Altered microtubule organization in small-calibre axons of mice lacking tau protein

Targeted mutation of the DNA methyltransferase gene results in embryonic lethality

Li, E., Bestor, T. H., & Jaenisch, R. (1992) · Cell · doi:10.1016/0092-8674(92)90611-f · Cited by 3,984

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915

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

Amyloid-β and tau--a toxic pas de deux in Alzheimer’s disease

Ittner, L. M., & Götz, J. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2967 · Cited by 1,269

Tau pathology and neurodegeneration

Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037

The many faces of tau

Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899

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

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

Genetic compensation: A phenomenon in search of mechanisms

El-Brolosy, M. A., & Stainier, D. Y. R. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006780 · Cited by 829

Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria

Tanaka, Y., Kanai, Y., Okada, Y., Nonaka, S., Takeda, S., Harada, A., & Hirokawa, N. (1998) · Cell · doi:10.1016/s0092-8674(00)81459-2 · Cited by 654

Tau phosphorylation in neuronal cell function and dysfunction

Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609

Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export

Lei, P., Ayton, S., Finkelstein, D. I., Spoerri, L., Ciccotosto, G. D., Wright, D. K., Wong, B. X. W., Adlard, P. A., Cherny, R. A., Lam, L. Q., et al. (2012) · Nature Medicine · doi:10.1038/nm.2613 · Cited by 594

Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease

Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494

Antisense oligonucleotide therapy for neurodegenerative disease

Smith, R. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25424 · Cited by 506

The role of tau in neurodegeneration

Gendron, T. F., & Petrucelli, L. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-13 · Cited by 478

Neurotrophins are required for nerve growth during development

Tucker, K. L., Meyer, M., & Barde, Y.-A. (2001) · Nature Neuroscience · doi:10.1038/82868 · Cited by 477

Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2959 · Cited by 440

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

Antisense Reduction of Tau in Adult Mice Protects against Seizures

DeVos, S. L., Goncharoff, D. K., Chen, G., Kebodeaux, C. S., Yamada, K., Stewart, F. R., Schuler, D. R., Maloney, S. E., Wozniak, D. F., Rigo, F., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2107-13.2013 · Cited by 311

Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases

Andreadis, A. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.010 · Cited by 311

Use of Caenorhabditis elegans as a model to study Alzheimer’s disease and other neurodegenerative diseases

Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310

Dendritic Tau in Alzheimer’s Disease

Ittner, A., & Ittner, L. M. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.003 · Cited by 278

Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin

Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283

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

Tau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies

Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments

Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226

Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies

Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220

Tau deletion promotes brain insulin resistance

Marciniak, E., Leboucher, A., Caron, E., Ahmed, T., Tailleux, A., Dumont, J., Issad, T., Gerhardt, E., Pagesy, P., Vileno, M., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20161731 · Cited by 205

Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport

Torroja, L., Chu, H., Kotovsky, I., & White, K. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80215-2 · Cited by 203

Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons.

Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179

GSK‐3 in Neurodegenerative Diseases

Lei, P., Ayton, S., Bush, A. I., & Adlard, P. A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/189246 · Cited by 177

Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease

Terwel, D., Dewachter, I., & Van Leuven, F. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:151 · Cited by 146

Selective suppression of the α isoform of p38 MAPK rescues late-stage tau pathology

Maphis, N., Jiang, S., Xu, G., Kokiko-Cochran, O. N., Roy, S. M., Van Eldik, L. J., Watterson, D. M., Lamb, B. T., & Bhaskar, K. (2016) · Alzheimer's Research & Therapy · doi:10.1186/s13195-016-0221-y · Cited by 147

Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion

Ahmed, T., Van der Jeugd, A., Blum, D., Galas, M.-C., D’Hooge, R., Buee, L., & Balschun, D. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.005 · Cited by 137

Pre‐synaptic C‐terminal truncated tau is released from cortical synapses in Alzheimer's disease

