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Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
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Neuronal inclusions comprised of the microtubule-associated protein tau are found in numerous neurodegenerative diseases, commonly known as tauopathies. In Alzheimer's disease - the most prevalent tauopathy - misfolded tau is probably a key pathological agent. The recent failure of amyloid-beta-targeted therapeutics in Phase III clinical trials suggests that it is timely and prudent to consider alternative drug discovery strategies for Alzheimer's disease. Here, we focus on strategies directed at reducing misfolded tau and compensating for the loss of normal tau function.
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“For example, reduced tau O-glycosylation could lead to increased phosphorylation, while the enhancement of O-glycosylation reduces the extent of tau phosphorylation [43–45].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [44]
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Cites
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
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
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
Self-citationTau-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
Self-citationBuée, 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
Flagged first, then by citations
Research works printed but not linked: 3
- Avila, J. Tau and tauopathies: tau phosphorylation and tau assembly. FEBS J. 273, 23 (2006).
- Alonso, A. D., GrundkeIqbal, I. & Iqbal, K. Abnormally phosphorylated tau from Alzheimer disease brain depolymerizes microtubules. Neurobiol. Aging 15, S37 (1994).
- Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E. & Mandelkow, E. M. Phosphorylation that detaches tau from microtubules S262 and S214 protects it against aggregation into Alzheimer paired helical filaments. J. Neurochem. 73, S26 (1999).
Cited by
Sorted by citations
Items 201–300 of 458
Yu, M., Risacher, S. L., Nho, K. T., Wen, Q., Oblak, A. L., Unverzagt, F. W., Apostolova, L. G., Farlow, M. R., Brosch, J. R., Clark, D. G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113691 · Cited by 36
Chen, P. C., Gaisina, I. N., El‐Khodor, B. F., Ramboz, S., Makhortova, N. R., Rubin, L. L., & Kozikowski, A. P. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200085z · Cited by 34
Hori, T., Eguchi, K., Wang, H.-Y., Miyasaka, T., Guillaud, L., Taoufiq, Z., Mahapatra, S., Yamada, H., Takei, K., & Takahashi, T. (2022) · eLife · doi:10.7554/elife.73542 · Cited by 34
Tolfenamic acid reduces tau and CDK 5 levels: implications for dementia and tauopathies
Adwan, L. I., Subaiea, G. M., Basha, R. M., & Zawia, N. H. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12960 · Cited by 34
Liquid-liquid phase separation in Alzheimer’s disease
Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33
Medina, M., & Ávila, J. (2013) · Expert Review of Neurotherapeutics · doi:10.1586/ern.13.39 · Cited by 33
Ballatore, C., Crowe, A., Piscitelli, F., James, M., Lou, K., Rossidivito, G., Yao, Y., Trojanowski, J. Q., Lee, V. M. ‐., Brunden, K. R., et al. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.05.027 · Cited by 32
Self-citationFrontiers in Alzheimer’s disease therapeutics
Stone, J. G., Casadesús, G., Rothenberg, K. G., Siedlak, S. L., Wang, X., Zhu, X., Perry, G. L., Castellani, R. J., & Smith, M. A. (2010) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622310382817 · Cited by 32
Mechanistic Insights into Selective Autophagy Subtypes in Alzheimer’s Disease
Guan, X., Iyaswamy, A., Sreenivasmurthy, S. G., Su, C.-F., Zhu, Z., Liu, J., Kan, Y., Cheung, K., Lu, J., Tan, J., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073609 · Cited by 32
Alzheimer’s Disease: Lessons Learned from Amyloidocentric Clinical Trials
Soejitno, A., Tjan, A., & Purwata, T. E. (2015) · CNS Drugs · doi:10.1007/s40263-015-0257-8 · Cited by 32
Fukunaga, K., Sakai, D., Watanabe, K., Nakayama, K., Kohara, T., Tanaka, H., Sunada, S., Nabeno, M., Okamoto, M., Saito, K.-I., et al. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.01.005 · Cited by 32
Wilmes, A., O’Sullivan, D., Chan, A. H. L., Chandrahasen, C., Paterson, I., Northcote, P. T., Flamme, A. C. L., & Miller, J. H. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-010-1461-3 · Cited by 32
Fukushima, T., Nakamura, A., Iwakami, N., Nakada, Y., Hattori, H., Hoki, S., Yamaguchi, H., Nakagawa, M., Terashima, N., & Narita, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.091 · Cited by 31
