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The Microtubule-Stabilizing Agent, Epothilone D, Reduces Axonal Dysfunction, Neurotoxicity, Cognitive Deficits, and Alzheimer-Like Pathology in an Interventional Study with Aged Tau Transgenic Mice
Open accessAbstract
Neurodegenerative tauopathies, such as Alzheimer's disease (AD), are characterized by insoluble deposits of hyperphosphorylated tau protein within brain neurons. Increased phosphorylation and decreased solubility has been proposed to diminish normal tau stabilization of microtubules (MTs), thereby leading to neuronal dysfunction. Earlier studies have provided evidence that small molecule MT-stabilizing drugs that are used in the treatment of cancer may have utility in the treatment of tauopathies. However, it has not been established whether treatment with a small molecule MT-stabilizing compound will provide benefit in a transgenic model with pre-existing tau pathology, as would be seen in human patients with clinical symptoms. Accordingly, we describe here an interventional study of the brain-penetrant MT-stabilizing agent, epothilone D (EpoD), in aged PS19 mice with existing tau pathology and related behavioral deficits. EpoD treatment reduced axonal dystrophy and increased axonal MT density in the aged PS19 mice, which led to improved fast axonal transport and cognitive performance. Moreover, the EpoD-treated PS19 mice had less forebrain tau pathology and increased hippocampal neuronal integrity, with no dose-limiting side effects. These data reveal that brain-penetrant MT-stabilizing drugs hold promise for the treatment of AD and related tauopathies, and that EpoD could be a candidate for clinical testing.
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“Although tau aggregates are hallmarks of AD, several studies have suggested that oligomeric tau in soluble forms may be the most potent neurotoxic form 68–73.”
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Cites
Random-Effects Models for Longitudinal Data
Laird, N. M., & Ware, J. H. (1982) · Biometrics · doi:10.2307/2529876 · Cited by 8,923
Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade
Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806
Self-citationAssociation of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Self-citationNeurofibrillary 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
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-citationSynapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
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-citationGenome-wide association study reveals genetic risk underlying Parkinson's disease
Simón-Sánchez, J., Schulte, C., Bras, J. M., Sharma, M., Gibbs, J. R., Berg, D., Paisan-Ruiz, C., Lichtner, P., Scholz, S. W., Hernandez, D. G., et al. (2009) · Nature Genetics · doi:10.1038/ng.487 · Cited by 1,751
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
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
Flagged first, then by citations
4 of the 67 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Cleveland, 1977, Physical properties and cellular localization of tau, a microtubule-associated protein which induces assembly of purified tubulin, J Cell Biol, 75, A283
Cited by
Sorted by citations
Items 101–200 of 404
Gerson, J. E., Castillo‐Carranza, D. L., & Kayed, R. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500143n · Cited by 75
Impaired retrograde transport by the Dynein/Dynactin complex contributes to Tau-induced toxicity
Butzlaff, M., Hannan, S. B., Karsten, P., Lenz, S., Ng, J., Voßfeldt, H., Prüßing, K., Pflanz, R., Schulz, J. B., Rasse, T. M., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv107 · Cited by 74
GRP78 clustering at the cell surface of neurons transduces the action of exogenous alpha-synuclein