Sokolow, S., Henkins, K. M., Bilousova, T., Gonzalez, B., Vinters, H. V., Miller, C. A., Cornwell, L., Poon, W. W., & Gylys, K. H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12991 · Cited by 133

Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets

Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122

Molecular mechanisms of brain-derived neurotrophic factor in neuro-protection: Recent developments

Zhao, H., Alam, A., San, C.-Y., Eguchi, S., Chen, Q., Lian, Q., & Ma, D. (2017) · Brain Research · doi:10.1016/j.brainres.2017.03.029 · Cited by 122

Disease modifying therapy for AD?1

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117

Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00572 · Cited by 102

Targeting Aβ and tau in Alzheimer's disease, an early interim report

Golde, T. E., Petrucelli, L., & Lewis, J. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.035 · Cited by 89

Downregulation of the microtubule associated protein Tau impairs process outgrowth and myelin basic protein m RNA transport in oligodendrocytes

Seiberlich, V., Bauer, N. G., Schwarz, L., Ffrench‐Constant, C., Goldbaum, O., & Richter‐Landsberg, C. (2015) · Glia · doi:10.1002/glia.22832 · Cited by 84

Modeling the complex pathology of Alzheimer's disease in Drosophila

Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69

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

Identification of a novel polymorphism in the promoter region of the tau gene highly associated to progressive supranuclear palsy in humans

Ezquerra, M., Pastor, P., Valldeoriola, F., Luis Molinuevo, J., Blesa, R., Tolosa, E., & Oliva, R. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00738-7 · Cited by 58

Mechanisms of trafficking in axons and dendrites: implications for development and neurodegeneration

Sheetz, M. P., Pfister, K. K., Bulinski, J. C., & Cotman, C. W. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00021-5 · Cited by 55

Regulatory mechanisms for the axonal localization of tau protein in neurons

Iwata, M., Watanabe, S., Yamane, A., Miyasaka, T., & Misonou, H. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-03-0183 · Cited by 51

Cellular and molecular modifier pathways in tauopathies: the big picture from screening invertebrate models

Hannan, S. B., Dräger, N. M., Rasse, T. M., Voigt, A., & Jahn, T. R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13532 · Cited by 38

Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport

Nakajima, K., Takei, Y., Tanaka, Y., Nakagawa, T., Nakata, T., Noda, Y., Setou, M., & Hirokawa, N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.3.866-873.2002 · Cited by 31

The Homologous Carboxyl-Terminal Domains of Microtubule-Associated Protein 2 and TAU Induce Neuronal Dysfunction and Have Differential Fates in the Evolution of Neurofibrillary Tangles

Xie, C., Miyasaka, T., Yoshimura, S., Hatsuta, H., Yoshina, S., Kage-Nakadai, E., Mitani, S., Murayama, S., & Ihara, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089796 · Cited by 28

What does genetics tell us about imprinting and the placenta connection?

Varmuza, S., & Miri, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1714-0 · Cited by 22

Tau normal function influences Niemann-Pick type C disease pathogenesis in mice and modulates autophagy in NPC1-deficient cells.

Pacheco, C. D., Elrick, M. J., & Lieberman, A. P. (2009) · Autophagy · doi:10.4161/auto.5.4.8364 · Cited by 20

Multi-omic phenotyping of MAPT V337M neurons reveals early changes in axonogenesis and tau phosphorylation

Mohl, G. A., Dixon, G., Marzette, E., McKetney, J., Samelson, A. J., Serras, C. P., Jin, J., Ariqat, N., Keys, A., Chavira, C., et al. (2026) · npj Dementia · doi:10.1038/s44400-026-00076-w · Cited by 5

Graded regulation of microtubule-binding of Tau by the phosphorylation state of the proline-rich region in living neurons

Nakata, R., Torii, T., Miyasaka, T., & Misonou, H. (2026) · Neuroscience Research · doi:10.1016/j.neures.2025.104987 · Cited by 3