Tau: It’s Not What You Think

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · 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

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · 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

Identification of a Protein That Interacts with Tubulin Dimers and Increases the Catastrophe Rate of Microtubules

Belmont, L. D., & Mitchison, T. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81037-5 · Cited by 664 · see citing works

Developmentally regulated expression of specific tau sequences

Kosik, K. S., Orecchio, L. D., Bakalis, S., & Neve, R. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90077-9 · Cited by 598 · see citing works

Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration

Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553 · 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

The microtubule binding domain of tau protein

Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works

Near-atomic model of microtubule-tau interactions

Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416 · see citing works

Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction

Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 407 · see citing works

The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice

Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4922-11.2012 · Cited by 401 · see citing works

Microtubule-associated protein tau in development, degeneration and protection of neurons

Wang, J., & Liu, F. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.03.002 · Cited by 395 · see citing works

Motor-dependent microtubule disassembly driven by tubulin tyrosination

Peris, L., Wagenbach, M., Lafanéchère, L., Brocard, J., Moore, A. T., Kozielski, F., Job, D., Wordeman, L. G., & Andrieux, A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200902142 · Cited by 370 · see citing works

Individual microtubules in the axon consist of domains that differ in both composition and stability.

Baas, P. W., & Black, M. M. (1990) · The Journal of cell biology · doi:10.1083/jcb.111.2.495 · Cited by 362 · see citing works

Microtubule Reduction in Alzheimer's Disease and Aging Is Independent of τ Filament Formation

Cash, A., Aliev, G. M., Siedlak, S. L., Nunomura, A., Fujioka, H., Zhu, X., Raina, A. K., Vinters, H. V., Tabaton, M., Johnson, T., et al. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64296-4 · Cited by 309 · see citing works

Stability properties of neuronal microtubules

Baas, P. W., Rao, A. N., Matamoros, A. J., & Leo, L. (2016) · Cytoskeleton · doi:10.1002/cm.21286 · Cited by 304 · see citing works

Glycogen synthase kinase 3β phosphorylation of microtubule-associated protein 1B regulates the stability of microtubules in growth cones

Goold, R., Owen, R., & Gordon‐Weeks, P. R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.19.3373 · Cited by 281 · see citing works

Pathogenic Forms of Tau Inhibit Kinesin-Dependent Axonal Transport through a Mechanism Involving Activation of Axonal Phosphotransferases

Kanaan, N. M., Morfini, G. A., LaPointe, N. E., Pigino, G. F., Patterson, K. R., Song, Y., Andreadis, A., Fu, Y., Brady, S. T., & Binder, L. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0560-11.2011 · Cited by 273 · see citing works

Activity-Dependent Tau Protein Translocation to Excitatory Synapse Is Disrupted by Exposure to Amyloid-Beta Oligomers

Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works

Tau Is Enriched on Dynamic Microtubules in the Distal Region of Growing Axons

Black, M. M., Slaughter, T., Moshiach, S., Obrocka, M., & Fischer, I. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-11-03601.1996 · Cited by 270 · see citing works

Single-molecule investigation of the interference between kinesin, tau and MAP2c

Seitz, A., Kojima, H., Oiwa, K., Mandelkow, E.-M., Song, Y.-H., & Mandelkow, E. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf503 · Cited by 257 · see citing works

Tau Binds to the Distal Axon Early in Development of Polarity in a Microtubule- and Microfilament-Dependent Manner

Kempf, M., Clement, A. M., Faissner, A., Lee, G. S., & Brandt, R. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05583.1996 · Cited by 248 · see citing works

Tubulin requires tau for growth onto microtubule initiating sites.

Witman, G. B., Cleveland, D. W., Weingarten, M. D., & Kirschner, M. W. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.11.4070 · Cited by 238 · see citing works

Microtubules gate tau condensation to spatially regulate microtubule functions

Tan, R., Lam, A. J., Tan, T., Han, J., Nowakowski, D. W., Vershinin, M., Simó, S., Ori-McKenney, K. M., & McKenney, R. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0375-5 · Cited by 231 · see citing works

The Stathmin/Tubulin Interaction in Vitro

Curmi, P. A., Andersen, S. S. L., Lachkar, S., Gavet, O., Karsenti, E., Knossow, M., & Sobel, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25029 · Cited by 226 · see citing works

Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains

Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222 · see citing works

Competition between microtubule-associated proteins directs motor transport

Monroy, B. Y., Sawyer, D. L., Ackermann, B. E., Borden, M. M., Tan, T. C., & Ori-McKenney, K. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03909-2 · Cited by 213 · see citing works

Transglutaminase and Polyamination of Tubulin: Posttranslational Modification for Stabilizing Axonal Microtubules

Song, Y., Kirkpatrick, L., Schilling, A. B., Helseth, D. L., Chabot, N., Keillor, J. W., Johnson, G. V. W., & Brady, S. T. (2013) · Neuron · doi:10.1016/j.neuron.2013.01.036 · Cited by 209 · see citing works

The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture

Dotti, C. G., Banker, G., & Binder, L. (1987) · Neuroscience · doi:10.1016/0306-4522(87)90276-4 · Cited by 199 · see citing works

Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease.