Bellani, S., Mescola, A., Ronzitti, G., Tsushima, H., Tilve, S. M., Canale, C., Valtorta, F., & Chieregatti, E. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.111 · Cited by 72
Investigational drugs in Alzheimer's disease: current progress
Berk, C., Paul, G., & Sabbagh, M. N. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.905542 · Cited by 68
“Amyloid‐beta accumulation cycle” as a prevention and/or therapy target for Alzheimer's disease
Rao, C. V., Asch, A. S., Carr, D. J. J., & Yamada, H. Y. (2020) · Aging Cell · doi:10.1111/acel.13109 · Cited by 69
Hahn, I., Voelzmann, A., Liew, Y.-T., Costa-Gomes, B., & Prokop, A. (2019) · Neural Development · doi:10.1186/s13064-019-0134-0 · Cited by 66
Kovalevich, J., Cornec, A., Yao, Y., James, M., Crowe, A., Lee, V. M. Y., Trojanowski, J. Q., Smith, A. B., Ballatore, C., & Brunden, K. R. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.231175 · Cited by 66
Self-citationMicrotubule Organization Is Essential for Maintaining Cellular Morphology and Function
Huang, L., Peng, Y., Tao, X., Ding, X., Li, R., Jiang, Y., & Zuo, W. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1623181 · Cited by 64
Altered microtubule dynamics and vesicular transport in mouse and human MeCP2-deficient astrocytes
Delépine, C., Méziane, H., Nectoux, J., Opitz, M., Smith, A. B., Ballatore, C., Saillour, Y., Griscelli, A. B., Chang, Q., Williams, E. C., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv464 · Cited by 60
Self-citationFernandez-Valenzuela, J. J., Sanchez-Varo, R. M., Muñoz‐Castro, C., Castro, V. D., Sánchez‐Mejías, E., Navarro, V., Jiménez, S., Nuñez‐Diaz, C., Gómez-Arboledas, Á., Moreno‐González, I., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71767-4 · Cited by 63
Cognitive impairment in a rat model of neuropathic pain: role of hippocampal microtubule stability
You, Z., Zhang, S., Shen, S., Yang, J., Ding, W., Yang, L., Lim, G., Doheny, J. T., Tate, S., Chen, L. L., et al. (2018) · Pain · doi:10.1097/j.pain.0000000000001233 · Cited by 61
Onishi, T., Maeda, R., Terada, M., Sato, S., Fujii, T., Ito, M., Hashikami, K., Kawamoto, T., & Tanaka, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-94923-w · Cited by 61
Behind the curtain of tauopathy: a show of multiple players orchestrating tau toxicity
Huang, Y., Wu, Z., & Zhou, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2042-8 · Cited by 58
Curcumin improves tau-induced neuronal dysfunction of nematodes
Miyasaka, T., Xie, C., Yoshimura, S., Shinzaki, Y., Yoshina, S., Kage‐Nakadai, E., Mitani, S., & Ihara, Y. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.11.004 · Cited by 59
Crescenzi, R. L., DeBrosse, C., Nanga, R. P. R., Byrne, M. D., Krishnamoorthy, G., D’Aquilla, K., Nath, H., Morales, K. H., Iba, M., Hariharan, H., et al. (2016) · Hippocampus · doi:10.1002/hipo.22693 · Cited by 60
Self-citationAAV-mediated expression of anti-tau scFvs decreases tau accumulation in a mouse model of tauopathy
Ising, C., Gallardo, G., Leyns, C. E. G., Wong, C. H., Jiang, H., Stewart, F., Koscal, L. J., Roh, J., Robinson, G. O., Remolina Serrano, J., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20162125 · Cited by 57
Beyond amyloid: Getting real about nonamyloid targets in Alzheimer's disease
Herrup, K., Carrillo, M. C., Schenk, D., Cacace, A. M., DeSanti, S., Fremeau, R. T., Bhat, R. V., Glicksman, M. A., May, P. C., Swerdlow, R. H., et al. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.01.017 · Cited by 55
Voelzmann, A., Okenve-Ramos, P., Qu, Y., Chojnowska-Monga, M., del Caño-Espinel, M., Prokop, A., & Sánchez‐Soriano, N. (2016) · eLife · doi:10.7554/elife.14694 · Cited by 56
Co-expression of truncated and full-length tau induces severe neurotoxicity
Özcelik, S., Sprenger, F., Skachokova, Z. K., Fraser, G., Abramowski, D., Clavaguera, F., Probst, A., Frank, S., Müller, M. M., Staufenbiel, M., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.228 · Cited by 59
