Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

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

Memantine in Moderate-to-Severe Alzheimer's Disease

Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821

Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories

Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118

Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease

Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113

Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.

Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

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

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

Current and Future Treatments in Alzheimer Disease: An Update

Yiannopoulou, K. G., & Papageorgiou, S. G. (2020) · Journal of Central Nervous System Disease · doi:10.1177/1179573520907397 · Cited by 966

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949

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

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 893

Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau

Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881

Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843

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

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

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

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

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

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

Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

Liu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759

Peptide sequences that target cytosolic proteins for lysosomal proteolysis

Dice, J. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90019-8 · Cited by 755

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 723

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721

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

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor

Bowers, E. M., Yan, G., Mukherjee, C., Orry, A., Wang, L., Holbert, M. A., Crump, N. T., Hazzalin, C. A., Liszczak, G., Yuan, H., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.006 · Cited by 666

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

From Promiscuity to Precision: Protein Phosphatases Get a Makeover

Virshup, D. M., & Shenolikar, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.015 · Cited by 643

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

Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617

Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation

Yuzwa, S. A., Shan, X., Macauley, M. S., Clark, T., Skorobogatko, Y., Vosseller, K., & Vocadlo, D. J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.797 · Cited by 611

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609

Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2

Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565

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

Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543

A Phase II Trial of Tideglusib in Alzheimer's Disease

Lovestone, S., for the ARGO investigators, Boada, M., Dubois, B., Hüll, M., Rinne, J. O., Huppertz, H.-J., Calero, M., Andrés, M. V., Gómez-Carrillo, B., et al. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-141959 · Cited by 536

Neuroprotective effects of curcumin

Cole, G. M., Teter, B., & Frautschy, S. A. (2007) · ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY · doi:10.1007/978-0-387-46401-5_8 · Cited by 516

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516

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

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

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

CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

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

Multiple-motor based transport and its regulation by Tau

Vershinin, M., Carter, B. C., Razafsky, D. S., King, S. J., & Gross, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607919104 · Cited by 457

Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling

Myeku, N., Clelland, C. L., Emrani, S., Kukushkin, N. V., Yu, W. H., Goldberg, A. L., & Duff, K. E. (2016) · Nature Medicine · doi:10.1038/nm.4011 · Cited by 446

Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease

Liu, F., Shi, J., Tanimukai, H., Gu, J., Gu, J., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X. (2009) · Brain · doi:10.1093/brain/awp099 · Cited by 439

Disease-modifying properties of long-term lithium treatment for amnestic mild cognitive impairment: randomised controlled trial

Forlenza, O. V., Diniz, B. S., Radanovic, M., Santos, F. S., Talib, L. L., & Gattaz, W. F. (2011) · The British Journal of Psychiatry · doi:10.1192/bjp.bp.110.080044 · Cited by 411

Advanced Glycation End Products in Alzheimer's Disease and Other Neurodegenerative Diseases

Sasaki, N., Fukatsu, R., Tsuzuki, K., Hayashi, Y., Yoshida, T., Fujii, N., Koike, T., WAKAYAMA, I., Yanagihara, R. T., Garruto, R. M., et al. (1998) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65659-3 · Cited by 411

Xylulose 5-phosphate mediates glucose-induced lipogenesis by xylulose 5-phosphate-activated protein phosphatase in rat liver

Kabashima, T., Kawaguchi, T., Wadzinski, B. E., & Uyeda, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730817100 · Cited by 401

Protein phosphatase 2A: a target for anticancer therapy

Perrotti, D., & Neviani, P. (2013) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70558-2 · Cited by 400

Design of phosphodiesterase 4D (PDE4D) allosteric modulators for enhancing cognition with improved safety

Burgin, A. B., Magnússon, Ó. Þ., Singh, J., Witte, P., Staker, B. L., Björnsson, J. M., Þorsteinsdóttir, M., Hrafnsdóttir, S., Hagen, T. J., Kiselyov, A. S., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1598 · Cited by 396

PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)

Janssens, V., Longin, S., & Goris, J. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.004 · Cited by 390

Tau aggregation is driven by a transition from random coil to beta sheet structure

von Bergen�, M., Barghorn, S., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.010 · Cited by 389

O-GlcNAcase Uses Substrate-assisted Catalysis

Macauley, M. S., Whitworth, G. E., Debowski, A. W., Chin, D., & Vocadlo, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413819200 · Cited by 385

Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling

Kickstein, E., Krauss, S., Thornhill, P., Rutschow, D., Zeller, R., Sharkey, J., Williamson, R., Fuchs, M., Köhler, A., Glossmann, H., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912793107 · Cited by 380

Astrocytes are important mediators of Aβ-induced neurotoxicity and tau phosphorylation in primary culture

Garwood, C. J., Pooler, A. M., Atherton, J., Hanger, D. P., & Noble, W. (2011) · Cell Death & Disease · doi:10.1038/cddis.2011.50 · Cited by 379

Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder

Nunes, P. V., Forlenza, O. V., & Gattaz, W. F. (2007) · The British Journal of Psychiatry · doi:10.1192/bjp.bp.106.029868 · Cited by 369

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

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

Inducing Autophagy by Rapamycin Before, but Not After, the Formation of Plaques and Tangles Ameliorates Cognitive Deficits

Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 365

mTOR regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies

Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362

Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease

Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360

Tau and neuroinflammation: what impact for Alzheimer's disease and tauopathies?