Hempen, B., & Brion, J. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199609000-00003 · Cited by 177 · see citing works

Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases

Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05882.x · Cited by 177 · see citing works

Domains of Neuronal Microtubule-associated Proteins and Flexural Rigidity of Microtubules

Felgner, H., Frank, R. W., Biernat, J., Mandelkow, E., Mandelkow�, E., Ludin, B., Matus, A. I., & Schliwa, M. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.5.1067 · Cited by 177 · see citing works

Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons

Janning, D., Igaev, M., Sündermann, F., Brühmann, J., Beutel, O., Heinisch, J. J., Bakota, L., Piehler, J., Junge, W., & Brandt, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1099 · Cited by 168 · see citing works

ALZHEIMER'S DISEASE: PAIRED HELICAL FILAMENTS AND CYTOMEMBRANES

Gray, E. G., Paula-Barbosa, M., & Roher, A. (1987) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1987.tb00174.x · Cited by 165 · see citing works

Microtubule dynamics in axons and dendrites

Baas, P. W., Slaughter, T., Brown, A., & Black, M. M. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300115 · Cited by 150 · 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

Composite microtubules of the axon: quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules

Brown, A., Li, Y., Slaughter, T., & Black, M. M. (1993) · Journal of Cell Science · doi:10.1242/jcs.104.2.339 · Cited by 139 · see citing works

Knock-out and transgenic mouse models of tauopathies

Denk, F., & Wade‐Martins, R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.010 · Cited by 120 · see citing works

Dynamic Palmitoylation Targets MAP6 to the Axon to Promote Microtubule Stabilization during Neuronal Polarization

Tortosa, E., Adolfs, Y., Fukata, M., Pasterkamp, R. J., Kapitein, L. C., & Hoogenraad, C. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.042 · Cited by 120 · see citing works

The Microtubule-Associated Protein Tau Mediates the Organization of Microtubules and Their Dynamic Exploration of Actin-Rich Lamellipodia and Filopodia of Cortical Growth Cones

Biswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 119 · see citing works

Posttranslational modifications of α-tubulin in alzheimer disease

Zhang, F., Su, B., Wang, C., Siedlak, S. L., Mondragón‐Rodríguez, S., Lee, H., Wang, X., Perry, G. L., & Zhu, X. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0030-4 · Cited by 116 · see citing works

ADNP/NAP dramatically increase microtubule end-binding protein–Tau interaction: a novel avenue for protection against tauopathy

Ivashko‐Pachima, Y., Sayas, C. L., Malishkevich, A., & Gozes, I. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.255 · Cited by 102 · see citing works

Doublecortin Associates with Microtubules Preferentially in Regions of the Axon Displaying Actin-Rich Protrusive Structures

Tint, I. S., Jean, D. C., Baas, P. W., & Black, M. M. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3399-09.2009 · Cited by 100 · see citing works

Acute tau knockdown in the hippocampus of adult mice causes learning and memory deficits

Velázquez, R., Ferreira, E., Tran, A., Turner, E. C., Belfiore, R., Branca, C., & Oddo, S. (2018) · Aging Cell · doi:10.1111/acel.12775 · Cited by 96 · see citing works

tau confers drug stability but not cold stability to microtubules in living cells

Baas, P. W., Pienkowski, T. P., Cimbalnik, K. A., Toyama, K., Bakalis, S., Ahmad, F. J., & Kosik, K. S. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.1.135 · Cited by 84 · see citing works

Acute Inactivation of Tau Has No Effect on Dynamics of Microtubules in Growing Axons of Cultured Sympathetic Neurons

Tint, I. S., Slaughter, T., Fischer, I., & Black, M. M. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-21-08660.1998 · Cited by 83 · see citing works

Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases

Sudo, H., & Baas, P. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq521 · Cited by 78 · see citing works

MAP7 regulates axon morphogenesis by recruiting kinesin-1 to microtubules and modulating organelle transport

Tymanskyj, S. R., Yang, B. H., Verhey, K. J., & Ma, L. (2018) · eLife · doi:10.7554/elife.36374 · Cited by 77 · see citing works

MAP7 Regulates Axon Collateral Branch Development in Dorsal Root Ganglion Neurons

Tymanskyj, S. R., Yang, B. H., Falnikar, A., Lepore, A. C., & Ma, L. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3260-16.2017 · Cited by 63 · see citing works

Vertebrate Fidgetin Restrains Axonal Growth by Severing Labile Domains of Microtubules

