Tau pathology and neurodegeneration

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

Clinical and biomarker changes in dominantly inherited Alzheimer's disease

Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498

Stages in the development of Parkinson’s disease-related pathology

Braak, H., Ghebremedhin, E., Rüb, U., Bratzke, H., & Del Tredici, K. (2004) · Cell and Tissue Research · doi:10.1007/s00441-004-0956-9 · Cited by 2,689

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury

McKee, A. C., Cantu, R. C., Nowinski, C. J., Hedley-Whyte, E. T., Gavett, B. E., Budson, A. E., Santini, V. E., Lee, H.-S., Kubilus, C. A., & Stern, R. A. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181a9d503 · Cited by 2,295

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208

A Century of Alzheimer's Disease

Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,153

The spectrum of disease in chronic traumatic encephalopathy

McKee, A. C., Stein, T. D., Nowinski, C. J., Stern, R. A., Daneshvar, D. H., Alvarez, V. E., Lee, H.-S., Hall, G., Wojtowicz, S. M., Baugh, C. M., et al. (2013) · Brain · doi:10.1093/brain/aws307 · Cited by 2,098

Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

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

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

Alzheimer Mechanisms and Therapeutic Strategies

Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758

A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline

Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611

The distribution of tau in the mammalian central nervous system.

Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560

Editorial on Consensus Recommendations for the Postmortem Diagnosis of Alzheimer Disease from the National Institute on Aging and the Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer Disease

HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512

Uber eine eigenartige Erkrankung der Hirnrinde

Alzheimer, A. (1907) · Medical Entomology and Zoology · Cited by 1,503

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Propagation of Tau Misfolding from the Outside to the Inside of a Cell

Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252

100 years of Lewy pathology

Goedert, M., Spillantini, M. G., Del Tredici, K., & Braak, H. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.242 · Cited by 1,190

Trehalose, a Novel mTOR-independent Autophagy Enhancer, Accelerates the Clearance of Mutant Huntingtin and α-Synuclein

Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122

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

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036

Neuroprotective effects of brain-derived neurotrophic factor in rodent and primate models of Alzheimer's disease

Nagahara, A. H., Merrill, D. A., Coppola, G., Tsukada, S., Schroeder, B. E., Shaked, G. M., Wang, L., Blesch, A., Kim, A., Conner, J. M., et al. (2009) · Nature Medicine · doi:10.1038/nm.1912 · Cited by 1,034

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

Trans-Synaptic Spread of Tau Pathology In Vivo

Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994

Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease

Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939

Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 893

Neural stem cells improve cognition via BDNF in a transgenic model of Alzheimer disease

Blurton-Jones, M. M., Kitazawa, M., Martínez‐Coria, H., Castello, N. A., Müller, F.-J., Loring, J. F., Yamasaki, T. R., Poon, W. W., Green, K. N., & LaFerla, F. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901402106 · Cited by 869

A common inversion under selection in Europeans

Stefánsson, H., Helgason, A., Þorleifsson, G., Steinthórsdóttir, V., Másson, G., Barnard, J., Baker, A., Jónasdóttir, Á., Ingason, A., Gudnadottir, V. G., et al. (2005) · Nature Genetics · doi:10.1038/ng1508 · Cited by 847

Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843

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

The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease.

Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., Ghozali, F., Fallet-Bianco, C., Pasquier, F., Lebert, F., et al. (1999) · Neurology · doi:10.1212/wnl.52.6.1158 · Cited by 828

The pathological process underlying Alzheimer’s disease in individuals under thirty

Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807

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

Harada, A., Oguchi, K., Okabe, S., Kuno, J., Terada, S., Ohshima, T., Sato-Yoshitake, R., Takei, Y., Noda, T., & Hirokawa, N. (1994) · Nature · doi:10.1038/369488a0 · Cited by 802

Early-onset autosomal dominant Alzheimer disease: prevalence, genetic heterogeneity, and mutation spectrum

Campion, D., Dumanchin, C., Hannequin, D., Dubois, B., Belliard, S., Puel, M., Thomas-Anterion, C., Michon, A., Martin, C., Charbonnier, F., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302553 · Cited by 785