Chronic Administration of Dimebon Ameliorates Pathology in Tau P301S Transgenic Mice
Peters, O. M., Connor‐Robson, N., Sokolov, V. B., Aksinenko, A. Y., Kukharsky, M. S., Бачурин, С. О., Ninkina, N. N., & Buchman, V. L. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121732 · Cited by 54
Magen, I., & Gozes, I. (2013) · Neuropeptides · doi:10.1016/j.npep.2013.10.011 · Cited by 52
Kanakkanthara, A., Northcote, P. T., & Miller, J. H. (2016) · Natural Product Reports · doi:10.1039/c5np00146c · Cited by 55
A patient-derived stem cell model of hereditary spastic paraplegia with SPAST mutations
Abrahamsen, G., Fan, Y., Matigian, N., Wali, G., Bellette, B., Sutharsan, R., Raju, J., Wood, S. A., Veivers, D., Sue, C. M., et al. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.010884 · Cited by 56
Pharmacophore-based models for therapeutic drugs against phosphorylated tau in Alzheimer’s disease
Pradeepkiran, J. A., Reddy, A. P., & Reddy, P. H. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.11.005 · Cited by 53
Penazzi, L., Tackenberg, C., Ghori, A., Golovyashkina, N., Niewidok, B., Selle, K., Ballatore, C., Smith, A. B., Bakota, L., & Brandt, R. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.01.002 · Cited by 50
Self-citationMakani, V. S., Zhang, B., Han, H., Yao, Y., Lassalas, P., Lou, K., Paterson, I., Lee, V. M. ‐., Trojanowski, J. Q., Ballatore, C., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0378-4 · Cited by 52
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Sandner, B., Puttagunta, R., Motsch, M., Bradke, F., Ruschel, J., Blesch, A., & Weidner, N. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.01.018 · Cited by 51
Tau-directed approaches for the treatment of Alzheimer’s disease: focus on leuco-methylthioninium
Seripa, D., Solfrizzi, V., Imbimbo, B. P., Daniele, A., Santamato, A., Lozupone, M., Zuliani, G., Greco, A., Logroscino, G., & Panza, F. (2016) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2016.1140039 · Cited by 50
Cornec, A., Monti, L., Kovalevich, J., Makani, V. S., James, M. J., Vijayendran, K. G., Oukoloff, K., Yao, Y., Lee, V. M. ‐., Trojanowski, J. Q., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00475 · Cited by 50
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Friesen, D. E., Craddock, T. J. A., Kalra, A. P., & Tuszynski, J. A. (2015) · Biosystems · doi:10.1016/j.biosystems.2014.10.006 · Cited by 48
Wheeler, J. M., McMillan, P. J., Strovas, T. J., Liachko, N. F., Amlie‐Wolf, A., Kow, R. L., Klein, R. L., Szot, P., Robinson, L., Guthrie, C. R., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aao6545 · Cited by 44
Self-citationBolkan, B. J., & Kretzschmar, D. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22199 · Cited by 47
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Yarchoan, M. M., James, B. D., Shah, R. C., Arvanitakis, Z., Wilson, R. S., Schneider, J. A., Bennett, D. A., & Arnold, S. E. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160977 · Cited by 47
Azaphilones Inhibit Tau Aggregation and Dissolve Tau Aggregates in Vitro
Paranjape, S. R., Riley, A. P., Somoza, A. D., Oakley, C. E., Wang, C. C. C., Prisinzano, T. E., Oakley, B. R., & Gamblin, T. C. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00013 · Cited by 49
Brain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathies
Brunden, K. R., Ballatore, C., Lee, V. M. ‐., Smith, A. B., & Trojanowski, J. Q. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120010 · Cited by 46
Self-citationAn effective treatment for Alzheimer's disease must consider both amyloid and tau
Lansdall, C. J. (2014) · Bioscience Horizons The International Journal of Student Research · doi:10.1093/biohorizons/hzu002 · Cited by 46