Leo, L., Yu, W., D’Rozario, M., Waddell, E. A., Marenda, D. R., Baird, M. A., Davidson, M. W., Zhou, B., Wu, B., Baker, L. M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.08.017 · Cited by 61 · see citing works

Fidgetin-Like 2: A Microtubule-Based Regulator of Wound Healing

Charafeddine, R. A., Makdisi, J., Schairer, D. O., O'Rourke, B. P., Díaz‐Valencia, J. D., Chouake, J. S., Kutner, A. J., Krausz, A. E., Adler, B., Nacharaju, P., et al. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.94 · Cited by 61 · see citing works

Axonal tubulin and microtubules: morphologic evidence for stable regions on axonal microtubules

Sahenk, Z., & Brady, S. T. (1987) · Cell Motility · doi:10.1002/cm.970080207 · Cited by 59 · see citing works

MAP6-F Is a Temperature Sensor That Directly Binds to and Protects Microtubules from Cold-induced Depolymerization

Delphin, C., Bouvier, D., Seggio, M., Courriol, E., Saoudi, Y., Denarier, É., Bosc, C., Valiron, O., Bisbal, M., Arnal, I., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.398339 · Cited by 57 · see citing works

Tau kinases and phosphatases

Ávila, J. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00214.x · Cited by 51 · see citing works

Overexpression of tau protein in COS-1 cells results in the stabilization of centrosome-independent microtubules and extension of cytoplasmic processes

de Garcini, E. M., de la Luna, S., Domínguez, J. E., & Ávila, J. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01457399 · Cited by 29 · see citing works

Structural Basis for the Association of MAP6 Protein with Microtubules and Its Regulation by Calmodulin

Lefèvre, J., Savarin, P., Gans, P., Hamon, L., Clément, M., David, M.-O., Bosc, C., Andrieux, A., & Curmi, P. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457267 · Cited by 29 · see citing works

UNC-45A Is a Novel Microtubule-Associated Protein and Regulator of Paclitaxel Sensitivity in Ovarian Cancer Cells

Mooneyham, A., Iizuka, Y., Yang, Q., Coombes, C. E., McClellan, M., Shridhar, V., Emmings, E., Shetty, M., Chen, L., Ai, T., et al. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0670 · Cited by 23 · see citing works

Microtubules Gate Tau Condensation to Spatially Regulate Microtubule FunctionsPreprint

Tan, R., Lam, A. J., Tan, T. C., Han, J. S., Nowakowski, D. W., Vershinin, M. D., Simó, S., Ori-McKenney, K. M., & McKenney, R. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/423376 · Cited by 22 · see citing works

Epothilone D inhibits microglia-mediated spread of alpha-synuclein aggregates

Valdinocci, D., Grant, G. D., Dickson, T. C., & Pountney, D. L. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.006 · Cited by 20 · see citing works

The Microtubule-Modulating Drug Epothilone D Alters Dendritic Spine Morphology in a Mouse Model of Mild Traumatic Brain Injury

Chuckowree, J., Zhu, Z., Brizuela, M., Lee, K.-M., Blizzard, C. A., & Dickson, T. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00223 · Cited by 17 · see citing works

Acute inactivation of MAP1b in growing sympathetic neurons destabilizes axonal microtubules

Tint, I. S., Fischer, I., & Black, M. M. (2004) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20045 · Cited by 16 · see citing works

Sliding of STOP Proteins on Microtubules: A Model System for Diffusion‐Dependent Microtubule Motilitya

Margolis, R. L., Job, D., Pabion, M., & Rauch, C. T. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38402.x · Cited by 14 · see citing works

Mechanisms of Neuronal Microtubule Loss in Alzheimer’s Disease

Austin, T. O., Liang, Q., & Baas, P. W. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00004-1 · Cited by 9 · see citing works

Neuroprotection in Alzheimer’s Disease

Jain, K. K. (2011) · Humana Press eBooks · doi:10.1007/978-1-61779-049-2_8 · Cited by 7 · see citing works

Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects

Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet‐Nocca, C., Tsvetkov, P. O., Devred, F., & Landrieu, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00204 · Cited by 622 · see citing works

Microtubule-Associated Proteins: Structuring the Cytoskeleton

Bodakuntla, S., Jijumon, A. S., Villablanca, C., González-Billault, C. E., & Janke, C. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.07.004 · Cited by 366 · see citing works

GSK-3 and tau: a key duet in Alzheimer’s disease

Sayas, C. L., & Ávila, J. (2021) · Cells · doi:10.3390/cells10040721 · Cited by 314 · see citing works

Tau liquid‐liquid phase separation in neurodegenerative diseases

Boyko, S., & Surewicz, W. K. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.01.011 · Cited by 215 · see citing works

More than a marker: potential pathogenic functions of MAP2

DeGiosio, R. A., Grubisha, M. J., MacDonald, M., McKinney, B., Camacho, C., & Sweet, R. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.974890 · Cited by 151 · see citing works