Association of an Extended Haplotype in the Tau Gene with Progressive Supranuclear Palsy

Baker, M., Litvan, I., Houlden, H., Adamson, J., Dickson, D., Perez-Tur, J., Hardy, J., Lynch, T., Bigio, E., & Hutton, M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.4.711 · Cited by 781

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775

Punch drunk

MARTLAND, H. S. (1928) · Journal of the American Medical Association · doi:10.1001/jama.1928.02700150029009 · Cited by 774

Abundant Tau Filaments and Nonapoptotic Neurodegeneration in Transgenic Mice Expressing Human P301S Tau Protein

Allen, B., Ingram, E., Takao, M., Smith, M. J., Jakes, R., Virdee, K., Yoshida, H., Holzer, M., Craxton, M., Emson, P. C., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09340.2002 · Cited by 763

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 723

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721

Advanced Maillard reaction end products are associated with Alzheimer disease pathology.

Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5710 · Cited by 715

Critical role of soluble amyloid-β for early hippocampal hyperactivity in a mouse model of Alzheimer’s disease

Busche, M. A., Chen, X., Henning, H. A., Reichwald, J., Staufenbiel, M., Sakmann, B., & Konnerth, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206171109 · Cited by 715

über eigenartige Krankheitsfälle des späteren Alters

Alzheimer, A. (1911) · Zeitschrift für die gesamte Neurologie und Psychiatrie · doi:10.1007/bf02866241 · Cited by 712

Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo

Noble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709

Early Clinical PET Imaging Results with the Novel PHF-Tau Radioligand [F18]-T808

Chien, D. T., Szardenings, A. K., Bahri, S., Walsh, J. C., Mu, F., Xia, C. A., Shankle, W. R., Lerner, A. J., Su, M., Elizarov, A. M., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130098 · Cited by 683

Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons

Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 682

Frontotemporal dementia and parkinsonism linked to chromosome 17: A consensus conference

Foster, N. L., Wilhelmsen, K., Sima, A. A. F., Jones, M. Z., D'Amato, C., & Gilman, S. (1997) · Annals of Neurology · doi:10.1002/ana.410410606 · Cited by 664

Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy

Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664

Structure and novel exons of the human .tau. gene

Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 659

Discovery of previously unidentified genomic disorders from the duplication architecture of the human genome

Sharp, A. J., Hansen, S., Selzer, R. R., Cheng, Z., Regan, R., Hurst, J. A., Stewart, H., Price, S. M., Blair, E., Hennekam, R. C., et al. (2006) · Nature Genetics · doi:10.1038/ng1862 · Cited by 658

Amyloid-β/Fyn–Induced Synaptic, Network, and Cognitive Impairments Depend on Tau Levels in Multiple Mouse Models of Alzheimer's Disease

Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654

Early clinical PET imaging results with the novel PHF-tau radioligand [F-18]-T807

Chien, D. T., Bahri, S., Szardenings, A. K., Walsh, J. C., Mu, F., Su, M.-Y., Shankle, W. R., Elizarov, A., & Kolb, H. C. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-122059 · Cited by 651

Regulation of Tau Pathology by the Microglial Fractalkine Receptor

Bhaskar, K., Konerth, M., Kokiko-Cochran, O. N., Cardona, A., Ransohoff, R. M., & Lamb, B. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.023 · Cited by 639

Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles

Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636

The Prevalence and Malignancy of Alzheimer Disease

Katzman, R. (1976) · Archives of Neurology · doi:10.1001/archneur.1976.00500040001001 · Cited by 623

Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation

Yuzwa, S. A., Shan, X., Macauley, M. S., Clark, T., Skorobogatko, Y., Vosseller, K., & Vocadlo, D. J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.797 · Cited by 611

Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy

PSP Genetics Study Group, Höglinger, G. U., Melhem, N. M., Dickson, D. W., Sleiman, P. M. A., Wang, L.-S., Klei, L., Rademakers, R., de Silva, R., Litvan, I., et al. (2011) · Nature Genetics · doi:10.1038/ng.859 · Cited by 603

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

Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2

Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565

Trans-cellular Propagation of Tau Aggregation by Fibrillar Species

Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552

Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins

Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., & Hasegawa, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408714200 · Cited by 552

RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548

Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.