Laurent, C., Buée, L., & Blum, D. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.01.003 · Cited by 348

Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy

Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343

Treatment of Alzheimer's Disease with the GSK-3 Inhibitor Tideglusib: A Pilot Study

del Ser, T., Steinwachs, K. C., Gertz, H. J., Andrés, M. V., Gómez-Carrillo, B., Medina, M., Vericat, J. A., Redondo, P., Fleet, D., & León, T. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-120805 · Cited by 329

Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance

Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 325

Accelerated neurodegeneration through chaperone-mediated oligomerization of tau

Blair, L. J., Nordhues, B. A., Hill, S. E., Scaglione, K. M., O’Leary, J. C., Fontaine, S. N., Breydo, L., Zhang, B., Li, P., Wang, L., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69003 · Cited by 322

Chaperone-mediated autophagy in aging and disease

Massey, A. C., Zhang, C., & Cuervo, A. M. (2006) · Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)73007-6 · Cited by 315

Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage

Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314

Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312

Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway

Lu, M., Liu, T., Jiao, Q., Ji, J., Tao, M., Liu, Y., You, Q., & Jiang, Z. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.063 · Cited by 310

Current Advances on Different Kinases Involved in Tau Phosphorylation, and Implications in Alzheimers Disease and Tauopathies

Ferrer, I., Gómez‐Isla, T., Puig, B., Freixes, M., Ribé, E. M., Dalfó, E., & Ávila, J. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772713 · Cited by 309

Current and future treatments in Alzheimer’s disease

Atri, A. (2019) · Seminars in Neurology · doi:10.1055/s-0039-1678581 · Cited by 309

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

Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease

Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301

Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation

Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298

Autophagic degradation of tau in primary neurons and its enhancement by trehalose

Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297

Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo

Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297

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

Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer’s disease models

van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Götz, J., & Ittner, L. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009038107 · Cited by 284

Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models

Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283

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

Tau Aggregation Inhibitor Therapy: An Exploratory Phase 2 Study in Mild or Moderate Alzheimer's Disease

Wischik, C. M., Staff, R. T., Wischik, D. J., Bentham, P., Murray, A. D., Storey, J. M. D., Kook, K. A., & Harrington, C. R. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142874 · Cited by 269

Lithium Treatment and Risk of Dementia

Kessing, L. V., Søndergård, L., Forman, J. L., & Andersen, P. K. (2008) · Archives of General Psychiatry · doi:10.1001/archpsyc.65.11.1331 · Cited by 267

Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer's Disease

Nakamura, K., Greenwood, A., Binder, L. I., Bigio, E. H., Denial, S., Nicholson, L. K., Zhou, X. Z., & Lu, K. P. (2012) · Cell · doi:10.1016/j.cell.2012.02.016 · Cited by 260

NAG-thiazoline, An N-Acetyl-β-hexosaminidase Inhibitor That Implicates Acetamido Participation

Knapp, S., Vocadlo, D. J., Gao, Z., Kirk, B. A., Lou, J., & Withers, S. G. (1996) · Journal of the American Chemical Society · doi:10.1021/ja960826u · Cited by 248

Deletion of the Ubiquitin Ligase CHIP Leads to the Accumulation, But Not the Aggregation, of Both Endogenous Phospho- and Caspase-3-Cleaved Tau Species

Dickey, C. A., Yue, M., Lin, W.-L., Dickson, D. W., Dunmore, J. H., Lee, W. C., Zehr, C., West, G., Cao, S., Clark, A. M. K., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0746-06.2006 · Cited by 248

Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247

Selective inhibitors of the FK506-binding protein 51 by induced fit

Gaali, S., Kirschner, A., Cuboni, S., Hartmann, J., Kozany, C., Balsevich, G., Namendorf, C., Fernandez-Vizarra, P., Sippel, C., Zannas, A. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1699 · Cited by 245

Internalized Tau Oligomers Cause Neurodegeneration by Inducing Accumulation of Pathogenic Tau in Human Neurons Derived from Induced Pluripotent Stem Cells

Usenovic, M., Niroomand, S., Drolet, R. E., Yao, L., Gaspar, R. C., Hatcher, N. G., Schachter, J., Renger, J. J., & Parmentier-Batteur, S. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.1523-15.2015 · Cited by 245

Potential antidepressant activity of rolipram and other selective cyclic adenosine 3′,5′-monophosphate phosphodiesterase inhibitors

