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

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 · see citing works

Promotion of microtubule assembly in vitro by taxol

SCHIFF, P. B., FANT, J., & HORWITZ, S. B. (1979) · Nature · doi:10.1038/277665a0 · Cited by 3,600 · 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

Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics

Bialojan, C., & Takai, A. (1988) · Biochemical Journal · doi:10.1042/bj2560283 · Cited by 1,703 · 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 · cited 6× · see citing works

Okadaic acid: a new probe for the study of cellular regulation

Cohen, P., Holmes, C. F. B., & Tsukitani, Y. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90192-e · Cited by 1,373 · see citing works

Calyculin A and okadaic acid: Inhibitors of protein phosphatase activity

Ishihara, H., Martin, B. L., Brautigan, D. L., Karaki, H., Ozaki, H., Kato, Y., Fusetani, N., Watabe, S., Hashimoto, K., Uemura, D., et al. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92189-x · Cited by 1,044 · see citing works

Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.

Kilmartin, J. V., Wright, B., & Milstein, C. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.93.3.576 · Cited by 942 · 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

Phosphorylation affects the ability of tau protein to promote microtubule assembly.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works

Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.

Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873 · see citing works

Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms.

Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758 · see citing works

Pluripotent embryonal carcinoma clones derived from the human teratocarcinoma cell line Tera-2. Differentiation in vivo and in vitro.

Andrews, P. W., Damjanov, I., Simón, D., Banting, G. S., Carlin, C. R., Dracopoli, N. C., & Fogh, J. M. (1984) · PubMed · Cited by 613 · see citing works

Pure, postmitotic, polarized human neurons derived from NTera 2 cells provide a system for expressing exogenous proteins in terminally differentiated neurons

Pleasure, S., Page, C., & Lee, V. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-05-01802.1992 · Cited by 607 · 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

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

A taxol-dependent procedure for the isolation of microtubules and microtubule-associated proteins (MAPs).

Vallee, R. B. (1982) · The Journal of cell biology · doi:10.1083/jcb.92.2.435 · Cited by 551 · see citing works

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

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

Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo

Gundersen, G. G., Kalnoski, M. H., & Bulinski, J. C. (1984) · Cell · doi:10.1016/0092-8674(84)90273-3 · Cited by 536 · 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

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 · cited 1× · see citing works

Tubulin dynamics in cultured mammalian cells.

Saxton, W. M., Stemple, D. L., Leslie, R. J., Salmon, E. D., Zavortink, M., & McIntosh, J. R. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.6.2175 · Cited by 488 · see citing works

The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf

Cross, D. A. E., Alessi, D. R., Vandenheede, J. R., McDowell, H. E., Hundal, H. S., & Cohen, P. (1994) · Biochemical Journal · doi:10.1042/bj3030021 · Cited by 474 · see citing works

An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues

Cohen, P., Klumpp, S., & Schelling, D. L. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80803-8 · Cited by 471 · 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

NTera 2 Cells: A human cell line which displays characteristics expected of a human committed neuronal progenitor cell

Pleasure, S. J., & LEE, V. M.-Y. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490350603 · Cited by 437 · see citing works

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

Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41890-x · Cited by 430 · see citing works

Microtubules containing detyrosinated tubulin are less dynamic.

Kreis, T. E. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02550.x · Cited by 429 · see citing works

Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: a difference between dendritic and axonal cytoskeletons

Bernhardt, R., & Matus, A. (1984) · Journal of Comparative Neurology · doi:10.1002/cne.902260205 · Cited by 421 · see citing works

In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase

Gotoh, Y., Nishida, E., Matsuda, S., Shiina, N., Kosako, H., Shiokawa, K., Akiyama, T., Ohta, K., & Sakai, H. (1991) · Nature · doi:10.1038/349251a0 · Cited by 408 · 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

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

Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Bloom, G. S., & Mumby, M. C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80250-0 · Cited by 391 · see citing works

10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin.

Blose, S. H., Meltzer, D. I., & Feramisco, J. R. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.98.3.847 · Cited by 390 · 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

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

Posttranslational modification and microtubule stability.

Schulze, E., Asai, D. J., Bulinski, J. C., & Kirschner, M. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.5.2167 · Cited by 372 · see citing works

Individual microtubules in the axon consist of domains that differ in both composition and stability.

