Tau and tauopathies

Neocortical Neurofibrillary Tangles Correlate With Dementia Severity in Alzheimer's Disease

Bierer, L. M., Hof, P. R., Purohit, D. P., Carlin, L., Schmeidler, J., Davis, K. L., & Perl, D. P. (1995) · Archives of Neurology · doi:10.1001/archneur.1995.00540250089017 · Cited by 514

Pathologic Correlates of Nondemented Aging, Mild Cognitive Impairment, and Early-Stage Alzheimer's Disease

Morris, J. C., & Price, J. L. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:101 · Cited by 513

Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms

Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4637-04.2005 · Cited by 511

Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors.

Drubin, D. G., Feinstein, S. C., Shooter, E. M., & Kirschner, M. W. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1799 · Cited by 510

Frontotemporal dementia in The Netherlands: patient characteristics and prevalence estimates from a population-based study

Rosso, S. M. (2003) · Brain · doi:10.1093/brain/awg204 · Cited by 508

Cell cycle regulation in the postmitotic neuron: oxymoron or new biology?

Herrup, K., & Yang, Y. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2124 · Cited by 507

Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry

Molina, H., Horn, D. M., Tang, N., Mathivanan, S., & Pandey, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611217104 · Cited by 502

Tau imaging: early progress and future directions

Villemagne, V. L., Fodero-Tavoletti, M. T., Masters, C. L., & Rowe, C. C. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70252-2 · Cited by 501

The microtubule binding domain of tau protein

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

Tau promotes neurodegeneration through global chromatin relaxation

Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 495

Invited review: Neuropathology of tauopathies: principles and practice

Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492

Locus‐specific mutation databases for neurodegenerative brain diseases

Cruts, M., Theuns, J., & Broeckhoven, C. V. (2012) · Human Mutation · doi:10.1002/humu.22117 · Cited by 490

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

A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity

Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 484

Tau proteins with FTDP‐17 mutations have a reduced ability to promote microtubule assembly

Hasegawa, M., Smith, M. J., & Goedert, M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01217-4 · Cited by 482

Abnormal Alzheimer‐like phosphorylation of tau‐protein by cyclin‐dependent kinases cdk2 and cdk5

Baumann, K., Mandelkow, E., Biernat, J., Piwnica-Worms, H. M., & Mandelkow, E. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80849-p · Cited by 479

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

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

The importance of tau phosphorylation for neurodegenerative diseases

Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475

Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease.

Strittmatter, W. J., Saunders, A. M., Goedert, M., Weisgraber, K. H., Dong, L. M., Jakes, R., Huang, D. Y., Pericak-Vance, M., Schmechel, D., & Roses, A. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11183 · Cited by 474

The Transcellular Spread of Cytosolic Amyloids, Prions, and Prionoids

Aguzzi, A., & Rajendran, L. (2009) · Neuron · doi:10.1016/j.neuron.2009.12.016 · Cited by 473

Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472

Tau interacts with src-family non-receptor tyrosine kinases

Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 471

CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

Shimura, H., Schwartz, D., Gygi, S. P., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305838200 · Cited by 469

Hibernation in Black Bears: Independence of Metabolic Suppression from Body Temperature

Tøien, Ø., Blake, J. E., Edgar, D. M., Grahn, D. A., Heller, H. C., & Barnes, B. M. (2011) · Science · doi:10.1126/science.1199435 · Cited by 467

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

Freeze Avoidance in a Mammal: Body Temperatures Below 0°C in an Arctic Hibernator

Barnes, B. M. (1989) · Science · doi:10.1126/science.2740905 · Cited by 457

α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?

Kiely, A. P., Asi, Y. T., Kara, E., Limousin, P. D., Ling, H., Lewis, P. A., Proukakis, C., Quinn, N. P., Lees, A. J., Hardy, J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1096-7 · Cited by 457

Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis

Hanger, D. P., Byers, H. L., Wray, S., Leung, K.-Y., Saxton, M. J., Seereeram, A., Reynolds, C. H., Ward, M. A., & Anderton, B. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703269200 · Cited by 455

Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo

Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452

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

The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system

Tai, H.-C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., & Hyman, B. T. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 443

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

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

Alzheimer's Disease-Like Tau Neuropathology Leads to Memory Deficits and Loss of Functional Synapses in a Novel Mutated Tau Transgenic Mouse without Any Motor Deficits

Schindowski, K., Bretteville, A., Leroy, K., Bégard, S., Brion, J., Hamdane, M., & Buée, L. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060002 · Cited by 438

Frontal lobe dementia and motor neuron disease.

