The DOI matches its Crossref record; 173 of the 185 references it cites were found in a registry or an index.
Interaction between Aβ and Tau in the Pathogenesis of Alzheimer’s Disease
Open accessAbstract
Extracellular neuritic plaques composed of amyloid‑β (Aβ) protein and intracellular neurofibrillary tangles containing phosphorylated tau protein are the two hallmark proteins of Alzheimer's disease (AD), and the separate neurotoxicity of these proteins in AD has been extensively studied. However, interventions that target Aβ or tau individually have not yielded substantial breakthroughs. The interest in the interactions between Aβ and tau in AD is increasing, but related drug investigations are in their infancy. This review discusses how Aβ accelerates tau phosphorylation and the possible mechanisms and pathways by which tau mediates Aβ toxicity. This review also describes the possible synergistic effects between Aβ and tau on microglial cells and astrocytes. Studies suggest that the coexistence of Aβ plaques and phosphorylated tau is related to the mechanism by which Aβ facilitates the propagation of tau aggregation in neuritic plaques. The interactions between Aβ and tau mediate cognitive dysfunction in patients with AD. In summary, this review summarizes recent data on the interplay between Aβ and tau to promote a better understanding of the roles of these proteins in the pathological process of AD and provide new insights into interventions against AD.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“For instance, Aβ oligomers promote tau phosphorylation and mislocalization by activating kinases such as GSK-3, CDK5, and Fyn kinase, and by interfering with tau degradation [50].”
From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [50]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Through the cellular prion protein/mGluR5 complex, Aβ oligomers can trigger Fyn kinase activation, further driving tau toxicity [50].”
From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [50]
Experimental — accuracy not yet measuredIn the citing paper
“Since amyloid-beta (Aβ) plaques and tau tangles are characteristic of AD and are thought to be important in the onset and development of the disease, the main focus of these therapies has been on removing or reducing them.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [84]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Larson, M. E., Sherman, M. A., Amar, F., Nuvolone, M., Schneider, J. A., Bennett, D. A., Aguzzi, A., & Lesné, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1858-12.2012 · Cited by 290
RetractedProceedings of the National Academy of Sciences of the United States of America
Dowling, J. E., & Wald, G. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1981.tb06752.x · Cited by 17,937
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Astrocyte-endothelial interactions at the blood-brain barrier
Abbott, N. J., Rönnbäck, L., & Hansson, E. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1824 · Cited by 5,595
Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
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
Flagged first, then by citations
12 of the 185 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–500 of 685
Patel, H. (2024) · American Journal of Translational Research · doi:10.62347/ujqf5204 · Cited by 3
Virus-like Particles-based Vaccine to Combat Neurodegenerative Diseases
Lim, L. W. C., Jy, L., Chen, C. H., Voon, K., Koh, R. Y., & Chye, S. M. (2024) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010331763241002122854 · Cited by 3
He, J., Sun, S., Wang, H., Ying, Z., & Tam, K. Y. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01354-y · Cited by 3
“…can also modulate the production of Aβ by regulating different components of the APP processing system such as activating γ-secretase activity through PS-1 interaction [20] and inducing BACE1 expression through NF-κB activation [21], further mediating Aβ-dependent regulation of tau toxicity [64].”
Mondal, R., Deb, S., Shome, G., Sarkar, V., Lahiri, D., Datta, S. S., & Benito‐León, J. (2025) · Neurología (English Edition) · doi:10.1016/j.nrleng.2025.03.008 · Cited by 3
Liu, B., Zhao, Q., Shi, Q., Xu, W., Shi, F.-X., Yang, R., & Zhou, X. (2025) · Neurocritical Care · doi:10.1007/s12028-025-02293-2 · Cited by 4
“For instance, in AD, the hyper-phosphorylation of tau protein leads to the formation of neurofibrillary tangles (NFTs), a pathological hallmark of the disease [21–23].”