Wachtel, H. (1983) · Neuropharmacology · doi:10.1016/0028-3908(83)90239-3 · Cited by 242

Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes

Lee, M. J., Lee, B., Hanna, J. W., King, R. W., & Finley, D. J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r110.003871 · Cited by 239

SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination

Luo, H.-B., Xia, Y.-Y., Shu, X.-J., Liu, Z.-C., Feng, Y., Liu, X.-H., Yu, G., Yin, G., Xiong, Y.-S., Zeng, K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417548111 · Cited by 236

Pivotal role of glycogen synthase kinase-3: A therapeutic target for Alzheimer's disease

Maqbool, M., Mobashir, M., & Hoda, N. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.10.018 · Cited by 235

Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability

Jinwal, U. K., Miyata, Y., Koren, J., Jones, J. R., Trotter, J. H., Chang, L., O’Leary, J. C., Morgan, D., Lee, D. C., Shults, C. L., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3345-09.2009 · Cited by 233

PROTACs: An Emerging Targeting Technique for Protein Degradation in Drug Discovery

Gu, S., Cui, D., Chen, X., Xiong, X., & Zhao, Y. (2018) · BioEssays · doi:10.1002/bies.201700247 · Cited by 231

cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins

Lokireddy, S., Kukushkin, N. V., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522332112 · Cited by 228

Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.

Ozcelik, S., Fraser, G., Castets, P., Schaeffer, V., Skachokova, Z., Breu, K., Clavaguera, F., Sinnreich, M., Kappos, L., Goedert, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062459 · Cited by 226

Does lithium protect against dementia?

Kessing, L., Forman, J., & Andersen, P. (2010) · Bipolar Disorders · doi:10.1111/j.1399-5618.2009.00788.x · Cited by 222

Curcumin Suppresses Soluble Tau Dimers and Corrects Molecular Chaperone, Synaptic, and Behavioral Deficits in Aged Human Tau Transgenic Mice

Ma, Q., Zuo, X., Yang, F., Ubeda, O. J., Gant, D. J., Alaverdyan, M., Teng, E., Hu, S., Chen, P., Maiti, P., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393751 · Cited by 220

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.

Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219

Potential of Low Dose Leuco-Methylthioninium Bis(Hydromethanesulphonate) (LMTM) Monotherapy for Treatment of Mild Alzheimer’s Disease: Cohort Analysis as Modified Primary Outcome in a Phase III Clinical Trial

Wilcock, G. K., Gauthier, S., Frisoni, G. B., Jia, J., Hardlund, J. H., Moebius, H. J., Bentham, P., Kook, K. A., Schelter, B. O., Wischik, D. J., et al. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-170560 · Cited by 219

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules

Jinwal, U. K., Koren, J., Borysov, S. I., Schmid, A. B., Abisambra, J. F., Blair, L. J., Johnson, A. G., Jones, J. R., Shults, C. L., O'Leary, J. C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4815-09.2010 · Cited by 214

Association of Lithium in Drinking Water With the Incidence of Dementia

Kessing, L. V., Gerds, T. A., Knudsen, N. N., Jørgensen, L. F., Kristiansen, S. M., Voutchkova, D., Ernstsen, V., Schullehner, J., Hansen, B., Andersen, P. K., et al. (2017) · JAMA Psychiatry · doi:10.1001/jamapsychiatry.2017.2362 · Cited by 213

Proapoptotic Effects of Tau Cleavage Product Generated by Caspase-3

Chung, C.-W., Song, Y.-H., Kim, I.-K., Yoon, W. J., Ryu, B. R., Jo, D., Woo, H., Kwon, Y.-K., Kim, H., Gwag, B.-J., et al. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0335 · Cited by 211

Loss of O -GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration

Wang, A. C., Jensen, E. H., Rexach, J. E., Vinters, H. V., & Hsieh-Wilson, L. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606899113 · Cited by 211

Towards a Pharmacophore for Amyloid

Landau, M., Sawaya, M. R., Faull, K. F., Laganowsky, A. D., Jiang, L., Sievers, S. A., Liu, J., Barrio, J. R., & Eisenberg, D. S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001080 · Cited by 210

It’s all about tau

Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207

Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction

Zhang, T., Li, Y., Yu, Y., Zou, P., Jiang, Y., & Sun, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051532 · Cited by 202

The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture

Dotti, C. G., Banker, G., & Binder, L. (1987) · Neuroscience · doi:10.1016/0306-4522(87)90276-4 · Cited by 199

Lithium as a Treatment for Alzheimer’s Disease: A Systematic Review and Meta-Analysis

Matsunaga, S., Kishi, T., Annas, P., Basun, H., Hampel, H. J., & Iwata, N. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150437 · Cited by 196

Downregulation of Protein Phosphatase 2A Carboxyl Methylation and Methyltransferase May Contribute to Alzheimer Disease Pathogenesis

