The DOI matches its Crossref record; 275 of the 278 references it cites were found in a registry or an index.
Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance
Open accessAbstract
Alzheimer's disease (AD) is the most common form of dementia characterized by presence of extracellular amyloid plaques and intracellular neurofibrillary tangles composed of tau protein. Currently there are close to 50 million people living with dementia and this figure is expected to increase to 75 million by 2030 putting a huge burden on the economy due to the health care cost. Considering the effects on quality of life of patients and the increasing burden on the economy, there is an enormous need of new disease modifying therapies to tackle this disease. The current therapies are dominated by only symptomatic treatments including cholinesterase inhibitors and N-methyl-D-aspartate receptor blockers but no disease modifying treatments exist so far. After several failed attempts to develop drugs against amyloidopathy, tau targeting approaches have been in the main focus of drug development against AD. After an overview of the tauopathy in AD, this review summarizes recent findings on the development of small molecules as therapeutics targeting tau modification, aggregation, and degradation, and tau-oriented multi-target directed ligands. Overall, this work aims to provide a comprehensive and critical overview of small molecules which are being explored as a lead candidate for discovering drugs against tauopathy in 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?
In the citing paper
“Methylene blue blocks the polymerisation of tau in vitro by trapping the tau monomers in an aggregation-incompetent conformation.”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [190]
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
Janczura, K. J., Volmar, C.-H., Sartor, G. C., Rao, S. J., Ricciardi, N. R., Lambert, G., Brothers, S. P., & Wahlestedt, C. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805436115 · Cited by 183
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
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
Neurofibrillary 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
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Memantine in Moderate-to-Severe Alzheimer's Disease
Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories
Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118
Research works printed but not linked: 2
- Howard, 2020, vol. 77, 164
- Ballatore, 2012, Aminothienopyridazine inhibitors of tau aggregation: evaluation of structure-activity relationship leads to selection of candidates with desirable in vivo properties, Bioorg, Med. Chem., 20, 4451
Cited by
Sorted by citations
The Expanding Role of Pyridine and Dihydropyridine Scaffolds in Drug Design
Ling, Y., Hao, Z., Liang, D., Zhang, C., Liu, Y., & Wang, Y. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s329547 · Cited by 428
Challenges and hopes for Alzheimer’s disease
Tatulian, S. A. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.01.016 · Cited by 291
The SARS‐CoV‐2 main protease (M pro ): Structure, function, and emerging therapies for COVID‐19
Hu, Q., Xiong, Y., Zhu, G., Zhang, Y., Zhang, Y., Huang, P. C., & Ge, G. (2022) · MedComm · doi:10.1002/mco2.151 · Cited by 270
Kumar, V., Kim, S.-H., & Bishayee, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179540 · Cited by 116
Fišar, Z. (2022) · Biomolecules · doi:10.3390/biom12111676 · Cited by 113
The therapeutic landscape of tauopathies: challenges and prospects
Cummings, J. L., González, M. I., Pritchard, M. C., May, P. C., Toledo, L. M., & Harris, G. A. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01321-7 · Cited by 85
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63
“The methylene blue derivative LMTX (TRx0237) is a small-molecule tau protein aggregation inhibitor that prevents tau protein aggregation or degrades preexisting aggregates [190].”