Cheng, F., Fransson, L., & Mani, K. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70162 · Cited by 3
Ying, C., He, Y., Guo, Y., Fan, F., Wang, B., Gao, J., Li, Y., & Zhang, Y. (2025) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x25500624 · Cited by 4
Chen, H., Cao, J., Zhang, Y., Su, X., Kang, Y., Gao, L., & Jing, Y. (2025) · The FASEB Journal · doi:10.1096/fj.202501545rr · Cited by 4
“Synapse loss is closely associated with cognitive decline of all pathological changes in Alzheimer's disease (AD) [2, 3]. β-amyloid (Aβ) and Tau hyperphosphorylation play a fundamental role in AD pathology [4, 5].”
Wang, B., Wang, X., Liang, Y., Wang, J., Hua, S., Kong, J., Xu, S., Yang, Y.-C., Lin, Y., Li, C., et al. (2025) · International Journal of Surgery · doi:10.1097/js9.0000000000003465 · Cited by 4
“Specifically, A β aggregation and accumulation show tight correlations with AD development and aggravation [ 16 ] .”
The association between chronic rhinosinusitis and the risk of dementia: a longitudinal study
Zhang, X., Yin, Z., Luo, J., Yang, R., Wang, W., & Zhang, D. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1609790 · Cited by 3
Intratarget Microdosing for Deep Phenotyping of Multiple Drug Effects in the Live Brain
Kim, J. S., Ahn, S. W., Deans, K., Thompson, D., Ferland, B., Divakar, P., Dominas, C. A., & Jonas, O. H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.855755 · Cited by 3
VD/VDR-mediated ATG16L1 activation reduces Alzheimer’s disease-like pathology and cognitive decline
Huang, Z., Ang, W., Huang, H., & Wang, Y. (2024) · Molecular & Cellular Toxicology · doi:10.1007/s13273-024-00429-7 · Cited by 3
“However, stimulation with CCE significantly decreased APP content The core pathological characteristics of AD involve the buildup of Aβ and the phosphorylation of TAU protein (Zhang et al. 2021a, b).”
G-protein coupled estrogen receptor 1, amyloid-β, and tau tangles in older adults
Oveisgharan, S., Yu, L., Lopes, K. D. P., Petyuk, V., Tasaki, S., Vialle, R. A., Menon, V., Wang, Y., Jager, P. L. D., Schneider, J. A., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06272-9 · Cited by 4
Gao, J., Bi, X., Jiang, W., & Wang, Y. (2025) · Scientific Reports · doi:10.1038/s41598-025-12290-2 · Cited by 6
“Although hallmark pathologies—amyloid-β (Aβ) plaques and neurofibrillary tangles—have been well documented 2–4 , the molecular mechanisms that initiate and drive AD remain poorly understood, particularly in sporadic late-onset cases, which account for the vast majority of cases.”
Sarparast, M., Hinman, J., Pourmand, E., Vonarx, D., Ramirez, L., Ma, W., Liachko, N. F., Alan, J. K., & Lee, K. S. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.02.560527 · Cited by 4
NRN1 may Modulate Tau Phosphorylation and Neuronal Apoptosis in AD via the PIGU-CASP3 Axis
Cheng, W., Zhang, J., Zhu, H., Wang, Z., Li, M., Wang, J., Fu, H., Zhang, Y., Gao, Y., Chen, C., et al. (2025) · Current Alzheimer Research · doi:10.2174/0115672050361366250328040542 · Cited by 2
Badman, J., Parracino, A., Kumar, R., & Tambaro, S. (2025) · Science Signaling · doi:10.1126/scisignal.adt2272 · Cited by 3
Wang, Y., Zhou, Y., Tian, H., Li, Q., Chen, Y., Wang, L., Yin, Z., Zhou, J., & Liang, F. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149893 · Cited by 3
Advancing nanotheranostics for neuro-immunological disorders: current status and future prospects
