Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

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 · see citing works

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works

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 · see citing works

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 · see citing works

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 1,114 · see citing works

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 · see citing works

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 · see citing works

Ion spray interface for combined liquid chromatography/atmospheric pressure ionization mass spectrometry

Bruins, A. P., Covey, T. R., & Henion, J. D. (1987) · Analytical Chemistry · doi:10.1021/ac00149a003 · Cited by 880 · see citing works

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 · see citing works

A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 732 · see citing works

The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein

Uchida, Y., Takio, K., Titani, K., Ihara, Y., & Tomonaga, M. (1991) · Neuron · doi:10.1016/0896-6273(91)90272-2 · Cited by 700 · see citing works

Developmentally regulated expression of specific tau sequences

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

A Neuronal Antigen in the Brains of Alzheimer Patients

Wolozin, B. L., Pruchnicki, A., Dickson, D. W., & Davies, P. (1986) · Science · doi:10.1126/science.3083509 · Cited by 585 · see citing works

Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1

Ihara, Y., Nukina, N., Miura, R., & OGAWARA, M. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135662 · Cited by 527 · see citing works

Epitopes that span the tau molecule are shared with paired helical filaments

Kosik, K. S., Orecchio, L. D., Binder, L. I., Trojanowski, J. Q., Lee, V. M.-Y., & Lee, G. S. (1988) · Neuron · doi:10.1016/0896-6273(88)90129-8 · Cited by 497 · see citing works

Substrates for p34cdc2: In vivo veritas?

Moreno, S., & Nurse, P. (1990) · Cell · doi:10.1016/0092-8674(90)90463-o · Cited by 476 · see citing works

Alzheimer's Disease: Insolubility of Partially Purified Paired Helical Filaments in Sodium Dodecyl Sulfate and Urea

Selkoe, D. J., Ihara, Y., & Salazar, F. J. (1982) · Science · doi:10.1126/science.6120571 · Cited by 394 · see citing works

Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.

Kanai, Y., Takemura, R., Oshima, T., Mori, H., Ihara, Y., Yanagisawa, M., Masaki, T., & Hirokawa, N. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.3.1173 · Cited by 360 · see citing works

Neuritic pathology and dementia in alzheimer's disease

McKee, A. C., Kosik, K. S., & Kowall, N. W. (1991) · Annals of Neurology · doi:10.1002/ana.410300206 · Cited by 358 · see citing works

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 355 · see citing works

Deamidation of Glutaminyl and Asparaginyl Residues in Peptides and Proteins

Robinson, A. B., & Rudd, C. J. (1974) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152808-9.50013-4 · Cited by 348 · see citing works

Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease

Ihara, Y. (1988) · Brain Research · doi:10.1016/0006-8993(88)90293-4 · Cited by 304 · see citing works

Antibodies to paired helical filaments in Alzheimer's disease do not recognize normal brain proteins

Ihara, Y., Abraham, C. R., & Selkoe, D. J. (1983) · Nature · doi:10.1038/304727a0 · Cited by 254 · see citing works

Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.

Novak, M., Jakes, R., Edwards, P. C., Milstein, C., & Wischik, C. (1991) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.88.13.5837 · Cited by 217 · see citing works

Fetal‐Type Phosphorylation of the τ in Paired Helical Filaments

Kanemaru, K., Takio, K., Miura, R., Titani, K., & Ihara, Y. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10039.x · Cited by 197 · see citing works

Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease

Bancher, C., Grundke, I., Iqbal, K., Fried, V. A., Smith, H. T., & Wisniewski, H. M. (1991) · Brain Research · doi:10.1016/0006-8993(91)90681-k · Cited by 185 · see citing works

Identification of a Novel Proline-directed Serine/Threonine Protein Kinase in Rat Pheochromocytoma

Vulliet, P. R., Hall, F. L., Mitchell, J. P., & Hardie, D. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71620-7 · Cited by 160 · see citing works

Identification of 3‐ and 4‐repeat tau isoforms within the PHF in Alzheimer's disease.

Jakes, R., Novák, M., Davison, M., & Wischik, C. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07820.x · Cited by 149 · see citing works

Structural stability of paired helical filaments requires microtubule-binding domains of Tau: A model for self-association

Ksiȩżak-Reding, H., & Yen, S.-H. C. (1991) · Neuron · doi:10.1016/0896-6273(91)90169-z · Cited by 136 · see citing works

Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins.