Wischik, C. M., Edwards, P. C., Lai, R. Y., Roth, M., & Harrington, C. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.11213 · Cited by 547

Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.

Greenberg, S. G., Davies, P., Schein, J., & Binder, L. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48531-6 · Cited by 542

Brain imaging and fluid biomarker analysis in young adults at genetic risk for autosomal dominant Alzheimer's disease in the presenilin 1 E280A kindred: a case-control study

Reiman, E. M., Quiroz, Y. T., Fleisher, A. S., Chen, K., Velez-Pardo, C., Jimenez-Del-Rio, M., Fagan, A. M., Shah, A. R., Alvarez, S., Arbelaez, A., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70228-4 · Cited by 541

Small Misfolded Tau Species Are Internalized via Bulk Endocytosis and Anterogradely and Retrogradely Transported in Neurons

Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537

Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice

Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., & Vitek, M. P. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1179 · Cited by 527

Phosphoprotein Phosphatase Activities in Alzheimer Disease Brain

Gong, C., Singh, T. J., Grundke‐Iqbal, I., & Iqbal, K. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03603.x · Cited by 527

Prevalence and Malignancy of Alzheimer Disease

Lijtmaer, H., Fuld, P. A., & Katzman, R. (1976) · Archives of Neurology · doi:10.1001/archneur.1976.00500040088017 · Cited by 517

Caspase activation precedes and leads to tangles

de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506

PrionsPreprint

Colby, D. W., & Prusiner, S. B. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006833 · Cited by 492

Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport

Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486

The presenilin hypothesis of Alzheimer’s disease: Evidence for a loss-of-function pathogenic mechanism.

Shen, J., & Kelleher, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608332104 · Cited by 485

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

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D. A., & Eisenberg, D. S. (2011) · Nature · doi:10.1038/nature10154 · Cited by 472

A stop-codon mutation in the BRI gene associated with familial British dementia

Vidal, R., Frangione, B., Rostagno, A., Mead, S., Révész, T., Plant, G., & Ghiso, J. (1999) · Nature · doi:10.1038/21637 · Cited by 466

A new chromosome 17q21.31 microdeletion syndrome associated with a common inversion polymorphism

Koolen, D. A., Vissers, L. E. L. M., Pfundt, R., de Leeuw, N., Knight, S. J. L., Regan, R., Kooy, R. F., Reyniers, E., Romano, C., Fichera, M., et al. (2006) · Nature Genetics · doi:10.1038/ng1853 · Cited by 465

The Prevalence and Malignancy of Alzheimer Disease

Katzman, R. (1976) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2008.10.003 · Cited by 463

Frontotemporal Dementia and Corticobasal Degeneration in a Family with a P301S Mutation in Tau

Bugiani, O., Murrell, J. R., Giaccone, G., Hasegawa, M., Ghigo, G., Tabaton, M., Morbin, M., Primavera, A., Carella, F., Solaro, C., et al. (1999) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199906000-00011 · Cited by 450

The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development.

Goedert, M., Jakes, R., Crowther, R. A., Six, J., Lübke, U., Vandermeeren, M., Cras, P., Trojanowski, J. Q., & Lee, V. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5066 · Cited by 446

Staging of Argyrophilic Grains: An Age-Associated Tauopathy

Saito, Y., Ruberu, N. N., Sawabe, M., Arai, T., Tanaka, N., Kakuta, Y., Yamanouchi, H., & Murayama, S. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.9.911 · Cited by 444

Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform.

Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441

Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β

Nussbaum, J. M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al. (2012) · Nature · doi:10.1038/nature11060 · Cited by 427

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 424

Abnormal phosphorylation of the microtubule-associated protein? (tau) in Alzheimer cytoskeletal pathology

Grundke, I., Iqbal, K., Tung, Y.-C., Quinlan, M., Wisniewski, H., & Binder, L. (1987) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198701030-00020 · Cited by 410

Corticobasal degeneration and progressive supranuclear palsy share a common tau haplotype

Houlden, H., Baker, M., Morris, H. R., MacDonald, N., Pickering–Brown, S., Adamson, J., Lees, A. J., Rossor, M. N., Quinn, N. P., Kertesz, A., et al. (2001) · Neurology · doi:10.1212/wnl.56.12.1702 · Cited by 409

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

Massive CA1/2 Neuronal Loss with Intraneuronal and N-Terminal Truncated Aβ42 Accumulation in a Novel Alzheimer Transgenic Model

Casas, C., Sergeant, N., Itier, J.-M., Blanchard, V., Wirths, O., van der Kolk, N., Vingtdeux, V., van de Steeg, E., Ret, G., Canton, T., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63388-3 · Cited by 400

Regulation of the Phosphorylation State and Microtubule-Binding Activity of Tau by Protein Phosphatase 2A

Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Bloom, G. S., & Mumby, M. C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80250-0 · Cited by 397

Genetic evidence for the involvement of τ in progressive supranuclear palsy

Conrad, C., Andreadis, A., Trojanowski, J. Q., Dickson, D. W., Kang, D. E., Chen, X., Wiederholt, W. C., Hansen, L., Masliah, E., Thal, L. J., et al. (1997) · Annals of Neurology · doi:10.1002/ana.410410222 · Cited by 388

Anesthesia Leads to Tau Hyperphosphorylation through Inhibition of Phosphatase Activity by Hypothermia

Planel, E., Richter, K. E. G., Nolan, C. E., Finley, J. E., Liu, L., Wen, Y., Krishnamurthy, P., Herman, M., Wang, L., Schachter, J. B., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4854-06.2007 · Cited by 386

Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling

Kickstein, E., Krauss, S., Thornhill, P., Rutschow, D., Zeller, R., Sharkey, J., Williamson, R., Fuchs, M., Köhler, A., Glossmann, H., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912793107 · Cited by 380

Microdeletion encompassing MAPT at chromosome 17q21.3 is associated with developmental delay and learning disability

Shaw-Smith, C. J., Pittman, A. M., Willatt, L. R., Martin, H., Rickman, L., Gribble, S. M., Curley, R., Cumming, S., Dunn, C. A., Kalaitzopoulos, D. R., et al. (2006) · Nature Genetics · doi:10.1038/ng1858 · Cited by 377

Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy

Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen�, M., Gažová, Z., Mandelkow�, E., & Mandelkow, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507753200 · Cited by 366

Passive Immunization with Anti-Tau Antibodies in Two Transgenic Models

Chai, X., Wu, S., Murray, T. K., Kinley, R. D., Cella, C. V., Sims, H., Buckner, N., Hanmer, J. M., Davies, P., O’Neill, M. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229633 · Cited by 363

Tau protein as a differential biomarker of tauopathies

Sergeant, N., Delacourte, A., & Buée, L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.020 · Cited by 362

The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361

The car☐yl third of tau is tightly bound to paired helical filaments

Kondo, J., Honda, T., Mori, H., Hamada, Y., Miura, R., OGAWARA, M., & Ihara, Y. (1988) · Neuron · doi:10.1016/0896-6273(88)90130-4 · Cited by 357

Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals

Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., & Härtig, W. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-06972.2003 · Cited by 357

Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes

Mercken, M. H., Vandermeeren, M., Lübke, U., Six, J., Boons, J., VOORDE, A. V. D., Martin, J., & Gheuens, J. (1992) · Acta Neuropathologica · doi:10.1007/bf00227819 · Cited by 356

Repeat motifs of tau bind to the insides of microtubules in the absence of taxol

Kar, S., Fan, J., Smith, M. J., Goedert, M., & Amos, L. A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg001 · Cited by 355

Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease.

(1997) · Europe PMC (PubMed Central) · Cited by 354

In Vivo Microdialysis Reveals Age-Dependent Decrease of Brain Interstitial Fluid Tau Levels in P301S Human Tau Transgenic Mice

Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351

Localization of disinhibition-dementia-parkinsonism-amyotrophy complex to 17q21-22.