Neary, D., Snowden, J. S., Mann, D. M. A., Northen, B., Goulding, P., & MacDermott, N. (1990) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.53.1.23 · Cited by 437

Global Identification and Characterization of Both O-GlcNAcylation and Phosphorylation at the Murine Synapse

Trinidad, J. C., Barkan, D. T., Gulledge, B. F., Thalhammer, A., Šali, A., Schoepfer, R., & Burlingame, A. L. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.018366 · Cited by 437

Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease

Lee, G. S., Thangavel, R., Sharma, V. M., Litersky, J. M., Bhaskar, K., Fang, S. M., Lana, H., Andreadis, A., Hoesen, G. W. V., & Ksiȩżak-Reding, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4162-03.2004 · Cited by 435

Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: A third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques

Braak, H., Braak, E., Grundke-Iqbal, I., & Iqbal, K. (1986) · Neuroscience Letters · doi:10.1016/0304-3940(86)90288-0 · Cited by 432

High Prevalence of Mutations in the Microtubule-Associated Protein Tau in a Population Study of Frontotemporal Dementia in the Netherlands

Rizzu, P., Swieten, J. C. V., Joosse, M., Hasegawa, M., Stevens, M., Tibben, A., Niermeijer, M. F., Hillebrand, M., Ravid, R., Oostra, B. A., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302256 · Cited by 432

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

Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations

Mackenzie, I. R., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I. I., Kril, J. J., Kovács, G. G., Ghetti, B. F., Halliday, G. M., Holm, I. E., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0460-5 · Cited by 425

Abnormal expression of the cell cycle regulators P16 and CDK4 in Alzheimer's disease.

McShea, A., Harris, P. L. R., Webster, K. R., Wahl, A. F., & Smith, M. A. (1997) · Europe PMC (PubMed Central) · Cited by 422

Nuclear Tau, a Key Player in Neuronal DNA Protection

Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421

Microtubule-associated protein tau: A marker of paclitaxel sensitivity in breast cancer

Rouzier, R., Rajan, R., Wagner, P., Hess, K. R., Gold, D. L., Stec, J. J., Ayers, M., Ross, J. S., Zhang, P. G. Y., Buchholz, T. A., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408974102 · Cited by 421

Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP.

Hyman, A. A., Salser, S. J., Drechsel, D. N., Unwin, N., & Mitchison, T. J. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1155 · Cited by 420

Phosphorylation determines two distinct species of tau in the central nervous system

Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420

PARKINSONISM-DEMENTIA COMPLEX, AN ENDEMIC DISEASE ON THE ISLAND OF GUAM

Hirano, A., Kurland, L. T., Krooth, R. S., & Lessell, S. (1961) · Brain · doi:10.1093/brain/84.4.642 · Cited by 419

Alzheimer's disease in Down's syndrome: Clinicopathologic studies

Wisniewski, K. E., Dalton, A. J., McLachlan, D. R. C., Wen, G. Y., & Wisniewski, H. M. (1985) · Neurology · doi:10.1212/wnl.35.7.957 · Cited by 417

Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model

Zhang, B., Maiti, A., Shively, S., Lakhani, F., McDonald-Jones, G., Bruce, J., Lee, E. B., Xie, S. X., Joyce, S., Li, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406361102 · Cited by 413

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

Presenilin 1 associates with glycogen synthase kinase-3β and its substrate tau

Takashima, A., Murayama, M., Murayama, O., Kohno, T., Honda, T., Yasutake, K., Nihonmatsu, N., Mercken, M. H., Yamaguchi, H., Sugihara, S., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9637 · Cited by 409

Defects in Axonal Elongation and Neuronal Migration in Mice with Disrupted tau and map1b Genes

Takei, Y., Teng, J., Harada, A., & Hirokawa, N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.5.989 · Cited by 408

Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology

GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407

Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: Findings from the Nun Study

Riley, K. P., Snowdon, D. A., & Markesbery, W. R. (2002) · Annals of Neurology · doi:10.1002/ana.10161 · Cited by 406

Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis

Braak, H., & Braak, E. (1996) · Acta Neuropathologica · doi:10.1007/s004010050508 · Cited by 406

Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain

Gong, C.-X., Lidsky, T., Wegiel, J., Zuck, L., Grundke-Iqbal, I., & Iqbal, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5535 · Cited by 405

THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE

Terry, R. D. (1963) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-196310000-00005 · Cited by 403

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

Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels

Mertins, P., Yang, F., Liu, T., Mani, D. R., Petyuk, V. A., Gillette, M. A., Clauser, K. R., Qiao, J. W., Gritsenko, M. A., Moore, R. J., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036392 · Cited by 400

Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau

Goode, B., & Feinstein, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.5.769 · Cited by 399

Locus coeruleus neurofibrillary degeneration in aging, mild cognitive impairment and early Alzheimer's disease

Grudzien, A., Shaw, P., Weintraub, S., Bigio, E., Mash, D. C., & Mesulam, M. M. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.02.007 · Cited by 396

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

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

Microtubule-associated Protein/Microtubule Affinity-regulating Kinase (p110mark)

Meyer, H. E., Mandelkow, E.-M., Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmitt-Ulms, G., & Mandelkow, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7679 · Cited by 388

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10369 · Cited by 388

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

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

Mitotic mechanisms in Alzheimer's disease?

Vincent, I., Rosado, M., & Davies, P. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.3.413 · Cited by 386

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

Neuropathology of variants of progressive supranuclear palsy

Dickson, D. W., Ahmed, Z., Algom, A. A., Tsuboi, Y., & Josephs, K. A. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32833be924 · Cited by 386

Axonal transport defects: a common theme in neurodegenerative diseases

Roy, S., Zhang, B., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0952-x · Cited by 384

Emerging histomorphologic phenotypes of chronic traumatic encephalopathy in American athletes

Omalu, B., Bailes, J., Hamilton, R. L., Kamboh, M. I., Hammers, J., Case, M., & Fitzsimmons, R. (2011) · Neurosurgery · doi:10.1227/neu.0b013e318212bc7b · Cited by 381

Neuropathology of Frontotemporal Lobar Degeneration-Tau (FTLD-Tau)

Dickson, D. W., Kouri, N., Murray, M. E., & Josephs, K. A. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9589-0 · Cited by 380

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments.

Schweers, O., Mandelkow, E., Biernat, J., & Mandelkow, E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8463 · Cited by 379

α-Synuclein Binds to Tau and Stimulates the Protein Kinase A-catalyzed Tau Phosphorylation of Serine Residues 262 and 356

Jensen, P. H., Hager, H., Nielsen, M. S., Højrup, P., Gliemann, J., & Jakes, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25481 · Cited by 377

Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo

DuBoff, B., Götz, J., & Feany, M. B. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.026 · Cited by 377

Oxidative Stress and Neurodegeneration

Moreira, P. I., Smith, M. A., Zhu, X., Nunomura, A., Castellani, R. J., & Perry, G. L. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.062 · Cited by 370

MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum

Kosik, K., & Finch, E. (1987) · The Journal of Neuroscience · doi:10.1523/jneurosci.07-10-03142.1987 · Cited by 368

Comparative Biochemistry of Tau in Progressive Supranuclear Palsy, Corticobasal Degeneration, FTDP‐17 and Pick's Disease

Buée, L., & Delacourte, A. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00550.x · Cited by 368

Molecular Mechanisms of Prion Pathogenesis

Aguzzi, A., Sigurdson, C. J., & Heikenwaelder, M. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.154326 · Cited by 366

Straight and paired helical filaments in Alzheimer disease have a common structural unit.

Crowther, R. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2288 · Cited by 366

Cholinergic nucleus basalis tauopathy emerges early in the aging‐MCI‐AD continuum

Mesulam, M. M., Shaw, P. L., Mash, D. C., & Weıntraub, S. (2004) · Annals of Neurology · doi:10.1002/ana.20100 · Cited by 365

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

Tau Aggregation and Its Interplay with Amyloid-β

Nisbet, R. M., Polanco, J.-C., Ittner, L. M., & Götz, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1371-2 · Cited by 359

Preparation and Characterization of Neurotoxic Tau Oligomers

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359

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

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