The DOI matches its Crossref record; 222 of the 222 references it cites were found in a registry or an index.
Tau-targeting therapy in Alzheimer’s disease: critical advances and future opportunities
Open accessAbstract
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder characterized by two pathological hallmark lesions: extracellular plaques composed of β-amyloid (Aβ) peptide and intracellular neurofibrillary tangles made up of highly phosphorylated tau protein. Over the past two decades, most disease-modifying therapies against AD have been developed mainly on the basis of the amyloid cascade hypothesis with a focus on Aβ. However, these agents yielded only limited benefits against disease progression, which prompts us to revitalize the long-neglected tau hypothesis. Tau protein is a microtubule-associated protein, which can stabilize microtubules, regulate microtubule assembly, and affect the morphology and growth of neuronal axons. Much more importantly, the degree of tau pathology is more closely related to cognitive decline in AD patients than that of Aβ pathology. Therefore, tau-targeting therapy seems to be a promising approach to combat AD. This review describes the research progress of tau-targeting therapy in AD, with an emphasis on immunotherapy. The current challenges and future perspectives in this field are also discussed.
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“In clinical trials, immunotherapies make up the majority of tau-targeting treatments.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [96]
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Items 201–222 of 222
Red Ginseng Inhibits Tau Aggregation and Promotes Tau Dissociation In Vitro
Shin, S. J., Park, Y. H., Jeon, S. G., Kim, S., Nam, Y., Oh, S., Lee, Y. Y., & Moon, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7829842 · Cited by 38
Sagnou, M., Mavroidi, B., Kaminari, A., Boukos, N. K., & Pelecanou, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00208 · Cited by 37
MICROTUBULE ASSOCIATED PROTEIN TAU
Iqbal, K., Grundke‐Iqbal, I., & Smith, A. (1989) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198905000-00164 · Cited by 35
Active Vaccines for Alzheimer Disease Treatment
Sterner, R. M., Takahashi, P. Y., & Ballard, A. Y. (2016) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2016.06.009 · Cited by 33
Prion-like properties of Tau assemblies
Clavaguera, F., Duyckaerts, C. J., & Haı̈k, S. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.022 · Cited by 32
In-Cell NMR Study of Tau and MARK2 Phosphorylated Tau
Zhang, S., Wang, C., Lu, J., Ma, X., Liu, Z., Li, D., Liu, Z., & Liu, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010090 · Cited by 31
Galpern, W. R., Mercken, M. H., Kolen, K. V., Timmers, M., Katrin, H., Janssens, L., Triana‐Baltzer, G., Kolb, H. C., Jacobs, T., Nandy, P., et al. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.077 · Cited by 29
Probing Mechanisms and Therapeutic Potential of γ-Secretase in Alzheimer’s Disease
Wolfe, M. S. (2021) · Molecules · doi:10.3390/molecules26020388 · Cited by 28
Tashima, T. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14020411 · Cited by 27
Maina, M. B., Al‐Hilaly, Y. K., Oakley, S. S., Burra, G., Khanom, T., Biasetti, L., Mengham, K., Marshall, K. E., Rickard, J. E., Harrington, C. R., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167785 · Cited by 23
Czerkowicz, J., Chen, W., Wang, Q. L., Shen, C., Wager, C. G., Stone, I., Stebbins, C., Lamb, M., Setser, J. J., Cantone, G., et al. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.06.1903 · Cited by 22
Wang, H.-H., Li, Y., Li, A., Yan, F., Li, Z.-L., Liu, Z.-Y., Zhang, L., Zhang, J., Dong, W.-R., & Zhang, L. (2018) · Molecular Neurobiology · doi:10.1007/s12035-016-0348-7 · Cited by 19
Shamir, D. B., Deng, Y., Wu, Q., Modak, S., Congdon, E. E., & Sigurdsson, E. M. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.602292 · Cited by 19
Thiophene‐Based Dual Modulators of Aβ and Tau Aggregation
Ramesh, M., Acharya, A., Murugan, N. A., Ila, H., & Govindaraju, T. (2021) · ChemBioChem · doi:10.1002/cbic.202100383 · Cited by 18
Pathogenic cis p-tau levels in CSF reflects severity of traumatic brain injury
Sisakht, A. M., Ziarati, N. K., Jahanbakhshi, A., Shahpasand, K., Aghababaei, S., Ahmadvand, O., Azar, M., Fattahi, A., & Zamanzadeh, S. (2022) · Neurological Research · doi:10.1080/01616412.2021.2022921 · Cited by 18
Vivash, L. E., Malpas, C. B., Hovens, C. M., Brodtmann, A. G., Collins, S. J., Macfarlane, S., Velakoulis, D., & O'Brien, T. J. (2021) · BMJ Neurology Open · doi:10.1136/bmjno-2021-000223 · Cited by 16
Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates
Maina, M. B., Al‐Hilaly, Y. K., Burra, G., Rickard, J. E., Harrington, C. R., Wischik, C. M., & Serpell, L. C. (2021) · Cells · doi:10.3390/cells10030703 · Cited by 14
Singh, G., Liu, P., Yao, K. R., Strasser, J. M., Hlynialuk, C. J. W., Leinonen-Wright, K., Teravskis, P. J., Choquette, J. M., Ikramuddin, J., Bresinsky, M., et al. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00100 · Cited by 12
Son, S. H., Do, J. M., Yoo, J.-N., Lee, H. W., Kim, N. K., Yoo, H., Gee, M. S., Kim, J.-H., Seong, J., Inn, K., et al. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105022 · Cited by 9
Selective inhibition of phosphodiesterase 4D increases tau phosphorylation at Ser214 residue
Villa, V., Montalto, G., Caudano, F., Fedele, E., & Ricciarelli, R. (2022) · BioFactors · doi:10.1002/biof.1847 · Cited by 5
Gao, C., Chu, X., Gong, W., et al. (2020) · Figshare · doi:10.6084/m9.figshare.c.4977287 · Cited by 5
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Research works printed but not linked: 1
- Zhao Y, Wang C, He W, Cai Z. Ameliorating Alzheimer's-like pathology by Minocycline via inhibiting Cdk5/p25 signaling. Curr Neuropharmacol 2021. DOI PubMed · DOI
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Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies
Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509
Tau-targeting therapies for Alzheimer disease: Current status and future directions
Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371
Basheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159
Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease
Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56
Metadata
- Authors
- Guo, Y., Li, S., Zeng, L.-H., & Tan, J.
- Affiliations
- Guiyang Medical University (CN)
- First Affiliated Hospital of Dalian Medical University (CN)
- Corresponding author
- Tan, Jun
- Venue
- Ageing and Neurodegenerative Diseases
- Publisher
- OAE Publishing Inc.
- Published
- 2022
- Volume
- 2
- Issue
- 3
- Pages
- 11
- ISSN
- 2769-5301 (ISSN-L)
- OpenAlex
- W4286480258
- Cited by
- 61
- References
- 222
- Citations by year
- 2026: 6 · 2025: 20 · 2024: 16 · 2023: 16 · 2022: 3
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Ageing and Neurodegenerative Diseases (publishedVersion, cc-by)
- Funders
- High-level Talent Foundation of Guizhou Medical University (YJ19017, HY2020, J.T.)
- National Natural Science Foundation of China (NSFC) (82171423, 82060211, J.T.)
- 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
- Alzheimer's disease, tau protein, tau hypothesis, tau immunotherapy, amyloid hypothesis, neurofibrillary tangles, tau phosphorylation, microtubule stabilization, cognitive decline
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