The six brain‐specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes

Buchholz, S., & Zempel, H. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13784 · Cited by 145 · see citing works

Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation

Boyko, S., Surewicz, K. A., & Surewicz, W. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012460117 · Cited by 135 · see citing works

New Insights Into Drug Discovery Targeting Tau Protein

Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 133 · see citing works

Liquid–liquid phase separation of tau: From molecular biophysics to physiology and disease

Rai, S. K., Savastano, A., Singh, P., Mukhopadhyay, S., & Zweckstetter, M. (2021) · Protein Science · doi:10.1002/pro.4093 · Cited by 123 · see citing works

Oligomerization and Conformational Change Turn Monomeric β-Amyloid and Tau Proteins Toxic: Their Role in Alzheimer’s Pathogenesis

Penke, B., Szűcs, M., & Bogár, F. (2020) · Molecules · doi:10.3390/molecules25071659 · Cited by 115 · see citing works

Resurrecting the Mysteries of Big Tau

Fischer, I., & Baas, P. W. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.04.007 · Cited by 113 · see citing works

Tau in the Pathophysiology of Parkinson’s Disease

Pan, L., Meng, L., He, M., & Zhang, Z. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01776-5 · Cited by 110 · see citing works

Much More Than a Cytoskeletal Protein: Physiological and Pathological Functions of the Non-microtubule Binding Region of Tau

Brandt, R., Trushina, N. I., & Bakota, L. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590059 · Cited by 88 · see citing works

Myricetin slows liquid–liquid phase separation of Tau and activates ATG5-dependent autophagy to suppress Tau toxicity

Dai, B., Zhong, T., Chen, Z.-X., Chen, W., Zhang, N., Liu, X., Wang, L., Chen, J., & Liang, Y. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101222 · Cited by 83 · see citing works

Microglia and Wnt Pathways: Prospects for Inflammation in Alzheimer’s Disease

Yang, Y., & Zhang, Z. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00110 · Cited by 76 · see citing works

Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system

Lopes, D. M., Llewellyn, S. K., & Harrison, I. F. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00293-2 · Cited by 74 · see citing works

The Crosstalk Between Pathological Tau Phosphorylation and Mitochondrial Dysfunction as a Key to Understanding and Treating Alzheimer’s Disease

Guha, S. K., Johnson, G. V. W., & Nehrke, K. W. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02084-0 · Cited by 72 · see citing works

The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology

Hahn, I., Voelzmann, A., Liew, Y.-T., Costa-Gomes, B., & Prokop, A. (2019) · Neural Development · doi:10.1186/s13064-019-0134-0 · Cited by 68 · see citing works

Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review

Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works

Differences Between Human and Murine Tau at the N-terminal End

Hernández, F., Merchán‐Rubira, J., Vallés‐Saiz, L., Rodríguez-Matellán, A., & Ávila, J. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00011 · Cited by 59 · see citing works

Elucidating Tau function and dysfunction in the era of cryo-EM

Lippens, G. M., & Gigant, B. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.008031 · Cited by 56 · see citing works

Tau Aggregation

Hernández, F., Ferrer, I., Pérez, M., Zabala, J. C., del Rı́o, J. A., & Ávila, J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.04.024 · Cited by 48 · see citing works

Zinc enhances liquid-liquid phase separation of Tau protein and aggravates mitochondrial damages in cells

Gao, Y., Zhong, T., Wang, L., Zhang, N., Zeng, Y., Hu, J.-Y., Dang, H.-B., Chen, J., & Liang, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.04.034 · Cited by 49 · see citing works

Study liquid–liquid phase separation with optical microscopy: A methodology review

Zhang, X., Li, H., Ma, Y., Zhong, D., & Hou, S. (2023) · APL Bioengineering · doi:10.1063/5.0137008 · Cited by 43 · see citing works

Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons

Hahn, I., Voelzmann, A., Parkin, J., Fülle, J. B., Slater, P. G., Lowery, L. A., Sánchez‐Soriano, N., & Prokop, A. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009647 · Cited by 41 · see citing works

Tau Protein and Tauopathies: Exploring Tau Protein–Protein and Microtubule Interactions, Cross‐Interactions and Therapeutic Strategies

Lorenzo, D. D. (2024) · ChemMedChem · doi:10.1002/cmdc.202400180 · Cited by 40 · see citing works

The dopaminergic system and Alzheimer’s disease

Zhang, Y., Liang, Y., & Gu, Y. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00230 · Cited by 45 · see citing works

Microtubule dynamics in healthy and injured neurons

Rolls, M. M., Thyagarajan, P., & Feng, C. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22746 · Cited by 38 · see citing works

Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer’s Disease

Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 35 · see citing works

Tau suppresses microtubule-regulated pancreatic insulin secretion

Mangiafico, S. P., Tuo, Q., Li, X.-L., Liu, Y., Haralambous, C., Ding, X., Ayton, S., Wang, Q., Laybutt, D. R., Chan, J. Y., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02267-w · Cited by 32 · see citing works

