The DOI matches its Crossref record; 82 of the 83 references it cites were found in a registry or an index.
Current and future treatments for Alzheimer's disease
Open accessAbstract
Alzheimer's dementia (AD) is increasingly being recognized as one of the most important medical and social problems in older people in industrialized and non-industrialized nations. To date, only symptomatic treatments exist for this disease, all trying to counterbalance the neurotransmitter disturbance. Three cholinesterase inhibitors (CIs) are currently available and have been approved for the treatment of mild to moderate AD. A further therapeutic option available for moderate to severe AD is memantine, an N-methyl-D-aspartate receptor noncompetitive antagonist. Treatments capable of stopping or at least effectively modifying the course of AD, referred to as 'disease-modifying' drugs, are still under extensive research. To block the progression of the disease they have to interfere with the pathogenic steps responsible for the clinical symptoms, including the deposition of extracellular amyloid β plaques and intracellular neurofibrillary tangle formation, inflammation, oxidative damage, iron deregulation and cholesterol metabolism. In this review we discuss current symptomatic treatments and new potential disease-modifying therapies for AD that are currently being studied in phase I-III trials.
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
“After the sequential breakdown of the big precursor protein amyloid precursor protein (APP) by the β- and γ-e -secretase, Aβ peptides with A38, A40, and A42 being the most prevalent forms are generated (Yiannopoulou et al., 2013).”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Yiannopoulou et al., 2013
In the citing paper
“Memantine is known to be a non-competitive NMDA receptor antagonist that counteracts the negative effects of high glutamate concentrations in the brain (Yiannopoulou et al., 2013).”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Yiannopoulou et al., 2013
In the citing paper
“The most efficient and prospective class is passive Ab immunotherapy using mAbs. The chief disadvantages of this class of medicines are cerebral microhemorrhages and vasogenic edema (Yiannopoulou et al., 2013).”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Yiannopoulou et al., 2013
In the citing paper
“Memantine is a noncompetitive low-affinity NMDA-receptor open-channel blocker and affects glutamatergic transmission.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“AChEIs attempt at reducing the breakdown of acetylcholine levels in the brain of the patients with AD by inhibiting the responsible enzyme acetylcholinesterase in the synaptic cleft.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“According to the “amyloid hypothesis” Aβ production in the brain initiates a cascade of events leading to the clinical syndrome of AD.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The basic pathophysiology and neuropathology of AD that drives the current research suggests that the primary histopathologic lesions of AD are the extracellular amyloid plaques and the intracellular Tau neurofibrillary tangles (NFTs).5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The elements of the cascade include local inflammation, oxidation, excitoxicity (excessive glutamate), and tau hyperphosphorylation.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The acetylocholinesterase inhibitors (AChEIs) which are approved for the treatment of AD are donepezil, galantamine, and rivastigmine.4,5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“It is the forming of amyloid oligomers to which neurotoxicity is mainly attributed and initiates the amyloid cascade.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Progressive neuronal destruction leads to shortage and imbalance between various neurotransmitters (eg, acetylcholine, dopamine, serotonin) and to the cognitive deficiencies seen in AD.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“A further therapeutic agent approved for moderate to severe AD is the low-to-moderate affinity, noncompetitive N-methyl-d-aspartate (NMDA) receptor antagonist memantine.4,5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The APP cleavage by α-secretase leads to nonamyloidogenic pathway, whereas APP cleavage by β-secretase (BACE1) leads to amyloidogenic pathway.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The Aβ derives from a protein overexpressed in AD, APP through sequential proteolysis by β-secretase (BACE1) in the extracellular domain and γ-secretase in the transmembrane region.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Sequential cleavage of APP by BACE1 in the extracellular and γ-secretase in the transmembrane area results in the Aβ production.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“The crucial step in AD pathogenesis is the production of amyloid (Aβ), which forms SPs (insoluble and proteolysis-resistant fibrils).”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Aβ40 is somewhat aggregation-prone and it is mostly found in the cerebral vasculature as a main component of “cerebral amyloid angiopathy.””