Rai, S., Nair, A., Saleem, Z., Ray, S. K., Kanwar, J. R., & Mukherjee, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.08.051 · Cited by 2
Mathew, J., Maroky, A. S., SINDURAJ, S., & Chandrababu, A. (2025) · International Journal of Applied Pharmaceutics · doi:10.22159/ijap.2025v17i5.54564 · Cited by 3
Jiang, W., Liu, J., Wu, Y., Li, J., Jin, H., Cui, Z., Chen, X., Lian, T., Lv, H., Han, B., et al. (2025) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.70194 · Cited by 2
Active immunization: A novel therapeutic strategy for treating Alzheimer's disease
Mazahir, F. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178288 · Cited by 3
Lee, N., Youn, K., Kwon, H., Lee, J., Lee, E., Jung, J. W., Moon, M., Lee, D., Kim, D. H., Ho, C., et al. (2025) · Food & Function · doi:10.1039/d5fo04217h · Cited by 2
PolyGR-containing aggregates link with pathology and clinical features of Alzheimer’s disease
Phuong, H. T., Tomas, R. F., Akmese, C., Mijares, A. M. P., Gerstin, I. M., Guo, S., Bell, L. R., Ellwood, R., Yegorova, S., Ng, S. K., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02954-8 · Cited by 2
Therapeutic efficacy of rehmannioside A on 5×FAD mice in Alzheimer’s disease
Lai, Y., & Zhao, H. (2025) · Scientific Reports · doi:10.1038/s41598-025-23434-9 · Cited by 2
Yan, C., Qi, Y., Zhao, R., Zhu, Z., Yan, Z., Qian, C., Wang, Y., Li, Y., Liu, L., Zhang, N., et al. (2025) · ACS Applied Nano Materials · doi:10.1021/acsanm.5c03854 · Cited by 2
Yata, V. K., Das, O. P., Dansana, J., Gadtya, A., Meher, B. R., Bukke, S. P. N., & Kolliputi, N. (2025) · Frontiers in Artificial Intelligence · doi:10.3389/frai.2025.1709505 · Cited by 2
“Docking and molecular dynamics (MD) simulations have further elucidated A β interaction mechanisms (Urbanc et al., 2004; Mandal et al., 2006; Zhang et al., 2021).”
Das, S. K., Bashir, B., Kolekar, K. A., Harish, V., Patle, D., Vishwas, S., Mittal, N., Jha, S. K., Kumar, P., Gupta, G. K., et al. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.103000 · Cited by 2
Meprin β elevates hippocampal soluble Aβ in the APP/V717I mouse model
Keller, M., Gallagher, C., Marengo, L., Bickenbach, K., Schmitt, U., Abukhalaf, M., Tholey, A., Kreiselmaier, S., Becker-Pauly, C., Mittmann, T., et al. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115600 · Cited by 2
Lu, W., Gong, Q., Chen, Y., Qiu, S., & An, J. (2026) · Neural Networks · doi:10.1016/j.neunet.2026.108542 · Cited by 2
Mechanisms and therapeutic potential of migrasomes in neurological disorders
Zhang, S., Yang, Y., Zhang, T., Pan, Y., Xu, Q., & Lü, P. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112389 · Cited by 2
Manoharan, S. D., Usman, A. S., Hamid, H. A., Nassir, C. M. N. C. M., Cheema, M. S., Ramli, M. D. C., Moklas, M. A. M., & Mehat, M. Z. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04702-0 · Cited by 2
“Tau oligomerisation, primarily driven by tau hyperphosphorylation, is reported to arise from dysregulated kinases [17].”
Uzoechi, S. C., Johnson-Campbell, C., Badeaux, C. J., Kwak, S. S., Kim, D. Y., & Yun, Y. (2026) · Molecular Brain · doi:10.1186/s13041-026-01285-3 · Cited by 2
“Despite their different origins, both FAD and SAD converge on a common pathological signature, which includes extracellular amyloid beta (Aβ) plaques and intracellular hyperphosphorylated tau (p-tau) tangles [11].”