Krefft, O., Jabali, A., Iefremova, V., Koch, P., & Ladewig, J. (2018) · Journal of Visualized Experiments · doi:10.3791/56768 · Cited by 53
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Kounakis, K., & Tavernarakis, N. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-25650-0_12 · Cited by 45
Jiang, G., Xie, G., Li, X., & Xiong, J. (2025) · Biomolecules · doi:10.3390/biom15060831 · Cited by 48
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Woerman, A. L., Patel, S., Kazmi, S. A., Oehler, A., Freyman, Y., Espiritu, L., Cotter, R., Castaneda, J. A., Olson, S. H., & Prusiner, S. B. (2017) · JAMA Neurology · doi:10.1001/jamaneurol.2017.2822 · Cited by 44
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Iqbal, K., Liu, F., & Gong, C. (2018) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2018.1445084 · Cited by 46
Zhang, B., Yao, Y., Cornec, A., Oukoloff, K., James, M. J., Koivula, P. P., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., Ballatore, C., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0291-3 · Cited by 46
Self-citationXia, Y., Sorrentino, Z. A., Kim, J. D., Strang, K. H., Riffe, C. J., & Giasson, B. I. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010178 · Cited by 48
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Boiarska, Z., & Passarella, D. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.11.033 · Cited by 46
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Bhat, M. A., Mishra, A. K., Bhat, M. A., Banday, M. I., Bashir, O., Rather, I. A., Rahman, S., Shah, A. A., & Jan, A. T. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13081265 · Cited by 43
Yao, D., Li, T., Yu, L., Hu, M., He, Y., Zhang, R., Wu, J., Li, S., Kuang, W., Yang, X., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1351792 · Cited by 46
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Dias, M. S., Luo, X., Ribas, V. T., Petrs‐Silva, H., & Koch, J. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073935 · Cited by 48
It cuts two ways: microtubule loss during Alzheimer disease
Jean, D. C., & Baas, P. W. (2013) · EMBO Journal · doi:10.1038/emboj.2013.219 · Cited by 36
Feinstein, H. E., Benbow, S. J., LaPointe, N. E., Patel, N., Ramachandran, S., Do, T. D., Gaylord, M. R., Huskey, N. E., Dressler, N., Korff, M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13604 · Cited by 45
Early investigational drugs targeting tau protein for the treatment of Alzheimer’s disease
Anand, K., & Sabbagh, M. N. (2015) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2015.1075002 · Cited by 41
Interphase microtubules: chief casualties in the war on cancer?
Ogden, A., Rida, P. C. G., Reid, M. D., & Aneja, R. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.10.022 · Cited by 41
Daoust, A., Bohic, S., Saoudi, Y., Debacker, C., Gory‐Fauré, S., Andrieux, A., Barbier, E., & Deloulme, J. (2014) · NeuroImage · doi:10.1016/j.neuroimage.2014.03.071 · Cited by 41
Fan, Y., Wali, G., Sutharsan, R., Bellette, B., Crane, D. I., Sue, C. M., & Mackay‐Sim, A. (2014) · Biology Open · doi:10.1242/bio.20147641 · Cited by 41
Karanth, S. D., Katsumata, Y., Nelson, P. T., Fardo, D. W., McDowell, J. K., Schmitt, F. A., Kryscio, R. J., Browning, S. R., Braithwaite, D., Arnold, S. M., et al. (2022) · Brain · doi:10.1093/brain/awac035 · Cited by 38
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Vicario-Orri, E., Opazo, C. M., & Muñoz, F. J. (2014) · Journal of Alzheimer’s Disease · doi:10.3233/jad-141080 · Cited by 41
Liaci, C., Camera, M., Caslini, G., Rando, S., Contino, S., Romano, V., & Merlo, G. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116167 · Cited by 40
Rate of decline in progressive supranuclear palsy
Litvan, I., & Kong, M. (2014) · Movement Disorders · doi:10.1002/mds.25843 · Cited by 40