Tau Avoids the GTP Cap at Growing Microtubule Plus-Ends

Castle, B. T., McKibben, K. M., Rhoades, E. R., & Odde, D. J. (2020) · iScience · doi:10.1016/j.isci.2020.101782 · Cited by 31 · see citing works

Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer’s Disease and Other Tauopathies

Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32 · see citing works

Beyond Langmuir: surface-bound macromolecule condensates

Mitchison, T. J. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-06-0393 · Cited by 28 · see citing works

Tubulin and Tubulin Posttranslational Modifications in Alzheimer’s Disease and Vascular Dementia

Santiago-Mujika, E., Luthi‐Carter, R., Giorgini, F., Kalaria, R. N., & Mukaetova-Ladinska, E. B. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.730107 · Cited by 25 · see citing works

Cerebrospinal fluid: A specific biofluid for the biosensing of Alzheimer's diseases biomarkers

Mirzaie, A., Nasrollahpour, H., Khalilzadeh, B., Jamali, A., Spiteri, R., Yousefi, H., Isildak, I., & Rahbarghazi, R. (2023) · Trends in Analytical Chemistry (TrAC) · doi:10.1016/j.trac.2023.117174 · Cited by 26 · see citing works

Pathological and physiological functional cross-talks of α-synuclein and tau in the central nervous system

Jin, M., Wang, S., Gao, X., Zou, Z., Hirotsune, S., & Sun, L. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382231 · Cited by 27 · see citing works

A common theme for axonopathies? The dependency cycle of local axon homeostasis

Prokop, A. (2021) · Cytoskeleton · doi:10.1002/cm.21657 · Cited by 24 · see citing works

The tau isoform 1N4R confers vulnerability of MAPT knockout human iPSC‐derived neurons to amyloid beta and phosphorylated tau‐induced neuronal dysfunction

Buchholz, S., Kabbani, M. A. A., Bell‐Simons, M., Kluge, L., Cagmak, C., Klimek, J., Haag, N., Iohan, L. D. C. C., Coulon, A., Costa, M. R., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.14403 · Cited by 21 · see citing works

Cross-talk between α-synuclein and the microtubule cytoskeleton in neurodegeneration

Mazzetti, S., Calogero, A. M., Pezzoli, G., & Cappelletti, G. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114251 · Cited by 22 · see citing works

Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration

Yeboah, F., Kim, T., Bill, A., & Dettmer, U. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104543 · Cited by 22 · see citing works

Evolutionary perspective of Big tau structure: 4a exon variants of MAPT

Fischer, I. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1019999 · Cited by 20 · see citing works

Alzheimer’s disease: an axonal injury disease?

Liang, D., & Zhang, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1264448 · Cited by 18 · see citing works

Recent studies of atomic‐resolution structures of tau protein and structure‐based inhibitors

Zhu, L., & Qian, Z. (2021) · Quantitative Biology · doi:10.15302/j-qb-021-0271 · Cited by 16 · see citing works

Uncovering tau in wasteosomes (corpora amylacea) of Alzheimer’s disease patients

Riba, M., del Valle, J., Romera, C., Alsina, R., Molina‐Porcel, L., Pelegrı́, C., & Vilaplana, J. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1110425 · Cited by 16 · see citing works

Beyond uniformity: Exploring the heterogeneous and dynamic nature of the microtubule lattice

Motta, M. R., Biswas, S., & Schaedel, L. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151370 · Cited by 16 · see citing works

Early-life Pb exposure as a potential risk factor for Alzheimer’s disease: are there hazards for the Mexican population?

Chin-Chan, M., Cobos-Puc, L. E., Alvarado-Cruz, I., Bayar, M., & Ermolaeva, M. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01739-1 · Cited by 16 · see citing works

Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS

Kanaan, N. M. (2024) · Cytoskeleton · doi:10.1002/cm.21820 · Cited by 15 · see citing works

Intracellular tau fragment droplets serve as seeds for tau fibrils

Soeda, Y., Yoshimura, H., Bannai, H., Koike, R., Shiiba, I., & Takashima, A. (2024) · Structure · doi:10.1016/j.str.2024.06.018 · Cited by 15 · see citing works

UNC-45A Breaks MT Lattice Independent of its Effect on Non-Muscle Myosin II

Habicht, J., Mooneyham, A., Hoshino, A., Shetty, M., Zhang, X., Emmings, E., Yang, Q., Coombes, C., Gardner, M. K., & Bazzaro, M. (2020) · Journal of Cell Science · doi:10.1242/jcs.248815 · Cited by 15 · see citing works

Astrocyte‐targeting RNA interference against mutated superoxide dismutase 1 induces motoneuron plasticity and protects fast‐fatigable motor units in a mouse model of amyotrophic lateral sclerosis

