The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
A Phase II Trial of Tideglusib in Alzheimer's Disease
Abstract
BACKGROUND: The ARGO study was a phase II, double-blind, placebo controlled, four parallel arm trial of tideglusib in Alzheimer's disease (AD). OBJECTIVE: To prove the clinical efficacy of an inhibitor of glycogen synthase kinase-3 (GSK-3), in AD. METHODS: Mild to moderate (Mini-Mental State Examination (MMSE) score, 14-26) AD patients on cholinesterase inhibitor and/or memantine treatment were administered tideglusib or placebo for 26 weeks. The ADAS-cog15 was the primary efficacy measure; function, cognition, behavior, and quality of life were assessed as secondary measures; cerebral atrophy in MRI and the levels of tau, amyloid-β, and BACE1 in cerebrospinal fluid (CSF) were exploratory endpoints. RESULTS: 306 AD patients were randomized to active (1000 mg QD: n = 86, 1000 mg QOD: n = 90, and 500 mg QD: n = 50) or placebo (n = 85) in 55 sites in four European countries. There were no statistically significant differences between either active and placebo arms in the efficacy variables. However, BACE1 in CSF significantly decreased with treatment in a small subgroup of patients. Participants with mild AD in the 500 mg QD group showed significant responses on ADAS-cog15, MMSE, and word fluency. Diarrhea (14-18% in active, 11% placebo) and dose-dependent, mild to moderate, and fully reversible transaminase increase (9-16% in active, 3.5% placebo) were the most frequent adverse events. CONCLUSIONS: Short term (26 weeks) tideglusib was acceptably safe but produced no clinical benefit in this trial. However, given the non-linear dose response, especially in mildly affected patients, further dose finding studies in early disease stages and for longer duration are warranted to examine GSK-3 inhibition in AD patients.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Moreover, use of tau kinase inhibitors such as the GSK-3 inhibitor Tideglusib to attenuate pathological tau hyperphosphorylation also showed little or no efficacy in Phase 2 trials, probably due to the critical role of GSK-3 in multifunctional signaling pathways [650, 651].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [650]
In the citing paper
“Moreover, use of tau kinase inhibitors such as the GSK-3 inhibitor Tideglusib to attenuate pathological tau hyperphosphorylation also showed little or no efficacy in Phase 2 trials, probably due to the critical role of GSK-3 in multifunctional signaling pathways [650, 651].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [650]
In the citing paper
“The clinical studies in patients with mild-to-moderate AD (NCT01350362, NCT00948259) or PSP (NCT01049399) patients treated with tideglusib were negative on the clinical outcomes [218]; however, a subgroup analysis of PSP patients showed reduced brain atrophy [219].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [218]
In the citing paper
“However, a phase 2 trial in mild to moderate AD did not demonstrate any reduction in rate of cognitive or functional decline as compared to placebo (Lovestone et al., 2015)”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Lovestone et al., 2015
In the citing paper
“Tideglusib, a small-molecule GSK3β inhibitor, failed to improve cognition in a phase 2 clinical study, and CSF levels of Aβ42, total tau, and pTau181 were not altered, resulting in failure of the trial [175,176].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [176]
In the citing paper
“In a larger phase II study, tideglusib treatment was associated with significant cognitive improvement and a reduction in CSF levels of β-secretase in a subgroup of patients with mild AD122. However, when the entire study cohort was analysed, tideglusib was found to be well tolerated but produced no significant improvements122.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [122]
In the citing paper
“Another GSK-3 inhibitor, tideglusib, did not meet phase 2 clinical endpoints in patients with mild and moderate AD.80”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [80]
Citations
Cites
Folstein, M. F., Folstein, S. E., & McHugh, P. R. (1975) · Journal of Psychiatric Research · doi:10.1016/0022-3956(75)90026-6 · Cited by 88,282
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