Rüb, U., Stratmann, K., Heinsen, H., Seidel, K., Bouzrou, M., & Korf, H. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161102 · Cited by 31
Nikkel, A. L., Martino, B. R., Markosyan, S., Brederson, J., Medeiros, R., Möller, A., & Bitner, R. S. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.05.011 · Cited by 30
Potential synergy between tau aggregation inhibitors and tau chaperone modulators
Blair, L. J., Zhang, B., & Dickey, C. A. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt207 · Cited by 30
Qin, X., Wang, Y., & Paudel, H. K. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.04.018 · Cited by 29
Krinke, D., Jahnke, H., Mack, T. G. A., Hirche, A., Striggow, F., & Robitzki, A. A. (2010) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2010.06.002 · Cited by 29
Meng, L., Li, B., Li, D.-N., Wang, Y., Lin, Y., Meng, X., Sun, X., & Liu, N. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.09.025 · Cited by 28
Alginate-Derived Mannuronate Oligosaccharide Attenuates Tauopathy through Enhancing Autophagy
Bi, D., Xiao, S., Lin, Z., Yao, L., Fang, W., Wu, Y. L., Xu, H. Y., Lu, J., & Xu, X. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c00394 · Cited by 28
Effects of Deferasirox in Alzheimer’s Disease and Tauopathy Animal Models
Kwan, P., Ho, A. S.-W., & Baum, L. (2022) · Biomolecules · doi:10.3390/biom12030365 · Cited by 28
Salcedo‐Tello, P., Hernández‐Ortega, K., & Arias, C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130749 · Cited by 28
The Structure Biology of Tau and Clue for Aggregation Inhibitor Design
Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 27
Lipids and lipoproteins may play a role in the neuropathology of Alzheimer’s disease
Akyol, Ö., Akyol, S., Chou, M., Chen, S., Liu, C., Selek, S., Soares, J. C., & Chen, C. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1275932 · Cited by 27
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Sui, D., Liu, M., & Kuo, M. (2015) · Journal of Visualized Experiments · doi:10.3791/51537 · Cited by 28
Current Therapies and New Strategies for the Management of Alzheimer’s Disease
Aderinwale, O. G., Ernst, H. W., & Mousa, S. A. (2010) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317510372372 · Cited by 27
Froestl, W., Pfeifer, A., & Muhs, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121729 · Cited by 27
Protective Effects of Hydroxysafflor Yellow A on β-Amyloid-Induced Neurotoxicity in PC12 Cells
Kong, S., Xian, Y., Ip, S., Lai, X., Shi, X., Lin, Z., & Su, Z. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1002-7 · Cited by 26
Small molecule targeting of RNA structures in neurological disorders
Angelbello, A. J., Chen, J. L., & Disney, M. D. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14051 · Cited by 26
The Cellular Distribution and Ser262 Phosphorylation of Tau Protein Are Regulated by BDNF In Vitro
Chen, Q., Zhou, Z., Zhang, L., Xu, S., Chen, C., & Yu, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091793 · Cited by 26
Ferri, E., Arosio, B., D’Addario, C., Galimberti, D., Gussago, C., Pucci, M., Casati, M., Fenoglio, C., Abbate, C., Rossi, P. D., et al. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.02.004 · Cited by 26
Rational design of potent GSK3β inhibitors with selectivity for Cdk1 and Cdk2
Lesuisse, D., Dutruc-Rosset, G., Tiraboschi, G., Dreyer, M., Maignan, S., Chevalier, A., Halley, F., Bertrand, P., Burgevin, M., Quarteronet, D., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.114 · Cited by 26
Ng, P. Y., Chang, I. S., Koh, R. Y., & Chye, S. M. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00591-6 · Cited by 25
Li, S., Li, W., Wu, X., Li, J., Yang, J., Tu, C., Ye, X., & Ling, S. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.03.006 · Cited by 25
Martin, M. D., Calcul, L., Smith, C., Jinwal, U. K., Fontaine, S. N., Darling, A. L., Seeley, K. W., Wojtas, Ł., Narayan, M., Gestwicki, J. E., et al. (2015) · ACS Chemical Biology · doi:10.1021/cb501013w · Cited by 25
Identification of new BACE1 inhibitors for treating Alzheimer’s disease
Kushwaha, P., Singh, V., Somvanshi, P., Bhardwaj, T., Barreto, G. E., Ashraf, G. M., Mishra, B. N., Chundawat, R. S., & Haque, S. (2021) · Journal of Molecular Modeling · doi:10.1007/s00894-021-04679-3 · Cited by 24
Cerebrospinal fluid and blood biomarkers in the diagnostic assays of Alzheimer’s disease
Zhang, L., Liang, X., Zhang, Z., & Luo, H. (2021) · Journal of Innovative Optical Health Sciences · doi:10.1142/s1793545822300014 · Cited by 24
