtubule Dynamics at Steady State by Tau and Microtubule-Binding Domains of Tau

Panda, D., Goode, B. L., Feinstein, S. C., & Wilson, L. (1995) · Biochemistry · doi:10.1021/bi00035a017 · Cited by 185 · see citing works

Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach

Ishima, R., & Torchia, D. A. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1022851228405 · Cited by 179 · see citing works

Structural Characterization of Unfolded States of Apomyoglobin using Residual Dipolar Couplings

Mohana‐Borges, R., Goto, N. K., Kroon, G. J. A., Dyson, H. J., & Wright, P. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.022 · Cited by 177 · see citing works

Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

Sibille, N., Sillen, A., Leroy, A., Wieruszeski, J., Mulloy, B., Landrieu, I., & Lippens, G. M. (2006) · Biochemistry · doi:10.1021/bi060964o · Cited by 175 · see citing works

Characterization of Alzheimer’s-like Paired Helical Filaments from the Core Domain of Tau Protein Using Solid-State NMR Spectroscopy

Andronesi, O. C., Bergen, M. V., Biernat, J., Seidel, K., Griesinger, C., Mandelkow, E., & Baldus, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja7100517 · Cited by 167 · see citing works

The Role of Tau Phosphorylation in the Pathogenesis of Alzheimers Disease

Mi, K., & Johnson, G. V. W. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025279 · Cited by 166 · see citing works

Nuclear Magnetic Resonance Methods for Elucidation of Structure and Dynamics in Disordered States

Dyson, H. J., & Wright, P. E. (2001) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(01)39317-5 · Cited by 163 · see citing works

Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein

Lindorff‐Larsen, K., Kristjánsdóttir, S., Teilum, K., Fieber, W., Dobson, C. M., Poulsen, F. M., & Vendruscolo, M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039250g · Cited by 161 · see citing works

Swimming against the Tide: Mobility of the Microtubule-Associated Protein Tau in Neurons

Konzack, S., Thies, E., Marx, A., Mandelkow, E., & Mandelkow�, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0927-07.2007 · Cited by 157 · see citing works

Surface-decoration of Microtubules by Human Tau

Santarella, R. A., Skiniotis, G., Goldie, K. N., Tittmann, P., Gross, H., Mandelkow, E., Mandelkow, E., & Hoenger, A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.008 · Cited by 141 · see citing works

Residual Structure, Backbone Dynamics, and Interactions within the Synuclein Family

Sung, Y., & Eliezer, D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.008 · Cited by 137 · see citing works

NMR Investigation of the Interaction between the Neuronal Protein Tau and the Microtubules

Sillen, A., Barbier, P., Landrieu, I., Lefebvre, S., Wieruszeski, J., Leroy, A., Peyrot, V., & Lippens, G. M. (2007) · Biochemistry · doi:10.1021/bi061920i · Cited by 121 · see citing works

NMR Analysis of a Tau Phosphorylation Pattern

Landrieu, I., Lacosse, L., Leroy, A., Wieruszeski, J., Trivelli, X., Sillen, A., Sibille, N., Schwalbe, H., Saxena, K., Langer, T., et al. (2006) · Journal of the American Chemical Society · doi:10.1021/ja054656+ · Cited by 117 · see citing works

The ‘jaws’ model of tau-microtubule interaction examined in CHO cells

Preuß, U., Biernat, J., Mandelkow�, E., & Mandelkow�, E. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.6.789 · Cited by 108 · see citing works

Residual Structure in the Repeat Domain of Tau: Echoes of Microtubule Binding and Paired Helical Filament Formation

Eliezer, D., Barré, P., Kobašlija, M., Chan, D. K., Li, X., & Heend, L. (2004) · Biochemistry · doi:10.1021/bi048953n · Cited by 106 · see citing works

The effects of guanidine hydrochloride on the ’random coil‘ conformations and NMR chemical shifts of the peptide series GGXGG

Plaxco, K. W., Morton, C. J., Grimshaw, S. B., Jones, J. A., Pitkeathly, M. C., Campbell, I. D., & Dobson, C. M. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018340217891 · Cited by 100 · see citing works

Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy

Hiller, S., Wasmer, C., Wider, G., & Kurt Wüthrich, A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072564+ · Cited by 75 · see citing works

Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics

Zweckstetter, M., & Bax, A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016496h · Cited by 70 · see citing works

Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces

Barré, P., & Eliezer, D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.018 · Cited by 69 · see citing works