The Neuropsychiatric Inventory: Comprehensive assessment of psychopathology in dementia
Cummings, J. L., Mega, M., Gray, K., Rosenberg-Thompson, S., Carusi, D. A., & Gornbein, J. (1994) · Neurology · doi:10.1212/wnl.44.12.2308 · Cited by 7,568
Sheikh (1986) · doi:10.1300/j018v05n01_09 · Cited by 7,236
EQ-SD: a measure of health status from the EuroQol Group
Rabin, R., & Charro, F. D. (2001) · Annals of Medicine · doi:10.3109/07853890109002087 · Cited by 5,613
The Alzheimer’s disease neuroimaging initiative (ADNI): MRI methods
Jack, C. R., Bernstein, M. A., Fox, N. C., Thompson, P., Alexander, G., Harvey, D., Borowski, B., Britson, P. J., L. Whitwell, J., Ward, C., et al. (2008) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.21049 · Cited by 4,347
A New Rating Scale for Age-Related White Matter Changes Applicable to MRI and CT
Wahlund, L., Barkhof, F., Fazekas, F., Bronge, L., Augustin, M., Sjögren, M., Wallin, A., Adèr, H., Leys, D., Pantoni, L., et al. (2001) · Stroke · doi:10.1161/01.str.32.6.1318 · Cited by 1,838
Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease
Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668
The glamour and gloom of glycogen synthase kinase-3
Jope, R. S., & Johnson, G. V. W. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.12.004 · Cited by 1,535
Guy, W. L. (2025) · Springer Reference Medizin · doi:10.1007/978-3-662-65186-5_300379 · Cited by 1,441
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 556
Regulation of selective class switching provides long-term therapeutic benefits for hay fever
Morita, N., Yamamoto, K., Tamano, R., Gao, P., Nagatake, T., Inomata, T., Huang, T., Yamada, Y., Adachi, T., Sugai, M., et al. (2025) · JCI Insight · doi:10.1172/jci.insight.190240 · Cited by 4
Targeted tau protein degradation: a promising therapeutic approach for tauopathies
Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5
Huang, Y., Chan, H., Khoo, J.-Y., Chan, M.-L., Bender, D. A., Ponnusamy, V. K., Belaidi, A. A., & Ke, L. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.106104 · Cited by 4
Advances in Diagnostics and Treatments for Alzheimer’s Disease
Sunderland, A., Thatcher, A. L., Rackley, E. V., & Kuruvilla, T. (2025) · British Journal of Hospital Medicine · doi:10.12968/hmed.2025.0492 · Cited by 4
Alzheimer’s Disease: Evolving Therapeutics, Scientific Progress, and Key Challenges
Sai Yasasvi, K., Goswami, A. K., Prasad, M. R., Chauhan, V. S., & Yadav, N. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02468 · Cited by 4
Chen, M., Fang, Y., Zhang, M., Ge, Y., Junejo, S. Z., & Gong, R. (2026) · Metabolism · doi:10.1016/j.metabol.2026.156571 · Cited by 14
Targeting of kinases to treat neurodegenerative diseases
Shomali, T., & Trempe, J.-F. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100128 · Cited by 4
Chromatin-modifying agents convert fibroblasts to OCT4+ and VEGFR-2+ capillary tube-forming cells
Wary, A., Wary, N. K., Baruah, J., Mastej, V., & Wary, K. K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176496 · Cited by 4
Chen, T., Lin, S.-P., Huang, D.-F., Huang, H., Tsai, F., Lee, L.-J., Lin, H.-Y., & Huang, H. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06692-9 · Cited by 4
Recent Molecular Targets and their Ligands for the Treatment of Alzheimer Disease
Bayraktar, G., & Alptüzün, V. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266318722240809050235 · Cited by 4
Chau, S. A., Liu, C. S., Ruthirakuhan, M. T., Lanctôt, K. L., & Herrmann, N. (2016) · Mental health and illness worldwide · doi:10.1007/978-981-10-0370-7_20-1 · Cited by 5
Novel Modality of GSK-3 Inhibition For Treating Neurodegeneration
Rippin, I., & Eldar-Finkelman, H. (2018) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2018/6.1227 · Cited by 4
Neuropathology of a patient with Alzheimer disease treated with low doses of verubecestat
Querol‐Vilaseca, M., Sirisi, S., Molina‐Porcel, L., Molina-Esteve, B., Pegueroles, J., Ferrer‐Raventós, P., Núñez‐Llaves, R., Dols‐Icardo, O., Balasa, M., Iulita, M. F., et al. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12781 · Cited by 4
Evidence for investigating GSK-3 inhibitors as potential therapeutics for severe COVID-19
Ghazanfari, D., Courreges, M. C., Belinski, L., Bergmeier, S. C., McCall, K. D., & Goetz, D. J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.035 · Cited by 4