Lee, V. M., Otvos, L. P., Schmidt, M. L., & Trojanowski, J. Q. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.19.7384 · Cited by 124 · see citing works

Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1 II. Specificity and inhibition studies of Achromobacter protease I

Masaki, T., Fujihashi, T., Nakamura, K., & SOEJIMA, M. (1981) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(81)90107-8 · Cited by 121 · see citing works

Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties

Ksiezak‐Reding, H., Binder, L. I., & Yen, S.-H. C. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250320 · Cited by 113 · see citing works

Self assembly of microtubule associated protein tau into filaments resembling those found in alzheimer disease

de Garcini, E. M., Serrano, L. G., & Ávila, J. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80242-x · Cited by 110 · see citing works

A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities

Brion, J., Hanger, D. P., Couck, A. M., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2790831 · Cited by 109 · see citing works

Immunochemical evidence that fragments of phosphorylated MAP5 (MAP1B) are bound to neurofibrillary tangles in Alzheimer's disease

Hasegawa, M., Arai, T., & Ihara, Y. (1990) · Neuron · doi:10.1016/0896-6273(90)90144-5 · Cited by 107 · see citing works

A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope.

Ishiguro, K., Omori, A., Sato, K., Tomizawa, K., Imahori, K., & Uchida, T. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90259-v · Cited by 106 · see citing works

Characterization of two pathological Tau protein variants in Alzheimer brain cortices

Flament, S., Delacourte, A., Hémon, B., & Défossez, A. (1989) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(89)90131-7 · Cited by 101 · see citing works

Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau

Goedert, M., Spillantini, M. G., & Jakes, R. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90541-z · Cited by 86 · see citing works

A Novel Tubulin-Dependent Protein Kinase Forming a Paired Helical Filament Epitope on Tau

Ishiguro, K., Ihara, Y., Uchida, T., & Imahori, K. (1988) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a122465 · Cited by 80 · see citing works

A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments

Mori, H., Hamada, Y., Kawaguchi, M., Honda, T., Kondo, J., & Ihara, Y. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92240-7 · Cited by 50 · see citing works

Characterization of Antisera to Paired Helical Filaments and Tau

Ihara, Y., Kondo, J., Miura, R., Nakagawa, Y., Mori, H., & Honda, T. (2009) · Gerontology · doi:10.1159/000213229 · Cited by 33 · see citing works

Proteolytic Fragments of Alzheimer's Paired Helical Filaments1

Nukina, N., & Ihara, Y. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135443 · Cited by 27 · see citing works

Neuroscience Year–Supplement 1 to the Encyclopedia of Neuroscience

Frost, E. A. M. (1989) · Journal of Neurosurgical Anesthesiology · doi:10.1097/00008506-198912000-00019 · Cited by 10 · see citing works

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works

α-Synuclein is phosphorylated in synucleinopathy lesions

Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 1,906 · see citing works

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 2,007 · see citing works

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 · see citing works

Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death.

Ohshima, T., Ward, J. M., Huh, C. G., Longenecker, G., Veeranna, Pant, H. C., Brady, R. O., Martin, L. J., & Kulkarni, A. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.11173 · Cited by 897 · see citing works

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works

Tau and neurodegenerative disease: the story so far

Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806 · see citing works

Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796 · see citing works

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works

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 718 · see citing works

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease

Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595 · see citing works

A brain-specific activator of cyclin-dependent kinase 5

Lew, J., Huang, Q.-Q., Qi, R. Z., Winkfein, R. J., Aebersold, R. H., Hunt, T., & Wang, J. H.-C. (1994) · Nature · doi:10.1038/371423a0 · Cited by 580 · see citing works

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 · see citing works

Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments

Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E., & Mandelkow, E.-M. (1999) · Biochemistry · doi:10.1021/bi981874p · Cited by 564 · see citing works

Proline-directed and non-proline-directed phosphorylation of PHF-tau

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557 · see citing works

Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau

Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515 · see citing works

Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404

Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390607 · Cited by 488 · see citing works

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 · see citing works

Microtubules, microtubule-interfering agents and apoptosis

Mollinedo, F., & Gajate, C. (2003) · APOPTOSIS · doi:10.1023/a:1025513106330 · Cited by 477 · see citing works

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 · see citing works

Microtubules and microtubule-associated proteins

Mandelkow, E., & Mandelkow, E.-M. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80047-6 · Cited by 458 · see citing works

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 · see citing works

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

Billingsley, M., & Kincaid, R. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 469 · see citing works