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Oligomers can form Aβ-fibrils that will eventually form amyloid plaques.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Major sites of γ-secretase cleavage usually occur in positions 40 and 42 of Aβ, thus Aβ40 and Aβ42 oligomers are the main products of the sequential APP cleavage, as the amyloidogenic pathway is favored in neurons because of the greater plentifulness of BACE1.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Aβ40 usually constitutes more than 50% of total detected Aβ.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Unluckily, concerning γ-secretase, in addition to APP, this particular enzyme acts on many other substances and cleaves different transmembrane proteins. Notch receptor 1, which is essential for control of normal cell differentiation and communication, is among them.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Aβ42 is the most aggregation-prone form and has the tendency to cluster into oligomers.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Aβ38 is soluble, present in the vasculature of patients with sporadic and familial AD.”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“On the contrary, the nonamyloidogenic processing is more favored in other cells without BACE1 predominance.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Cerebral microhemorrhages and vasogenic edema are the main drawbacks in this group of agents.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
In the citing paper
“Abnormal accumulation or dyshomeostasis of metal ions such as iron, copper, and zinc has been associated with the pathophysiology of AD.5”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [5]
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
Sperling, R. A., Aisen, P. S., Beckett, L. A., Bennett, D. A., Craft, S., Fagan, A. M., Iwatsubo, T., Jack, C. R., Kaye, J., Montine, T. J., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.03.003 · Cited by 7,155
The cholinergic hypothesis of geriatric memory dysfunction
Bartus, R. T., Dean, R. L., Beer, B., & Lippa, A. S. (1982) · Science · doi:10.1126/science.7046051 · Cited by 5,545
Global prevalence of dementia: a Delphi consensus study
Ferri, C. P., Prince, M. J., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K. S., Hasegawa, K., Hendrie, H. C., Huang, Y., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)67889-0 · Cited by 5,336
Cholinesterase inhibitors for Alzheimer's disease
Birks, J. S. (2006) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd005593 · Cited by 1,906
Revising the definition of Alzheimer's disease: a new lexicon
Dubois, B., Feldman, H. H., Jacova, C., Cummings, J. L., DeKosky, S. T., Barberger-Gateau, P., Delacourte, A., Frisoni, G., Fox, N. C., Galasko, D., et al. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70223-4 · Cited by 1,869
Statins and the risk of dementia
Jick, H., Zornberg, G. L., Jick, S. S., Seshadri, S. S., & Drachman, D. (2000) · The Lancet · doi:10.1016/s0140-6736(00)03155-x · Cited by 1,764
Tariot, P. N., Farlow, M. R., Grossberg, G. T., Graham, S. M., McDonald, S., Gergel, I., & for the Memantine Study Group (2004) · JAMA · doi:10.1001/jama.291.3.317 · Cited by 1,403
Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329
McShane, R., Areosa Sastre, A., & Minakaran, N. (2006) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd003154.pub5 · Cited by 1,155
Clinical trial of indomethacin in Alzheimer's disease
Rogers, J., Kirby, L., Hempelman, S. R., Berry, D. A., McGeer, P. L., Kaszniak, A. W., Zalinski, J., Cofield, M., Mansukhani, L., Willson, P., et al. (1993) · Neurology · doi:10.1212/wnl.43.8.1609 · Cited by 991
Research works printed but not linked: 6
- Alva G., 2008, Psychiatry (Edgmont), 5, 27
- Ballard C., 2010, CNS Drugs, 24, 729
- Cummings J., 2008, Primary Psychiatry, 15, 66
- Hansen R., 2008, Clin Interv Aging, 3, 211
- Hey J., Koelsch G., Bilcer G., Jacobs A., Tolar M., Tang J. (2008) Single dose administration of the b-secretase inhibitor CTS21166 (ASP1720) reduces plasma Aβ40 in human subjects. Presented by Dr Koelsch in the International Conference on Alzheimer’s Disease (ICAD), Chicago, IL, USA, 26–31 July 2008. Available at: http://www.alzforum.org/new/detail.asp?id=1790
- Yiannopoulou K., 2009, Primary Psychiatry, 16, 29
Cited by
Sorted by citations
Items 201–300 of 682
Caneus, J., Akanda, N., Rumsey, J. W., Guo, X., Jackson, M., Long, C. J., Sommerhage, F., Georgieva, S., Kanaan, N. M., Morgan, D., et al. (2020) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12029 · Cited by 29
Kumar, A., & Singh, N. (2017) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000294 · Cited by 28