Regions of Tau Implicated in the Paired Helical Fragment Core as Defined by NMR

Sillen, A., Leroy, A., Wieruszeski, J., Loyens, A., Beauvillain, J., Buée, L., Landrieu, I., & Lippens, G. M. (2005) · ChemBioChem · doi:10.1002/cbic.200400452 · Cited by 43 · see citing works

X‐ray structure of the PHF core C‐terminus: Insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease

Ševčı́k, J., Škrabana, R., Dvorský, R., Csokova, N. T., Iqbal, K., & Novák, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.067 · Cited by 29 · see citing works

Intensity modulated HSQC and HMQC: Two simple methods to measure 3JHNH α in proteins

Permi, P., Kilpeläinen, I., Annila, A., & Heikkinen, S. (2000) · Journal of Biomolecular NMR · doi:10.1023/a:1008343926502 · Cited by 17 · see citing works

Untitled work

(1997) · doi:10.1002/(sici)1097-4547(19970415)48:2

Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings

Blackledge, M. (2005) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2004.11.002

Tau protein liquid–liquid phase separation can initiate tau aggregation

Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works

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 · doi:10.1038/s41467-017-00480-0 · Cited by 782 · see citing works

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 · doi:10.1073/pnas.1504081112 · Cited by 524 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase

Hernández-Vega, A., Braun, M., Scharrel, L., Jahnel, M., Wegmann, S., Hyman, B. T., Alberti, S., Diez, S., & Hyman, A. A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.042 · Cited by 395 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

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 · doi:10.1016/j.cell.2014.01.037 · Cited by 318 · see citing works

Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade

Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313 · see citing works

Role of tau protein in Alzheimer’s disease: The prime pathological player

Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works

Tau immunotherapy for Alzheimer's disease

Pedersen, J. T., & Sigurdsson, E. M. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.03.003 · Cited by 247 · see citing works

Interplay of pathogenic forms of human tau with different autophagic pathways

Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works

Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry

Abyzov, A., Blackledge, M., & Zweckstetter, M. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00774 · Cited by 215 · see citing works

Acetylation Disfavors Tau Phase Separation

Ferreon, J. C., Jain, A., Choi, K.-J., Tsoi, P. S., MacKenzie, K. R., Jung, S. Y., & Ferreon, A. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051360 · Cited by 183 · see citing works

Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers

Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170 · see citing works

Identification of an Aggregation-Prone Structure of Tau

Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149 · see citing works

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 · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works

Tau Structures

Avila, J., Jiménez, J. S., Sayas, C. L., Bolós, M., Zabala, J. C., Rivas, G., & Hernández, F. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00262 · Cited by 140 · see citing works

Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies

Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138 · see citing works

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 · doi:10.1038/s41467-018-06880-0 · Cited by 100 · see citing works

Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment

Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103 · see citing works

AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function

Laurents, D. V. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.906437 · Cited by 95 · see citing works

Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles

Prezel, E., Elie, A., Delaroche, J., Stoppin-Mellet, V., Bosc, C., Serre, L., Fourest-Lieuvin, A., Andrieux, A., Vantard, M., & Arnal, I. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0429 · Cited by 83 · see citing works

Role of the Lipid Membrane and Membrane Proteins in Tau Pathology

Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61 · see citing works

Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network

Lopez, A., Dahiya, V., Delhommel, F., Freiburger, L., Stehle, R., Asami, S., Rutz, D., Blair, L., Buchner, J., & Sattler, M. (2021) · Science Advances · doi:10.1126/sciadv.abl7295 · Cited by 59 · see citing works

Regional vulnerability and spreading of hyperphosphorylated tau in seeded mouse brain

Detrez, J. R., Maurin, H., Van Kolen, K., Willems, R., Colombelli, J., Lechat, B., Roucourt, B., Van Leuven, F., Baatout, S., Larsen, P., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.010 · Cited by 39 · see citing works

N368-Tau fragments generated by legumain are detected only in trace amount in the insoluble Tau aggregates isolated from AD brain

Schlegel, K., Awwad, K., Heym, R. G., Holzinger, D., Doell, A., Barghorn, S., Jahn, T. R., Klein, C., Mordashova, Y., Schulz, M., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0831-2 · Cited by 30 · see citing works

The metamorphic nature of the Tau protein: dynamic flexibility comes at a cost

Sabbagh, J. J., & Dickey, C. A. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00003 · Cited by 31 · see citing works

Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy

Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28 · see citing works