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

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

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 · see citing works

Near-atomic model of microtubule-tau interactions

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

Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments

Ishiguro, K., Shiratsuchi, A., Sato, S., Omori, A., Arioka, M., Kobayashi, S., Uchida, T., & Imahori, K. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81066-9 · Cited by 402 · see citing works

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 · see citing works

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

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

Liquid-liquid phase separation induces pathogenic tau conformations in vitro

Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397 · see citing works

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 · see citing works

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 · see citing works

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 378 · see citing works

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

Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375 · see citing works

Therapeutic approaches to Alzheimer's disease

Klafki, H., Staufenbiel, M., Kornhuber, J., & Wiltfang, J. (2006) · Brain · doi:10.1093/brain/awl280 · Cited by 359 · see citing works

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 · see citing works

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 361 · see citing works

MAPs, MARKs and microtubule dynamics

Drewes, G., Ebneth, A., & Mandelkow, E. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01245-6 · Cited by 346 · see citing works

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 · see citing works

Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.

Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E. M., & Mandelkow, E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1887 · Cited by 340 · see citing works

Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90063-w · Cited by 332 · see citing works

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 · see citing works

C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease

Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326 · see citing works

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 317 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313 · see citing works

Tau domains, phosphorylation, and interactions with microtubules

Mandelkow, E.-M., Biernat, J., Drewes, G., Gustke, N., Trinczek, B., & Mandelkow, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00025-a · Cited by 308 · see citing works

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 312 · see citing works

Assembly of recombinant tau into filaments identical to those of Alzheimer’s disease and chronic traumatic encephalopathy

Lövestam, S., Koh, F. A., van Knippenberg, B., Kotecha, A., Murzin, A. G., Goedert, M., & Scheres, S. H. W. (2022) · eLife · doi:10.7554/elife.76494 · Cited by 306 · see citing works

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 · see citing works

Physiological and pathological phosphorylation of tau by Cdk5

Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 297 · see citing works

Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments.

Paudel, H. K., Lew, J., Ali, Z., & Wang, J. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49492-1 · Cited by 285 · see citing works

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 · see citing works

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 · see citing works

Implications of GABAergic Neurotransmission in Alzheimer’s Disease

Li, Y., Sun, H., Chen, Z., Xu, H.-X., Bu, G.-J., & Zheng, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00031 · Cited by 252 · see citing works

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

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

Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B

Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4854 · Cited by 269 · see citing works

A Spatial Gradient of Tau Protein Phosphorylation in Nascent Axons

Mandell, J. W., & Banker, G. A. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05727.1996 · Cited by 270 · see citing works

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 · see citing works

Proteomic landscape of Alzheimer’s Disease: novel insights into pathogenesis and biomarker discovery

Bai, B., Vanderwall, D., Li, Y., Wang, X., Poudel, S., Wang, H., Dey, K. K., Chen, P., Yang, K., & Peng, J. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00474-z · Cited by 252 · see citing works

Genetic modifiers of tauopathy in Drosophila

Shulman, J. M., & Feany, M. B. (2003) · Genetics · doi:10.1093/genetics/165.3.1233 · Cited by 256 · see citing works

Tau Proteins and Tauopathies in Alzheimer’s Disease

Chong, F. P., Ng, K. Y., Koh, R. Y., & Chye, S. M. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0574-1 · Cited by 248 · see citing works

Tau immunotherapy for Alzheimer's disease

Pedersen, J. T., & Sigurdsson, E. M. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.03.003 · Cited by 247 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 246 · see citing works

A cdc2‐related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline‐directed protein kinase associated with microtubule

Kobayashi, S., Ishiguro, K., Omori, A., Takamatsu, M., Arioka, M., Imahori, K., & Uchida, T. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80723-8 · Cited by 234 · see citing works

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 232 · see citing works

In vivo phosphorylation sites in fetal and adult rat tau

Watanabe, A., Hasegawa, M., Suzuki, M., Takio, K., Morishima-Kawashima, M., Titani, K., Arai, T., Kosik, K. S., & Ihara, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74447-0 · Cited by 231 · see citing works

Hyperphosphorylation of tau in PHF.