Zhang, H., Chen, W., Li, Z., Huang, Q., Wen, J., Chang, S., Pei, H., Ma, L., & Li, H. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116985 · Cited by 4
An Emerging Role for Megalin as a Regulator of Protein Leak in Acute Lung Injury
Suber, T. L., & Mallampalli, R. K. (2017) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2017-0224ed · Cited by 4
Drug Discovery from Medicinal Plants against Alzheimer's Disease
Marzouk, M. M., Farid, M. M., Hegazi, N. M., & Ezzat, S. M. (2023) · Wiley eBooks · doi:10.1002/9781119794127.ch3 · Cited by 4
Cognitive Enhancers and Treatments for Alzheimer’s Disease
Devanand, D. P., & Fremont, R. (2023) · Springer eBooks · doi:10.1007/978-3-030-42825-9_139-1 · Cited by 3
Role of GSK-3 Inhibition in Alzheimer’s Disease Therapy
Algazzawi, H., Abujamai, J. Z., Alshanberi, A. M., Satar, R., & Ansari, S. A. (2025) · Current Alzheimer Research · doi:10.2174/0115672050400781250904082943 · Cited by 3
Wang, J., Wang, D., Liu, F., Ji, Y., Peng, X., & Li, G. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109053 · Cited by 3
Odabaş, E. V., Ünal, S., Alemdag, B., Gündüz, O., Tekkeşin, M. S., Türet, D. M., Kuru, L., & Ağralı, Ö. B. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149333 · Cited by 3
Alzheimer’s disease: a clinical update on diagnosis and treatment
Shir, D., & Lachner, C. (2026) · Neurologia i Neurochirurgia Polska · doi:10.5603/pjnns.109190 · Cited by 3
Post-translational modifications as a regulatory code for tau function in health and disease
Nordbeck, A. J., Sharma, B., Garcia, C. A., & Tseng, J. (2026) · Frontiers in Dementia · doi:10.3389/frdem.2026.1834737 · Cited by 3
Yang, Y., Lin, T., & Huang, Y. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176615 · Cited by 3
Mehrani, R., Mondal, J., Ghazanfari, D., Goetz, D. J., McCall, K. D., Bergmeier, S. C., & Sharma, S. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00311 · Cited by 3
Niazi, S. K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810211 · Cited by 3
Emmerich, T. D., Taylor-Chilton, E. J., Caballero, E., Hushcha, I., Dickens, K., Stasik, I., Alder, J. E., Saavedra-Castano, S., Berenschot, E., Tas, N. R., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00377 · Cited by 3
Saini, M., Rohilla, S., & Kumar, R. (2025) · Current Aging Science · doi:10.2174/0118746098376646250715094707 · Cited by 3
Zakaria, N. H., Tap, F. M., Aljohani, G. F., & Majid, F. A. A. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2298726 · Cited by 3
Immunotherapeutics for AD: A Work in Progress
Sharma, A., Anand, J. S., & Kumar, Y. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666210903101522 · Cited by 3
Elturki, F. F., Farid, M., & Adawy, H. (2021) · Al-Azhar Dental Journal for Girls · doi:10.21608/adjg.2021.28291.1248 · Cited by 3
Singh, A., Singh, D., Tiwari, N. K., Mittal, P., Siddiqui, M. H., & Mittal, N. (2024) · In Silico Pharmacology · doi:10.1007/s40203-024-00238-9 · Cited by 3
Cognitive Enhancers and Treatments for Alzheimer’s Disease
Devanand, D. P., & Fremont, R. (2024) · Springer eBooks · doi:10.1007/978-3-030-51366-5_139 · Cited by 3
How does “Protein Corona” Affect the In vivo Efficiency of Polymeric Nanoparticles? State of Art
(2017) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781681084930117020011 · Cited by 4
Antoniou, N., Prodromidou, K., Kouroupi, G., Samiotaki, M. K., Panayotou, G., Xilouri, M., Stefanis, L., Grailhe, R., Taoufik, E., & Matsas, R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.12.148031 · Cited by 3
Boesger, H. A., Williams, K., Abdullai, S. A., Hubble, B., Noori, M. S., Orac, C. M., Amesaki, D., Ghazanfari, D., Fairchild, E. A., Fatunbi, O. O., et al. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.130074 · Cited by 2
Querfurth, H. W., Lemere, C. A., Ciola, J., Havas, D., Xia, W., & Lee, H. K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083473 · Cited by 2
Tau protein aggregation: A therapeutic target for neurodegenerative diseases
Duggal, A., Mahindru, D., Baghel, K., Mehrotra, S., & Prajapati, V. K. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.012 · Cited by 2
Imaging microtubule dynamics: A new frontier in biomarker development for neurodegenerative diseases
Damuka, N., Lockhart, S. N., & Sai, K. K. S. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70670 · Cited by 4