Wilhelmsen, K. C., Lynch, T., Pavlou, E., Higgins, M., & Nygaard, T. G. (1994) · PubMed · Cited by 347

Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy

Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343

Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments

Spillantini, M. G., Goedert, M., Crowther, R. A., Murrell, J. R., Farlow, M. R., & Ghetti, B. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4113 · Cited by 339

Analysis of microtubule-associated protein tau glycation in paired helical filaments.

Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333

Promotion of Hyperphosphorylation by Frontotemporal Dementia Tau Mutations

Alonso, A. D. C., Mederlyova, A., Novák, M., Grundke, I., & Iqbal, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405131200 · Cited by 330

Proteasomal degradation of tau protein

David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327

MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., & Milligan, R. A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201048 · Cited by 327

Apolipoprotein E4 Causes Age- and Tau-Dependent Impairment of GABAergic Interneurons, Leading to Learning and Memory Deficits in Mice

Andrews-Zwilling, Y., Bien-Ly, N., Xu, Q., Li, G., Bernardo, A., Yoon, S. Y., Zwilling, D., Yan, T. X., Chen, L., & Huang, Y. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4040-10.2010 · Cited by 326

Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments

Delacourte, A., & Défossez, A. (1986) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(86)90167-x · Cited by 325

Epothilone D Improves Microtubule Density, Axonal Integrity, and Cognition in a Transgenic Mouse Model of Tauopathy

Brunden, K. R., Zhang, B., Carroll, J., Yao, Y., Potuzak, J. S., Hogan, A.-M. L., Iba, M., James, M. J., Xie, S. X., Ballatore, C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3059-10.2010 · Cited by 320

Small Ubiquitin-like Modifier (SUMO) Modification of Natively Unfolded Proteins Tau and α-Synuclein

Dorval, V., & Fraser, P. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510127200 · Cited by 319

Tau Protein Is Required for Amyloid β-Induced Impairment of Hippocampal Long-Term Potentiation

Shipton, O. A., Leitz, J. R., Dworzak, J., Acton, C. E. J., Tunbridge, E. M., Denk, F., Dawson, H. N., Vitek, M. P., Wade-Martins, R., Paulsen, O., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2610-10.2011 · Cited by 315

Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312

Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306

Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study.

Hampel, H. J., Ewers, M., Bürger, K., Annas, P., Mörtberg, A., Bogstedt, A., Frölich, L., Schröder, J., Schönknecht, P., Riepe, M. W., et al. (2009) · PubMed · Cited by 305

A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred

Vidal, R., Révész, T., Rostagno, A., Kim, E., Holton, J. L., Bek, T., Bojsen-Møller, M., Braendgaard, H., Plant, G., Ghiso, J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080076097 · Cited by 300

Autophagic degradation of tau in primary neurons and its enhancement by trehalose

Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297

Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo

Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297

Lithium Trial in Alzheimer's Disease

Hampel, H. J., Ewers, M., Bürger, K., Annas, P., Mörtberg, A., Bogstedt, A., Frölich, L., Schröder, J., Schönknecht, P., Riepe, M. W., et al. (2009) · The Journal of Clinical Psychiatry · doi:10.4088/jcp.08m04606 · Cited by 297

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 292

Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

Xu, Y., Chen, Y., Zhang, P., Jeffrey, P. D., & Shi, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.006 · Cited by 290

Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure

Berriman, J. A., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., & Crowther, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1530287100 · Cited by 288

Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer’s disease models

van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Götz, J., & Ittner, L. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009038107 · Cited by 284

Microtubule-Associated Protein Tau

Yen, S.-H. C., Nacharaju, P., Ko, L., Kenessey, Á., & Liu, W.-K. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50012-9 · Cited by 284

Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice

Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281

Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies

Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281

PP2A mRNA Expression Is Quantitatively Decreased in Alzheimer's Disease Hippocampus

Vogelsberg-Ragaglia, V., Schuck, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7630 · Cited by 281

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies

Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., Moulick, K., Aguirre, J., Wu, N. F., Greengard, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701055104 · Cited by 274

p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease

Goedert, M., Cohen, E. S., Jakes, R., & Cohen, P. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81418-l · Cited by 272

Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model

Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272

Allopregnanolone reverses neurogenic and cognitive deficits in mouse model of Alzheimer's disease

Wang, J. M., Singh, C., Liu, L., Irwin, R. W., Chen, S., Chung, E. J., Thompson, R. F., & Brinton, R. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001422107 · Cited by 269

Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer's Disease

Nakamura, K., Greenwood, A., Binder, L. I., Bigio, E. H., Denial, S., Nicholson, L. K., Zhou, X. Z., & Lu, K. P. (2012) · Cell · doi:10.1016/j.cell.2012.02.016 · Cited by 260

Alterations in Glucose Metabolism Induce Hypothermia Leading to Tau Hyperphosphorylation through Differential Inhibition of Kinase and Phosphatase Activities: Implications for Alzheimer's Disease

Planel, E., Miyasaka, T., Launey, T., Chui, D.-H., Tanemura, K., Sato, S., Murayama, O., Ishiguro, K., Tatebayashi, Y., & Takashima, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5561-03.2004 · Cited by 260

MAPT expression and splicing is differentially regulated by brain region: relation to genotype and implication for tauopathies

Trabzuni, D., Wray, S., Vandrovcova, J., Ramasamy, A., Walker, R., Smith, C., Luk, C., Gibbs, J. R., Dillman, A., Hernandez, D. G., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds238 · Cited by 252

Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments

Ksiȩżak-Reding, H., Liu, W.-K., & Yen, S.-H. C. (1992) · Brain Research · doi:10.1016/0006-8993(92)91476-u · Cited by 249

Evidence for Irreversible Inhibition of Glycogen Synthase Kinase-3β by Tideglusib

Domı́nguez, J. M., Fuertes, A., Orozco, L., del Monte-Millán, M., Delgado, E., & Medina, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306472 · Cited by 249

Florbetapir PET analysis of amyloid-β deposition in the presenilin 1 E280A autosomal dominant Alzheimer's disease kindred: a cross-sectional study

Fleisher, A., Chen, K., Quiroz, Y. T., Jakimovich, L. J., Gomez, M. G., Langois, C. M., Langbaum, J. B. S., Ayutyanont, N., Roontiva, A., Thiyyagura, P., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70227-2 · Cited by 246

Abnormal Tau proteins in progressive supranuclear palsy

Flament, S., Delacourte, A., Verny, M., Hauw, J., & Javoy-Agid, F. (1991) · Acta Neuropathologica · doi:10.1007/bf00296367 · Cited by 245

Insulin Dysfunction InducesIn VivoTau Hyperphosphorylation through Distinct Mechanisms

Planel, E., Tatebayashi, Y., Miyasaka, T., Liu, L., Wang, L., Herman, M., Yu, W. H., Luchsinger, J. A., Wadzinski, B. E., Duff, K., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3949-07.2007 · Cited by 242

Extracellular tau is toxic to neuronal cells

Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241

τ in Paired Helical Filaments Is Functionally Distinct from Fetal τ: Assembly Incompetence of Paired Helical Filament‐τ

Yoshida, H., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03642.x · Cited by 236

Mutations in the chromatin modifier gene KANSL1 cause the 17q21.31 microdeletion syndrome

Koolen, D. A., Kramer, J. M., Neveling, K., Nillesen, W. M., Moore-Barton, H. L., Elmslie, F. V., Toutain, A., Amiel, J., Malan, V., Tsai, A. C.-H., et al. (2012) · Nature Genetics · doi:10.1038/ng.2262 · Cited by 232

An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice

Corre, S. L., Klafki, H., Plesnila, N., Hübinger, G., Obermeier, A., Sahagún, H., Monse, B., Seneci, P., Lewis, J. M., Eriksen, J. L., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602913103 · Cited by 232

Chronic traumatic encephalopathy in an Iraqi war veteran with posttraumatic stress disorder who committed suicide

Omalu, B. I., Hammers, J., Bailes, J. E., Hamilton, R. L., Kamboh, M. I., Webster, G., & Fitzsimmons, R. P. (2011) · Neurosurgical FOCUS · doi:10.3171/2011.9.focus11178 · Cited by 229

