The DOI matches its Crossref record; 87 of the 88 references it cites were found in a registry or an index.
GSK3β and tau protein in Alzheimer's disease and epilepsy
Open accessAbstract
Alzheimer's disease (AD) is the most common form of dementia present in older adults; its etiology involves genetic and environmental factors. In recent years, epidemiological studies have shown a correlation between AD and chronic epilepsy since a considerable number of patients with AD may present seizures later on. Although the pathophysiology of seizures in AD is not completely understood, it could represent the result of several molecular mechanisms linked to amyloid beta-peptide (Aβ) accumulation and the hyperphosphorylation of tau protein, which may induce an imbalance in the release and recapture of excitatory and inhibitory neurotransmitters, structural alterations of the neuronal cytoskeleton, synaptic loss, and neuroinflammation. These changes could favor the recurrent development of hypersynchronous discharges and epileptogenesis, which, in a chronic state, favor the neurodegenerative process and influence the cognitive decline observed in AD. Supporting this correlation, histopathological studies in the brain tissue of temporal lobe epilepsy (TLE) patients have revealed the presence of Aβ deposits and the accumulation of tau protein in the neurofibrillary tangles (NFTs), accompanied by an increase of glycogen synthase kinase-3 beta (GSK3β) activity that may lead to an imminent alteration in posttranslational modifications of some microtubule-associated proteins (MAPs), mainly tau. The present review is focused on understanding the pathological aspects of GSK3β and tau in the development of TLE and 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
“Both GSK-3β and CDK5 play a role in neuronal excitability through involvement in GABAergic and glutamatergic neurotransmission, and inhibiting their activity can affect network activity through various mechanisms (Sen et al., 2008; Jaworski, 2020; Toral-Rios et al., 2020; Banerjee et al., 2021).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Toral-Rios et al., 2020
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“One relevant kinase responsible for tau phosphorylation is glycogen synthase kinase-3β (GSK-3β) (Toral-Rios et al., 2020).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Toral-Rios et al., 2020
In the citing paper
“Furthermore, increased GSK-3β activity also induces Aβ deposition extracellularly (Griebel et al., 2019;Toral-Rios et al., 2020).”
From Multi-target neuroprotective effects of herbal medicines for Alzheimer's disease (2022) · cites this paper as Toral-Rios et al., 2020
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
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
Buée, 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 2,142
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
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
The GSK3 hypothesis of Alzheimer’s disease
Hooper, C., Killick, R., & Lovestone, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05194.x · Cited by 1,191
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899
Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859
Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 763
Flagged first, then by citations
1 of the 88 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–159 of 159
Cai, H.-Y., Hou, F., Wang, Y., Wu, L.-H., Wang, Z.-J., Wu, M., Wang, X., & Hölscher, C. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177347 · Cited by 7
Ma, L., Wang, J., Zhou, R., Chen, M., Huang, Z., & Lin, S. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1528919 · Cited by 9
