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

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

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

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

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

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

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · 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

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

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

Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588 · see citing works

The distribution of tau in the mammalian central nervous system.

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

Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease

Gómez‐Isla, T., Hollister, R., West, H., Mui, S., Growdon, J. H., Petersen, R. C., Parisi, J. E., & Hyman, B. T. (1997) · Annals of Neurology · doi:10.1002/ana.410410106 · Cited by 1,489 · see citing works

A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

Kamal, A., Thao, L., Sensintaffar, J., Zhang, L., Boehm, M. F., Fritz, L. C., & Burrows, F. J. (2003) · Nature · doi:10.1038/nature01913 · Cited by 1,380 · see citing works

GSK-3α regulates production of Alzheimer's disease amyloid-β peptides

Phiel, C. J., Wilson, C., Lee, V. M. ‐., & Klein, P. S. (2003) · Nature · doi:10.1038/nature01640 · Cited by 1,200 · see citing works

A decade of CDK5

Dhavan, R., & Tsai, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096019 · Cited by 1,052 · see citing works

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012 · see citing works

Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17

Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003 · see citing works

Lithium induces autophagy by inhibiting inositol monophosphatase

Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985 · see citing works

Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.

Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 971 · see citing works

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

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

Decreased nuclear β‐catenin, tau hyperphosphorylation and neurodegeneration in GSK‐3β conditional transgenic mice

Lucas, J. J., Hernández, F., Gómez‐Ramos, P., Morán, M. A., Hen, R., & Avila, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.27 · Cited by 903 · 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

Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859 · see citing works

Impaired Proteasome Function in Alzheimer's Disease

Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics

Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 816 · see citing works

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

Harada, A., Oguchi, K., Okabe, S., Kuno, J., Terada, S., Ohshima, T., Sato-Yoshitake, R., Takei, Y., Noda, T., & Hirokawa, N. (1994) · Nature · doi:10.1038/369488a0 · Cited by 806 · see citing works

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

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

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717 · see citing works

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

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

Rapamycin alleviates toxicity of different aggregate-prone proteins

Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657 · see citing works

Domains of tau Protein and Interactions with Microtubules

Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655 · see citing works

Hyperphosphorylation of Microtubule-Associated Protein Tau: A Promising Therapeutic Target for Alzheimer Disease

Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 649 · see citing works

The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642 · see citing works

Structure and novel exons of the human .tau. gene

Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 625 · see citing works

Plaques, tangles and dementia

Wilcock, G. K., & Esiri, M. M. (1982) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(82)90155-1 · Cited by 608 · 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

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

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

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

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

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

Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., & Hasegawa, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408714200 · Cited by 542 · see citing works

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

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

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo

Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · see citing works

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 · see citing works

Proteasome inhibition by paired helical filament‐tau in brains of patients with Alzheimer's disease

Keck, S., Nitsch, R., Grune, T., & Ullrich, O. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01642.x · Cited by 483 · see citing works

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 · see citing works

Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases

Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459 · see citing works

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 · see citing works

Post-translational modifications of tau protein in Alzheimer’s disease

Gong, C.-X., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-004-0221-0 · 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

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 414 · see citing works

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 · see citing works

Rapid Assembly of Alzheimer-like Paired Helical Filaments from Microtubule-Associated Protein Tau Monitored by Fluorescence in Solution

Friedhoff, P., Schneider, A., Mandelkow, E., & Mandelkow�, E. (1998) · Biochemistry · doi:10.1021/bi980537d · Cited by 401 · see citing works

Targeting multiple signal transduction pathways through inhibition of Hsp90

Zhang, H., & Burrows, F. J. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0549-9 · Cited by 377 · see citing works

Spatial learning deficit in transgenic mice that conditionally over‐express GSK‐3β in the brain but do not form tau filaments

Hernández, F., Borrell, J., Guaza, C., Avila, J., & Lucas, J. J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01269.x · Cited by 372 · see citing works

Distribution, Levels, and Activity of Glycogen Synthase Kinase-3 in the Alzheimer Disease Brain

PEI, J.-J., TANAKA, T., TUNG, Y.-C., BRAAK, E., IQBAL, K., & GRUNDKE-IQBAL, I. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199701000-00007 · Cited by 371 · see citing works

Phosphorylation of Tau at Both Thr 231 and Ser 262 Is Required for Maximal Inhibition of Its Binding to Microtubules

Sengupta, A., Kabat, J., Novak, M., Wu, Q., Grundke-Iqbal, I., & Iqbal, K. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0813 · Cited by 363 · see citing works

Transport of paclitaxel (Taxol) across the blood-brain barrier in vitro and in vivo

Fellner, S., Bauer, B., Miller, D. S., Schaffrik, M., Fankhänel, M., Spruß, T., Bernhardt, G., Graeff, C., Färber, L., Gschaidmeier, H., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15451 · Cited by 359 · see citing works

Transport of paclitaxel (Taxol) across the blood-brain barrier in vitro and in vivo

Fellner, S., Bauer, B., Miller, D. S., Schaffrik, M., Fankhänel, M., Spruß, T., Bernhardt, G., Graeff, C., Färber, L., Gschaidmeier, H., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215451 · Cited by 359 · see citing works