Jiang, E., Ullah, S., Waheed, I., Han, J., & Zhang, X. (2026) · Clinical Interventions in Aging · doi:10.2147/cia.s585864 · Cited by 2
Brain-heart interaction: direct and indirect circuits in health and diseases
Wang, Y., Liu, L.-L., Zhang, T.-A., Wang, Y.-Y., Zhou, H., Jiang, P.-F., Lv, S., Zhang, J.-P., & Hu, Y. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.04.024 · Cited by 3
Meesala, S., Nageswara, S., Kolakota, R., Dokka, M. K., Giri, M., Bada, P., & Jerra, V. S. (2026) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-026-00858-0 · Cited by 2
The mechanisms and strategies for Alzheimer’s disease prevention: An update
Han, M., Wang, N., Song, M., Liu, C., Wu, Y., Yin, J., Jin, L., Jin, W., & Gao, Z. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.04.007 · Cited by 3
“Currently, the core mechanisms that have been extensively studied and recognized predominantly revolve around the beta-amyloid cascade hypothesis and the tau protein hypothesis 12,13 .”
Wang, S., Liu, M., Shi, X., Xiong, T., Li, R., Zheng, W., Huang, Q., Nan, Y., & Ai, K. (2026) · 中国科学通报：英文版 · doi:10.1016/j.scib.2026.05.020 · Cited by 2
Baskar, G., & Kandasamy, M. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.05.012 · Cited by 2
Abbasi, A. A., Norouziyan, F., & Moradikor, N. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261461161 · Cited by 2
Quach, B., Salehi, S. N., Roufegarinejad, R., Guleria, V. S., Mante, M., Florio, J. B., Rissman, R. A., & Winston, C. N. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.115893 · Cited by 2
Yin, J., Tuo, C.-M., Yu, K.-Y., Hu, X.-H., Fan, Y., & Wu, M. (2023) · NeuroMolecular Medicine · doi:10.1007/s12017-023-08767-w · Cited by 2
“The typical pathological features of AD are senile plaques formed by the aggregation of β-amyloid protein (Aβ), neurofibrillary tangles (NFTs) formed by hyperphosphorylation of tau protein, and dysfunction of neurons and synapses (Ma et al., 2022; Zhang et al., 2021).”
Promising Prospects for Human Cerebral Organoids to Advance Alzheimer's Disease Research
López, V., Rosca, A., Liste, I., Mateos-Martínez, P., Coronel, R., González-Sastre, R., Martín-Benito, S., & López, V. (2023) · Progress in Neurobiology · doi:10.60124/j.pneuro.2023.20.05 · Cited by 1
Intérêt du régime cétogène dans la prise en charge de la maladie d’Alzheimer
Charlot, A., Lernould, A., Plus, I., & Zoll, J. (2023) · Biologie Aujourd hui · doi:10.1051/jbio/2023031 · Cited by 2
ALZHEIMER HASTALIĞI, RİSK FAKTÖRLERİ VE TEDAVİ
Yıldırım, N., & Eke, B. C. (2024) · Ankara Universitesi Eczacilik Fakultesi Dergisi · doi:10.33483/jfpau.1441827 · Cited by 4
“Bunların yanı sıra Aβ ve taunun, mitokondriye hasar vermek için birlikte hareket ettiği [137,139], nöronal olmayan hücrelerde mikroglia [140,141] ve astrositler [142] üzerindeki ortak etkileri; Aβ plaklarının, nöritik plak tau agregasyonunu ve yayılmasını kolaylaştırdığı belirtilmektedir [136].”
Revisiting the focal role of endostatin and environmental factors in Alzheimer’s disease
Behl, T., Dahim, M. A., & Aleya, L. (2024) · Environmental Science and Pollution Research · doi:10.1007/s11356-024-34113-z · Cited by 2
“Aggregation of aberrant proteins in the brain leads to the production of Aβ plaques and tau proteins (Zhang et al. 2021).”
