Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein

Neuropathological stageing of Alzheimer-related changes.

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

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

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668

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

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

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

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

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

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

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

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

Blood phosphorylated tau 181 as a biomarker for Alzheimer's disease: a diagnostic performance and prediction modelling study using data from four prospective cohorts

Karikari, T. K., Pascoal, T. A., Ashton, N. J., Janelidze, S., Benedet, A. L., Rodriguez, J. L., Chamoun, M., Savard, M., Kang, M. S., Therriault, J., et al. (2020) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30071-5 · Cited by 1,316

Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease

Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998

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

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint

Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 897

GSK3 inhibitors: development and therapeutic potential

Cohen, P., & Goedert, M. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1415 · Cited by 801

tau protein in cerebrospinal fluid: A biochemical marker for axonal degeneration in Alzheimer disease?

Blennow, K., Wallin, A., Ågren, H., Spenger, C., Siegfried, J., & Vanmechelen, E. (1995) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815140 · Cited by 789

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

Tau protein and the neurofibrillary pathology of Alzheimer's disease

Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721

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

Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205

Goedert, M., Jakes, R., & Vanmechelen, E. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11484-e · Cited by 608

Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau.

Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588

Age-Dependent Emergence and Progression of a Tauopathy in Transgenic Mice Overexpressing the Shortest Human Tau Isoform

Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564

Abnormal Hyperphosphorylation of Tau: Sites, Regulation, and Molecular Mechanism of Neurofibrillary Degeneration

Wang, J., Xia, Y., Grundke, I., & Iqbal, K. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129031 · Cited by 547

Insulin and Insulin-like Growth Factor-1 Regulate Tau Phosphorylation in Cultured Human Neurons

Hong, M., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19547 · Cited by 522

Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: a sandwich ELISA with a synthetic phosphopeptide for standardization

Vanmechelen, E., Vanderstichele, H., Davidsson, P., Kerschaver, E. V., Perre, B. V. D., Sjögren, M. J. C., Andreasen, N. C., & Blennow, K. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01036-3 · Cited by 487

Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3

Hong, M., Chen, D. C. R., Klein, P. S., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25326 · Cited by 476

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration

Billingsley, M. L., & Kincaid, R. L. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 466

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

Measurement of Phosphorylated Tau Epitopes in the Differential Diagnosisof Alzheimer Disease: A Comparative Cerebrospinal Fluid Study

Hampel, H., Buerger, K., Zinkowski, R., Teipel, S. J., Goernitz, A., Andreasen, N., Sjoegren, M., DeBernardis, J., Kerkman, D., Ishiguro, K., et al. (2004) · Archives of General Psychiatry · doi:10.1001/archpsyc.61.1.95 · Cited by 434

Increased level of active GSK‐3β in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration

Leroy, K., Yilmaz, Z., & Brion, J. ‐. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00795.x · Cited by 404

Inducing Autophagy by Rapamycin Before, but Not After, the Formation of Plaques and Tangles Ameliorates Cognitive Deficits

Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 365

Novel tau biomarkers phosphorylated at T181, T217 or T231 rise in the initial stages of the preclinical Alzheimer’s continuum when only subtle changes in Aβ pathology are detected

Suárez‐Calvet, M., Karikari, T. K., Ashton, N. J., Lantero Rodríguez, J., Milà‐Alomà, M., Gispert, J. D., Salvadó, G., Minguillon, C., Fauria, K., Shekari, M., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012921 · Cited by 401

Total and phosphorylated tau protein as biological markers of Alzheimer’s disease

Hampel, H., Blennow, K., Shaw, L. M., Hoessler, Y. C., Zetterberg, H., & Trojanowski, J. Q. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2009.10.010 · Cited by 389

Histone deacetylase 6 interacts with the microtubule‐associated protein tau

Ding, H., Dolan, P. J., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05564.x · Cited by 387

Prominent Axonopathy in the Brain and Spinal Cord of Transgenic Mice Overexpressing Four-Repeat Human tau Protein

Spittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390

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

Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062465.x · Cited by 386

Tau and Aβ42 in Cerebrospinal Fluid from Healthy Adults 21–93 Years of Age: Establishment of Reference Values