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

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Structure, Microtubule Interactions, and Paired Helical Filament Aggregation by Tau Mutants of Frontotemporal Dementias

Barghorn, S., Zheng‐Fischhöfer, Q., Ackmann, M., Biernat, J., von Bergen�, M., Mandelkow�, E., & Mandelkow�, E. (2000) · Biochemistry · doi:10.1021/bi000850r · Cited by 351 · see citing works

Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy

Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen�, M., Gažová, Z., Mandelkow�, E., & Mandelkow, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507753200 · Cited by 350 · see citing works

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

Spillantini, M. G., Goedert, M., Crowther, R. A., Murrell, J. R., Farlow, M. R., & Ghetti, B. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4113 · Cited by 334 · see citing works

Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells

Pickhardt, M., Gažová, Z., von Bergen�, M., Khlistunova, I., Wang, Y., Hascher, A., Mandelkow, E., Biernat, J., & Mandelkow�, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410984200 · Cited by 334 · see citing works

Promotion of Hyperphosphorylation by Frontotemporal Dementia Tau Mutations

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

PAR-1 Kinase Plays an Initiator Role in a Temporally Ordered Phosphorylation Process that Confers Tau Toxicity in Drosophila

Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324 · see citing works

Autophagy in neurodegenerative disease: friend, foe or turncoat?

Nixon, R. A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.07.003 · Cited by 315 · see citing works

Microtubule Reduction in Alzheimer's Disease and Aging Is Independent of τ Filament Formation

Cash, A., Aliev, G. M., Siedlak, S. L., Nunomura, A., Fujioka, H., Zhu, X., Raina, A. K., Vinters, H. V., Tabaton, M., Johnson, T., et al. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64296-4 · Cited by 309 · see citing works

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

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

Lithium Trial in Alzheimer's Disease

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

Neuroprotective Effects of Regulators of the Glycogen Synthase Kinase-3β Signaling Pathway in a Transgenic Model of Alzheimer's Disease Are Associated with Reduced Amyloid Precursor Protein Phosphorylation

Rockenstein, E. M., Torrance, M., Adame, A., Mante, M., Bar‐On, P., Rose, J. B., Crews, L. A., & Masliah, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4321-06.2007 · Cited by 288 · see citing works

Aggregate‐Prone Proteins Are Cleared from the Cytosol by Autophagy: Therapeutic Implications

Williams, A. J., Jahreiss, L., Sarkar, S., Saiki, S., Menzies, F. M., Ravikumar, B., & Rubinsztein, D. C. (2006) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)76003-3 · Cited by 284 · see citing works

Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations

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Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression

Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283 · see citing works

Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease

Panda, D., Samuel, J. C., Massie, M., Feinstein, S. C., & Wilson, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633508100 · Cited by 280 · see citing works

Protein Kinase MARK/PAR-1 Is Required for Neurite Outgrowth and Establishment of Neuronal Polarity

Biernat, J., Wu, Y.-Z., Timm, T., Zheng-Fischhöfer, Q., Mandelkow, E., Meijer, L., & Mandelkow, E.-M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-03-0046 · Cited by 279 · see citing works

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

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

The Generation of a 17 kDa Neurotoxic Fragment: An Alternative Mechanism by which Tau Mediates β-Amyloid-Induced Neurodegeneration

Park, S.-Y., & Ferreira, A. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1125-05.2005 · Cited by 262 · see citing works

Small-molecule aggregates inhibit amyloid polymerization

Feng, B. Y., Toyama, B. H., Wille, H., Colby, D. W., Collins, S. R., May, B. C. H., Prusiner, S. B., Weissman, J. S., & Shoichet, B. K. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.65 · Cited by 257 · see citing works

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

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Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II

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Expression of heat shock proteins in Alzheimer's disease

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Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 244 · see citing works

Selectivity and therapeutic inhibition of kinases: to be or not to be?

Ghoreschi, K., Laurence, A. D. J., & O’Shea, J. J. (2009) · Nature Immunology · doi:10.1038/ni.1701 · Cited by 241 · see citing works

Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.

Imahori, K., & Uchida, T. (1997) · PubMed · Cited by 236 · see citing works

MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons

Mandelkow, E.-M., Thies, E., Trinczek, B., Biernat, J., & Mandelkow, E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401085 · Cited by 236 · see citing works

Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration

Pei, J.-J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., & Cowburn, R. F. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00296-0 · Cited by 226 · see citing works

Chronic lithium administration to FTDP‐17 tau and GSK‐3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre‐formed neurofibrillary tangles do not revert

Engel, T., Goñi‐Oliver, P., Lucas, J. J., Avila, J., & Hernández, F. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04139.x · Cited by 223 · see citing works

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A Neuronal Microtubule-Interacting Agent, NAPVSIPQ, Reduces Tau Pathology and Enhances Cognitive Function in a Mouse Model of Alzheimer’s Disease

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

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A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains

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p25/Cyclin-Dependent Kinase 5 Induces Production and Intraneuronal Accumulation of Amyloid βIn Vivo

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Axonal Transport RatesIn VivoAre Unaffected by Tau Deletion or Overexpression in Mice

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

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Rhodanine‐Based Tau Aggregation Inhibitors in Cell Models of Tauopathy

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Pseudophosphorylation and Glycation of Tau Protein Enhance but Do Not Trigger Fibrillization in Vitro

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Nucleation-dependent Tau Filament Formation

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High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation

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Microtubule-Affinity Regulating Kinase (MARK) Is Tightly Associated with Neurofibrillary Tangles in Alzheimer Brain: A Fluorescence Resonance Energy Transfer Study

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Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic.