Gong, S., Han, L., Wang, Y., Feng, Y., Wang, R., Zhang, S., Nie, K., Wang, B., Du, F., Guan, J., et al. (2026) · PLoS ONE · doi:10.1371/journal.pone.0345372 · Cited by 2
Demuro, S., Russo, D., Penna, I., Grabska, S., Grabski, H., Vedove, A. D., Valeri, A., Sauvey, C., Ottonello, G., Summa, M., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01810 · Cited by 3
Tkemaladze, J. (2026) · Longevity Horizon · doi:10.65649/9347j1ap · Cited by 2
HMGB1 signalling in Alzheimer’s disease: pathogenic roles and therapeutic prospects
Tyagi, P., Kumari, S., Sharma, P., Dhapola, R., Paidlewar, M., Medhi, B., & HariKrishnaReddy, D. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117204 · 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
Highlights from the Literature
Huse, J. T., Abounader, R., Purow, B. W., Hegi, M. E., Soffietti, R., & Aldape, K. (2016) · Neuro-Oncology · doi:10.1093/neuonc/now215 · Cited by 2
Frontotemporal lobar degeneration
Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3
Memory formation in old age requires GSK-3β
Koike, R., Takaichi, Y., Soeda, Y., & Takashima, A. (2021) · Aging Brain · doi:10.1016/j.nbas.2021.100022 · Cited by 2
Targeted engagement of β-catenin-Ikaros complexes in refractory B-cell malignanciesPreprint
Cosgun, K. N., Jumaa, H., Robinson, M. E., Kistner, K. M., Xu, L., Xiao, G., Chan, L. N., Lee, J. W., Kume, K., Léveillé, E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.13.532152 · Cited by 2
Tau-Centric Therapies for Treating Alzheimer’s Disease
Quraishe, S., Cowan, C. M., & Mudher, A. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00005-3 · Cited by 1
Opitz, A., Seitz, L.-M., Kryštof, V., Baselious, F., Holzer, M., Sippl, W., & Hilgeroth, A. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2022-0061 · Cited by 1
Inhibition of TGF-beta signaling protects from alpha-synuclein induced toxicity
Chua, O. W. H., Duan, L., Bothe, S., Evsyukov, V., Moebius, C., Bickle, M., Höglinger, G. U., & Höllerhage, M. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02901-2 · Cited by 1
Treatment options for Alzheimer’s Disease: An overview of the amyloid, tau, and alternate hypotheses
Eroltu, K. (2023) · Journal of High School Science · doi:10.64336/001c.89250 · Cited by 1
Ahmad, H. A., Zafar, M., Khan, T., & Khan, M. I. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-026-05505-1 · Cited by 1
Targeting Wnt signaling in Alzheimer’s disease: mechanisms and therapeutic opportunities
Zhao, X., Yang, R., Wu, J., & Sima, J. (2026) · Aging Research · doi:10.26599/agr.2026.9340068 · Cited by 1
Developments in the design and therapeutic applications of GSK3β inhibitors
Daoud, S., & Taha, M. O. (2026) · Future Medicinal Chemistry · doi:10.1080/17568919.2026.2675873 · Cited by 1
Advances in the treatment of Alzheimer’s disease
Goceroglu, R. T., & Hacımüftüoğlu, A. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1819165 · Cited by 1
Cao, K., Shang, H., Li, Y., Tan, Y., Li, M., M, Y., Cai, X., & Tang, Z. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s621268 · Cited by 1
Molecular Imaging and Precision Medicine in Dementia and Movement Disorders
Mallik, A. K., Drzezga, A. E., & Minoshima, S. (2016) · PET Clinics · doi:10.1016/j.cpet.2016.08.003 · Cited by 1
[Progress of clinical trials in Alzheimer’s disease drugs].
Peng, Y., Li, P., Li, L., Zhang, Y., Hou, W.-Z., Cui, D.-D., Li, J., Wang, L., Wang, Q., & Wang, X. (2016) · PubMed · Cited by 1
Comprehensive Review on Alzheimer’s Disease: Natural Therapeutics, Gaps, and Challenges
Mishra, P. S., Mishra, R., & Kumar, A. (2024) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/0118715249307525240614073143 · Cited by 1
Chettupalli, A. K., Gupta, N., Bukke, S. P. N., Singh, M. P., & Mandal, C. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118803 · Cited by 1
Tau Phosphorylation as a Therapeutic Target in Alzheimer’s Disease
Medina, M., & Ávila, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00012-5 · Cited by 1
In search of Alzheimer’s disease treatment methods: trends of clinical trials
Pakulaite-Kazliene, G., Regelskytė, V., Audronytė, E., Kuzmickienė, J., & Kaubrys, G. (2018) · Neurologijos seminarai · doi:10.29014/ns.2018.03 · Cited by 1
Anti-Tau-Therapien – was können wir erwarten?