Morishima-kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Watanabe, A., Titani, K., & Ihara, Y. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00027-c · Cited by 238 · see citing works

Phosphorylation Regulates Tau Interactions with Src Homology 3 Domains of Phosphatidylinositol 3-Kinase, Phospholipase Cγ1, Grb2, and Src Family Kinases

Reynolds, C. H., Garwood, C. J., Wray, S., Price, C., Kellie, S., Perera, T. P. S., Zvelebil, M., Yang, A., Sheppard, P. W., Varndell, I. M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709715200 · Cited by 226 · see citing works

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 · see citing works

“Don’t Phos Over Tau”: recent developments in clinical biomarkers and therapies targeting tau phosphorylation in Alzheimer’s disease and other tauopathies

Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 218 · see citing works

Isoaspartate Formation and Neurodegeneration in Alzheimer's Disease

Shimizu, T., Watanabe, A., OGAWARA, M., Mori, H., & Shirasawa, T. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1955 · Cited by 216 · see citing works

Melatonin in Alzheimer’s Disease

Li, L., Qiong-xia, H., Yang, S.-S., Chu, J., Wang, J., & Tian, Q. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714575 · Cited by 216 · see citing works

REVIEW: tau protein pathology in Alzheimer’s disease and related disorders

Tolnay, M., & Probst (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00182.x · Cited by 210 · see citing works

cAMP-Dependent Protein Kinase Phosphorylations on Tau in Alzheimer’s Disease

Jicha, G. A., Weaver, C. L., Lane, E., Vianna, C., Kress, Y., Rockwood, J. M., & Davies, P. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07486.1999 · Cited by 207 · see citing works

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 · see citing works

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 205 · see citing works

τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinase

Wang, J.-Z., Wu, Q., Smith, A., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01090-4 · Cited by 199 · see citing works

It’s all about tau

Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 195 · see citing works

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 197 · see citing works

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 195 · see citing works

Assembly of two distinct dimers and higher‐order oligomers from full‐length tau

Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · see citing works

The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

Ihara, Y., Morishima-Kawashima, M., & Nixon, R. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006361 · Cited by 190 · see citing works

MARK4 Is a Novel Microtubule-associated Proteins/Microtubule Affinity-regulating Kinase That Binds to the Cellular Microtubule Network and to Centrosomes

Trinczek, B., Brajenovic, M., Ebneth, A., & Drewes, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m304528200 · Cited by 188 · see citing works

Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: the 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity

Arendt, T. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.09.007 · Cited by 188 · see citing works

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 · see citing works

Neuronal cdc2-like kinase

Lew, J., & Wang, J. H.-C. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)88948-3 · Cited by 177 · see citing works

Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

Sibille, N., Sillen, A., Leroy, A., Wieruszeski, J., Mulloy, B., Landrieu, I., & Lippens, G. M. (2006) · Biochemistry · doi:10.1021/bi060964o · Cited by 175 · see citing works

Collapsin Response Mediator Protein-2 Is Associated with Neurofibrillary Tangles in Alzheimer's Disease

Yoshida, H., Watanabe, A., & Ihara, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9761 · Cited by 173 · see citing works

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 167 · see citing works

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 166 · see citing works

Proline-directed phosphorylation of human Tau protein.

Vulliet, R., Halloran, S. M., Braun, R., Smith, A. J., & Lee, G. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41710-3 · Cited by 164 · see citing works

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · see citing works

Secreted beta-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation.

Greenberg, S. M., Koo, E. H., Selkoe, D. J., Qiu, W. Q., & Kosik, K. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7104 · Cited by 161 · see citing works

Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A

Gong, C., Grundke, I., & Iqbal, K. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90400-6 · Cited by 156 · see citing works

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 156 · see citing works

Does modulation of tau hyperphosphorylation represent a reasonable therapeutic strategy for Alzheimer’s disease? From preclinical studies to the clinical trials

Basheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159 · see citing works

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 155 · see citing works

Oligomer Formation of Tau Protein Hyperphosphorylated in Cells

Tepper, K., Biernat, J., Kumar, S., Wegmann, S., Timm, T., Hübschmann, S., Redecke, L., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611368 · Cited by 154 · see citing works

Assembly of Alzheimer‐like filaments from full‐length tau protein

Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80260-2 · Cited by 154 · see citing works

Abnormal tau proteins from Alzheimer's disease brains. Purification and amino acid analysis.

Liu, W. K., Ksiȩżak-Reding, H., & Yen, S. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54696-2 · Cited by 52 · see citing works

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 378 · see citing works

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works

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

Księżak-Reding, H., Liu, W.-K., & Shu, H.-Y. C. (1992) · Brain Research · doi:10.1016/0006-8993(92)91476-u · Cited by 237 · see citing works

Alzheimer's Disease Abnormally Phosphorylated τ Is Dephosphorylated by Protein Phosphatase‐2B (Calcineurin)

Gong, C., Singh, T. J., Grundke, I., & Iqbal, K. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62020803.x · Cited by 145 · see citing works