Baas, P. W., & Black, M. M. (1990) · The Journal of cell biology · doi:10.1083/jcb.111.2.495 · Cited by 362 · see citing works

Distribution of tau proteins in the normal human central and peripheral nervous system.

Trojanowski, J. Q., Schuck, T., Schmidt, M. L., & Lee, V. M. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.2.2492045 · Cited by 329 · see citing works

Selective stabilization of microtubules oriented toward the direction of cell migration.

Gundersen, G. G., & Bulinski, J. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.16.5946 · Cited by 303 · see citing works

A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle.

Sontag, E., Nunbhakdi‐Craig, V., Bloom, G. S., & Mumby, M. C. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.6.1131 · Cited by 301 · see citing works

Stabilization and post‐translational modification of microtubules during cellular morphogenesis

Bulinski, J. C., & Gundersen, G. G. (1991) · BioEssays · doi:10.1002/bies.950130605 · Cited by 279 · see citing works

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

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

Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level

Khawaja, S., Gundersen, G. G., & Bulinski, J. C. (1988) · The Journal of cell biology · doi:10.1083/jcb.106.1.141 · Cited by 272 · see citing works

Differential turnover of tyrosinated and detyrosinated microtubules

Webster, D. R., Gundersen, G. G., Bulinski, J. C., & Borisy, G. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9040 · Cited by 261 · see citing works

Cdc2 H1 kinase is negatively regulated by a type 2A phosphatase in the Xenopus early embryonic cell cycle: evidence from the effects of okadaic acid.

Félix, M., Cohen, P., & Karsenti, E. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08159.x · Cited by 248 · see citing works

Differentiation of NTERA-2 clonal human embryonal carcinoma cells into neurons involves the induction of all three neurofilament proteins

Lee, V., & Andrews, P. W. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-02-00514.1986 · Cited by 245 · see citing works

Microtubule dynamics in axons and dendrites

Baas, P. W., Slaughter, T., Brown, A., & Black, M. M. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300115 · Cited by 150 · see citing works

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 · see citing works

Assembly and turnover of detyrosinated tubulin in vivo.

Webster, D. R., Gundersen, G. G., Bulinski, J. C., & Borisy, G. G. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.1.265 · Cited by 128 · see citing works

Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins).

Bramblett, G. T., Trojanowski, J. Q., & Lee, V. M. (1992) · PubMed · Cited by 115 · see citing works

Rapid changes in the distribution of GAP-43 correlate with the expression of neuronal polarity during normal development and under experimental conditions.

Goslin, K., & Banker, G. A. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.4.1319 · Cited by 113 · see citing works

Association of Tau Protein with Microtubules in Living Cells

Drubin, D. G., KOBAYASHI, S., & Kirschner, M. W. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38398.x · Cited by 91 · see citing works

Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells.

Gurland, G., & Gundersen, G. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.8827 · Cited by 87 · see citing works

Expression of microtubule-associated protein 2 by reactive astrocytes.

Geisert, E. E., Johnson, H. G., & Binder, L. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3967 · Cited by 86 · see citing works

Neurofilament-associated protein phosphatase 2A: Its possible role in preserving neurofilaments in filamentous states

Saito, T., Shima, H., Osawa, Y., Nagao, M., Hemmings, B. A., Kishimoto, T., & Hisanaga, S.-I. (1995) · Biochemistry · doi:10.1021/bi00022a010 · Cited by 83 · see citing works

Site-specific Dephosphorylation of Tau Protein at Ser202/Thr205 in Response to Microtubule Depolymerization in Cultured Human Neurons Involves Protein Phosphatase 2A

Merrick, S. E., Demoise, D. C., & Lee, V. M. ‐. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5589 · Cited by 81 · see citing works

The Neurofibrillary Pathology of Alzheimer's Disease

Goedert, M. (1997) · The Neuroscientist · doi:10.1177/107385849700300212 · Cited by 77 · see citing works

Mapping of the Alz 50 epitope in microtubule‐associated proteins tau

Ksiezak‐Reding, H., Chien, C.-H., LEE, V. M.-Y., & Yen, S.-H. C. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250319 · Cited by 61 · see citing works

Site-specific phosphorylation of the middle molecular weight human neurofilament protein in transfected non-neuronal cells

Pleasure, S., Lee, V., & Nelson, D. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-07-02428.1990 · Cited by 35 · see citing works

cdc2 kinase-induced destabilization of map2-coated microtubules in Xenopus egg extracts