Navigating the treatment landscape of Alzheimer's disease: Current strategies and future directions
Mohapatra, T. K., Nayak, R. R., Ganeshpurkar, A., Tiwari, P. K., & Kumar, D. (2025) · Ibrain · doi:10.1002/ibra.12197 · Cited by 8
Majid, H., Dahalia, M., Hussain, S., Saini, S., & Nidhi, N. (2025) · Diabetology International · doi:10.1007/s13340-025-00830-0 · Cited by 7
Tong, M., Homans, C., Pelit, W. S., Delikkaya, B., & de la Monte, S. M. (2025) · Biomolecules · doi:10.3390/biom15030413 · Cited by 7
An updated research of glycogen synthase kinase-3β inhibitors: a review
Liu, S.-K., Xie, H.-X., Ge, Y.-X., Zhang, J., & Jiang, C. (2021) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-020-02718-y · Cited by 7
Dalvi, S., & Bhatt, L. K. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03757-6 · Cited by 7
Calcineurin inhibition may prevent Alzheimer disease in people with Down syndrome
Dohl, J., Treadwell, Z., Norris, C. M., & Head, E. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70034 · Cited by 6
Alves, S. S., Rossi, L., de Oliveira, J. A. C., Servilha‐Menezes, G., Grigório-de-Sant’Ana, M., Mazzei, R. F., Almeida, S. S., Sebollela, A. S., da Silva-Júnior, R. M. P., & Garcia‐Cairasco, N. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04844-2 · Cited by 6
Nader, S., Karlovich, E., Cortes, E. P., Insausti, R., Meloni, G., Jacobs, M. M., Crary, J. F., & Morgello, S. (2023) · Journal of NeuroVirology · doi:10.1007/s13365-023-01181-9 · Cited by 7
Dysregulated mTOR networks in experimental sporadic Alzheimer’s disease
de la Monte, S. M., & Tong, M. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1432359 · Cited by 6
Alhassan, H. H., Surti, M., Adnan, M., & Patel, M. B. (2025) · Pharmaceuticals · doi:10.3390/ph18060826 · Cited by 5
Yao, Q., dos Santos, A. C. M., Zhang, H., Mañas, A., Hussaini, A., Kim, U., Xu, C., Basheer, S., Tasaki, S., & Xiang, J. (2023) · Biomolecules · doi:10.3390/biom13060970 · Cited by 5
de Oliveira, B. A., de Oliveira, F. G., Cruz, O. D. A., de Assis, P. M., Glanzmann, N., da Silva, A. D., Raposo, N. R. B., & Goliatt, P. V. Z. C. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202401629 · Cited by 5
Alsfouk, B. A. A., Al-Kuraishy, H. M., Albuhadily, A. K., Al-Gareeb, A. I., Abdelaziz, A. M., Alexiou, A. T., Papadakis, M., Alruwaili, M., & Batiha, G. E. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111189 · Cited by 5
Animal models in Alzheimer's disease: Biological plausibility and mood disorders
Castillo-Rangel, C., Marín, G., Díaz-Chiguer, D. L., Zarate-Calderon, C., Viveros-Martínez, I., Salazar, F., Torres-Pasillas, J. G., Hernández-Contreras, K. A., Vega-Quesada, L. A., Cano-Ortega, Y., et al. (2023) · Neurology Perspectives · doi:10.1016/j.neurop.2023.100110 · Cited by 5
Akbari, S., Haghani, M., Ghobadi, M., Hooshmandi, E., Borhani‐Haghighi, A., Salehi, M. S., Pandamooz, S., Azarpira, N., Afshari, A., Zabihi, S., et al. (2023) · Stem Cells International · doi:10.1155/2023/3784843 · Cited by 5
Seo, S., Ham, D.-W., Lee, J.-E., & Shin, E. (2025) · Scientific Reports · doi:10.1038/s41598-025-00271-4 · Cited by 4
Yao, M., Liu, A., Song, J., Xing, L., Huang, Y., & Li, H. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149852 · Cited by 4
Londhe, S. G., Mangala, S. S., Kini, S. G., Walhekar, V. S., & Kumar, D. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266295740240602122613 · Cited by 4
Fukutin regulates tau phosphorylation and synaptic function: Novel properties of fukutin in neurons
Tsukui, R., Yamamoto, T., Okamura, Y., Kato, Y., & Shibata, N. (2022) · Neuropathology · doi:10.1111/neup.12797 · Cited by 4