Specific Pathological Tau Protein Variants Characterize Pickʼs Disease

Delacourte, A., Robitaille, Y., Sergeant, N., Buée, L., Hof, P. R., Wattez, A., Laroche-Cholette, A., Mathieu, J., Chagnon, P., & Gauvreau, D. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199602000-00004 · Cited by 224

β-Sheet Core of Tau Paired Helical Filaments Revealed by Solid-State NMR

Daebel, V., Chinnathambi, S., Biernat, J., Schwalbe, M., Habenstein, B., Loquet, A., Akoury, E., Tepper, K., Müller, H., Baldus, M., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305470p · Cited by 224

Induction of Inflammatory Mediators and Microglial Activation in Mice Transgenic for Mutant Human P301S Tau Protein

Bellucci, A., Westwood, A. J., Ingram, E., Casamenti, F., Goedert, M., & Spillantini, M. G. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63421-9 · Cited by 221

Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice

Ikegami, S. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00964-7 · Cited by 221

Neurofibrillary tangles of Alzheimer's disease: an immunohistochemical study.

Brion, J., Couck, A. M., Passareiro, E., & Flament-Durand, J. (1985) · PubMed · Cited by 209

The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush

Wegmann, S., Medalsy, I. D., Mandelkow�, E., & Müller, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212100110 · Cited by 201

Targeting Phospho-Ser422 by Active Tau Immunotherapy in the THYTau22 Mouse Model: A Suitable Therapeutic Approach

Zommer, N., Sergeant, N., Schraen-Maschke, S., Blum, D., & Buee, L. (2012) · Current Alzheimer Research · doi:10.2174/156720512800492503 · Cited by 193

Tau protein and tau aggregation inhibitors

Bulic, B., Pickhardt, M., Mandelkow, E., & Mandelkow�, E. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.01.016 · Cited by 190

Abnormal Tau-Containing Filaments in Neurodegenerative Diseases

Crowther, R. A., & Goedert, M. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4270 · Cited by 188

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo

Wu, J., Tolstykh, T., Lee, J., Boyd, K., Stock, J. B., & Broach, J. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5672 · Cited by 186

Extracellular Tau Levels Are Influenced by Variability in Tau That Is Associated with Tauopathies

Karch, C. M. M., Jeng, A. T., & Goate, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380642 · Cited by 185

Brain injury biomarkers are not dependent on β‐amyloid in normal elderly

Knopman, D. S., Jack, C. R., Wiste, H. J., Weigand, S. D., Vemuri, P., Lowe, V. J., Kantarci, K., Gunter, J. L., Senjem, M. L., Mielke, M. M., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23816 · Cited by 183

Ultrastructure and biochemical composition of paired helical filaments in corticobasal degeneration.

Ksiȩżak-Reding, H., Morgan, K., Mattiace, L. A., Davies, P., Liu, W. K., Yen, S. H., Weidenheim, K. M., & Dickson, D. W. (1994) · PubMed Central · Cited by 183

Nonoverlapping but synergetic tau and APP pathologies in sporadic Alzheimer’s disease

Delacourte, A., Sergeant, N., Champain, D., Wattez, A., Maurage, C., Lebert, F., Pasquier, F., & David, J. (2002) · Neurology · doi:10.1212/wnl.59.3.398 · Cited by 182

Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden

O’Leary, J. C., Li, Q., Marinec, P. S., Blair, L. J., Congdon, E. E., Johnson, A. G., Jinwal, U. K., Koren, J., Jones, J. R., Kraft, C., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-45 · Cited by 180

Gerstmann‐Straussler‐Scheinker disease II. Neurofibrillary tangles and plaques with PrP‐amyloid coexist in an affected family

Ghetti, B. F., Tagliavini, F., Masters, C. L., Beyreuther, K. T., Giaccone, G., Verga, L., Farlow, M. R., Conneally, P. M., Dlouhy, S. R., Azzarelli, B., et al. (1989) · Neurology · doi:10.1212/wnl.39.11.1453 · Cited by 178

Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice

Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., & Rosenmann, H. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.05.010 · Cited by 174