Sjögren, M., Vanderstichele, H., Ågren, H., Zachrisson, O., Edsbagge, M., Wikkelsø, C., Skoog, I., Wallin, A., Wahlund, L.-O., Marcusson, J., et al. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.10.1776 · Cited by 436

Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein

Probst, A., Götz, J., Wiederhold, K., Tolnay, M., Mistl, C., Jaton, A., Hong, M., Ishihara, T., Lee, V., Trojanowski, J., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010051148 · Cited by 362

Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau

Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345

The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase

Woods, Y. L., Cohen, P., Becker, W. B., Jakes, R., Goedert, M., Wang, X., & Proud, C. G. (2001) · Biochemical Journal · doi:10.1042/bj3550609 · 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

Glycogen Synthase Kinase-3β Phosphorylates Protein Tau and Rescues the Axonopathy in the Central Nervous System of Human Four-repeat Tau Transgenic Mice

Spittaels, K., den Haute, C. V., Dorpe, J. V., Geerts, H., Mercken, M. H., Bruynseels, K., Lasrado, R., Vandezande, K., Laenen, I., Boon, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006219200 · Cited by 324

Characterization of Pathology in Transgenic Mice Over-Expressing Human Genomic and cDNA Tau Transgenes

Duff, K., Knight, H., Refolo, L. M., Sanders, S., Yu, X., Picciano, M., Malester, B., Hutton, M., Adamson, J., Goedert, M., et al. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0279 · Cited by 269

The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease

Illenberger, S., Zheng‐Fischhöfer, Q., Preuß, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E., & Mandelkow�, E. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1495 · Cited by 305

Phosphorylation of microtubule‐associated protein tau by stress‐activated protein kinases

Goedert, M., Hasegawa, M., Jakes, R., Lawler, S., Cuenda, A., & Cohen, P. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00483-3 · Cited by 308

Time sequence of maturation of dystrophic neurites associated with Aβ deposits in APP/PS1 transgenic mice

Blanchard, V., Moussaoui, S., Czech, C., Touchet, N., Bonici, B., Planche, M., Canton, T., Jedidi, I., Gohin, M., Wirths, O., et al. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00252-8 · Cited by 283

Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules

Cho, J., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02155.x · Cited by 282

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

Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP.

Ghetti, B. F., Piccardo, P., Spillantini, M. G., Ichimiya, Y., Porro, M., Perini, F., Kitamoto, T., Tateishi, J., Seiler, C. E., Frangione, B., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.2.744 · Cited by 281

A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation

Paquet, D., Bhat, R. V., Sydow, A., Mandelkow, E., von Berg, S., Hellberg, S., Fälting, J. M., Distel, M., Köster, R. W., Schmid, B., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37537 · Cited by 284

Changed Conformation of Mutant Tau-P301L Underlies the Moribund Tauopathy, Absent in Progressive, Nonlethal Axonopathy of Tau-4R/2N Transgenic Mice

Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Haesendonck, C. V., Borghgraef, P., & LEUVEN, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409876200 · Cited by 267

Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites

Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266

A Conformation‐ and Phosphorylation‐Dependent Antibody Recognizing the Paired Helical Filaments of Alzheimer's Disease

Jicha, G. A., Lane, E., Vincent, I. J., Ötvös, L., Hoffmann, R., & Davies, P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052087.x · Cited by 264

Quantification of plasma phosphorylated tau to use as a biomarker for brain Alzheimer pathology: pilot case-control studies including patients with Alzheimer’s disease and down syndrome

Tatebe, H., Kasai, T., Ohmichi, T., Kishi, Y., Kakeya, T., Waragai, M., Kondo, M., Allsop, D., & Tokuda, T. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0206-8 · Cited by 265

Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation

Wagner, U., Utton, M. A., Gallo, J., & Miller, C. C. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1537 · Cited by 258

Both total and phosphorylated tau are increased in Alzheimer's disease

Sjögren, M. J. C. (2001) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.70.5.624 · Cited by 253

Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17

Varani, L., Hasegawa, M., Spillantini, M. G., Smith, M. J., Murrell, J. R., Ghetti, B. F., Klug, A., Goedert, M., & Varani, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.8229 · Cited by 248