Faruki, S., Dorée, M., & Karsenti, E. (1992) · Journal of Cell Science · doi:10.1242/jcs.101.1.69 · Cited by 33 · see citing works

Tau proteins and their significance in the pathobiology of Alzheimer's disease

Lee, V. M. ‐., & Trojanowski, J. Q. (1995) · Elsevier eBooks · doi:10.1016/b978-012286965-5/50005-4 · Cited by 7 · see citing works

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,890 · see citing works

Direct Binding of Reelin to VLDL Receptor and ApoE Receptor 2 Induces Tyrosine Phosphorylation of Disabled-1 and Modulates Tau Phosphorylation

Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916 · see citing works

The many faces of tau

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

History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works

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

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

Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation

Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · 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

Microtubules and signal transduction

Gundersen, G. G., & Cook, T. A. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80010-6 · Cited by 407 · see citing works

Protein phosphatase 2A: the Trojan Horse of cellular signaling

Sontag, E. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(00)00123-6 · Cited by 328 · see citing works

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

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

Molecular Interactions among Protein Phosphatase 2A, Tau, and Microtubules

Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Brandt, R., Kamibayashi, C., Kuret, J., White, C. L., Mumby, M. C., & Bloom, G. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25490 · Cited by 305 · see citing works

Okadaic Acid: More than a Diarrheic Toxin

Valdiglesias, V., Prego-Faraldo, M. V., Pásaro, E., Méndez, J., & Laffón, B. (2013) · Marine Drugs · doi:10.3390/md11114328 · Cited by 276 · see citing works

Tau alteration and neuronal degeneration in tauopathies: mechanisms and models

Brandt, R., Hundelt, M., & Shahani, N. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.018 · Cited by 222 · see citing works

Tau Is Hyperphosphorylated at Multiple Sites in Mouse Brain In Vivo After Streptozotocin-Induced Insulin Deficiency

Clodfelder‐Miller, B., Zmijewska, A. A., Johnson, G. V. W., & Jope, R. S. (2006) · Diabetes · doi:10.2337/db06-0485 · Cited by 185 · see citing works

Inhibition of protein phosphatase 2A- and protein phosphatase 1-induced tau hyperphosphorylation and impairment of spatial memory retention in rats

Sun, L., Liu, S. Y., Zhou, X. W., Wang, X. C., Liu, R., Wang, Q., & Wang, J. Z. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00697-8 · Cited by 168 · see citing works

Regional Selective Neuronal Degeneration after Protein Phosphatase Inhibition in Hippocampal Slice Cultures: Evidence for a MAP Kinase-Dependent Mechanism

Rundén‐Pran, E., Seglen, P. O., Haug, F. Š., Ottersen, O. P., Wieloch, T. W., Shamloo, M., & Laake, J. H. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-18-07296.1998 · Cited by 167 · see citing works

The characterization of microtubule-stabilizing drugs as possible therapeutic agents for Alzheimer's disease and related tauopathies

Brunden, K. R., Yao, Y., Potuzak, J. S., Ferrer, N. I., Ballatore, C., James, M. J., Hogan, A. L., Trojanowski, J. Q., Smith, A. B., & Lee, V. M. ‐. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2010.12.002 · Cited by 159 · see citing works

Neurofilament protein synthesis and phosphorylation

Grant, P. G., & Pant, H. C. (2000) · Journal of Neurocytology · doi:10.1023/a:1010999509251 · Cited by 159 · see citing works

Homocysteine induces tau phosphorylation by inactivating protein phosphatase 2A in rat hippocampus

Zhang, C.-E., Tian, Q., Wei, W., Peng, J.-H., Liu, G., Zhou, X., Wang, Q., Wang, D. W., & Wang, J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.015 · Cited by 159 · see citing works

Phosphorylated Tau Interacts with c-Jun N-terminal Kinase-interacting Protein 1 (JIP1) in Alzheimer Disease

Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156 · see citing works

A Caenorhabditis elegans model of tau hyperphosphorylation: induction of developmental defects by transgenic overexpression of Alzheimer's disease-like modified tau.