Al‐Keridis, L. A., Al-Shuraym, L. A. M., Alshammari, N., Adnan, M., & Patel, M. B. (2024) · South African Journal of Botany · doi:10.1016/j.sajb.2024.10.008 · Cited by 3
Habib, M. Z., Kamar, S. A., Mostafa, M. O., Aboul-Ela, Y. M., Rabei, M. R., Kamel, M. M., Abdelrahman, S. E., Salama, A. A., Elshaer, M. M. A., Olama, N. K., et al. (2026) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2026.104958 · Cited by 3
Exploring Withanolides from Withania somnifera: A Promising Avenue for Alzheimer’s Disease Treatment
Pullaiah, C. P., Preethi Priyadharshini, S. P., Phareedha, S. K., Yamini, N., Birudala, G., Lahari, S., Vippamakula, S., Shakila, R., Ganjayi, M. S., & Raghavendra, M. (2025) · Current Pharmacology Reports · doi:10.1007/s40495-025-00394-2 · Cited by 4
Berezutsky, М. А., Дурнова, Н. А., Kurchatova, M. N., & Matvienko, U. A. (2025) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro20251250217 · Cited by 3
Varshini, M. S., Shanavas, S., Pindiprolu, S. S. S. K. S., Nagappan, K., More, S., Chaudhury, D., Reddy, R. A., Singh, M. T., Wadhwani, A., Bose, B., et al. (2025) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5c00329 · Cited by 4
Aladdin, N., & Ghareib, S. A. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70082 · Cited by 3
RetractedFeuer, K. L., Peng, X., Yovo, C., & Avramopoulos, D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.19.517191 · Cited by 3
Sindi, G., Ismael, S., Uddin, R., Slepchenko, K. G., Colvin, R. A., & Lee, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.02.597022 · Cited by 3
Phytotherapeutic targeting of the mitochondria in neurodegenerative disorders
Sarkar, P., Kumar, A. A., Behera, P. S., & Thirumurugan, K. (2023) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.02.013 · Cited by 2
Alzheimer’s Disease: An Attempt of Total Recall
Bolshakov, A. P., Gerasimov, K., & Dobryakova, Y. V. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240620 · Cited by 2
Khalilpour, J., Zangbar, H. S., Alipour, M. R., Pakdel, F. Q., Zavari, Z., & Shahabi, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03763-4 · Cited by 2
Reticulocalbin‐2 in the Hippocampus Improves Cognitive Function of Diabetic Mice
Zhang, T., Tang, S., Cheng, J., Hu, B., Xie, L., Cheng, Y., Chen, X., & Xie, G. (2026) · Brain and Behavior · doi:10.1002/brb3.71336 · Cited by 1
Mitochondrial Dysfunction in Alzheimer’s Disease and Mitochondria-Targeted Therapeutics
Bisht, J., Rawat, P., Shin, A. C., & Hegde, V. (2026) · Cells · doi:10.3390/cells15110990 · Cited by 1
Angarita-Rodríguez, A., Vargas-López, V., Pinzón, A., Sandoval-Hernandez, A., Kang, K., Li, L., Papin, J., Rozo, P. J. P., Aristizábal, A., & González, J. (2026) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2026.1816121 · Cited by 1
Uso de lenguaje R en la exploración de hallazgos neurocientíficos en México:
Aguilar, X. T., Lozada, E. R. P. B., & Olvera, D. M. C. F. (2024) · Transdigital · doi:10.56162/transdigital289 · Cited by 1
Inhalation exposure-induced toxicity and disease mediated via mTOR dysregulation
Shinde, A., & Shannahan, J. H. (2024) · Experimental Biology and Medicine · doi:10.3389/ebm.2024.10135 · Cited by 1
Vitamin E (Tocopherol): Implications in Cardiovascular Health and Neuroprotection
Parameswari, R., Anand, M. A. V., Wang, C., Babaujanarthanam, R., & Nagarajan, P. (2024) · Advances in biochemistry in health and disease · doi:10.1007/978-3-031-55489-6_12 · Cited by 1
Parkinson’s Disease and Epilepsy: A bioinformatics analysisPreprint
Aryaee, A., Azedi, F., Ketabforoush, A. H. M. E., Rad, N. A., & Golab, F. (2023) · Research Square · doi:10.21203/rs.3.rs-3257860/v1
Pereira, A. L. (2023) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2023.tde-10112023-155452