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

Pivotal role of glycogen synthase kinase-3: A therapeutic target for Alzheimer's disease

Maqbool, M., Mobashir, M., & Hoda, N. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.10.018 · Cited by 235

Role of glycogen synthase kinase-3 in TNF-α-induced NF-κB activation and apoptosis in hepatocytes

Schwabe, R. F., & Brenner, D. A. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00016.2002 · Cited by 229

Vulnerable neuronal subsets in Alzheimer's and Pick's disease are distinguished by their τ isoform distribution and phosphorylation

Delacourte, A., Sergeant, N., Wattez, A., Gauvreau, D., & Robitaille, Y. (1998) · Annals of Neurology · doi:10.1002/ana.410430209 · Cited by 235

A GSK3‐binding peptide from FRAT1 selectively inhibits the GSK3‐catalysed phosphorylation of Axin and β‐catenin

Thomas, G. M., Frame, S., Goedert, M., Näthke, I. S., Polakis, P. G., & Cohen, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01161-8 · Cited by 234

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

Are tau aggregates toxic or protective in tauopathies?

Cowan, C. M., & Mudher, A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00114 · Cited by 215

Wnt-3a overcomes β-amyloid toxicity in rat hippocampal neurons

Alvarez, A. R., Godoy, J. A., Müllendorff, K., Olivares, G. H., Bronfman, M., & Inestrosa, N. C. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.02.028 · Cited by 212

Characterization of Novel CSF Tau and ptau Biomarkers for Alzheimer’s Disease

Meredith Jr., J. E., Sankaranarayanan, S., Guss, V., Lanzetti, A. J., Berisha, F., Neely, R. J., Slemmon, J. R., Portelius, E., Zetterberg, H., Blennow, K., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076523 · Cited by 209

Activation of Ras-ERK Signaling and GSK-3 by Amyloid Precursor Protein and Amyloid Beta Facilitates Neurodegeneration in Alzheimer’s Disease

Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017) · eneuro · doi:10.1523/eneuro.0149-16.2017 · Cited by 207

Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells

Sperbera, B. R., Leight, S., Goedert, M., & Lee, V. M.-Y. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11902-9 · Cited by 204

Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice

Kins, S., Crameri, A., Evans, D. R. H., Hemmings, B. A., Nitsch, R. M., & Götz, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102621200 · Cited by 203

Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans

Hasegawa, M., Crowther, R. A., Jakes, R., & Goedert, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33118 · Cited by 207

Amyloid-β and Tau at the Crossroads of Alzheimer’s Disease

Gallardo, G., & Holtzman, D. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_16 · Cited by 212

FTDP-17 Mutations in tau Transgenic Mice Provoke Lysosomal Abnormalities and Tau Filaments in Forebrain

Lim, F., Hernández, F., Lucas, J. J., Gómez‐Ramos, P., Morán, M. A., & Ávila, J. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.1051 · Cited by 205

Transgenic Expression of the Shortest Human Tau Affects Its Compartmentalization and Its Phosphorylation as in the Pretangle Stage of Alzheimer's Disease

Brion, J., Tremp, G. L., & Octave, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65272-8 · Cited by 203

Tau protein, the paired helical filament and Alzheimer's disease

Goedert, M., Klug, A., & Crowther, R. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s323 · Cited by 205

Evaluation of 8-Arylsulfanyl, 8-Arylsulfoxyl, and 8-Arylsulfonyl Adenine Derivatives as Inhibitors of the Heat Shock Protein 90

Llauger, L., He, H., Kim, J., Aguirre, J., Rosen, N. X., Peters, U., Davies, P., & Chiosis, G. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049012b · Cited by 191

Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment

Probst, A., Tolnay, M., Langui, D., Goedert, M., & Spillantini, M. G. (1996) · Acta Neuropathologica · doi:10.1007/s004010050565 · Cited by 192

Combined effects of scanning ultrasound and a tau-specific single chain antibody in a tau transgenic mouse model

Nisbet, R. M., Van der Jeugd, A., Leinenga, G., Evans, H. T., Janowicz, P. W., & Götz, J. (2017) · Brain · doi:10.1093/brain/awx052 · Cited by 187

Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo

Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187

Phosphorylation of microtubule‐associated protein tau by isoforms of c‐Jun N‐terminal kinase (JNK)

Yoshida, H., Hastie, C. J., McLauchlan, H., Cohen, P., & Goedert, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02479.x · Cited by 185

Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model

Pérez, M., Hernández, F., Lim, F., Díaz‐Nido, J., & Ávila, J. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5405 · Cited by 180

The role of tau kinases in Alzheimer's disease.