Brandt, R., Gergou, A., Wacker, I., Fath, T., & Hutter, H. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.011 · Cited by 126 · see citing works

Gene Expression Profiles of Cholinergic Nucleus Basalis Neurons in Alzheimer's Disease

Mufson, E. J., Counts, S., & Ginsberg, S. D. (2002) · Neurochemical Research · doi:10.1023/a:1020952704398 · Cited by 138 · see citing works

Acceleration and persistence of neurofibrillary pathology in a mouse model of tauopathy following anesthesia

Planel, E., Bretteville, A., Liu, L., Virág, L., Du, A. L., Yu, W. H., Dickson, D. W., Whittington, R. A., & Duff, K. (2009) · The FASEB Journal · doi:10.1096/fj.08-122424 · Cited by 138 · see citing works

Cholesterol‐dependent modulation of tau phosphorylation in cultured neurons

Fan, Q.-W., Yu, W., Senda, T., Yanagisawa, K., & Michikawa, M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00063.x · Cited by 138 · see citing works

Cholesterol‐dependent modulation of dendrite outgrowth and microtubule stability in cultured neurons

Fan, Q., Yu, W., Gong, J., Zou, K., Sawamura, N., Senda, T., Yanagisawa, K., & Michikawa, M. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00686.x · Cited by 134 · see citing works

Tau and Axonopathy in Neurodegenerative Disorders

Higuchi, M., Lee, V. M.-Y., & Trojanowski, J. Q. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:131 · Cited by 134 · see citing works

Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease

Vafai, S. B., & Stock, J. B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02702-3 · Cited by 129 · see citing works

Detyrosinated (Glu) microtubules are stabilized by an ATP-sensitive plus-end cap

Infante, A. S., Stein, M. S., Zhai, Y., Borisy, G. G., & Gundersen, G. G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.22.3907 · Cited by 127 · see citing works

Evidence that Non-Fibrillar Tau Causes Pathology Linked to Neurodegeneration and Behavioral Impairments

Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14406 · Cited by 125 · see citing works

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

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

Different Contributions of Microtubule Dynamics and Transport to the Growth of Axons and Collateral Sprouts

Gallo, G., & Letourneau, P. C. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-10-03860.1999 · Cited by 118 · see citing works

Targeting dysregulated lipid metabolism for the treatment of Alzheimer's disease and Parkinson's disease: Current advancements and future prospects

Tong, B., Ba, Y., Li, Z., Yang, C., Su, K., Qi, H., Zhang, D., Liu, X., Wu, Y., Chen, Y., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106505 · Cited by 117 · see citing works

Therapeutic strategies for the treatment of tauopathies: Hopes and challenges

Khanna, M. R., Kovalevich, J., Lee, V. M. ‐., Trojanowski, J. Q., & Brunden, K. R. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.006 · Cited by 112 · see citing works

Brain protein serine/threonine phosphatases

Price, N. E., & Mumby, M. C. (1999) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(99)80049-x · Cited by 109 · see citing works

Ginsenoside Rg1 attenuates okadaic acid induced spatial memory impairment by the GSK3β/tau signaling pathway and the Aβ formation prevention in rats

Song, X., Hu, J.-F., Chu, S., Zhang, Z., Xu, S., Yuan, Y., Han, N., Liu, Y., Niu, F., He, X., et al. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.03.051 · Cited by 107 · see citing works

Cholinotrophic Molecular Substrates of Mild Cognitive Impairment in the Elderly

Mufson, E. J., Counts, S., Fahnestock, M. L., & Ginsberg, S. D. (2007) · Current Alzheimer Research · doi:10.2174/156720507781788855 · Cited by 100 · see citing works

Identification of Aminothienopyridazine Inhibitors of Tau Assembly by Quantitative High-Throughput Screening

Crowe, A., Huang, W., Ballatore, C., Johnson, R. L., Hogan, A. L., Huang, R., Wichterman, J., McCoy, J. G., Huryn, D. M., Auld, D. S., et al. (2009) · Biochemistry · doi:10.1021/bi9006435 · Cited by 101 · see citing works

Reduced Binding of Protein Phosphatase 2A to Tau Protein with Frontotemporal Dementia and Parkinsonism Linked to Chromosome 17 Mutations

Goedert, M., Satumtira, S., Jakes, R., Smith, M. J., Kamibayashi, C., White, C. L., & Sontag, E. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752155.x · Cited by 100 · see citing works

Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease

Brunden, K. R., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., & Ballatore, C. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.12.046 · Cited by 94 · see citing works

Tau-directed drug discovery for alzheimer's disease and related tauopathies: a focus on tau assembly inhibitors

Brunden, K. R., Ballatore, C., Crowe, A., Smith, Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.08.031 · Cited by 93 · see citing works