Fließbach, K., McCormick, C., Kaulen, B., & Schneider, A. (2019) · Der Nervenarzt · doi:10.1007/s00115-019-0758-7 · Cited by 1
Lee, M. J. (2019) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2019.169 · Cited by 1
Therapieentwicklungen bei der Alzheimer-Krankheit
Grimmer, T. (2022) · Fortschritte der Neurologie · Psychiatrie · doi:10.1055/a-1802-4837 · Cited by 1
Deshpande, R. (2022) · Medicinal & Analytical Chemistry International · doi:10.23880/macij-16000174 · Cited by 1
Alzheimer's disease therapeutics
Sang, Z., & Huang, L. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18611-0.00031-0 · Cited by 1
The evolution of Alzheimer’s disease therapies: A comprehensive review
Paul, P., Bhattacharjee, A., Bordoloi, S. K., & Paul, U. K. (2024) · Annals of Medical Science and Research · doi:10.4103/amsr.amsr_37_23 · Cited by 1
Current and Prospective Treatments for Alzheimer's Disease (and Other Neurodegenerative Diseases)
Pedrini, S., Morici, M., & Martins, R. N. (2019) · Wiley eBooks · doi:10.1002/9781119356752.ch14 · Cited by 1
Broad kinase inhibition mitigates early neuronal dysfunction and cognitive deficits in tauopathyPreprint
Koren, S. A., Hamm, M. J., Cloyd, R., Fontaine, S. N., Chishti, E. A., Lanzillotta, C., Rodriguez-Rivera, J., Ingram, A., Bell, M. C., Escobar, S. M. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.31.229583 · Cited by 1
Cooper, A. S., Richardson, B., Ruiz, E., Zhang, Y., Batchelor, B., Chithran, A. V., Liu, J., Lian, T., Moreno, M. R., Boehme, B., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.22.629946 · Cited by 1
Gottlieb, S., Zeliff, D., O'Rourke, B., Rogers, W. D., & Miles, M. F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.03.647116 · Cited by 1
Strategies for Neuroprotection in Alzheimer's Disease
Jasutkar, H. G. (2025) · Wiley eBooks · doi:10.1002/9783527844678.ch5 · Cited by 1
Steady-State Visually Evoked Potentials as Readouts for Abnormal GSK3β Activity in DrosophilaPreprint
Solis, O., Shaw-McGrath, T., Wade, A. R., & Hahn, I. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.24.684304 · Cited by 1
Kilimann, I., Grothe, M. J., Thyrian, J. R., & Teipel, S. J. (2016) · InFo Neurologie + Psychiatrie · doi:10.1007/s15005-016-1588-9
Inhibition of Alzheimer’s type toxic aggregates of tau with fungal secondary metabolites
Paranjape, S. R. (2015) · KU ScholarWorks (University of Kansas)
Substanz(en) Firma/Institution Studienname Phase/Status Teilnehmer (Anzahl) Ergebnisse Referenzen
Janssen, B., Lilly, S. E., & Uni, W. (2016)
Present and Future Therapies for Alzheimer’s Disease
Nagase, H., & Nakayama, K. (2018) · InTech eBooks · doi:10.5772/intechopen.75449
Molecular Defects in the DM Central Nervous System
Kimura, T. (2018) · Springer eBooks · doi:10.1007/978-981-13-0508-5_7
Muthuraman, A., Ramesh, M., & Kumar, T. V. R. (2020) · Springer eBooks · doi:10.1007/978-981-15-5167-3_6
Effects of anle138b treatment on amyloid-β neurotoxicity
Thomas, C. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8233
Pathogenesis of Alzheimer’s disease and its treatments: A systematic review
Lou, Y., Sun, S., & Tan, J. (2021) · E3S Web of Conferences · doi:10.1051/e3sconf/202130802012
Highlights from the Literature
Schiff, D., Lawler, S. E., Chamberlain, M. C., Wright, K. D., & Bhat, K. (2016) · Neuro-Oncology · doi:10.1093/neuonc/now264
Evaluation of Pathological Perspectives Related to Alzheimer’s Disease
Song, Q. (2023) · Lecture Notes in Education Psychology and Public Media · doi:10.54254/2753-7048/3/2022582
Deciphering New Drug Targets in Alzheimer’s Disease
Verma, N., Thapa, K., Kanojia, N., Kaur, G., Sood, P., & Dua, K. (2023) · Springer eBooks · doi:10.1007/978-981-99-2657-2_1