Dolan, P. J., & Johnson, G. V. W. (2010) · PubMed · Cited by 178

A mutation at codon 279 (N279K) in exon 10 of the Tau gene causes a tauopathy with dementia and supranuclear palsy

Delisle, M., Murrell, J. R., Richardson, R., Trofatter, J. A., Rascol, O., Soulages, X., Mohr, M., Calvas, P., & Ghetti, B. F. (1999) · Acta Neuropathologica · doi:10.1007/s004010051052 · Cited by 171

Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease

Seward, M. E., Swanson, E., Norambuena, A., Reimann, A., Cochran, J. N., Li, R., Roberson, E. D., & Bloom, G. S. (2013) · Journal of Cell Science · doi:10.1242/jcs.1125880 · Cited by 178

Analytical performance and clinical utility of the INNOTEST® PHOSPHO-TAU(181P) assay for discrimination between Alzheimer's disease and dementia with Lewy bodies

Vanderstichele, H., de Vreese, K., Blennow, K., Andreasen, N., Sindic, C. J. M., Ivanoiu, A., Hampel, H. J., Bürger, K., Parnetti, L., Lanari, A., et al. (2006) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2006.258 · Cited by 173

Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease

Goedert, M., & Spillantini, M. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00037-5 · Cited by 175

Tau and Tauopathies

Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173

Tau and transgenic animal models

Götz, J. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00055-8 · Cited by 166

Involvement of perineuronal and perisynaptic extracellular matrix in Alzheimer's disease neuropathology

Morawski, M., Brückner, G., Jäger, C., Seeger, G., Matthews, R. T., & Arendt, T. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00557.x · Cited by 157

Neurons associated with aggrecan-based perineuronal nets are protected against tau pathology in subcortical regions in Alzheimer's disease

Morawski, M., Brückner, G., Jäger, C., Seeger, G., & Arendt, T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.05.022 · Cited by 156

TauGene Mutation K257T Causes a Tauopathy Similar to Pick's Disease

Rizzini, C., Goedert, M., Hodges, J. R., Smith, M. J., Jakes, R., Hills, R., Xuereb, J. H., Crowther, R. A., & Spillantini, M. G. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.11.990 · Cited by 161

Characterization of mAb AP422, a novel phosphorylation‐dependent monoclonal antibody against tau protein

Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 163

Diagnostic and prognostic value of serum NfL and p-Tau 181 in frontotemporal lobar degeneration

Benussi, A., Karikari, T. K., Ashton, N. J., Gazzina, S., Premi, E., Benussi, L., Ghidoni, R., Lantero‐Rodriguez, J., Emeršič, A., Simrén, J., et al. (2020) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2020-323487 · Cited by 162

AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease

Buée‐Scherrer, V., Condamines, O., Mourton-Gilles, C., Jakes, R., Goedert, M., Pau, B., & Delacourte, A. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00003-4 · Cited by 161

The Development of Cell Processes Induced by tau Protein Requires Phosphorylation of Serine 262 and 356 in the Repeat Domain and Is Inhibited by Phosphorylation in the Proline-rich Domains

Biernat, J., & Mandelkow, E.-M. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.3.727 · Cited by 149

Unique Alzheimer's Disease Paired Helical Filament Specific Epitopes Involve Double Phosphorylation at Specific Sites

Hoffmann, R., Lee, V. M. ‐., Leight, S., Varga, I., & Ötvös, L. (1997) · Biochemistry · doi:10.1021/bi970380+ · Cited by 152

Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356

Litersky, J. M., Johnson, G. V. W., Jakes, R., Goedert, M., Lee, M., & Seubert, P. A. (1996) · Biochemical Journal · doi:10.1042/bj3160655 · Cited by 150

Signature Tau Neuropathology in Gray and White Matter of Corticobasal Degeneration