Kumari, P., Sarwa, N., Meena, D., Eesha, A., & Chaudhary, N. S. (2024) · Current Enzyme Inhibition · doi:10.2174/0115734080296802240528073027 · Cited by 2
Low-dose diazepam improves cognitive function in APP/PS1 mouse models: Involvement of AMPA receptors
Chen, J., Zhang, M., Shen, Z., Tang, M., Zeng, Y., Bai, D., Zhao, P., & Jiang, G. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149207 · Cited by 3
Wang, Y., Wu, Z., Zheng, Y., Wang, H., Cheng, B., & Xia, J. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251329517 · Cited by 2
Ojha, V. P., Riahi, S., Bobo, R. H., Moravveji, S., Meteumba, L. G., & Yarahmadian, S. (2025) · Discover Psychology · doi:10.1007/s44202-025-00335-6 · Cited by 2
“Studies have always argued about the role of amyloid-beta and tau proteins in the development of AD but have indicated them as a strong indicator [6, 11, 15, 26, 33, 42].”
Higashi, Y., Ikuno, K., Saito, T., Saido, T. C., Miyasaka, T., Kakuda, N., & Funamoto, S. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152025 · Cited by 2
Therapeutic Modalities Targeting Tau Protein in Alzheimer’s Disease
Schreiner, T. G., Iacob, L., Vasilache, C., & Schreiner, O. D. (2025) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad2030032 · Cited by 2
Farhana, A., & Khan, Y. S. (2021) · Springer eBooks · doi:10.1007/978-981-16-4558-7_2 · Cited by 2
Qiu-Yue, X., Tian-Yuan, Y., Wang, X., Qi, D., & Xiao-Rui, C. (2022) · Current Alzheimer Research · doi:10.2174/1567205020666221201143323 · Cited by 2
Holcom, A., Fuentealba, M., Sivapatham, R., King, C. D., Osman, H., Foulger, A., Bhaumik, D., Schilling, B., Furman, D., Andersen, J. K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.01.542377 · Cited by 1
Zhen, W., Wang, Y., Zhen, H., Zhang, W., Shao, W., Sun, Y., Qiao, Y., Jia, S., Zhou, Z., Wang, Y., et al. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1513930 · Cited by 1
Toxicological mechanisms of carbon polymers in accelerating cognitive decline in Alzheimer’s disease
Qi, Z., Cao, J., Liu, J., Chen, J., Chen, S., Zhang, L., Xu, J., Wu, D., Wu, Y., & Li, G. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.02.017 · Cited by 2
The Role of the Progesterone Receptor Family in Alzheimer’s Disease
Zhu, T., & Hua, F. (2025) · Biocell · doi:10.32604/biocell.2025.064879 · Cited by 1
Neurodegenerative Disorder: An Overview
Verma, M., Shukla, S., Shrivastava, S., & Puranik, N. (2025) · Springer eBooks · doi:10.1007/978-981-96-6202-9_1 · Cited by 2
Neuroprotective effects of SOUL-tang and isoacteoside via antioxidant properties
Kim, H., Jeong, K.-M., Choi, Y., Jung, H., Park, J., Kim, H.-M., & Jeong, H. (2025) · Molecular & Cellular Toxicology · doi:10.1007/s13273-025-00559-6 · Cited by 1
“AD pathology begins with the cleavage of amyloid precursor protein, leading to amyloid-β (Aβ) plaque formation and tau protein abnormalities that disrupt neuronal communication and cause synaptic dysfunction (Scheltens et al. 2021; ZhaNg et al. 2021).”
Biomarkers of heavy metal–induced neurotoxicity: insights into mechanisms and disease impact
Bharadava, K., Kumar, S., & Kaushal, R. S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-36575-1.00015-7 · Cited by 2
Protein misfolding and neurodegeneration: Mechanisms, implications, and therapeutic strategies
Shah, A., Karthikeyan, T., Hashem, S., Kumar, R., Bhat, A. A., & Macha, M. A. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.08.012 · Cited by 2
Zhu, X., Ma, J., Guo, C., Hopke, P. K., Tian, Y., Li, Q., Wei, Y., & Zhang, Y. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.119004 · Cited by 1
Behera, P., Rangappa, N., Chandrashekar, M., Mishra, A., Chinnathambi, S., & Mishra, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.08.003 · Cited by 2
Mind the gap – Interthalamic adhesions in prodromal and clinical Alzheimer’s disease
Forno, G., Vidal, J. P. C., Rush, P., Tan, R. H., Aggleton, J. P., Barbeau, E. J., & Hornberger, M. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111559 · Cited by 1
“While A β 42 levels are still within the normal range, increased accumulation of intracellular neurofibrillary tangles in the IA could lead to neuronal and synaptic loss (Iqbal et al., 2010; Zhang et al., 2021).”