BackgroundKim, S., Kim, D. K., Jeong, S., & Lee, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23115894 · Cited by 71
Chen, Y., Hamidu, S., Yang, X., Yan, Y., Wang, Q., Li, L., Oduro, P. K., & Li, Y. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.880421 · Cited by 62
Neurodegeneration cell per cell
Balusu, S., Praschberger, R., Lauwers, E., Strooper, B. D., & Verstreken, P. (2023) · Neuron · doi:10.1016/j.neuron.2023.01.016 · Cited by 53
Zaib, S., Munir, R., Younas, M. T., Kausar, N., Ibrar, A., Aqsa, S., Shahid, N., Asif, T. T., Alsaab, H. O., & Khan, I. A. (2021) · Molecules · doi:10.3390/molecules26216573 · Cited by 49
Tau Aggregation Inhibiting Peptides as Potential Therapeutics for Alzheimer Disease
Aillaud, I., & Funke, S. A. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01230-7 · Cited by 51
Liu, Y., Uras, G., Onuwaje, I., Li, W., Yao, H., Xu, S., Li, X., Li, X., Phillips, J. B., Allen, S., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114305 · Cited by 46
Argueti-Ostrovsky, S., Alfahel, L., Kahn, J., & Israelson, A. (2021) · Cells · doi:10.3390/cells10092438 · Cited by 46
Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities
Wang, L., Banesh, S., Kumar, R., Schedin‐Weiss, S., Tjernberg, L. O., & Winblad, B. G. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70048 · Cited by 47
Disrupting pathologic phase transitions in neurodegeneration
Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 40
Lorenzo, D. D. (2024) · ChemMedChem · doi:10.1002/cmdc.202400180 · Cited by 46
Carbamate as a potential anti‐Alzheimer's pharmacophore: A review
Singh, Y. P., Kumar, N., Chauhan, B. S., & Garg, P. (2023) · Drug Development Research · doi:10.1002/ddr.22113 · Cited by 36
Munir, R., Zia‐ur‐Rehman, M., Murtaza, S., Zaib, S., Javid, N., Awan, S. J., Iftikhar, K., Athar, M., & Khan, I. A. (2021) · Molecules · doi:10.3390/molecules26030656 · Cited by 31
Shen, X., Li, H., Zhang, B., Li, Y., & Zhu, Z. (2025) · Cells · doi:10.3390/cells14191506 · Cited by 33
Ravindar, L., Hasbullah, S. A., Rakesh, K. P., Raheem, S., Ismail, N., Ling, L. Y., & Hassan, N. I. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129992 · Cited by 28
Cacabelos, R., Martínez-Iglesias, O. A., Cacabelos, N., Carrera, I., Corzo, L., & Naidoo, V. (2024) · Life · doi:10.3390/life14121555 · Cited by 33
Thioxanthenone-based derivatives as multitarget therapeutic leads for Alzheimer's disease
Tonelli, M., Catto, M., Sabaté, R., Francesconi, V., Laurini, E., Pricl, S., Pisani, L., Miniero, D. V., Liuzzi, G. M., Gatta, E., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115169 · Cited by 26
Dual Drug Repurposing: The Example of Saracatinib
Ramos, R., & Vale, N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084565 · Cited by 24
Targeting of PP2 A/GSK3β/PTEN Axis in Alzheimer Disease: The Mooting Evidence, Divine, and Devil
Alqahtani, S. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Abdel‐Fattah, M. M., Alsaiari, A. A., Alruwaili, M., Papadakis, M., Alexiou, A. T., & Batiha, G. E. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01554-0 · Cited by 26
Bagga, S., & Kumar, M. (2022) · Current Molecular Medicine · doi:10.2174/1566524022666220404112843 · Cited by 25
Cyclic dipeptide‐based small molecules modulate zinc‐mediated liquid–liquid phase separation of tau
Ramesh, M., Balachandra, C., Baruah, P., & Govindaraju, T. (2022) · Journal of Peptide Science · doi:10.1002/psc.3465 · Cited by 25
The innate immune response in tauopathies
Johnson, A. M., & Lukens, J. R. (2023) · European Journal of Immunology · doi:10.1002/eji.202250266 · Cited by 22
Das, B., Mathew, A. T., Baidya, A. T. K., Devi, B., Rampa, R. S., & Kumar, R. (2023) · Molecular Diversity · doi:10.1007/s11030-023-10645-3 · Cited by 19
Dey, A., Ghosh, S., Rajendran, R. L., Bhuniya, T., Das, P., Bhattacharjee, B., Das, S., Mahajan, A. A., Samant, A., Anand, K., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179690 · Cited by 20
Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics
Arar, S. H., Haque, M. A., & Kayed, R. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26561 · Cited by 20
New insights into the therapeutic approaches for the treatment of tauopathies