Inhibition of JNK by a Peptide Inhibitor Reduces Traumatic Brain Injury–Induced Tauopathy in Transgenic Mice

Tran, H., Sanchez, L., & Brody, D. L. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182456aed · Cited by 92 · see citing works

Age-dependent axonal transport and locomotor changes and tau hypophosphorylation in a “P301L” tau knockin mouse

Gilley, J., Seereeram, A., Ando, K., Mosely, S. I. S., Andrews, S., Kerschensteiner, M., Misgeld, T., Brion, J., Anderton, B. H., Hanger, D. P., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.014 · Cited by 92 · see citing works

The slow axonal transport of cytoskeletal proteins

Nixon, R. A. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80090-2 · Cited by 90 · see citing works

α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly

Oikawa, T., Nonaka, T., Terada, M., Tamaoka, A., Hisanaga, S., & Hasegawa, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.736355 · Cited by 87 · see citing works

The role of tau in Alzheimer's disease

Trojanowski, J. Q., & Lee, V. M.-Y. (2002) · Medical Clinics of North America · doi:10.1016/s0025-7125(02)00002-0 · Cited by 85 · see citing works

Neural Stem Cells Improve Learning and Memory in Rats with Alzheimer’s Disease

Wu, S., Sasaki, A., Yoshimoto, R. U., Kawahara, Y., Manabe, T., Kataoka, K., Asashima, M., & Yuge, L. (2008) · Pathobiology · doi:10.1159/000124979 · Cited by 84 · see citing works

Overexpression of the Protein Phosphatase 2A Regulatory Subunit Bγ Promotes Neuronal Differentiation by Activating the MAP Kinase (MAPK) Cascade

Strack, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203767200 · Cited by 81 · see citing works

Anesthesia-Induced Hyperphosphorylation Detaches 3-Repeat Tau from Microtubules without Affecting Their Stability<i>In Vivo</i>

Planel, E., Krishnamurthy, P., Miyasaka, T., Liu, L., Herman, M., Kumar, A., Bretteville, A., Figueroa, H. Y., Haung Yu, W., Whittington, R. A., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4101-08.2008 · Cited by 79 · see citing works

Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases

Sudo, H., & Baas, P. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq521 · Cited by 78 · see citing works

Developmental regulation of MURF ubiquitin ligases and autophagy proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly and turnover

Perera, S., Holt, M., Mankoo, B. S., & Gautel, M. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.12.024 · Cited by 75 · see citing works

Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17).

Matsumura, N., Yamazaki, T., & Ihara, Y. (1999) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65420-x · Cited by 81 · see citing works

Proteasome Inhibition Stabilizes Tau Inclusions in Oligodendroglial Cells that Occur after Treatment with Okadaic Acid

Goldbaum, O., Oppermann, M., Handschuh, M., Dabir, D. V., Zhang, B., Forman, M. S., Trojanowski, J. Q., Lee, V. M. ‐., & Richter‐Landsberg, C. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08872.2003 · Cited by 73 · see citing works

Reduction of Detyrosinated Microtubules and Golgi Fragmentation Are Linked to Tau-Induced Degeneration in Astrocytes

Yoshiyama, Y., Zhang, B., Bruce, J., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10662.2003 · Cited by 72 · see citing works

Expression of protein phosphatase 2A mutants and silencing of the regulatory Bα subunit induce a selective loss of acetylated and detyrosinated microtubules

Nunbhakdi‐Craig, V., Schüchner, S., Sontag, J., Montgomery, L. G., Pallas, D. C., Juno, C., Mudrak, I., Ogris, E., & Sontag, E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04503.x · Cited by 72 · see citing works

Sequence of neurodegeneration and accumulation of phosphorylated tau in cultured neurons after okadaic acid treatment

Kim, D., Su, J. H., & Cotman, C. W. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01724-2 · Cited by 70 · see citing works

Effect of microcystin-LR and cyanobacterial extract from polish reservoir of drinking water on cell cycle progression, mitotic spindle, and apoptosis in CHO-K1 cells

Lankoff, A., Banasik, A., Obe, G., Deperas-Kamińska, M., Kuzminski, K., Tarczyńska, M., Jurczak, T., & Wójcik, A. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00094-2 · Cited by 69 · see citing works