Huang, Y., Wei, F., Cheng, X., Shi, Y., Liu, Z., & Ye, L. (2025) · BioScience Trends · doi:10.5582/bst.2025.01220 · Cited by 2
“The intricate interaction between Aβ and Tau synergistically contributes to AD pathogenesis ( 6 ).”
Insights into the coaggregation mechanisms of amyloid-α and amyloid-β
Xu, Z., Yan, X., Xia, P., Zhu, Y., Chen, Y., Guo, C., & Li, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148086 · Cited by 1
Wei, C., Chen, X., Sun, M., Cao, J., Liao, D.-C., Zhou, C., & Wang, H. (2025) · Antioxidants · doi:10.3390/antiox14101255 · Cited by 1
“In AD progression, A β deposition and senile plaque formation elicit various secondary effects, including facilitating the development of hyperphosphorylated tau, to cause neuronal dysfunction and synaptic damage [19].”
Omar, S. H., & Ghani, M. A. (2025) · Journal of Vascular Diseases · doi:10.3390/jvd4040044 · Cited by 1
“This interaction plays a key role in causing cognitive dysfunction in people with AD [40].”
Wang, X., Shen, Y., Lei, C., Chai, J., Tan, Q., & Qin, Y. (2025) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000549394 · Cited by 1
“The presence of β-Amyloid (Aβ) aggregates, a defining feature of AD pathology, facilitates abnormal p-tau through activation of key kinases, particularly GSK-3β and CDK-5, which phosphorylate tau at various serine and threonine sites [31].”
Rehman, S. U., Khan, S., Usman, M., & Ibrahim, S. K. (2025) · International Journal of Biosciences (IJB) · doi:10.12692/ijb/27.5.204-216 · Cited by 1
Chen, M., Tang, G., Zhang, Y., & Qian, Z. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00739 · Cited by 1
Wang, Y., Lv, M., Zhu, W., Yan, J., Shi, J., Qin, Z., Zhang, X., Yao, H., Meng, L., Liu, H., et al. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c05070 · Cited by 1
Alzheimer’s Disease and Gut Microbiota
Pandey, S., & Yadav, P. K. (2025) · Interdisciplinary biotechnological advances · doi:10.1007/978-981-95-2104-3_5 · Cited by 1
Understanding molecular role of lipids for Alzheimer’s disease
Upadhyay, R., Velmurugan, G., Krishnan, D., Sivasamy, R., Sevanan, M., & Chinnathambi, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.011 · Cited by 1
Catalytic Effect of Amyloid-β on Native Tau Aggregation at Physiologically Relevant Concentrations
Chowdhury, R., Das, A. C., van Deventer, R., Shlyakhtenko, L. S., & Lyubchenko, Y. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262412128 · Cited by 1
“Increasing evidence points to a synergistic relationship between A β and tau in AD [11–13].”
InfluentialCurcumin as a modulator of IL-18: A promising therapeutic approach for inflammatory diseases
Kavyani, M., Ghoflchi, S., Disfani, S. M., Jalili‐Nik, M., Sadeghi, A., Karav, S., Kesharwani, P., Hosseini, H., & Sahebkar, A. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.108211 · Cited by 2
Yu, W., Zhuang, D., Wang, K., & Qu, Y. (2026) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2025.2610481 · Cited by 1
Recent Advances of the Role of Dl-3-n-Butylphthalide in the Treatment of Alzheimer’s Disease
Huang, H., Wu, J., Fang, Z., Wang, Y., Xie, J., & Guan, Y. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05616-8 · Cited by 1
Liu, Z., Zhang, H., Wan, B., Yin, S., & Yue, R. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s580330 · Cited by 2
“170 Furthermore, tau was identified as the secondary agent in mixed pathology forms of PD, 171 MS, 172 and HD.”