Sontag, E., Hladik, C. L., Montgomery, L. G., Luangpirom, A., Mudrak, I., Ogris, E., & White, C. L. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.10.1080 · Cited by 195

Enhanced Phosphatase Activity Attenuates α-Synucleinopathy in a Mouse Model

Lee, K.-W., Chen, W. W., Junn, E., Im, J., Grosso, H., Sonsalla, P. K., Feng, X., Ray, N., Fernandez, J. R., Chao, Y., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6513-10.2011 · Cited by 194

Specific Targeting of Tau Oligomers in Htau Mice Prevents Cognitive Impairment and Tau Toxicity Following Injection with Brain-Derived Tau Oligomeric Seeds

Castillo‐Carranza, D. L., Gerson, J. E., Sengupta, U., Guerrero‐Munoz, M. J., Lasagna‐Reeves, C. A., & Kayed, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132477 · Cited by 190

Microdose Lithium Treatment Stabilized Cognitive Impairment in Patients with Alzheimer’s Disease

Nunes, M. A., Viel, T. A., & Buck, H. S. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310010014 · Cited by 183

Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden

O’Leary, J. C., Li, Q., Marinec, P. S., Blair, L. J., Congdon, E. E., Johnson, A. G., Jinwal, U. K., Koren, J., Jones, J. R., Kraft, C., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-45 · Cited by 180

Curcumin‐Derived Pyrazoles and Isoxazoles: Swiss Army Knives or Blunt Tools for Alzheimer's Disease?

Narlawar, R., Pickhardt, M., Leuchtenberger, S., Baumann, K., Krause, S., Dyrks, T., Weggen, S., Mandelkow�, E., & Schmidt, B. (2007) · ChemMedChem · doi:10.1002/cmdc.200700218 · Cited by 177

The Cochaperone BAG2 Sweeps Paired Helical Filament- Insoluble Tau from the Microtubule

Carrettiero, D. C., Hernández, I., Neveu, P. A., Papagiannakopoulos, T. Y., & Kosik, K. S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4660-08.2009 · Cited by 175

Sequence and Structure Classification of Kinases

Cheek, S., Zhang, H., & Grishin, N. V. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00538-7 · Cited by 174

Nilotinib: A second-generation tyrosine kinase inhibitor for the treatment of chronic myelogenous leukemia

DeRemer, D. L., Ustun, C., & Natarajan, K. (2008) · Clinical Therapeutics · doi:10.1016/j.clinthera.2008.11.014 · Cited by 172

Clinical and biological effects of long-term lithium treatment in older adults with amnestic mild cognitive impairment: randomised clinical trial

Forlenza, O. V., Radanovic, M., Talib, L. L., & Gattaz, W. F. (2019) · British Journal of Psychiatry · doi:10.1192/bjp.2019.76 · Cited by 171

Protein-Capped Metal Nanoparticles Inhibit Tau Aggregation in Alzheimer’s Disease

Sonawane, S. K., Ahmad, A., & Chinnathambi, S. (2019) · ACS Omega · doi:10.1021/acsomega.9b01411 · Cited by 170

A phase Ib multiple ascending dose study of the safety, tolerability, and central nervous system availability of AZD0530 (saracatinib) in Alzheimer’s disease

Nygaard, H. B., Wagner, A. F., Bowen, G. S., Good, S. P., MacAvoy, M. G., Strittmatter, K. A., Kaufman, A. C., Rosenberg, B. J., Sekine-Konno, T., Varma, P., et al. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0119-0 · Cited by 168

Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice

Hastings, N. B., Wang, X., Song, L., Butts, B. D., Grotz, D., Hargreaves, R., Fred Hess, J., Hong, K.-L. K., Huang, C. R.-R., Hyde, L., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0181-0 · Cited by 164

Targeting Fyn Kinase in Alzheimer’s Disease

Nygaard, H. B. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.06.004 · Cited by 162

HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites

Dickey, C. A., Dunmore, J., Lu, B., Wang, J., Lee, W. C., Kamal, A., Burrows, F., Eckman, C., Hutton, M., & Petrucelli, L. (2006) · The FASEB Journal · doi:10.1096/fj.05-5343fje · Cited by 160

Rhodanine‐Based Tau Aggregation Inhibitors in Cell Models of Tauopathy

Bulic, B., Pickhardt, M., Khlistunova, I., Biernat, J., Mandelkow, E., Mandelkow�, E., & Waldmann, H. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200704051 · Cited by 158

Broad-spectrum caspase inhibitors: from myth to reality?