Characterization of Brain-Penetrant Pyrimidine-Containing Molecules with Differential Microtubule-Stabilizing Activities Developed as Potential Therapeutic Agents for Alzheimer’s Disease and Related Tauopathies

Kovalevich, J., Cornec, A., Yao, Y., James, M., Crowe, A., Lee, V. M. Y., Trojanowski, J. Q., Smith, A. B., Ballatore, C., & Brunden, K. R. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.231175 · Cited by 65 · see citing works

The protein serine/threonine phosphatases PP2A, PP1 and calcineurin: A triple threat in the regulation of the neuronal cytoskeleton

Hoffman, A., Taleski, G., & Sontag, E. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.01.005 · Cited by 65 · see citing works

Transcriptome profiling in neurodegenerative disease

Courtney, E., Kornfeld, S., Janitz, K., & Janitz, M. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.08.018 · Cited by 61 · see citing works

Okadaic acid induces morphological changes, apoptosis and cell cycle alterations in different human cell types

Valdiglesias, V., Laffón, B., Pásaro, E., & Méndez, J. (2011) · Journal of Environmental Monitoring · doi:10.1039/c0em00771d · Cited by 60 · see citing works

Regulation of cell adhesion by PP2A and SV40 small tumor antigen: An important link to cell transformation

Sontag, J. M., & Sontag, E. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6300-7 · Cited by 57 · see citing works

Acetyl-L-Carnitine Attenuates Okadaic Acid Induced Tau Hyperphosphorylation and Spatial Memory Impairment in Rats

Yin, Y., Liu, H., Cong, X.-B., Liu, Z., Wang, Q., Wang, J., & Zhu, L. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1272 · Cited by 56 · see citing works

Folate/vitamin-B12 Prevents Chronic Hyperhomocysteinemia-Induced Tau Hyperphosphorylation and Memory Deficits in Aged Rats

Wei, W., Liu, Y., Zhang, C.-E., Wang, Q., Wei, Z., Mousseau, D. D., Wang, J., Tian, Q., & Liu, G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110770 · Cited by 55 · see citing works

Spinocerebellar ataxia type 12

O’Hearn, E., Holmes, S. E., & Margolis, R. L. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00034-6 · Cited by 54 · see citing works

Early Growth Response 1 (Egr-1) Regulates Phosphorylation of Microtubule-associated Protein Tau in Mammalian Brain

Lu, Y., Li, T., Qureshi, H. Y., Han, D. C., & Paudel, H. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220962 · Cited by 53 · see citing works

The B′ Protein Phosphatase 2A Regulatory Subunit well-rounded Regulates Synaptic Growth and Cytoskeletal Stability at the Drosophila Neuromuscular Junction

Viquez, N. M., Li, C. R., Wairkar, Y. P., & DiAntonio, A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1740-06.2006 · Cited by 53 · see citing works

Go or Stop? Divergent Roles of Reelin in Radial Neuronal Migration

Zhao, S., & Frotscher, M. (2010) · The Neuroscientist · doi:10.1177/1073858410367521 · Cited by 51 · see citing works

Evaluation of the brain-penetrant microtubule-stabilizing agent, dictyostatin, in the PS19 tau transgenic mouse model of tauopathy

Makani, V. S., Zhang, B., Han, H., Yao, Y., Lassalas, P., Lou, K., Paterson, I., Lee, V. M. ‐., Trojanowski, J. Q., Ballatore, C., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0378-4 · Cited by 51 · see citing works

Microtubule stabilization by peloruside A and paclitaxel rescues degenerating neurons from okadaic acid‐induced tau phosphorylation

Das, V., & Miller, J. H. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08084.x · Cited by 49 · see citing works

Process formation of podocytes: morphogenetic activity of microtubules and regulation by protein serine/threonine phosphatase PP2A

Kobayashi, N., Reiser, J., Schwarz, K., Sakai, T., Kriz, W., & Mundel, P. H. (2001) · Histochemistry and Cell Biology · doi:10.1007/s004180000242 · Cited by 48 · see citing works

Melatonin protects SH‐SY5Y neuroblastoma cells from calyculin A‐induced neurofilament impairment and neurotoxicity

Li, S. P., Deng, Y., Wang, X. C., Wang, Y. P., & Wang, J. (2004) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2004.00116.x · Cited by 48 · see citing works

PP2A regulatory subunit Bα controls endothelial contractility and vessel lumen integrity via regulation of HDAC7