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Cartelli, D., & Cappelletti, G. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0188-5 · Cited by 41
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Coughlin, D. G., & Irwin, D. J. (2017) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-017-0779-1 · Cited by 42
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Novák, P., Cehlár, O., Škrabana, R., & Novák, M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179942 · Cited by 38
Fournet, V., de Lavilléon, G., Schweitzer, A., Bruno Giros, A., Andrieux, A., & Martres, M. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12027 · Cited by 37
Altered brain arginine metabolism in a mouse model of tauopathy
Vemula, P., Yu, J., Zhang, H., Hunt, J. B., Sandusky‐Beltran, L. A., Lee, D. C., & Liu, P. (2019) · Amino Acids · doi:10.1007/s00726-018-02687-x · Cited by 37
Therapeutic Targeting Strategies for Early- to Late-Staged Alzheimer’s Disease
Kang, Y. J., Diep, Y. N., Tran, M., & Cho, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249591 · Cited by 36
Tau in Alzheimer’s Disease: Pathological Alterations and an Attractive Therapeutic Target
Gu, J., & Liu, F. (2020) · Current Medical Science · doi:10.1007/s11596-020-2282-1 · Cited by 41
Photodynamic sensitizers modulate cytoskeleton structural dynamics in neuronal cells
Dubey, T., & Chinnathambi, S. (2021) · Cytoskeleton · doi:10.1002/cm.21655 · Cited by 36
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Jabali, A., Hoffrichter, A., Uzquiano, A., Marsoner, F., Wilkens, R., Siekmann, M. T., Bohl, B., Rossetti, A. C., Horschitz, S., Koch, P., et al. (2022) · EMBO Reports · doi:10.15252/embr.202154027 · Cited by 35
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Uchida, S., & Shumyatsky, G. P. (2015) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2015.07.011 · Cited by 41
Brunden, K. R., Gardner, N. M., James, M. J., Yao, Y., Trojanowski, J. Q., Lee, V. M. ‐., Paterson, I., Ballatore, C., & Smith, A. B. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml400233e · Cited by 35
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Brody, A. H., Nies, S. H., Guan, F., Smith, L. M., Mukherjee, B., Salazar, S. A., Lee, S., Lam, T. K. T., & Strittmatter, S. M. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00526-y · Cited by 36
Bakrim, S., Aboulaghras, S., Menyiy, N. E., Omari, N. E., Assaggaf, H. M., Lee, L., Montesano, D., Gallo, M., Zengin, G., Al-Dhaheri, Y., et al. (2022) · Molecules · doi:10.3390/molecules27249043 · Cited by 34
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Coughlin, D. G., Dickson, D. W., Josephs, K. A., & Litvan, I. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_11 · Cited by 33
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Lauretti, E., & Praticò, D. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1737012 · Cited by 34
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Jang, E., Sim, A. M., Im, S., & Hur, E. (2016) · Neural Plasticity · doi:10.1155/2016/5056418 · Cited by 31
Duggal, P., Jadaun, K. S., Siqqiqui, E. M., & Mehan, S. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666201007120112 · Cited by 31
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Dorigatti, A. O., Riordan, R., Yu, Z., Ross, G., Wang, R., Reynolds-Lallement, N. C., Magnusson, K. R., Galván, V., & Pérez, V. (2022) · GeroScience · doi:10.1007/s11357-022-00531-5 · Cited by 34
Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model
Nishioka, C., Liang, H.-F., Barsamian, B., & Sun, S.-W. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.01.007 · Cited by 30
“Additionally, previous studies utilizing EpoD as well as microtubule-stabilizing peptide NAP have both shown ability to reduce p-tau pathology in AD model mice over several months of treatment (Zhang et al., 2012; Matsuoka et al., 2007, 2008).”