Chauvier, D., Ankri, S., Charriaut‐Marlangue, C., Casimir, R., & Jacotot, E. D. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402044 · Cited by 157

N‐Acetylgucosaminono‐1,5‐lactone oxime and the corresponding (phenylcarbamoyl)oxime

Horsch, M., Hoesch, L., Vasella, A. T., & Rast, D. M. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15976.x · Cited by 156

Why Pleiotropic Interventions are Needed for Alzheimer's Disease

Frautschy, S. A., & Cole, G. M. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8137-1 · Cited by 152

The history of Z-VAD-FMK, a tool for understanding the significance of caspase inhibition

Noorden, C. J. F. V. (2001) · Acta Histochemica · doi:10.1078/0065-1281-00601 · Cited by 152

An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons

Boselli, M. G., Lee, B., Robert, J., Prado, M. A., Min, S., Cheng, C., Silva, M. C., Seong, C., Elsasser, S., Hatle, K. M., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815126 · Cited by 151

SIRT1 Deacetylates Tau and Reduces Pathogenic Tau Spread in a Mouse Model of Tauopathy

Min, S., Sohn, P., Li, Y., Devidze, N., Johnson, J. R., Krogan, N. J., Masliah, E., Mok, S., Gestwicki, J. E., & Gan, L. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.2369-17.2018 · Cited by 151

Effect of AZD0530 on Cerebral Metabolic Decline in Alzheimer Disease

van Dyck, C. H., Nygaard, H. B., Chen, K., Donohue, M., Raman, R., Rissman, R. A., Brewer, J. B., Koeppe, R. A., Chow, T. W., Rafii, M. S., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2019.2050 · Cited by 150

Discovery of MK-8719, a Potent O-GlcNAcase Inhibitor as a Potential Treatment for Tauopathies

Selnick, H. G., Hess, J. F., Tang, C., Liu, K., Schachter, J. B., Ballard, J. E., Marcus, J., Klein, D. J., Wang, X., Pearson, M. S., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01090 · Cited by 144

Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation

Crowe, A., James, M. J., Lee, V. M.-Y., Smith, A. B., Trojanowski, J. Q., Ballatore, C., & Brunden, K. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.436006 · Cited by 143

An acetylation–phosphorylation switch that regulates tau aggregation propensity and function

Carlomagno, Y., Chung, D.-E. C., Yue, M., Castanedes-Casey, M., Madden, B. J., Dunmore, J., Tong, J., DeTure, M., Dickson, D. W., Petrucelli, L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.794602 · Cited by 143

High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK

Chang, L., Bertelsen, E. B., Wisén, S., Larsen, E. M., Zuiderweg, E. R. P., & Gestwicki, J. E. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.08.020 · Cited by 142

The structural requirements for ceramide activation of serine-threonine protein phosphatases

Chalfant, C. E., Szulc, Z. M., Roddy, P. L., Bielawska, A. E., & Hannun, Y. A. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m300347-jlr200 · Cited by 141

Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease

Mena, R., Edwards, P. C., Harrington, C. R., Mukaetova‐Ladinska, E. B., & Wischik, C. M. (1996) · Acta Neuropathologica · doi:10.1007/s004010050477 · Cited by 139

Does Lithium Protect Against Dementia

Dubovsky, S. L. (2008) · Journal watch · doi:10.1056/jp200812220000002 · Cited by 137

Synthesis and Initial Evaluation of YM-08, a Blood-Brain Barrier Permeable Derivative of the Heat Shock Protein 70 (Hsp70) Inhibitor MKT-077, Which Reduces Tau Levels

Miyata, Y., Li, X., Lee, H.-F., Jinwal, U. K., Srinivasan, S. R., Seguin, S. P., Young, Z. T., Brodsky, J. L., Dickey, C. A., Sun, D., et al. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn300210g · Cited by 135

Carnosic acid modulates Akt/IKK/NF-κB signaling by PP2A and induces intrinsic and extrinsic pathway mediated apoptosis in human prostate carcinoma PC-3 cells

Kar, S., Palit, S., Ball, W. B., & Das, P. K. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0715-4 · Cited by 130

Quantitative Decrease in Synaptophysin Message Expression and Increase in Cathepsin D Message Expression in Alzheimer Disease Neurons Containing Neurofibrillary Tangles

Callahan, L. M., Vaules, W. A., & Coleman, P. D. (1999) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199903000-00007 · Cited by 129

Increased O-GlcNAcylation reduces pathological tau without affecting its normal phosphorylation in a mouse model of tauopathy

Graham, D. L., Gray, A. J., Joyce, J. A., Yu, D., O’Moore, J., Carlson, G. A., Shearman, M. S., Dellovade, T., & Hering, H. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.11.025 · Cited by 129

Hsp90 activator Aha1 drives production of pathological tau aggregates

Shelton, L. B., Baker, J. D., Zheng, D., Sullivan, L. E., Solanki, P. K., Webster, J. M., Sun, Z., Sabbagh, J. J., Nordhues, B. A., Koren, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707039114 · Cited by 128

Nilotinib Effects on Safety, Tolerability, and Biomarkers in Alzheimer’s Disease

Turner, R. S., Hebron, M. L., Lawler, A., Mundel, E. E., Yusuf, N., Starr, J. N., Anjum, M., Pagan, F., Torres‐Yaghi, Y., Shi, W., et al. (2020) · Annals of Neurology · doi:10.1002/ana.25775 · Cited by 126