Demencia frontotemporal variante conductual: aproximación clínica y terapéutica
Fernández‐Matarrubia, M., Matías‐Guiu, J. A., Moreno‐Ramos, T., & Matías‐Guiu, J. (2013) · Neurología · doi:10.1016/j.nrl.2013.03.001 · Cited by 24
Fedotova, J., Soultanov, V., Nikitina, T. V., Roschin, V., & Ordayn, N. (2012) · Phytomedicine · doi:10.1016/j.phymed.2011.09.073 · Cited by 24
Ghosal, K., Fan, Q., Dawson, H. N., & Pimplikar, S. W. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159435 · Cited by 24
Giguère, F. S.-C., Essis, S. A., Chagniel, L., Germain, M., Cyr, M., & Massicotte, G. (2017) · Brain Research · doi:10.1016/j.brainres.2017.01.014 · Cited by 24
Anderson, A. M. L., Croteau, D. J., Ellis, R. J., Cookson, D. R., Potter, M., Guillemin, G. J., Brew, B. J., Woods, S. P., & Letendre, S. L. (2018) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2018.03.007 · Cited by 24
Shemesh, O. A., & Spira, M. E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0689-7 · Cited by 24
Cellular Uptake of Mildly Oxidized Nanographene for Drug-Delivery Applications
Mugnano, M., Lama, G. C., Castaldo, R., Marchesano, V., Merola, F., del Giudice, D., Calabuig, A., Gentile, G., Ambrogi, V., Cerruti, P., et al. (2019) · ACS Applied Nano Materials · doi:10.1021/acsanm.9b02035 · Cited by 23
Crowe, A., Henderson, M. J., Anderson, J. D., Titus, S. A., Zakharov, A. V., Simeonov, A. M., Buist, A., Delay, C., Moechars, D., Trojanowski, J. Q., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010532 · Cited by 23
Self-citationTau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23
Job, N., Thimmakondu, V. S., & Thirumoorthy, K. (2023) · Molecules · doi:10.3390/molecules28031388 · Cited by 23
Modulation of biomolecular phase behavior by metal ions
Sołtys, K., Tarczewska, A., & Bystranowska, D. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119567 · Cited by 23
Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism
Haslbeck, V., Drazic, A., Eckl, J. M., Alte, F., Helmuth, M., Popowicz, G. M., Schmidt, W., Braun, F., Weiwad, M., Fischer, G. S., et al. (2015) · Bioscience Reports · doi:10.1042/bsr20150042 · Cited by 23
Martin, M. D., Baker, J. D., Suntharalingam, A., Nordhues, B. A., Shelton, L. B., Zheng, D., Sabbagh, J. J., Haystead, T., Gestwicki, J. E., & Dickey, C. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00223 · Cited by 23
Zang, X., Cheng, Z.-Y., Sun, Y., Hua, N., Zhu, L.-H., & He, L. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.09.017 · Cited by 23
Sarkar, S., Bhui, U., Kumar, B., Ashique, S., Kumar, P., Sharma, H., Bhowmick, M., Pal, R., & Kumar, T. (2024) · Current Psychiatry Research and Reviews · doi:10.2174/0126660822329981241007105405 · Cited by 25
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Ishikawa, M., Yoshitomi, T., Covey, D. F., Zorumski, C. F., & Izumi, Y. (2018) · Neuropsychiatry · doi:10.4172/neuropsychiatry.1000356 · Cited by 22
Rescue of tau-induced synaptic transmission pathology by paclitaxel
Erez, H., Shemesh, O. A., & Spira, M. E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00034 · Cited by 22
Fisher, E., Zhao, Y., Richardson, R., Janik, M. A., Buell, A. K., Aigbirhio, F. I., & Tóth, G. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00228 · Cited by 22
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Chang, J. K., Leso, A., Subaiea, G. M., Lahouel, A., Masoud, A. M., Mushtaq, F., Deeb, R., Eid, A., Dash, M. E., Bihaqi, S. W., et al. (2018) · Current Alzheimer Research · doi:10.2174/1567205015666180119104036 · Cited by 22
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González-Quevedo, A. (2012) · InTech eBooks · doi:10.5772/2174 · Cited by 21
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Cummings, J. L., & Zhong, K. (2013) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2013.205 · Cited by 21
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Li, T., & Paudel, H. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160635 · Cited by 21
Tubulin modifying enzymes as target for the treatment of tau-related diseases
Rogowski, K., Hached, K., Crozet, C., & van der Laan, S. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107681 · Cited by 21
Apostolakou, A. E., Sula, X. K., Nastou, K. C., Nasi, G. I., & Iconomidou, V. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-83892-9 · Cited by 21
Zhao, H., Huang, X., & Tong, Z. (2021) · ChemMedChem · doi:10.1002/cmdc.202100428 · Cited by 21
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Prior, M., Shi, Q., Hu, X., He, W., Levey, A. I., & Yan, R. (2010) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2010.01.017 · Cited by 21