The biochemical pathways of Alzheimer's disease
El-Gammal, M. A., & Kodous, F. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15702-8.00001-4
Elfaki, E. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Albuhadily, A. K., Eliwa, D., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.10.045
Khare, N., Kumar, A., Jain, T., & Singh, S. (2026) · Next research. · doi:10.1016/j.nexres.2026.101463
Su, R., & Yang, Q.-Y. (2026) · New cell · doi:10.61958/ncjg8269
Tau Accumulation Increases the Susceptibility to Effective Seizures of Electroconvulsive Therapy
Ohya, T., Arakawa, R., Sakayori, T., Nogami, T., Uchiyama, S., & Tateno, A. (2026) · Translational Psychiatry · doi:10.1038/s41398-026-04016-3
Mewada, D., Tomar, M., & Goyal, M. (2026) · Premier journal of science. · doi:10.70389/pjs.100272
Shanmuganathan, D. K., Pranav, D. H., & Ariharasivakumar, G. (2026) · In Silico Research in Biomedicine · doi:10.1016/j.insi.2026.100338
Corneal Immune Cell Alterations and Tau Pathology in a Mouse Model of Alzheimer’s Disease
Zhang, D., Huang, D., He, J., Shen, Y., Dai, L., & Shi, L. (2026) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.67.5.20
Trivedi, S. J., Roy, S. M., & Roy, D. R. (2026) · Interactions · doi:10.1007/s10751-026-02575-x
Dietary anthocyanins and the MAPK signaling pathway: from food sources to molecular mechanisms
Luo, J., Luo, J., Han, B., & Xu, B. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119932
Wang, Y., Qin, S., Gong, X., Bai, H., Li, S., Cai, H., Hu, Y., Zhao, Y., Bai, M., Song, C., et al. (2026) · Brain Research · doi:10.1016/j.brainres.2026.150474
Anwer, T., Verma, A., Asiri, A., Alaklobie, M., Albaqami, A., ALSHAHRANI, F., Aly, K., Sharma, M., Siddiqui, S., Alam, N., et al. (2026) · Journal of Molecular Neuroscience · doi:10.1007/s12031-026-02587-w
Xu, Y., Xia, X., Wang, Y., Xue, K., Wei, Y., Li, L., & Meng, X. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1879851
Kaur, R., Lang, D. K., Sood, A., Singh, T. G., Chandrasekaran, B., & Al-Sha’er, M. A. (2026) · RSC Advances · doi:10.1039/d6ra03269a
Chen, H., Zhang, L., Jiao, B., Sun, X., Guan, L., Niu, R., Li, B., Jiang, X., & Wu, Z. (2026) · Pharmaceuticals · doi:10.3390/ph19091457
Nimavard, R. T., Sadeghi, S. A., Colón-Rosado, J. A., Yue, Y., Fang, F., Hagar, H. C., Kuo, M.-H., & Sun, L. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00539
BindingDB (2023) · UC San Diego · doi:10.7270/q2zg6xb2
BindingDB Entry 50019411: Glycogen synthase kinase-3: A potential target for diabetes.
BindingDB (2024) · UC San Diego · doi:10.7270/q2rn3d6s
Metadata
- Authors
- Toral-Rios, D., Pichardo-Rojas, P. S., Alonso-Vanegas, M., & Campos-Peña, V.
- Affiliations
- Universidad Autónoma de Baja California (MX)
- Venue
- Frontiers in Cellular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2020-03-17
- Volume
- 14
- Pages
- 19-19
- ISSN
- 1662-5102 (ISSN-L)
- PMC
- PMC7089874
- OpenAlex
- W3012558556
- Cited by
- 158
- References
- 88
- Citations by year
- 2026: 18 · 2025: 28 · 2024: 35 · 2023: 31 · 2022: 25 · 2021: 15 · 2020: 6
- FWCI
- 11.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Greater South Information System
- Funders
- Consejo Nacional de Ciencia y Tecnología (S0008)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Epilepsy research and treatment
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, epilepsy, temporal lobe epilepsy, GSK3β, tau protein, tau hyperphosphorylation, amyloid-beta, neurofibrillary tangles, epileptogenesis, seizures, neuroinflammation, synaptic loss, cognitive decline, microtubule-associated 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