Apolipoprotein E and Peptide Mimetics Modulate Inflammation by Binding the SET Protein and Activating Protein Phosphatase 2A

Christensen, D. J., Ohkubo, N., Oddo, J., Van Kanegan, M. J., Neil, J., Li, F., Colton, C. A., & Vitek, M. P. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002847 · Cited by 125

Involvement of in the abnormal hyperphosphorylation of tau and its reversal by Memantine

Chohan, M. O., Khatoon, S., Iqbal, I.-G., & Iqbal, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.06.021 · Cited by 124

Versatility of the Curcumin Scaffold: Discovery of Potent and Balanced Dual BACE-1 and GSK-3β Inhibitors

Martino, R. M. C. D., Simone, A. D., Andrisano, V., Bisignano, P., Bisi, A., Gobbi, S., Rampa, A., Fato, R., Bergamini, C., Pérez, D. I., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00894 · Cited by 124

Acetylation changes tau interactome to degrade tau in Alzheimer’s disease animal and organoid models

Choi, H., Kim, H. J., Yang, J., Chae, S., Lee, W., Chung, S., Kim, J., Choi, H., Song, H., Lee, C. K., et al. (2019) · Aging Cell · doi:10.1111/acel.13081 · Cited by 124

Minocycline reduces the development of abnormal tau species in models of Alzheimer's disease

Noble, W., Garwood, C., Stephenson, J., Kinsey, A. M., Hanger, D., & Anderton, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-113795 · Cited by 123

Dual modification of Alzheimer’s disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach

Thomas, S. N., Funk, K. E., Wan, Y., Liao, Z., Davies, P., Kuret, J., & Yang, A. J. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0893-0 · Cited by 123

Temsirolimus attenuates tauopathy in vitro and in vivo by targeting tau hyperphosphorylation and autophagic clearance

Jiang, T., Yu, J., Zhu, X., Zhang, Q.-Q., Cao, L., Wang, H.-F., Tan, M., Gao, Q., Qin, H., Zhang, Y., et al. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.05.032 · Cited by 118

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 116

Interaction of Cinnamaldehyde and Epicatechin with Tau: Implications of Beneficial Effects in Modulating Alzheimer's Disease Pathogenesis

George, R. C., Lew, J., & Graves, D. J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122113 · Cited by 114

Differential Effects of an O-GlcNAcase Inhibitor on Tau Phosphorylation

Yu, Y., Zhang, L., Li, X., Run, X., Liang, Z., Li, Y., Liu, Y., Lee, M. H., Grundke, I., Iqbal, K., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035277 · Cited by 113

Allosteric Heat Shock Protein 70 Inhibitors Rapidly Rescue Synaptic Plasticity Deficits by Reducing Aberrant Tau

Abisambra, J. F., Jinwal, U. K., Miyata, Y., Rogers, J. T., Blair, L. J., Li, X., Seguin, S. P., Wang, L., Jin, Y. L., Bacon, J. A., et al. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2013.02.027 · Cited by 110

Supranutritional Sodium Selenate Supplementation Delivers Selenium to the Central Nervous System: Results from a Randomized Controlled Pilot Trial in Alzheimer's Disease

Cardoso, B. R., Roberts, B. R., Malpas, C. B., Vivash, L. E., Genc, S., Saling, M. M., Desmond, P. M., Steward, C. E., Hicks, R. J., Callahan, J., et al. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0662-z · Cited by 110

Ligand-Dependent Inhibition and Reversal of Tau Filament Formation

Chirita, C. N., Necula, M., & Kuret, J. (2004) · Biochemistry · doi:10.1021/bi036094h · Cited by 104

Human High Temperature Requirement Serine Protease A1 (HTRA1) Degrades Tau Protein Aggregates

Tennstaedt, A., Poepsel, S., Truebestein, L., Hauske, P., Brockmann, A., Schmidt, N., Irle, I., Saccà, B., Niemeyer, C. M., Brandt, R., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316232 · Cited by 104

A First-in-Class Small-Molecule that Acts as a Dual Inhibitor of HDAC and PDE5 and that Rescues Hippocampal Synaptic Impairment in Alzheimer’s Disease Mice

Cuadrado‐Tejedor, M., García, C., Sánchez-Arias, J. A., Rabal, O., Pérez-González, M., Mederos, S., Ugarte, A., Franco, R., Segura, V., Perea, G., et al. (2016) · Neuropsychopharmacology · doi:10.1038/npp.2016.163 · Cited by 104

Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment

Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103

Small Molecule Enhancement of 20S Proteasome Activity Targets Intrinsically Disordered Proteins

Jones, C. L., Njomen, E., Sjögren, B., Dexheimer, T. S., & Tepe, J. J. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00489 · Cited by 100