Singh, H., Das, A., Khan, M. M., & Pourmotabbed, T. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385288 · Cited by 19
Decoupling phase separation and fibrillization preserves activity of biomolecular condensates
Mahendran, T. S., Singh, A. A., Srinivasan, S., Jennings, C. M., Neureuter, C., Gindra, B. H., Parekh, S. H., & Banerjee, P. R. (2026) · Nature Communications · doi:10.1038/s41467-026-69244-z · Cited by 20
Islam, M. F., Ullah, S. M., Khan, A., Batool, Z., Mali, S. N., Gurav, S. S., Dahlous, K. A., Mohammad, S., Hussain, J., Al-Harrasi, A., et al. (2025) · Scientific Reports · doi:10.1038/s41598-024-83386-4 · Cited by 16
Islam, M. F., Khan, A., Khan, M., Halim, S. A., Ullah, S. M., Hussain, J., Al-Harrasi, A., Shafiq, Z., Tasleem, M., & El‐Gokha, A. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135387 · Cited by 15
Therapies for Tau-associated neurodegenerative disorders: targeting molecules, synapses, and cells
Robbins, M. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.373670 · Cited by 16
Blocking tau transmission by biomimetic graphene nanoparticles
Zhu, R., Makwana, K. M., Zhang, Y., Rajewski, B. H., Valle, J. R. D., & Wang, Y. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb00850a · Cited by 18
Sharo, C., Zhai, T., & Huang, Z. J. (2024) · Pharmaceuticals · doi:10.3390/ph17010137 · Cited by 13
Design and synthesis of phenoxy methyl‐oxadiazole compounds against Alzheimer's disease
Evren, A. E., Nuha, D., Özkan, B. N. S., Kahraman, Ç., Gönülalan, E. M., & Yurttaş, L. (2024) · Archiv der Pharmazie · doi:10.1002/ardp.202400115 · Cited by 13
Emerging paradigms in Alzheimer's therapy
Agnes Preethy, H., Rajendran, K., Sukumar, A. J., & Krishnan, U. M. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176872 · Cited by 15
González‐Cuesta, M., Herrera‐González, I., García‐Moreno, M. I., Ashmus, R. A., Vocadlo, D. J., Fernández, J. M. G., Nanba, E., Higaki, K., & Mellet, C. O. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2073444 · Cited by 15
Das, B., Baidya, A. T. K., Chakrabarti, S., Chouhan, D., Thakur, B., Darreh‐Shori, T., Chen, G., Tiwari, V. K., & Kumar, R. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107373 · Cited by 12
Role of Tau protein in long COVID and potential therapeutic targets
Marwaha, B. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1280600 · Cited by 11
Amylin and Secretases in the Pathology and Treatment of Alzheimer’s Disease
Singh, S. P., Yang, F., Sivils, A., Cegielski, V., & Chu, X. (2022) · Biomolecules · doi:10.3390/biom12070996 · Cited by 11
Hu, Y., Yang, D., Tu, Y., Chai, K., Chu, L., Shi, S., & Yao, T. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00554 · Cited by 11
New Approaches to the Treatment of Alzheimer’s Disease
Kruk-Słomka, M., Kuceł, D., Małysz, M., Machnikowska, A., Orzelska‐Górka, J., & Biała, G. (2025) · Pharmaceuticals · doi:10.3390/ph18081117 · Cited by 12
Systems biology of Alzheimer’s Disease: a scoping review of key pathways and mechanisms
Bice, P. J., Nho, K. T., Ertekin‐Taner, N., & Saykin, A. J. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00934-4 · Cited by 14
Exploring Chemistry with Pyridine Derivatives
Pal, S. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.100792 · Cited by 10
Svobodová, B., Pulkrabkova, L., Panek, D., Misiachna, A., Kolcheva, M., Andrýs, R., Handl, J., Čapek, J., Nyvltová, P., Roušar, T., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119124 · Cited by 10
Targeting mitochondrial dysfunction in Alzheimer's disease: New findings and perspectives
Hroudová, J., & Fišar, Z. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111491 · Cited by 9
Joshi, B., Singh, D., Wasan, H., Sharma, U., & Reeta, K. H. (2022) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2022.106349 · Cited by 9
Recent advances and future therapy development for Alzheimer's disease and related disorders
Hong, M., & Bitan, G. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.391182 · Cited by 9
Diverse influences on tau aggregation and implications for disease progressionPreprint
Alstyne, M. V., Pratt, J., & Parker, R. (2025) · Genes & Development · doi:10.1101/gad.352551.124 · Cited by 11
Tian, S., Liu, Y., Hong, H., & Li, S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05280-y · Cited by 8