Kubota, H., Kunisawa, K., Wulaer, B., Hasegawa, M., Kurahashi, H., Sakata, T., Tezuka, H., Kugita, M., Nagao, S., Nagai, T., et al. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16093 · Cited by 20
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Inda, C., Bolaender, A., Wang, T., Gandu, S. R., & Koren, J. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160413141350 · Cited by 20
Savonenko, A. V., Melnikova, T., Li, T., Price, D. L., & Wong, P. C. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-398270-4.00021-5 · Cited by 20
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Shao, H., Li, X., Hayashi, S., Bertron, J. L., Schwarz, D. M. C., Tang, B. C., & Gestwicki, J. E. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128025 · Cited by 20
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Zamani, F., & Suzuki, T. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00154 · Cited by 20
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Zhao, Z., Zhou, H., Peng, Y., Qiu, C. H., Sun, Q. Y., Wang, F., & Xie, H. N. (2014) · Genetics and Molecular Research · doi:10.4238/2014.october.20.19 · Cited by 19
Bar, S., Wilson, K. A., Hilsabeck, T. A. U., Alderfer, S. A., Dammer, E. B., Burton, J. B., Shah, S., Holtz, A. N., Carrera, E. M., Beck, J. N., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01314-w · Cited by 20
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Boxer, A. L., & Tsai, R. M. (2014) · Seminars in Neurology · doi:10.1055/s-0034-1381739 · Cited by 19
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Rogers, B. S., & Lippa, C. F. (2012) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317512444000 · Cited by 19
Trojanowski, J. Q., Arnold, S. E., Karlawish, J. H., Naylor, M. D., Brunden, K. R., & Lee, V. M. ‐. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.08.005 · Cited by 19
Self-citationFang, G., Shi, B., Wu, K., Chen, S., Gao, X., Xiao, S., Kang, J. X., Li, W., & Huang, R. (2018) · International Journal of Neuroscience · doi:10.1080/00207454.2018.1533824 · Cited by 19
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Zhu, R., Makwana, K. M., Zhang, Y., Rajewski, B. H., Valle, J. R. D., & Wang, Y. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb00850a · Cited by 18
Miller, J. H., & Das, V. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200621171302 · Cited by 18
Nguyen, T. T., Vo, T. K., & Vo, G. V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-55035-6_13 · Cited by 18
Chen, J. L., Moss, W. N., Spencer, A., Zhang, P., Childs‐Disney, J. L., & Disney, M. D. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219210 · Cited by 18
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Shimojo, M., Ono, M., Takuwa, H., Mimura, K., Nagai, Y., Fujinaga, M., Kikuchi, T., Okada, M., Seki, C., Tokunaga, M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021107757 · Cited by 18
Killick, R., Hughes, T. R., Morgan, B. P., & Lovestone, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2012.11.008 · Cited by 17
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Kumar, S., Saha, S., Singh, K., Singh, T., Miahra, A. K., Dubey, B. N., & Singh, S. (2024) · Current Functional Foods · doi:10.2174/0126668629269256231222092721 · Cited by 17
Li, H., & Wu, W. (2017) · European Journal of Neuroscience · doi:10.1111/ejn.13585 · Cited by 17
Cortés, N., Sabogal-Guáqueta, A. M., Cardona‐Gómez, G. P., & Osorio, E. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.013 · Cited by 17
Ke, Y. D., Chan, G., Stefanoska, K., Au, C. G., Bi, M., Müller, J., Przybyla, M., Feiten, A., Prikas, E., Halliday, G. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005263 · Cited by 16
Amyloid beta peptide-degrading microbial enzymes and its implication in drug design
Dhanavade, M. J., & Sonawane, K. D. (2020) · 3 Biotech · doi:10.1007/s13205-020-02240-2 · Cited by 16
ELISA Evaluation of Tau Accumulation in the Brains of Patients with Alzheimer Disease
Shinohara, M., Hirokawa, J., Shimodaira, A., Tashiro, Y., Suzuki, K., Gheni, G., Fukumori, A., Matsubara, T., Morishima, M., Saito, Y., et al. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab047 · Cited by 16
Plum, S., Steinbach, S., Abel, L., Marcus, K., Helling, S., & May, C. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400030 · Cited by 16
Dayton, R. D., Wang, D. B., Cain, C. D., Schrott, L. M., Ramirez, J. J., King, M. A., & Klein, R. L. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.12.002 · Cited by 16
New insights on Alzheimer's disease diagnostic.