Lithium and dementia: A preliminary study

Terao, T., Nakano, H., Inoue, Y., Okamoto, T., Nakamura, J., & Iwata, N. (2006) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2006.04.020 · Cited by 98

A farnesyltransferase inhibitor activates lysosomes and reduces tau pathology in mice with tauopathy

Hernández, I., Luna, G., Rauch, J. N., Reis, S. A., Giroux, M., Karch, C. M. M., Boctor, D., Sibih, Y., Storm, N. J., Díaz, A., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat3005 · Cited by 95

SUMO and Alzheimer’s Disease

Lee, L., Sakurai, M., Matsuzaki, S., Arancio, O., & Fraser, P. E. (2013) · NeuroMolecular Medicine · doi:10.1007/s12017-013-8257-7 · Cited by 94

Does Lithium Therapy Protect Against the Onset of Dementia?

Dunn, N., Holmes, C., & Mullee, M. (2005) · Alzheimer Disease & Associated Disorders · doi:10.1097/01.wad.0000155068.23937.9b · Cited by 94

Lithium treatment and risk for dementia in adults with bipolar disorder: Population-based cohort study

Gerhard, T., Devanand, D. P., Huang, C., Crystal, S., & Olfson, M. (2015) · British Journal of Psychiatry · doi:10.1192/bjp.bp.114.154047 · Cited by 94

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Tell, V., & Hilgeroth, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00189 · Cited by 92

Resveratrol induces dephosphorylation of Tau by interfering with the MID1-PP2A complex

Schweiger, S., Matthes, F., Posey, K. L., Kickstein, E., Weber, S. S., Hettich, M. M., Pfurtscheller, S., Ehninger, D., Schneider, R., & Krauß, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-12974-4 · Cited by 92

Effects of cilostazol on cognition and regional cerebral blood flow in patients with Alzheimer's disease and cerebrovascular disease: A pilot study

Sakurai, H., Hanyu, H., Sato, T., Kume, K., Hirao, K., Kanetaka, H., & Iwamoto, T. (2012) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/j.1447-0594.2012.00866.x · Cited by 91

Cyanine Dye N744 Inhibits Tau Fibrillization by Blocking Filament Extension: Implications for the Treatment of Tauopathic Neurodegenerative Diseases

Necula, M., Chirita, C. N., & Kuret, J. (2005) · Biochemistry · doi:10.1021/bi050387o · Cited by 91

cGMP via PKG activates 26S proteasomes and enhances degradation of proteins, including ones that cause neurodegenerative diseases

VerPlank, J. J. S., Tyrkalska, S. D., Fleming, A., Rubinsztein, D. C., & Goldberg, A. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003277117 · Cited by 91

CIP2A Causes Tau/APP Phosphorylation, Synaptopathy, and Memory Deficits in Alzheimer’s Disease

Shentu, Y.-P., Huo, Y., Feng, X.-L., Gilbert, J., Zhang, Q., Liuyang, Z.-Y., Wang, X.-L., Wang, G., Zhou, H., Wang, X.-C., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.009 · Cited by 90

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Dolai, S., Shi, W., Corbo, C. P., Sun, C., Averick, S. E., Obeysekera, D., Farid, M., Alonso, A. D. C., Banerjee, P., & Raja, K. S. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200088r · Cited by 88

Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: Implications of autophagy promotion

Shimada, K., Motoi, Y., Ishiguro, K., Kambe, T., Matsumoto, S., Itaya, M., Kunichika, M., Mori, H., Shinohara, A., Chiba, M., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.050 · Cited by 87

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Young, Z. T., Rauch, J. N., Assimon, V. A., Jinwal, U. K., Ahn, M., Li, X., Dunyak, B. M., Ahmad, A., Carlson, G. A., Srinivasan, S. R., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.04.014 · Cited by 85

Design and synthesis of curcumin derivatives as tau and amyloid β dual aggregation inhibitors

Okuda, M., Hijikuro, I., Fujita, Y., Teruya, T., Kawakami, H., Takahashi, T., & Sugimoto, H. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.08.092 · Cited by 85

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Vitek, M. P., Christensen, D. J., Wilcock, D. M., Davis, J., Nostrand, W. E. V., Li, F. Q., & Colton, C. A. (2012) · Neurodegenerative Diseases · doi:10.1159/000334914 · Cited by 84

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Ryan, P., Xu, M., Davey, A. K., Danon, J. J., Mellick, G. D., Kassiou, M., & Rudrawar, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00143 · Cited by 84

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Kargbo, R. B. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00083 · Cited by 82

Sulforaphane Upregulates the Heat Shock Protein Co‐Chaperone CHIP and Clears Amyloid‐β and Tau in a Mouse Model of Alzheimer's Disease

Lee, S., Choi, B., Kim, J., LaFerla, F. M., Park, J. H. Y., Han, J., Lee, K. W., & Kim, J. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201800240 · Cited by 80

Natural products and their derivatives as multifunctional ligands against Alzheimer's disease