Matton, A., Axenhus, M., Bogdanović, N., Winblad, B. G., Schedin‐Weiss, S., Nilsson, P., & Tjernberg, L. O. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.735334 · Cited by 9
Tauopathies: The Role of Tau in Cellular Crosstalk and Synaptic Dysfunctions
Caamaño-Moreno, M., & Gargini, R. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.02.034 · Cited by 7
β-Bracelets: Macrocyclic Cross-β Epitope Mimics Based on a Tau Conformational Strain
Rajewski, B. H., Makwana, K. M., Angera, I. J., Geremia, D. K., Zepeda, A. R., Hallinan, G. I., Vidal, R., Ghetti, B. F., Serrano, A. L., & Valle, J. R. D. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c06830 · Cited by 8
Fišar, Z., & Hroudová, J. (2025) · Biomolecules · doi:10.3390/biom15040495 · Cited by 6
Thành, N. Đ., Giang, N. T. K., Toán, V. N., Van, H. T. K., Tri, N. M., Anh, H. H., & Hai, D. S. (2023) · ChemistrySelect · doi:10.1002/slct.202301632 · Cited by 6
Jung, J., Kim, Y., Cirunduzi, A. C., Yoon, S., Bang, S., & Yang, S. (2026) · CNS Neuroscience & Therapeutics · doi:10.1002/cns.70919 · Cited by 5
Hybrid/Chimera Drugs - Part 1 - Drug Hybrids Affecting Diseases of the Central Nervous System
Nudelman, A. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673305662240702071354 · Cited by 5
Polyoxometalates bind multiple targets involved in Alzheimer’s disease
Zaken, K. B., Bouhnik, R., Omer, N., Bloch, N., & Samson, A. O. (2025) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-025-02111-2 · Cited by 6
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
Carbohydrate-Derived Polytriazole Nanoparticles Enhance the Anti-Inflammatory Activity of Cilostazol
Rivas, M. V., Musikant, D., Peña, R. D., Álvarez, D. S., Pelazzo, L., Rossi, E., Martínez, K. D., Errea, M. I., Pérez, O. E., Varela, O. J., et al. (2022) · ACS Omega · doi:10.1021/acsomega.2c02969 · Cited by 4
Small molecules to target tau amyloid aggregation
Manglano-Artuñedo, Z., Peña‐Díaz, S., & Ventura, S. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.380900 · Cited by 4
Metallic and polymeric green nanoplatforms in oncology
Jadhav, M., & Prabhu, A. (2022) · Journal of Applied Microbiology · doi:10.1093/jambio/lxac044 · Cited by 4
Hussein, S., Tolba, M. F., Michel, H. E., Albohy, A., & Azab, S. S. (2025) · NeuroToxicology · doi:10.1016/j.neuro.2025.01.003 · Cited by 3
Discovery of a new class of triazole based inhibitors of acetyl transferase KAT2A
Pacifico, R., Gaudio, N. D., Bove, G., Altucci, L., Siragusa, L., Cruciani, G., Ruvo, M., Bellavita, R., Grieco, P., & Adamo, M. F. A. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2097447 · Cited by 3
Sharo, C., Zhang, J., Zhai, T., Bao, J., Garcia-Epelboim, A. D., Mamourian, E., Shen, L., & Huang, Z. J. (2024) · Targets · doi:10.3390/targets2040025 · Cited by 3
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
Güzel, A., Isık, Z., Gök, Y., Taşkın‐Tok, T., & Aktaş, A. (2023) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026623666230614150520 · Cited by 2
Chacko, L., Nag, S., Dewanjee, S., Ghosh, S., Vallamkondu, J., Mitra, O., Dey, A., Bhuniya, T., Paluru, H. P. R., Reddy, P. H., et al. (2022) · Preprints.org · doi:10.20944/preprints202211.0032.v1 · Cited by 2
Inhibition and Disassembly of Tau Aggregates by Engineered Graphene Quantum DotsPreprint
Zhu, R., Makwana, K. M., Zhang, Y., Rajewski, B. H., Valle, J. R. D., & Wang, Y. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.29.522245 · Cited by 2
Jung, H. G., Park, D., Bang, J., Kim, Y. H., Jang, J. W., Kim, Y.-H., Kim, H., Lee, S., Moon, W., Hwang, K. S., et al. (2025) · Aggregate · doi:10.1002/agt2.70139 · Cited by 1
The Expanding Role of Pyridine Derivatives as Privileged Scaffolds in Cardiac Ionic Channels
Janapati, Y. K., Cheweti, S., Chidipi, B., Srinivas, M., & Junapudi, S. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.106759 · Cited by 1
Benzo[d]thiazol-5-yl Compounds as O-GlcNAcase Inhibitors for Treating Alzheimer’s Disease
Sabnis, R. W. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00259 · Cited by 1
Pradhan, R., Petrovic, Z., Sakib, M. S., Schröder, S., Krüger, D. M., Peña, T., Diniz, E., Burckhardt, S., Schütz, A., Grządzielewska, I., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.01.657217 · Cited by 1