Anschuetz, A., Listyono, R., Vorley, T., Platt, B., Harrington, C. R., Riedel, G., & Schwab, K. (2026) · Journal of Integrative Neuroscience · doi:10.31083/jin48581 · Cited by 1
Husain, A., Khanam, A., Khan, H., Rafi, Z., Shahab, U., Rab, S. O., Puri, P., & Ahmad, S. (2026) · Journal of Food Science · doi:10.1111/1750-3841.70817 · Cited by 2
Yang, Z., Zhang, M., Zhi, W., Lizhen, Hu, X., Zou, Y., & Wang, L. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27031492 · Cited by 3
“Consequently, therapeutic strategies developed over the past decades, largely rooted in the amyloid cascade hypothesis [15], have frequently encountered setbacks in clinical trials [16,17], highlighting the need for a more nuanced understanding of cell-type-specific responses and intercellular…”
Zhao, P., Fadel, O. E., Le, A., Mangleburg, C. G., Dhindsa, J. S., Wu, T., Zhao, J., Huang, M., Amoh, B. K., Marella, A. S., et al. (2026) · Molecular Psychiatry · doi:10.1038/s41380-026-03479-6 · Cited by 1
Idowu, A. O., Uti, D. E., Saliu, O. A., Tijjani, H., Akiode, S. O., Alum, E. U., Arise, R. O., Egbung, J. E., Almohaimeed, H. M., & Chatterjee, A. (2026) · In Silico Research in Biomedicine · doi:10.1016/j.insi.2026.100253 · Cited by 1
Zhao, M., Qu, Y., Zhang, S., Zhang, M., Wang, H. H., Yang, Y., Gu, X. F., Hou, X., & Yan, X. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1707688 · Cited by 1
“Overall, The deposition of A β is closely associated with tau protein pathological changes, and the two processes reinforce each other (Zhang et al., 2021).”
Jang, K.-B., Kang, D., Lee, M.-H., Lukianenko, N., Kim, Y. K., Lim, S., Kim, S., & Cho, H. J. (2026) · Scientific Reports · doi:10.1038/s41598-026-42195-7 · Cited by 1
“…amyloid beta and tau are reported to interact with each other rather than acting independently, accelerating the progression of neurodegeneration 54 and related studies were performed, which support the hypothesis that the synergistic interplay between amyloid beta and tau in Alzheimer’s…”
Pradhan, R., Kumari, S., Singh, A. K., Rao, A. R., Yadav, Y., Upadhyay, A. D., Mehta, P. K., Dey, A. B., & Dey, S. (2026) · The Indian Journal of Medical Research · doi:10.25259/ijmr_2164_2025 · Cited by 1
Pyo, B.-J., Lee, J., Lee, H. A., Won, K. S., & Kim, H. W. (2026) · Topics in Clinical Nutrition · doi:10.1097/tin.0000000000000416 · Cited by 1
Kushawaha, S. K., Vashisht, K., Kumar, H., Ankalgi, A. D., Ashawat, M. S., & Baldi, A. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02215-4 · Cited by 1
Natale, F., Dellaria, A., Sarrapochiello, I. N., Leone, L., Spinelli, M., Rinaudo, M., Garofalo, N., Grassi, C., & Fusco, S. (2026) · Alzheimer s Research & Therapy · doi:10.1186/s13195-026-02014-7 · Cited by 1
“It is now widely accepted that AD is characterized by the accumulation of amyloid-beta (Aβ) oligomers and the formation of neurofibrillary tangles (NFTs), which are neuropathological hallmarks also used as biomarkers or tracers in neuroimaging techniques [3–5].”
Singh, A., Sahu, S. K., & Sah, A. K. (2026) · BioMed Research International · doi:10.1155/bmri/5968529 · Cited by 1
“Tau and A β interact in feed-forward loops, where pathogenic tau increases synaptic dysfunction and neuronal death while A β oligomers drive tau phosphorylation and mislocalization [15].”