Forman, M. S., Zhukareva, V. A., Bergeron, C., Chin, S. S., Grossman, M., Clark, C. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61154-6 · Cited by 149

Transgenic Mouse Model of Tauopathies with Glial Pathology and Nervous System Degeneration

Higuchi, M., Ishihara, T., Zhang, B., Hong, M., Andreadis, A., Trojanowski, J. Q., & Lee, V. M. ‐. (2002) · Neuron · doi:10.1016/s0896-6273(02)00789-4 · Cited by 149

Accumulation of Aspartic Acid 421 - and Glutamic Acid 391 -Cleaved Tau in Neurofibrillary Tangles Correlates With Progression in Alzheimer Disease

Basurto‐Islas, G., Luna‐Muñoz, J., Guillozet-Bongaarts, A. L., Binder, L. I., Mena, R., & García‐Sierra, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31817275c7 · Cited by 163

Pathological properties of the Parkinson?s disease-associated protein DJ-1 in a-synucleinopathies and tauopathies: relevance for multiple system atrophy and Pick?s disease

Neumann, M., M�ller, V., G�rner, K., Kretzschmar, H. A., Haass, C., & Kahle, P. J. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0834-2 · Cited by 148

Rapid Accumulation of Endogenous Tau Oligomers in a Rat Model of Traumatic Brain Injury

Hawkins, B. E., Krishnamurthy, S., Castillo‐Carranza, D. L., Sengupta, U., Prough, D. S., Jackson, G. R., DeWitt, D. S., & Kayed, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.472746 · Cited by 153

Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells)

Merrick, S. E., Trojanowski, J. Q., & Lee, V. M.-Y. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05726.1997 · Cited by 143

The Core of Tau-Paired Helical Filaments Studied by Scanning Transmission Electron Microscopy and Limited Proteolysis

von Bergen�, M., Barghorn, S., Müller, S. A., Pickhardt, M., Biernat, J., Mandelkow, E., Davies, P., Aebi, U., & Mandelkow�, E. (2006) · Biochemistry · doi:10.1021/bi052530j · Cited by 141

The role of tau phosphorylation and cleavage in neuronal cell death

Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 144

Transient Cerebral Ischemia Induces Aberrant Neuronal Cell Cycle Re-entry and Alzheimer's Disease-like Tauopathy in Female Rats

Wen, Y., Yang, S., Liu, R., Brun-Zinkernagel, A. M., Koulen, P., & Simpkins, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311768200 · Cited by 143

Abnormally phosphorylated tau is associated with neuronal and axonal loss in experimental autoimmune encephalomyelitis and multiple sclerosis

Anderson, J. M., Hampton, D. W., Patani, R., Pryce, G., Crowther, R. A., Reynolds, R., Franklin, R. J. M., Giovannoni, G., Compston, D. A. S., Baker, D., et al. (2008) · Brain · doi:10.1093/brain/awn119 · Cited by 141

The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.

Mawal-Dewan, M., Henley, J., VOORDE, A. V. D., Trojanowski, J. Q., & Lee, V. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47378-4 · Cited by 140

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Hoffmann, R., Lee, V. M. ‐., Leight, S., Varga, I., & Ötvös, L. (1997) · Biochemistry · doi:10.1021/bi970380+ · Cited by 152

The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments

Kenessey, Á., & Yen, S.-H. C. (1993) · Brain Research · doi:10.1016/0006-8993(93)90478-6 · Cited by 175

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

404 Molecular characterization of the epitopes of two anti PHF-Tau monoclonal antibodies used in an immunoassay for the mapping of neurofibrillary degeneration in Alzheimer's disease

Gougat, C., Perachon, S., Goedert, M., Condamines, O., Delacourte, A., Pau, B., Granier, C., & Mourton-Gilles, C. (1996) · Neurobiology of Aging · doi:10.1016/s0197-4580(96)80406-4

Developmental Changes in τ Phosphorylation: Fetal τ Is Transiently Phosphorylated in a Manner Similar to Paired Helical Filament‐τ Characteristic of Alzheimer's Disease

Brion, J., Smith, C. J., Couck, A., Gallo, J., & Anderton, B. H. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07444.x · Cited by 202