CULTURE OF LEARNING AND PERFORMANCE GOALS IN THE UAE EDUCATION
Alkaabi, A. M. (2014) · ICERI proceedings
Wang, Z., Tao, P.-F., Sun, Y.-Y., Song, X., & Huang, H. (2023) · Research Square · doi:10.21203/rs.3.rs-2964826/v1
Karacic, J., Eggmann, F., Weiger, R., & Zaugg, L. K. (2024) · SWISS DENTAL JOURNAL SSO – Science and Clinical Topics · doi:10.61872/sdj-2024-01-01
Polyphenol: Development of Polyphenol-Inspired Derivatives Targeting Pathological Factors of AD
Das, B., Baidya, A. T. K., & Kumar, R. (2023) · Springer eBooks · doi:10.1007/978-981-99-6038-5_10
Szłapa‐Kula, A., Kaźmierski, Ł., Biernasiuk, A., Latocha, M. T., Kuśmierz, D., Płonka-Czerw, J. M., Kałkus, M., Siębor, Z., Erfurt, K., Kula, S., et al. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.126991
Öztürk, O., Oyardı, Ö., Sağkan, R. I., & Dündar, Y. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118445 · Cited by 1
AHA1 regulates Aβ production via modulation of APP expression and γ-secretase assemblyPreprint
Noorani, A. A., Islam, S., Catalfano, K. C., Wilkins, H., Blagg, B. S. J., Zou, K., & Wolfe, M. S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.03.686106
Signaling cascades of microtubule-associated protein Tau in Alzheimer’s disease
Velmurugan, G., Krishnan, D., Upadhyay, R., Sivasamy, R., Sevanan, M., & Chinnathambi, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.013
Luo, X., Wu, W., Yu, B., Chen, S., Zhao, J., Min, J., & Gu, X. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04621-6
Additional file 1 of The therapeutic landscape of tauopathies: challenges and prospects
Cummings, J. L., González, M. I., Pritchard, M. C., May, P. C., Toledo‐Sherman, L., & Harris, G. A. (2024) · Figshare · doi:10.6084/m9.figshare.26623807
Biosimilars: Antibody and nanobody-based therapeutic approaches towards protein misfolding diseases
Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.014
Neuid: A Novel Neuron‐Enriched LncRNA that Connects Epigenetic Gene Silencing to Alzheimer's Disease
Pradhan, R., Petrovic, Z., Sakib, M. S., Schröder, S., Krüger, D. M., Peña, T., Diniz, E., Burkhardt, S., Schütz, A., Gisa, V., et al. (2026) · Advanced Science · doi:10.1002/advs.202514972 · Cited by 1
AHA1 Regulates Aβ Production via Modulation of APP Abundance and γ‐Secretase Assembly
Noorani, A. A., Islam, S., Filip, E., Catalfano, K. C., Paswan, S. K., Nagarajan, V., Wilkins, H., Blagg, B. S. J., Zou, K., & Wolfe, M. S. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70544
BindingDB (2024) · UC San Diego · doi:10.7270/q2tt4w9n
Metadata
- Authors
- Wang, L., Bharti, Kumar, R., Pavlov, P. F., & Winblad, B.
- Affiliations
- Karolinska Institutet (SE)
- Karolinska University Hospital (SE)
- Corresponding author
- Winblad, Bengt
- Venue
- European Journal of Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 209
- Pages
- 112915
- ISSN
- 0223-5234 (ISSN-L)
- OpenAlex
- W3092711150
- Cited by
- 92
- References
- 278
- Citations by year
- 2026: 5 · 2025: 21 · 2024: 15 · 2023: 22 · 2022: 21 · 2021: 7
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- European Journal of Medicinal Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Loo och Hans Ostermans Stiftelse för Medicinsk Forskning
- Gun och Bertil Stohnes Stiftelse
- Margareta af Ugglas Foundation
- Vetenskapsrådet (2015\u201302774, 2018\u201302843)
- Banaras Hindu University
- Karolinska Institutet
- Hjärnfonden
- Magnus Bergvalls Stiftelse
- Gunvor och Josef Anérs Siftelse
- Stiftelsen för Gamla Tjänarinnor
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, tauopathy, tau protein, small molecule drugs, tau aggregation, tau degradation, multi-target-directed ligands, disease-modifying therapy, drug development, neurofibrillary tangles
- MeSH terms
- Alzheimer Disease, Animals, Cholinesterase Inhibitors, Cholinesterases, Curcumin, Humans, Phosphorylation, Protein Processing, Post-Translational, Quinazolines, Thiadiazoles, Receptors, N-Methyl-D-Aspartate, Neurofibrillary Tangles, tau Proteins, Neuroprotective Agents, Benzodioxoles, Plaque, Amyloid, Molecular Targeted Therapy, Protein Aggregation, Pathological
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