Second Sphere Interactions in Amyloidogenic Diseases
Roy, M., Nath, A. K., Pal, I., & Dey, S. G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00941 · Cited by 29
Tarawneh, H. Y., Jayakody, D. M. P., Sohrabi, H. R., Martins, R. N., & Mulders, W. H. A. M. (2022) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220035 · Cited by 30
Kaur, P., & Sodhi, R. K. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.12.033 · Cited by 28
Total synthesis of (±)-galanthamine from GABA through regioselective aryne insertion
Venkatesh, T., Mainkar, P. S., & Chandrasekhar, S. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob03123a · Cited by 28
Singh, K., Gupta, J. K., Kumar, S., & Soni, U. (2024) · Current Protein and Peptide Science · doi:10.2174/0113892037275221240327042353 · Cited by 32
Multiple Instance Learning for Classification of Dementia in Brain MRI
Tong, T., Wolz, R., Gao, Q., Hajnal, J. V., & Rueckert, D. (2013) · Lecture notes in computer science · doi:10.1007/978-3-642-40763-5_74 · Cited by 29
Li, J., Ebrahimi, A., & Ali, A. B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105169 · Cited by 27
Sugandhi, V. V., Gadhave, D. G., Ugale, A. R., Kulkarni, N. N., Nangare, S., Patil, H. P., Rath, S., Saxena, R., Lavate, A., Patel, A. T., et al. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102775 · Cited by 32
Hoang, T. H. X., Hồ, Đ. V., Phan, K. V., Le, Q. V., Raal, A., & Nguyen, H. T. (2020) · Pharmaceutical Biology · doi:10.1080/13880209.2020.1841810 · Cited by 27
Inhibition of scopolamine‐induced memory and mitochondrial impairment by betanin
Salimi, A., Sabur, M., Dadkhah, M., & Shabani, M. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23076 · Cited by 26
Şahin, S. (2022) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2022.105514 · Cited by 28
ALNasser, M. N., Mellor, I. R., & Carter, W. G. (2022) · Molecules · doi:10.3390/molecules27154891 · Cited by 26
Effects of baicalein with memantine on aluminium chloride-induced neurotoxicity in Wistar rats
Jadhav, R., & Kulkarni, Y. A. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1034620 · Cited by 30
Ge, Y., Tohda, C., Zhu, S., He, Y., Yoshimatsu, K., & Komatsu, K. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00329 · Cited by 26
Novel carbamate derivatives as selective butyrylcholinesterase inhibitors
Bajda, M., Łątka, K., Hebda, M., Jończyk, J., & Malawska, B. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.03.003 · Cited by 26
Amyloid Pan-inhibitors: One Family of Compounds To Cope with All Conformational Diseases
Espargaró, A., Pont, C., Gámez, P., Muñoz‐Torrero, D., & Sabaté, R. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00398 · Cited by 27
Lan, T. T., Anh, D. T., Pham‐The, H., Dung, D. T. M., Hương, L. T. T., Park, E. J., Jeon, H. W., Kang, J. S., Thuần, N. T. D., Han, S., et al. (2019) · Medicinal Chemistry Research · doi:10.1007/s00044-019-02488-1 · Cited by 26
Schaf, J., Damstra‐Oddy, J., & Williams, R. S. B. (2019) · The International Journal of Developmental Biology · doi:10.1387/ijdb.190228rw · Cited by 24
Current Findings and Potential Mechanisms of KarXT (Xanomeline–Trospium) in Schizophrenia Treatment
Azargoonjahromi, A. (2024) · Clinical Drug Investigation · doi:10.1007/s40261-024-01377-9 · Cited by 30
Epigenetic biomarkers in Alzheimer's disease: Diagnostic and prognostic relevance
Behl, T., Kyada, A., Roopashree, R., Nathiya, D., Arya, R., Kumar, M., Khalid, M., Gulati, M., Sachdeva, M., Fareed, M., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102556 · Cited by 31
Drug Development in Alzheimer’s Disease: The Contribution of PET and SPECT
Declercq, L., Vandenberghe, R. R., Laere, K. V., Verbruggen, A., & Bormans, G. M. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00088 · Cited by 27
Effects of Curcumin on Cognitive Function—A Systematic Review of Randomized Controlled Trials
Seddon, N., D'Cunha, N. M., Mellor, D. D., McKune, A. J., Georgousopoulou, E. N., Panagiotakos, D. B., Kellett, J., & Naumovski, N. (2019) · Exploratory Research and Hypothesis in Medicine · doi:10.14218/erhm.2018.00024 · Cited by 25
The Mitochondrial Hsp90 TRAP1 and Alzheimer’s Disease
Dekker, F. A., & Rüdiger, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.697913 · Cited by 28
Thomas, J., Smith, H., Smith, C. A., Coward, L. U., Gorman, G. S., Luca, M. D., & Jumbo‐Lucioni, P. P. (2021) · Pathophysiology · doi:10.3390/pathophysiology28020020 · Cited by 25
Mzezewa, S. C., Omoruyi, S. I., Zondagh, L. S., Malan, S. F., Ekpo, O. E., & Joubert, J. (2021) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2021.1913137 · Cited by 26
Microfluidic Platforms to Unravel Mysteries of Alzheimer’s Disease: How Far Have We Come?