Hyperdynamic Microtubules, Cognitive Deficits, and Pathology Are Improved in Tau Transgenic Mice with Low Doses of the Microtubule-Stabilizing Agent BMS-241027

Barten, D. M., Fanara, P., Andorfer, C. A., Hoque, N., Wong, P. A., Husted, K. H., Cadelina, G. W., DeCarr, L. B., Yang, L., Liu, V., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0188-12.2012 · Cited by 173

Mutations in KANSL1 cause the 17q21.31 microdeletion syndrome phenotype

Zollino, M., Orteschi, D., Murdolo, M., Lattante, S., Battaglia, D., Stefanini, C., Mercuri, E. M., Chiurazzi, P., Neri, G., & Marangi, G. (2012) · Nature Genetics · doi:10.1038/ng.2257 · Cited by 158

Frontotemporal Dementia: Implications for Understanding Alzheimer DiseasePreprint

Goedert, M., Ghetti, B. F., & Spillantini, M. G. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006254 · Cited by 156

Tau-Targeted Immunization Impedes Progression of Neurofibrillary Histopathology in Aged P301L Tau Transgenic Mice

Bi, M., Ittner, A., Ke, Y. D., Götz, J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026860 · Cited by 153

Mechanistic Basis of Phenothiazine‐Driven Inhibition of Tau Aggregation

Akoury, E., Pickhardt, M., Gajda, M. J., Biernat, J., Mandelkow�, E., & Zweckstetter, M. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208290 · Cited by 151

Paired Helical Filaments from Alzheimer Disease Brain Induce Intracellular Accumulation of Tau Protein in Aggresomes

Santa‐María, I., Varghese, M., Ksiȩżak-Reding, H., Dzhun, A., Wang, J., & Pasinetti, G. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323279 · Cited by 145

Oskar Fischer and the study of dementia

Goedert, M. (2008) · Brain · doi:10.1093/brain/awn256 · Cited by 144

Tau Nitration Occurs at Tyrosine 29 in the Fibrillar Lesions of Alzheimer's Disease and Other Tauopathies

Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2143-06.2006 · Cited by 143

Ageing as a risk factor for neurodegenerative disease

Hou, Y., Dan, X., Babbar, M., Wei, Y., Hasselbalch, S. G., Croteau, D. L., & Bohr, V. A. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0244-7 · Cited by 3,310

Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease

Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740

Pathology of Neurodegenerative Diseases

Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665

Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets

Gao, C., Jiang, J., Tan, Y., & Chen, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01588-0 · Cited by 1,616

The sleep-wake cycle regulates brain interstitial fluid tau in mice and CSF tau in humans

Holth, J. K., Fritschi, S. K., Wang, C., Pedersen, N. P., Cirrito, J. R., Mahan, T. E., Finn, M. B., Manis, M., Geerling, J. C., Fuller, P. M., et al. (2019) · Science · doi:10.1126/science.aav2546 · Cited by 813

Validation of the Movement Disorder Society Criteria for the Diagnosis of 4‐Repeat Tauopathies

Respondek, G., Grimm, M., Piot, I., Arzberger, T., Compta, Y., Englund, E. M., Ferguson, L. W., Gelpí, E., Roeber, S., Giese, A., et al. (2019) · Movement Disorders · doi:10.1002/mds.27872 · Cited by 79

4-repeat tauopathy sharing pathological and biochemical features of corticobasal degeneration and progressive supranuclear palsy

Katsuse, O., Iseki, E., Arai, T., Akiyama, H., Togo, T., Uchikado, H., Kato, M., de Silva, R., Lees, A. J., & Kosaka, K. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0728-8 · Cited by 46

Tau gene mutations and their effects

Goedert, M. (2005) · Movement Disorders · doi:10.1002/mds.20539 · Cited by 134

Mutations causing neurodegenerative tauopathies

Goedert, M., & Jakes, R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.007 · Cited by 438

Relevance of Mutations in Tau for Understanding the Tauopathies

Goedert, M. (2003) · Current Medicinal Chemistry - Immunology Endocrine & Metabolic Agents · doi:10.2174/1568013033483258 · Cited by 3