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

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

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

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

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

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

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 2,133

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

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

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

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

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

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

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 1,211

A decade of CDK5

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

Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17.

Hong, M., Zhukareva, V., Vogelsberg-Ragaglia, V., Wszolek, Z., Reed, L., Miller, B., Geschwind, D., Bird, T., McKeel, D., Goate, A., et al. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,024

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

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

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 1,011

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

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

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 913

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

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

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

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

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 829

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 802

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

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

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

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

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 672

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

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

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

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

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

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

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

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

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

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

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 552

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

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

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

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

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

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

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

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

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

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 434

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

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

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

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 383

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

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

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 366

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

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

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

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

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

Spillantini, M. G., Goedert, M., Crowther, R. A., Murrell, J. R., Farlow, M. R., & Ghetti, B. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4113 · Cited by 339

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

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

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

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 321

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

Cash, A., Aliev, G., 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 316

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

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

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 292

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

Nacharaju, P., Lewis, J. M., Easson, C., Yen, S. H., Hackett, J., Hutton, M., & Yen, S.-H. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00294-x · Cited by 283

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

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

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

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

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

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

Yamaguchi, H., Ishiguro, K., Uchida, T., Takashima, A., Lemere, C. A., & Imahori, K. (1996) · Acta Neuropathologica · doi:10.1007/s004010050513 · Cited by 260

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

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

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

Expression of heat shock proteins in Alzheimer's disease

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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 244

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

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

Williams, A., Jahreiss, L., Sarkar, S., Saiki, S., Menzies, F. M., Ravikumar, B., & Rubinsztein, D. C. (2006) · Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)76003-3 · Cited by 239

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

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

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

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 235

An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice

Corre, S. L., Klafki, H., Plesnila, N., Hübinger, G., Obermeier, A., Sahagún, H., Monse, B., Seneci, P., Lewis, J. M., Eriksen, J. L., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602913103 · Cited by 232

Lithium Reduces Tau Phosphorylation but Not Aβ or Working Memory Deficits in a Transgenic Model with Both Plaques and Tangles

Caccamo, A., Oddo, S., Tran, L. X., & LaFerla, F. M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.061178 · Cited by 227

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

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

Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice

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