Prasanna, P., Rathee, S., Rahul, V., Mandal, D., Goud, M. S. C., Yadav, P., Hawthorne, S. J., Sharma, A., Gupta, P. K., Ojha, S. K., et al. (2021) · Life · doi:10.3390/life11101022 · Cited by 25
de Torre, M. P., Cavero, R. Y., & Calvo, M. I. (2022) · Molecules · doi:10.3390/molecules27207100 · Cited by 27
Khot, K. B., Gopan, G., Bandiwadekar, A., & Jose, J. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101806 · Cited by 28
Lancioni, G. E., Singh, N. N., O’Reilly, M. F., Sigafoos, J., D’Amico, F., Laporta, D., Cattaneo, M. G., Scordamaglia, A., & Pinto, K. (2018) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317518775038 · Cited by 25
Alzheimer's Disease and Its Potential Alternative Therapeutics.
Kisby, B. R., Jarrell, J. T., Me, A., Ds, C., Er, R., Cm, C., Rogers, J. T., & Huang, X. (2019) · PubMed · doi:10.4172/2161-0460.1000477 · Cited by 25
Fereidooni, F., Komeili, G., Fanaei, H., Safari, T., Khorrami, S., & Feizabad, A. K. (2020) · Neurology Psychiatry and Brain Research · doi:10.1016/j.npbr.2020.08.001 · Cited by 25
Frenkel‐Pinter, M., Tal, S., Scherzer‐Attali, R., Abu-Hussien, M., Alyagor, I., Eisenbaum, T., Gazit, E., & Segal, D. (2016) · Neurodegenerative Diseases · doi:10.1159/000448518 · Cited by 24
Invasive and non-invasive therapies for Alzheimer’s disease and other amyloidosis
Pandey, G., & Ramakrishnan, V. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00752-y · Cited by 26
Alternative Targets to Fight Alzheimer’s Disease: Focus on Astrocytes
Valenza, M., Facchinetti, R., Menegoni, G., Steardo, L., & Scuderi, C. (2021) · Biomolecules · doi:10.3390/biom11040600 · Cited by 25
DOTA: Deep Learning Optimal Transport Approach to Advance Drug Repositioning for Alzheimer’s Disease
Chyr, J., Gong, H., & Zhou, X. (2022) · Biomolecules · doi:10.3390/biom12020196 · Cited by 24
Corbin, D., & Lesage, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-09719-3 · Cited by 24
Chinese Medicine: A Hope for Neurodegenerative Diseases?
Law, B. Y. K., Wu, A., Wang, M. J., & Zhu, Y. Z. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170374 · Cited by 25
Protein and Peptides for Elderly Health
Shang, N., Chalamaiah, M., Bandara, N., & Wu, J. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.03.003 · Cited by 24
Vermeulen, R. J., Andersson, V., Banken, J., Hannink, G., Govers, T. M., Rovers, M. M., & Rikkert, M. O. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70069 · Cited by 25
Ding, Y., Luo, C., Li, C., Lan, T., & Qin, Z. (2019) · Biomedical Signal Processing and Control · doi:10.1016/j.bspc.2019.101564 · Cited by 24
Bioactivity of the Geranium Genus: A Comprehensive Review
Graça, V. C., Ferreira, I. C. F. R., & Santos, P. F. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200114110323 · Cited by 23
Peroxidase activity of heme bound amyloid β peptides associated with Alzheimer's disease
Roy, M., Pal, I., Nath, A. K., & Dey, S. G. (2020) · Chemical Communications · doi:10.1039/c9cc09758a · Cited by 24
Baruah, P., Das, A., Paul, D., Chakrabarty, S., Aguan, K., & Mitra, S. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00168 · Cited by 25
Preventing Alzheimer's disease within reach by 2025: Targeted‐risk‐AD‐prevention (TRAP) strategy
Vitali, F., Branigan, G. L., & Brinton, R. D. (2021) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12190 · Cited by 24
Panda, S. P., & Soni, U. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101560 · Cited by 22
Malik, S., Miana, G. A., Ata, A., Kanwal, M., Maqsood, S., Malik, I., & Kazmi, Z. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106175 · Cited by 23
Carroll, J. A., Race, B., Phillips, K. L., Striebel, J. F., & Chesebro, B. W. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000876 · Cited by 26
Mishra, C. B., Shalini, S., Gusain, S., Prakash, A., Kumari, J., Kumari, S., Yadav, A. K., Lynn, A. M., & Tiwari, M. (2020) · RSC Advances · doi:10.1039/d0ra00663g · Cited by 22
Firdaus, Z., & Singh, T. D. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557520666200730155928 · Cited by 23