Rochat, C., Bernard‐Marissal, N., Källstig, E., Pradervand, S., Perrin, F. E., Aebischer, P., Raoul, C., & Schneider, B. L. (2022) · Glia · doi:10.1002/glia.24140 · Cited by 13 · see citing works

Selective disruption of Drp1-independent mitophagy and mitolysosome trafficking by an Alzheimer’s disease relevant tau modification in a novelCaenorhabditis elegansmodel

Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2022) · Genetics · doi:10.1093/genetics/iyac104 · Cited by 11 · see citing works

TauP301L disengages from the proteosome core complex and neurogranin coincident with enhanced neuronal network excitability

Hole, K. L., Zhu, B., Huggon, L., Brown, J. T., Mason, J. M., & Williams, R. J. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06815-2 · Cited by 11 · see citing works

Tau oligomerization on microtubules in health and disease

Ori‐McKenney, K. M., & McKenney, R. J. (2024) · Cytoskeleton · doi:10.1002/cm.21785 · Cited by 8 · see citing works

Big tau: What, how, where and why

Fischer, I. (2023) · Cytoskeleton · doi:10.1002/cm.21772 · Cited by 10 · see citing works

Antagonistic roles of tau and MAP6 in regulating neuronal development

Sun, X., Yu, W., Baas, P. W., Toyo‐oka, K., & Qiang, L. (2024) · Journal of Cell Science · doi:10.1242/jcs.261966 · Cited by 10 · see citing works

Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures

Sun, K. T., & Mok, S. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00512 · Cited by 10 · see citing works

Why kiss‐and‐hop explains that tau does not stabilize microtubules and does not interfere with axonal transport (at physiological conditions)

Bakota, L., & Brandt, R. (2023) · Cytoskeleton · doi:10.1002/cm.21787 · Cited by 10 · see citing works

A Role for Second Messengers in Axodendritic Neuronal Polarity

Urrutia, P. J., & González-Billault, C. (2023) · The Journal of Neuroscience · doi:10.1523/jneurosci.1065-19.2023 · Cited by 9 · see citing works

Activation of PI3k/Akt/mTOR Signaling Induces Deposition of p-tau to Promote Aluminum Neurotoxicity

Xu, Y., Zhang, G., Zhao, Y., Bu, F., & Zhang, Y. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00573-9 · Cited by 9 · see citing works

Focusing on oligomeric tau as a therapeutic target in Alzheimer’s disease and other tauopathies

Rayman, J. B. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2206561 · Cited by 9 · see citing works

Modeling and Predicting Second-Harmonic Generation from Protein Molecular Structure

Asadipour, B., Beaurepaire, E., Zhang, X., Chessel, A., Mahou, P., Supatto, W., Schanne‐Klein, M., & Stringari, C. (2024) · Physical Review X · doi:10.1103/physrevx.14.011038 · Cited by 8 · see citing works

Tauopathies: Emerging discoveries on tau protein, with a special focus on Alzheimer's disease

Hattiholi, A., Hegde, H., & Shetty, S. K. (2025) · Neuropeptides · doi:10.1016/j.npep.2025.102536 · Cited by 10 · see citing works

Exploring the interaction of clonazepam and diazepam with tau protein: Multispectral and molecular docking studies

Gholami, A., Dehghan, G., Rashtbari, S., & Jouyban, A. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.132669 · Cited by 8 · see citing works

Progress in Analysis of Tau Protein

Li, L., & Wang, X. (2020) · Chinese Journal of Analytical Chemistry · doi:10.1016/s1872-2040(20)60024-x · Cited by 7 · see citing works

Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axonsPreprint

Hahn, I., Voelzmann, A., Parkin, J., Fülle, J. B., Slater, P. G., Lowery, L. A., Sánchez‐Soriano, N., & Prokop, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.19.257808 · Cited by 7 · see citing works

Tau and MAP6 establish labile and stable domains on microtubules

Kirimtay, K., Huang, W., Sun, X., Qiang, L., Wang, D. V., Sprouse, F. C., Craig, E. M., & Baas, P. W. (2025) · iScience · doi:10.1016/j.isci.2025.111785 · Cited by 5 · see citing works

The role of microtubule-associated protein tau in netrin-1 attractive signaling

Huang, H., Majumder, T., Khot, B., Suriyaarachchi, H., Yang, T., Shao, Q., Tirukovalluru, S., & Liu, G. (2024) · Journal of Cell Science · doi:10.1242/jcs.261244 · Cited by 5 · see citing works

Probing the Interactions of Lamotrigine and Phenobarbital with Tau Protein: Experimental and Molecular Modeling Studies

Gholami, A., Dehghan, G., Rashtbari, S., & Jouyban, A. (2022) · Iranian journal of pharmaceutical research · doi:10.5812/ijpr-129599 · Cited by 5 · see citing works