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Microtubule Stabilizing Agents as Potential Treatment for Alzheimer’s Disease and Related Neurodegenerative Tauopathies

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Brain-targeted co-delivery of therapeutic gene and peptide by multifunctional nanoparticles in Alzheimer's disease mice

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Mitochondrial Dysfunction in Alzheimers Disease: Opportunities forDrug Development

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Selenium and Alzheimer's Disease: A Systematic Review

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Precortical Phase of Alzheimer's Disease ( AD )‐Related Tau Cytoskeletal Pathology

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

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Microtubule Targeting Agents in Disease: Classic Drugs, Novel Roles

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Tau and Tauopathies

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Enhanced neuroprotection of anthocyanin-loaded PEG-gold nanoparticles against Aβ1-42-induced neuroinflammation and neurodegeneration via the NF-KB /JNK/GSK3β signaling pathway

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Amyloidogenesis of Tau protein

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

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Small molecule recognition of disease-relevant RNA structures

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

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Osmotin attenuates amyloid beta-induced memory impairment, tau phosphorylation and neurodegeneration in the mouse hippocampus

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Roles of Glycogen Synthase Kinase 3 in Alzheimer’s Disease

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Tau Pathology in Chronic Traumatic Encephalopathy and Alzheimer's Disease: Similarities and Differences

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FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

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Neuronal apolipoprotein E4 increases cell death and phosphorylated tau release in alzheimer disease

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Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation

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Tau: From research to clinical development

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Strategies for the Inhibition of Protein Aggregation in Human Diseases

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Divergent CSF   alterations in two common tauopathies: Alzheimer's disease and progressive supranuclear palsy

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Macrocyclic β-Sheet Peptides That Inhibit the Aggregation of a Tau-Protein-Derived Hexapeptide

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Tau‐targeted treatment strategies in Alzheimer's disease

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Sex dimorphism profile of Alzheimer’s disease-type pathologies in an APP/PS1 mouse model

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Lessons from Tau-Deficient Mice

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Immunotherapy for Alzheimer‘s Disease: From Anti-β-Amyloid to Tau-Based Immunization Strategies

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The Binding Sites of Microtubule-Stabilizing Agents

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New perspectives on the role of tau in Alzheimer's disease. Implications for therapy

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Progress and Developments in Tau Aggregation Inhibitors for Alzheimer Disease

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Zinc Binding Directly Regulates Tau Toxicity Independent of Tau Hyperphosphorylation

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Glycogen Synthase Kinase 3β: A New Gold Rush in Anti-Alzheimer’s Disease Multitarget Drug Discovery?: Miniperspective

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Alzheimer, mitochondria and gender

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Brain Intraventricular Injection of Amyloid-β in Zebrafish Embryo Impairs Cognition and Increases Tau Phosphorylation, Effects Reversed by Lithium

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Alzheimer’s Disease: Etiology, Neuropathology and Pathogenesis

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Amyloid-based immunotherapy for Alzheimer's disease in the time of prevention trials: the way forward

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G-protein coupled receptor, PI3K and Rho signaling pathways regulate the cascades of Tau and amyloid-β in Alzheimer’s disease

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Tau as a Therapeutic Target for Alzheimers Disease

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Tau mis-splicing in the pathogenesis of neurodegenerative disorders

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Baicalein suppresses Repeat Tau fibrillization by sequestering oligomers

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The selective GSK3 inhibitor, SAR502250, displays neuroprotective activity and attenuates behavioral impairments in models of neuropsychiatric symptoms of Alzheimer's disease in rodents

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Tau Ser262 phosphorylation is critical for A 42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease

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Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease

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The Conundrum of GSK3 Inhibitors: Is it the Dawn of a New Beginning?

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TREM2 in Alzheimer’s Disease: Microglial Survival and Energy Metabolism

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

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Fulvic Acid Inhibits Aggregation and Promotes Disassembly of Tau Fibrils Associated with Alzheimer's Disease

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Parkinsonian Neurotoxin 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-Synuclein Mutations Promote Tau Protein Phosphorylation at Ser262 and Destabilize Microtubule Cytoskeleton in Vitro

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Targeting Tau Protein in Alzheimerʼs Disease

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Cell-based Models To Investigate Tau Aggregation

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Design, Optimization, and Study of Small Molecules That Target Tau Pre-mRNA and Affect Splicing

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Opioid System and Alzheimer’s Disease

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Recent Tau-Targeted Clinical Strategies for the Treatment of Alzheimer's Disease

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