Martin, M., Geudens, I., Bruyr, J., Potente, M., Bleuart, A., Lebrun, M., Simonis, N., Deroanne, C., Twizere, J., Soubeyran, P., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.187 · Cited by 47 · see citing works

Neurotoxic and Synaptic Effects of Okadaic Acid, an Inhibitor of Protein Phosphatases

Tapia, R., Peña‐Ortega, F., & Arias, C. (1999) · Neurochemical Research · doi:10.1023/a:1022588808260 · Cited by 47 · see citing works

Brain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathies

Brunden, K. R., Ballatore, C., Lee, V. M. ‐., Smith, A. B., & Trojanowski, J. Q. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120010 · Cited by 46 · see citing works

Genetic variability in the insulin signalling pathway may contribute to the risk of late onset Alzheimer's disease

Liolitsa, D. (2002) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.73.3.261 · Cited by 45 · see citing works

A brain-penetrant triazolopyrimidine enhances microtubule-stability, reduces axonal dysfunction and decreases tau pathology in a mouse tauopathy model

Zhang, B., Yao, Y., Cornec, A., Oukoloff, K., James, M. J., Koivula, P. P., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., Ballatore, C., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0291-3 · Cited by 45 · see citing works

Activation of PP2A‐like phosphatase and modulation of tau phosphorylation accompany stress‐induced apoptosis in cultured oligodendrocytes

Goldbaum, O., & Richter‐Landsberg, C. (2002) · Glia · doi:10.1002/glia.10119 · Cited by 44 · see citing works

New insights into genetic and molecular mechanisms of brain degeneration in tauopathies

Forman, M. S., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(00)00100-9 · Cited by 43 · see citing works

Role of Protein Phosphatases in Estrogen-Mediated Neuroprotection

Yi, K. D., Chung, J., Pang, P. S., & Simpkins, J. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1328-05.2005 · Cited by 42 · see citing works

Partial deletion of theMAPTgene: A novel mechanism of FTDP-17

Rovelet‐Lecrux, A., Lecourtois, M., Thomas-Antérion, C., Ber, I. L., Brice, A., Frébourg, T., Hannequin, D., & Campion, D. (2009) · Human Mutation · doi:10.1002/humu.20979 · Cited by 42 · see citing works

Neuronal gene expression profiling: uncovering the molecular biology of neurodegenerative disease.

Mufson, E., Counts, S., Che, S.-L., & Ginsberg, S. D. (2006) · Progress in Brain Research · doi:10.1016/s0079-6123(06)58010-0 · Cited by 42 · see citing works

BACE inhibitor reduces APP-β-C-terminal fragment accumulation in axonal swellings of okadaic acid-induced neurodegeneration

Yoon, S. Y., Choi, J. E., Yoon, J. H., Huh, J., & Kim, D. H. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.12.013 · Cited by 39 · see citing works

Effect of microcystin-LR on protein phosphatase 2A and its function in human amniotic epithelial cells

Liang, J. L., Tan, L., Zhang, Y., Guo, Z., & Xu, L. (2011) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1100121 · Cited by 37 · see citing works

Inhibition of protein phosphatases impairs the ability of astrocytes to detoxify hydrogen peroxide

Ferrero-Gutiérrez, A., Pérez‐Gómez, A., Novelli, A., & Fernández‐Sánchez, M. T. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.029 · Cited by 34 · see citing works

Protein Kinase CK2 Impairs Spatial Memory Formation through Differential Cross Talk with PI-3 Kinase Signaling: Activation of Akt and Inactivation of SGK1

Chao, C.-C., Ma, Y., & Lee, E. H. Y. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1531-07.2007 · Cited by 35 · see citing works

Monitoring protein phosphatase 1 isoform levels as a marker for cellular stress

Camões, F., Henriques, A. G., Silva, O. A. B. D. C. E., & Silva, E. F. D. C. E. (2004) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2003.12.007 · Cited by 34 · see citing works

Crassostrea gigas exposure to the dinoflagellate Prorocentrum lima: Histological and gene expression effects on the digestive gland

Romero-Geraldo, R. D. J., García-Lagunas, N., & Hernández-Saavedra, N. Y. (2016) · Marine Environmental Research · doi:10.1016/j.marenvres.2016.07.011 · Cited by 33 · see citing works