Microtubule stabilising peptides: new paradigm towards management of neuronal disorders

Bhargava, S., Kulkarni, R., Dewangan, B., Kulkarni, N., Jiaswar, C., Kumar, K., Kumar, A., Bodhe, P. R., Kumar, H., & Sahu, B. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00012e · Cited by 5 · see citing works

AlphaScreen Identifies MSUT2 Inhibitors for Tauopathy-Targeting Therapeutic Discovery

Baker, J. D., Uhrich, R. L., Strovas, T., Saxton, A. D., & Kraemer, B. (2020) · SLAS discovery : advancing life sciences R & D · doi:10.1177/2472555220958387 · Cited by 3 · see citing works

Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)

Adler, A., Kjaer, L. F., Beugelink, J. W., Baldus, M., & van Ingen, H. (2023) · Biomolecular NMR Assignments · doi:10.1007/s12104-023-10124-8 · Cited by 5 · see citing works

Intra-axonal Nanomagnetic Forces Differentially Impact hTau40 Transport Dynamics in Primary Cortical and Hippocampal Neurons

Landis, M. K., & Kunze, A. (2025) · ACS Nano · doi:10.1021/acsnano.4c14767 · Cited by 4 · see citing works

Tauopathies: Calmodulin Regulates Tau Hyperphosphorylation and Its Transformation into Disease-Specific Aggregates

O’Day, D. H. (2025) · Biomolecules · doi:10.3390/biom15081133 · Cited by 4 · see citing works

Is Gulf War Illness a prolonged early phase tauopathy?

Baas, P. W., Sullivan, K. A., Terry, A. V., Case, K., Yates, P. L., Sun, X., Raghupathi, R., Huber, B. R., & Qiang, L. (2023) · Cytoskeleton · doi:10.1002/cm.21786 · Cited by 4 · see citing works

Modeling and predicting second harmonic generation from protein molecular structure

Asadipour, B., Beaurepaire, E., Zhang, X., Chessel, A., Mahou, P., Supatto, W., Schanne‐Klein, M., & Stringari, C. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2023.11.2806 · Cited by 4 · see citing works

Complex regulation of tau phosphorylation by the endothelin system in brain microvascular endothelial cells (BMVECs): link to barrier function

Karakaya, E., Abdul, Y., Edwards, J. M., Jamil, S., Albayram, Ö., & Ergul, A. (2024) · Clinical Science · doi:10.1042/cs20240616 · Cited by 4 · see citing works

Tau from SPAM Transgenic Mice Exhibit Potent Strain-Specific Prion-Like Seeding Properties Characteristic of Human Neurodegenerative Diseases

Smith, E. D., Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2025) · Neuromolecular medicine · doi:10.1007/s12017-025-08850-4 · Cited by 2 · see citing works

The protein–surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18

Kaur, J., Giri, A., & Bhattacharya, M. (2020) · European Biophysics Journal · doi:10.1007/s00249-020-01447-8 · Cited by 4 · see citing works

Analyses of exon 4a structure reveal unique properties of Big tauPreprint

Fischer, I., & Baas, P. W. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.04.674244 · Cited by 4 · see citing works

Is tau pathology a relevant factor in neuronal damage induced by alcohol and other drugs?

Olesen, M. A., Ancía, A., & Quintanilla, R. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168059 · Cited by 3 · see citing works

Analyses of exon 4a structure reveal the properties of Big tau related to distribution, function and aggregation

Fischer, I., & Baas, P. W. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1707820 · Cited by 3 · see citing works

Evolving alterations of structural organization and functional connectivity in feedforward neural networks after induced P301L tau mutation

Weir, J. S., Hanssen, K. S., Winter‐Hjelm, N., Sandvig, A., & Sandvig, I. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16625 · Cited by 3 · see citing works

Reevaluating tau reduction as a therapeutic approach for tauopathies: Insights and perspectives

Sun, X., Ogbolu, V. C., Baas, P. W., & Qiang, L. (2023) · Cytoskeleton · doi:10.1002/cm.21790 · Cited by 2 · see citing works

Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture

Pais, E., & Schou, K. B. (2026) · Cells · doi:10.3390/cells15141289 · Cited by 2 · see citing works

The emerging nontraditional roles for tau in the brain

Tseng, J., & Cohen, T. J. (2023) · Cytoskeleton · doi:10.1002/cm.21811 · Cited by 2 · see citing works

The changes of neurogenesis in the hippocampal dentate gyrus of SAMP8 mice and the effects of acupuncture and moxibustion

Liu, X., Chen, J., Du, Y., Tian, Q., Wang, L., Li, W., Liu, G., Tan, Q., Wang, J., & Deng, X. (2024) · Brain Research · doi:10.1016/j.brainres.2024.148814 · Cited by 2 · see citing works