E3 ubiquitin ligases in neurodegenerative diseases
Hou, D. L., Ho, J., Guan, T., Dong, X.-X., Zeng, L., Sanders, L. H., Wu, Y., Tan, E., & Zhou, Z. D. (2026) · Military Medical Research · doi:10.1016/j.mmr.2026.100032 · Cited by 1
“…glial cytoplasmic inclusions (GCIs) [76]; extracellular A plaques and intracellular neurofibrillary tangles of hyperphosphorylated tau in AD [77,78] and cytoplasmic inclusions of TDP-43 or superoxide dismutase 1 (SOD1) in ALS, as well as cytoplasmic and nuclear aggregates of mHtt in HD [79-81].”
Zang, Z., Chen, F., Tang, Q., Luo, W., Lin, Y., Li, J., & Yu, Y. (2026) · Metabolites · doi:10.3390/metabo16050314 · Cited by 1
Caenorhabditis elegans as a Model Organism for Proteinopathies
Vimal, P., Verma, D., Bhunia, P. K., & Kasturi, P. (2026) · Springer eBooks · doi:10.1007/978-981-92-0038-2_9 · Cited by 2
Biberoğlu, K., & Tacal, Ö. (2026) · Drug Development Research · doi:10.1002/ddr.70330 · Cited by 1
Efficacy of antioxidants as a therapy for Alzheimer's disease: a meta-analysis
Li, J., Chen, B., Jiang, J., Feng, Y., Zhang, R., Li, D. M., Wang, R., Long, Z., Ge, L., Guo, Y., et al. (2026) · Frontiers in Nutrition · doi:10.3389/fnut.2026.1878597 · Cited by 1
“…as the primary pathogenic mechanism—wherein A β aggregation triggers tau hyperphosphorylation, synaptic dysfunction, and chronic neuroinflammation, and oxidative stress emerges as a key downstream mediator that amplifies neuronal damage, particularly in the hippocampus and cerebral cortex (9–11).”
Deepika, D., Kumar, J., Ali, S. A., Namdeo, A. G., & Flora, S. J. S. (2026) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2026.127929 · Cited by 1
Pharmacological Effects and Molecular Mechanisms of Lignans in the Treatment of Alzheimer’s Disease
Sun, L., Zhu, X., Fan, C., Wang, Y., Chen, Q., Zhang, L., Zhang, Y., & Liu, Y. (2026) · Molecules · doi:10.3390/molecules31152594 · Cited by 1
Ultrasensitive Assay Technologies
Yang, C. S.-Y., & Sabbagh, M. N. (2026) · Springer eBooks · doi:10.1007/978-3-032-23863-4_1 · Cited by 1
Metadata
- Authors
- Zhang, H., Wei, W., Zhao, M., Ma, L., Jiang, X., Pei, H., Cao, Y., & Li, H.
- Affiliations
- Xiyuan Hospital (CN)
- Beijing University of Chinese Medicine (CN)
- Corresponding author
- Cao, Yu
- Li, Hao
- Venue
- International Journal of Biological Sciences
- Publisher
- Ivyspring International Publisher
- Published
- 2021
- Volume
- 17
- Issue
- 9
- Pages
- 2181-2192
- ISSN
- 1449-2288 (ISSN-L)
- PMC
- PMC8241728
- OpenAlex
- W3166313369
- Cited by
- 689
- References
- 185
- Citations by year
- 2026: 182 · 2025: 268 · 2024: 141 · 2023: 73 · 2022: 22 · 2021: 3
- FWCI
- 37.38
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- International Journal of Biological Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81873350, 7202174)
- National Science and Technology Major Project
- 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, amyloid-beta, tau protein, tau phosphorylation, neuritic plaques, neurofibrillary tangles, microglia, astrocytes, tau aggregation, cognitive impairment, neurotoxicity
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Humans, Phosphorylation, Amyloid beta-Peptides, tau Proteins
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