Fita, I. G., Enciu, A., & Stănoiu, B. (2011) · PubMed · Cited by 16
Pathology of Neurodegenerative Diseases
Kim, Y. S., Kim, Y.-K., Hwang, O., & Dong, J. (2012) · InTech eBooks · doi:10.5772/38028 · Cited by 16
Insights into tau function and dysfunction through single-molecule fluorescence
Melo, A. M., Elbaum‐Garfinkle, S., & Rhoades, E. R. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.010 · Cited by 15
Laronze‐Cochard, M., Cochard, F., Daras, E., Lansiaux, A., Brassart, B., Vanquelef, E., Prost, É., Nuzillard, J., Baldeyrou, B., Goosens, J. F., et al. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00149j · Cited by 15
A critical overview of therapeutic strategy and advancement for Alzheimer's disease treatment
Kuo, Y., & Rajesh, R. (2017) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2017.05.011 · Cited by 15
Borgen, M. A., Giles, A. C., Wang, D., & Grill, B. J. (2019) · eLife · doi:10.7554/elife.44040 · Cited by 15
Birol, M., & Melo, A. M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00309 · Cited by 15
Soltan, O. M., Abdelrahman, K. S., Bass, A. K. A., Takizawa, K., Narumi, A., & Konno, H. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107651 · Cited by 14
Protective role of 6-Hydroxy-1-H-Indazole in an MPTP-induced mouse model of Parkinson's disease
Liang, X., Wen-ting, Z., Xu, Y., Chong-Fa, L., Lu, Z., Jin-jun, R., & Wang, W. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.08.011 · Cited by 14
Nakhjiri, E., Vafaee, M. S., Hojjati, S. M. M., Shahabi, P., & Shahpasand, K. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02061-7 · Cited by 14
Hajipour, M. J., Mohammad‐Beigi, H., Nabipour, I., Mahmoudi, N., Azhdarzadeh, M., Derakhshankhah, H., Dawud, D. E., Mohammadinejad, R., & Otzen, D. E. (2020) · Nano Today · doi:10.1016/j.nantod.2020.100983 · Cited by 14
Park, S. S., Jung, H., Kim, Y., Park, T. K., Kim, C., Choi, H., Mook‐Jung, I. H., Koo, E. H., & Park, S. A. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12032 · Cited by 14
Metadata
- Authors
- Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Brunden, Kurt R.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2009-10
- Volume
- 8
- Issue
- 10
- Pages
- 783-793
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- PMC
- PMC2787232
- OpenAlex
- W2021370614
- Cited by
- 440
- References
- 140
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 20 · 2023: 12 · 2022: 17 · 2021: 31 · 2020: 28 · 2019: 23 · 2018: 22 · 2017: 30 · 2016: 30 · 2015: 22 · 2014: 40 · 2013: 31 · 2012: 43
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Drug Discovery (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5u01ag024904-10)
- National Institute on Aging (U01-AG-024904, P01AG014382, P01 AG11542, P01-AG09215, P30AG10124, P01AG011542, P01 AG-17586, P01AG014449, P01 AG14382, P30AG010124, P01AG009215, P01AG017586, P01 AG14449, UO1 AG24904, U19AG010483, P01-AG19724, P01AG019724)
- National Institute of Neurological Disorders and Stroke (P01NS044233)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, tauopathy, Alzheimer's disease, tau misfolding, neurodegeneration, tau functions, microtubule-associated proteins
- MeSH terms
- Alzheimer Disease, Animals, Humans, tau Proteins, Tauopathies, Drug Discovery
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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