Current Drugs Strategies for Treatment of Rare Neurodegenerative Diseases
Al-Kaf, A. G., & Alyahawi, A. A. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1005438
A Comprehensive Review on Alzheimer’s Disease; Pathophysiology and Treatment
Nandini, N., & Cyriac, K. S. (2024) · International Journal of Pharmaceutical Sciences Review and Research · doi:10.47583/ijpsrr.2024.v84i06.007
Treatment strategies used for Alzheimer's disease
Kar, K. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15540-6.00007-0
Chan, D., Spires‐Jones, T. L., Provenzano, F. A., Glennon, E. B. C., & Duff, K. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780190065324.003.0020
Saadh, M. J., Hussein, W. S., Alfarttoosi, K. H., Bishoyi, A. K., Roopashree, R., Kundlas, M., Chennakesavulu, K., Kubaev, A., Taher, W. M., Alwan, M., et al. (2025) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416525500565
Amyloid- and Tau-Targeted Therapies in Alzheimer’s Disease
Rajic, A. J., Galasko, D. R., & Tuszynski, M. H. (2025) · Springer eBooks · doi:10.1007/978-3-031-89307-0_17
Tripathi, S., Sharma, Y., & Kumar, D. (2025) · Current Signal Transduction Therapy · doi:10.2174/0115743624366360250630070154
Elgamily, M., Denewar, M., Emam, A. A., Othman, B., & Sultan, N. (2025) · Odontology · doi:10.1007/s10266-025-01203-4
Fanlo-Ucar, H., Planas-Clopes, C., Bagudanch, O., Pardo, C., Troncoso-Cotal, S., Alvarez, A. R., Oliva, B., & Muñoz, F. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.03.686297
Neuronal GSK3β Protects Against Amyloid Pathology by Regulating APP Degradation
Zhang, Y., Zhang, Y., Ge, C., Liu, Y., Wang, Z., & Chen, G. (2025) · The FASEB Journal · doi:10.1096/fj.202502996r
Hallucinogenic Therapy in Alzheimer’s Disease targeting Mitochondria-Associated Membranes
Minauro‐Sanmiguel, F., & Vargas-Pérez, H. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.02.028
Singh, S., Kaur, A., Banerjee, S., Sharma, T., & Singh, T. (2026) · Metabolic Brain Disease · doi:10.1007/s11011-026-01804-0
Metadata
- Authors
- Lovestone, S., for the ARGO investigators, Boada, M., Dubois, B., Hüll, M., Rinne, J. O., Huppertz, H.-J., Calero, M., Andrés, M. V., Gómez-Carrillo, B., León, T., & del Ser, T.
- Affiliations
- University of Oxford (GB)
- Fundació ACE (ES)
- Memory Clinic of Fundació ACE, Institut Català de Neurociències Aplicades, Barcelona, Spain
- Inserm (FR)
- University of Turku (FI)
- Instituto de Salud Carlos III (ES)
- Clinical Department, Noscira SA, Madrid, Spain
- Medical Department, Noscira SA, Madrid, Spain
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2015-03-03
- Volume
- 45
- Issue
- 1
- Pages
- 75-88
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- OpenAlex
- W1522284801
- Cited by
- 536
- References
- 47
- Citations by year
- 2026: 44 · 2025: 67 · 2024: 59 · 2023: 46 · 2022: 38 · 2021: 59 · 2020: 61 · 2019: 31 · 2018: 46 · 2017: 39 · 2016: 31 · 2015: 14
- FWCI
- 32.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion)
- Funders
- National Institute for Health and Care Research (NF-SI-0512-10053)
- 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
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Keywords
- tideglusib, Alzheimer's disease
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Apolipoproteins E, Dose-Response Relationship, Drug, Double-Blind Method, Enzyme-Linked Immunosorbent Assay, Female, Follow-Up Studies, Humans, Male, Middle Aged, Psychiatric Status Rating Scales, Thiadiazoles, Amyloid beta-Peptides, Neuroprotective Agents
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