InfluentialDo Cancer Drugs Counteract Neurodegeneration? Repurposing for Alzheimer’s Disease
Monacelli, F., Cea, M., Borghi, R., Odetti, P. R., & Nencioni, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160840 · Cited by 31
Guo, T., Dakkak, D., Rodríguez-Martín, T., Noble, W. J., & Hanger, D. P. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0651-9 · Cited by 27
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Barbiero, I., Rosa, R. D., & Kilstrup‐Nielsen, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174075 · Cited by 27
Cornec, A., James, M. J., Kovalevich, J., Trojanowski, J. Q., Lee, V. M. ‐., Smith, A. B., Ballatore, C., & Brunden, K. R. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.03.002 · Cited by 30
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Pianu, B., Lefort, R., Thuiliere, L., Tabourier, E., & Bartolini, F. (2014) · Journal of Cell Science · doi:10.1242/jcs.143750 · Cited by 30
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Kern, F., Dier, T. K. F., Khatri, Y., Ewen, K. M., Jacquot, J., Volmer, D. A., & Bernhardt, R. (2015) · Scientific Reports · doi:10.1038/srep14881 · Cited by 30
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Pineda, J. J., Miller, M. A., Song, Y., Kuhn, H., Mikula, H., Tallapragada, N. P., Weissleder, R., & Mitchison, T. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800047115 · Cited by 30
Zhao, X., Zeng, W., Xu, H. W., Sun, Z., Hu, Y., Peng, B., McBride, J. D., Duan, J., Deng, J., Zhang, B., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo6889 · Cited by 31
Self-citationLeighton, P. L. A., & Allison, W. T. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160361 · Cited by 31
Duquette, A., Pernègre, C., Carpentier, A. V., & Leclerc, N. M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.607680 · Cited by 38
Yang, Y., Chen, X., Feng, Z., Cai, X., Zhu, X., Cao, M., Yang, L., Chen, Y., Wang, Y., & Feng, H. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15493 · Cited by 28
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Xiong, G.-J., & Sheng, Z. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202401145 · Cited by 29
Dehhaghi, M., Mohammadipanah, F., & Guillemin, G. J. (2018) · NeuroToxicology · doi:10.1016/j.neuro.2018.02.017 · Cited by 29
Mezencev, R., & Chernoff, Y. O. (2020) · Cancers · doi:10.3390/cancers12040796 · Cited by 27
Yang, T., Liu, H., Tran, K. C., Leng, A., Massa, S. M., & Longo, F. M. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01034-0 · Cited by 31
Oukoloff, K., Nzou, G., Varricchio, C., Lucero, B., Alle, T., Kovalevich, J., Monti, L., Cornec, A., Yao, Y., James, M. J., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01605 · Cited by 28
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Santiago-Mujika, E., Luthi‐Carter, R., Giorgini, F., Kalaria, R. N., & Mukaetova-Ladinska, E. B. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.730107 · Cited by 26
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Yue, X., Sheng, D., Li, Z., & Li, Y. (2023) · Engineering Microbiology · doi:10.1016/j.engmic.2023.100075 · Cited by 28
Verstraelen, P., Detrez, J. R., Verschuuren, M., Kuijlaars, J., Nuydens, R., Timmermans, J., & Vos, W. H. D. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00173 · Cited by 28
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Peña‐Ortega, F., Robles-Gómez, Á. A., & Cueva, L. X. (2022) · Cells · doi:10.3390/cells11060923 · Cited by 31
Yang, Y., Zhang, K., Zhong, J., Ju, W., Yu, Z., Lei, X., Chen, X., Quan, Y., Xian, J., Chen, Y., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-31056-7 · Cited by 26
Metadata
- Authors
- Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., Lee, V. M.-Y., & Brunden, K. R.
- Affiliations
- University of Pennsylvania (US)
- Institute on Aging (US)
- Corresponding author
- Brunden, Kurt R.
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2012-03-14
- Volume
- 32
- Issue
- 11
- Pages
- 3601-3611
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3321513
- OpenAlex
- W1969129718
- Cited by
- 401
- References
- 67
- Citations by year
- 2026: 18 · 2025: 19 · 2024: 22 · 2023: 11 · 2022: 31 · 2021: 36 · 2020: 37 · 2019: 24 · 2018: 27 · 2017: 28 · 2016: 44 · 2015: 26 · 2014: 40 · 2013: 23 · 2012: 14
- FWCI
- 22.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Bristol-Myers Squibb
- University of Pennsylvania
- National Institutes of Health
- National Institute on Aging (U01AG029213)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- epothilone D, microtubule stabilization, tauopathy, Alzheimer's disease, tau phosphorylation, axonal dystrophy, axonal transport, cognitive impairment, hippocampal neurons, PS19 mice, neuroprotection, drug repurposing
- MeSH terms
- Aging, Alzheimer Disease, Animals, Axons, Cognition Disorders, Humans, Male, Mice, Transgenic, Microtubules, tau Proteins, Neurotoxicity Syndromes, Tauopathies, Epothilones, Tubulin Modulators, Mice
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