AMPK Ameliorates Tau Acetylation and Memory Impairment Through Sirt1

Wang, L., Shi, F.-X., Li, N., Cao, Y., Lei, Y., Wang, J., Tian, Q., & Zhou, X. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02079-x · Cited by 34 · see citing works

Protein Aggregation in Alzheimers Disease and Other Neoropathological Disorders

Dimakopoulos, A. C. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772795 · Cited by 32 · see citing works

An anchoring factor targets protein phosphatase 2A to brain microtubules

Price, N. E., Wadzinski, B. E., & Mumby, M. C. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00237-5 · Cited by 32 · see citing works

Bcl-2 protects against apoptosis-related microtubule alterations in neuronal cells

Nuydens, R., Dispersyn, G., Kieboom, G. V. D., de Jong, M., Connors, R., Ramaekers, F. C. S., Borgers, M. J., & Geerts, H. (2000) · APOPTOSIS · doi:10.1023/a:1009685609275 · Cited by 31 · see citing works

Lower motor neuron disease with respiratory failure caused by a novel MAPT mutation

Fonzo, A. D., Ronchi, D., Gallia, F., Cribiù, F. M., Trezzi, I., Vetro, A., Mina, E. D., Limongelli, I., Bellazzi, R., Ricca, I., et al. (2014) · Neurology · doi:10.1212/wnl.0000000000000476 · Cited by 29 · see citing works

Modulation of hippocampal calcium signalling and plasticity by serine/threonine protein phosphatases

Koss, D. J., Hindley, K. P., Riedel, G., & Platt, B. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04579.x · Cited by 28 · see citing works

Protein Phosphatase 2A

Silverstein, A. M., Davis, A. J., Bielinski, V. A., Esplin, E. D., Mahmood, N. A., & Mumby, M. C. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00168-6 · Cited by 28 · see citing works

Microtubules as Regulators of Neural Network Shape and Function: Focus on Excitability, Plasticity and Memory

Peña‐Ortega, F., Robles-Gómez, Á. A., & Cueva, L. X. (2022) · Cells · doi:10.3390/cells11060923 · Cited by 27 · see citing works

Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylation

Lyons, S. P., Greiner, E. C., Cressey, L. E., Adamo, M. E., & Kettenbach, A. N. (2021) · Scientific Reports · doi:10.1038/s41598-021-02456-z · Cited by 27 · see citing works

Identification of differentially expressed genes in SHSY5Y cells exposed to okadaic acid by suppression subtractive hybridization

Valdiglesias, V., Fernandez-Tajes, J. J., Pásaro, E., Méndez, J., & Laffón, B. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-46 · Cited by 27 · see citing works

The involvement of glycogen synthase kinase‐3 and protein phosphatase‐2A in lactacystin‐induced tau accumulation

Ren, Q., Liao, X., Wang, X., Qu, Z.-S., & Wang, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.073 · Cited by 26 · see citing works

Tau proteins with frontotemporal dementia-17 mutations have both altered expression levels and phosphorylation profiles in differentiated neuroblastoma cells

Mack, T. G. A., Dayanandan, R., van Slegtenhorst, M., Whone, A. L., Hutton, M. L., Lovestone, S., & Anderton, B. H. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00434-1 · Cited by 26 · see citing works

Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases.

Trojanowski, J. Q., & Lee, V. M. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.15.8529836 · Cited by 216 · see citing works

Site-specific Dephosphorylation of Tau Protein at Ser202/Thr205 in Response to Microtubule Depolymerization in Cultured Human Neurons Involves Protein Phosphatase 2A

Merrick, S. E., Demoise, D. C., & Lee, V. M. ‐. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5589 · Cited by 81 · see citing works

Pharmacological targets to inhibit alzheimer neurofibrillary degeneration

Iqbal, K., del Alonso, A. C., El-Akkad, E., Gong, C., Haque, N., Khatoon, S., Tsujio, I., & Grundke, I. (2002) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6139-5_29 · Cited by 15 · see citing works

Mechanism of neurofibrillary degeneration in Alzheimer's disease

Iqbal, K., Alonso, A. D. C., Gong, C., Khatoon, S., Singh, T. J., & Grundke, I. (1994) · Molecular Neurobiology · doi:10.1007/bf02816111 · Cited by 72 · see citing works

Molecular Mechanism of Alzheimer's Neurofibrillary Degeneration and Therapeutic Interventiona

Iqbal, K., & Grundke, I. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34411.x · Cited by 38 · see citing works