Structure and function of Full-length Tau

Vallés‐Saiz, L., Domene-Serrano, I., Picher, Á. J., Pérez, M., García‐Escudero, V., Hernández, F., & Ávila, J. (2025) · PLoS ONE · doi:10.1371/journal.pone.0335251 · Cited by 2 · see citing works

Validation of recombinant human protein purified from bacteria: An important step to increase scientific rigor

Umstead, A., Soliman, A. S., Lamp, J. A., & Vega, I. E. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113999 · Cited by 2 · see citing works

Epigenetic Mechanisms Shaping Spine Regulation: Unveiling the Role of Cytoskeletal Dynamics and Localized Protein Synthesis

Gupta, S., Kishore, A., Rishi, V., & Aggarwal, A. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05045-7 · Cited by 1 · see citing works

Constancy of olfactory cilia in rodents

Ukhanov, K., Uytingco, C. R., de Celis, C., Xie, C., Munger, S. D., & Martens, J. R. (2025) · Chemical Senses · doi:10.1093/chemse/bjaf048 · Cited by 1 · see citing works

Actin-associated growth cone of Tau and its intracellular localization

Velmurugan, G., Chandrashekar, M., & Chinnathambi, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.025 · Cited by 1 · see citing works

Cell-Internal Nanomagnetic Forces Alter Cytoskeletal Protein Transport Dynamics in Developing Excitatory Axons

Landis, M. K., & Kunze, A. (2026) · Nano Letters · doi:10.1021/acs.nanolett.5c05742 · Cited by 1 · see citing works

Tau interferes with axonal neurite stabilization and cytoskeletal composition independently of its ability to associate with microtubules

Boumil, E. F., Vohnoutka, R. B., Lee, S., & Shea, T. B. (2020) · Biology Open · doi:10.1242/bio.052530 · Cited by 1 · see citing works

Break and accelerator—The mechanics of Tau (and amyloid) toxicity

Cruz, E., Nisbet, R. M., & Götz, J. (2023) · Cytoskeleton · doi:10.1002/cm.21781 · Cited by 1 · see citing works

Epothilone D Modulates Autism-like Behaviors in the BTBR Mouse Model of Autism Spectrum Disorder

Zhao, M., Chang, Q., Yang, H., Wang, M., Liu, Y., Lv, N., Lei, Q., & Wei, H. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.02.025 · Cited by 1 · see citing works

Expression of a miRNA targeting mutated SOD1 in astrocytes induces motoneuron plasticity and improves neuromuscular function in ALS micePreprint

Rochat, C., Bernard‐Marissal, N., Pradervand, S., Perrin, F. E., Raoul, C., Aebischer, P., & Schneider, B. L. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.08.425706 · Cited by 1 · see citing works

ACETYLATED α-TUBULIN LYSINE 394 IS CRITICAL FOR AXON OUTGROWTH IN THE ADULT MUSHROOM BODIES OF DROSOPHILA MELANOGASTERPreprint

Welch, C. J., Mueller, L. O., Trujillo, S. P., & Wildonger, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.10.681650 · Cited by 1 · see citing works

Dynamic conformational ensembles of soluble Tau encode neuronal toxicity prior to aggregationPreprint

Georgescauld, F., Okekenwa, S., Boyd, T., Donahue, C., Quittot, N., Dickson, J., Fan, Z.-Y., Brady, S., Blackstone, C., Hyman, B., et al. (2026) · bioRxiv · doi:10.64898/2026.01.26.701882 · Cited by 2 · see citing works

Selective Disruption of Drp1-Independent Mitophagy and Mitolysosome Trafficking by an Alzheimer’s Disease Relevant Tau Modification in a Novel C. elegans ModelPreprint

Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2021) · Research Square · doi:10.21203/rs.3.rs-1096882/v1

Epothilone D Modulates Autism-Like Behaviors in the BTBR Mouse Model of Autism Spectrum DisorderPreprint

Zhao, M., Chang, Q., Yang, H., Wang, M., Liu, Y., Lv, N., Lei, Q., & Wei, H. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3980061

Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains

Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222 · see citing works

Acute Inactivation of Tau Has No Effect on Dynamics of Microtubules in Growing Axons of Cultured Sympathetic Neurons

Tint, I. S., Slaughter, T., Fischer, I., & Black, M. M. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-21-08660.1998 · Cited by 83 · see citing works

Tau Protein Function in Axonal Formation

Paglini, M. G., Peris, L., Mascotti, F., Quiroga, S., & Cáceres, A. (2000) · Neurochemical Research · doi:10.1023/a:1007531230651 · Cited by 50 · see citing works

Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects

Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet‐Nocca, C., Tsvetkov, P. O., Devred, F., & Landrieu, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00204 · Cited by 622 · see citing works

New understanding of the effects of microtubule-associated proteins on dynamic instability, including the role of tau in neuronal function and disease

Austin, T. O., Baas, P. W., & Cunningham, T. J. (2018) · doi:10.17918/d86q28