Patil, P., Thakur, A., Sharma, A., & Flora, S. J. S. (2019) · Drug Development Research · doi:10.1002/ddr.21587 · Cited by 80

Synthesis, Inhibitory Activity of Cholinesterases, and Neuroprotective Profile of Novel 1,8-Naphthyridine Derivatives

Rı́os, C. D. L., Egea, J., Marco, J. L., Leon, R. M., Samadi, A., Iriepa, I., Moraleda, I., Galvez‐Ruano, E., Garcı́a, A. G., López, M. G., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901902w · Cited by 79

Elevation of Global O-GlcNAc in Rodents Using a Selective O-GlcNAcase Inhibitor Does Not Cause Insulin Resistance or Perturb Glucohomeostasis

Macauley, M. S., Shan, X., Yuzwa, S. A., Gloster, T. M., & Vocadlo, D. J. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.07.005 · Cited by 78

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Fajardo, V. A., Fajardo, V. A., LeBlanc, P. J., & MacPherson, R. E. K. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170744 · Cited by 78

Nanoparticle-mediated approaches for Alzheimer’s disease pathogenesis, diagnosis, and therapeutics

Hettiarachchi, S. D., Zhou, Y., Seven, E. S., Lakshmana, M. K., Kaushik, A. K., Chand, H. S., & Leblanc, R. M. (2019) · Journal of Controlled Release · doi:10.1016/j.jconrel.2019.10.034 · Cited by 77

Small Molecule Modulation of Proteasome Assembly

Njomen, E., Osmulski, P. A., Jones, C. L., Gaczynska, M. E., & Tepe, J. J. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00579 · Cited by 76

Curcumin intervention for cognitive function in different types of people: A systematic review and meta-analysis

Zhu, L., Mei, X., Zhang, Z., Xie, Y., & Lang, F. (2019) · Phytotherapy Research · doi:10.1002/ptr.6257 · Cited by 76

Sildenafil for the Treatment of Alzheimer’s Disease: A Systematic Review

Sanders, O. D. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200166 · Cited by 76

Are NSAIDs useful to treat Alzheimer’s disease or mild cognitive impairment

Imbimbo (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00019 · Cited by 75

Cilostazol Add-On Therapy in Patients with Mild Dementia Receiving Donepezil: A Retrospective Study

Ihara, M., Nishino, M., Taguchi, A., Yamamoto, Y., Hattori, Y., Saitô, S., Takahashi, Y., Tsuji, M., Kasahara, Y., Takata, Y., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089516 · Cited by 75

A Phase IIa Randomized Control Trial of VEL015 (Sodium Selenate) in Mild-Moderate Alzheimer’s Disease

Malpas, C. B., Vivash, L. E., Genc, S., Saling, M. M., Desmond, P. M., Steward, C. E., Hicks, R. J., Callahan, J., Brodtmann, A. G., Collins, S. J., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160544 · Cited by 75

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Ling, Y., Hao, Z., Liang, D., Zhang, C., Liu, Y., & Wang, Y. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s329547 · Cited by 428

Challenges and hopes for Alzheimer’s disease

Tatulian, S. A. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.01.016 · Cited by 291

The SARS‐CoV‐2 main protease (M pro ): Structure, function, and emerging therapies for COVID‐19

Hu, Q., Xiong, Y., Zhu, G., Zhang, Y., Zhang, Y., Huang, P. C., & Ge, G. (2022) · MedComm · doi:10.1002/mco2.151 · Cited by 270

Dysfunctional Glucose Metabolism in Alzheimer’s Disease Onset and Potential Pharmacological Interventions

Kumar, V., Kim, S.-H., & Bishayee, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179540 · Cited by 116

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Fišar, Z. (2022) · Biomolecules · doi:10.3390/biom12111676 · Cited by 113

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Sahu, K. K., Chaudhary, R., Farooqi, M. A., & Kaurav, M. (2024) · Drug Delivery Letters · doi:10.2174/0122103031331346241122152643 · Cited by 1

Development of tau-directed Small Molecule Modulators for Alzheimer’s Disease: a Recent Patent Review (2014–2018)

Lee, H. E., Lim, D., Lee, J. Y., Lim, S. M., & Pae, A. N. (2019) · Pharmaceutical Patent Analyst · doi:10.4155/ppa-2019-0003 · Cited by 11

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Jurcău, A., & Nunkoo, V. S. (2021) · Frontiers in clinical drug research. Dementia · doi:10.2174/9789815039474121020004 · Cited by 6

Chapter 17. Tau-targeting Therapeutic Strategies for Alzheimer's Disease

Gopinath, P., Ramesh, M., & Govindaraju, T. (2022) · Royal Society of Chemistry eBooks · doi:10.1039/9781839162732-00487 · Cited by 3

Tau-Directed Therapies for Alzheimer’s Disease and Other Tauopathies

(2013) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608057221113010006