Séguy, L., Groo, A., & Malzert‐Fréon, A. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.02.022 · Cited by 23
Jadhav, R., & Kulkarni, Y. A. (2023) · Antioxidants · doi:10.3390/antiox12030707 · Cited by 22
Yu, L., Wu, A., Wong, V. K. W., Qu, L., Zhang, N., Qin, D., Wu, J., Tang, B., Wang, H.-M., Wang, Q., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00194 · Cited by 22
Cerebrospinal Fluid Concentrations of Extracellular Matrix Proteins in Alzheimer’s Disease
Minta, K., Portelius, E., Janelidze, S., Hansson, O., Zetterberg, H., Blennow, K., & Andréasson, U. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190187 · Cited by 24
Evaluation of attention in APP/PS1 mice shows impulsive and compulsive behaviours
Shepherd, A. L., May, C., Churilov, L. P., Adlard, P. A., Hannan, A. J., & Burrows, E. L. (2019) · Genes Brain & Behavior · doi:10.1111/gbb.12594 · Cited by 24
Tanshinone IIA Alleviates the AD Phenotypes in APP and PS1 Transgenic Mice
Li, F., Guo-sheng, H., & Wu, K.-X. (2016) · BioMed Research International · doi:10.1155/2016/7631801 · Cited by 22
A cellular model of amyloid precursor protein processing and amyloid-β peptide production
Macias, M. P., Gonzales, A. M., Siniard, A. L., Walker, A. W., Corneveaux, J. J., Huentelman, M. J., Sabbagh, M. N., & Decourt, B. (2013) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2013.11.024 · Cited by 21
Cholinergic symptoms and QTc prolongation following donepezil overdose
Pourmand, A., Shay, C., Redha, W., Aalam, A., & Mazer-Amirshahi, M. E. (2017) · The American Journal of Emergency Medicine · doi:10.1016/j.ajem.2017.06.044 · Cited by 21
High ligand efficiency quinazoline compounds as novel A2A adenosine receptor antagonists
Bolteau, R., Duroux, R., Laversin, A., Vreulz, B., Shiriaeva, A., Stauch, B., Han, G. W., Cherezov, V., Renault, N., Barczyk, A., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114620 · Cited by 21
Gohel, D., Zhang, P., Gupta, A. K., Li, Y., Chiang, C., Li, L., Hou, Y., Pieper, A. A., Cummings, J. L., & Cheng, F. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231391 · Cited by 25
Research Progress on the Pathogenesis, Diagnosis, and Drug Therapy of Alzheimer’s Disease
Yang, Y., & Qiu, L. (2024) · Brain Sciences · doi:10.3390/brainsci14060590 · Cited by 22
Zondagh, L. S., Malan, S. F., & Joubert, J. (2020) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2020.1801673 · Cited by 22
Malar, D. S., Prasanth, M. I., Jeyakumar, M., Balamurugan, K., & Devi, K. P. (2020) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22632 · Cited by 21
Natarajan, S., Govindaraju, A., Rajmohamed, M., Palanisamy, P., & Abdulkader, A. (2017) · Pharmacognosy Magazine · doi:10.4103/pm.pm_57_17 · Cited by 20
Yaacob, W. M. H. W., Long, I., Zakaria, R., & Othman, Z. (2018) · Current Nutrition & Food Science · doi:10.2174/1573401315666181130103456 · Cited by 20
Exploiting Natural Niches with Neuroprotective Properties: A Comprehensive Review
Moukham, H., Lambiase, A., Barone, G. D., Tripodi, F., & Coccetti, P. (2024) · Nutrients · doi:10.3390/nu16091298 · Cited by 23
Semuyaba, I., Safiriyu, A. A., Ayikobua, E. T., & Niurka, R. F. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/3720380 · Cited by 20
Lim, H.-S., Kim, Y. J., Sohn, E., Yoon, J., Kim, B., & Jeong, S. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219886269 · Cited by 20
Fluorinated Molecules and Nanotechnology: Future ‘Avengers’ against the Alzheimer’s Disease?
Dabur, M., Loureiro, J. A., & Pereira, M. D. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082989 · Cited by 20
Lei, K., Zhou, L., Dan, M., Yang, F., Jian, T., Xin, J., Yu, Z., & Wang, Y. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17030280 · Cited by 20
The next step of neurogenesis in the context of Alzheimer’s disease
Moradi, H. R., Hajali, V., Khaksar, Z., Vafaee, F., Forouzanfar, F., & Negah, S. S. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06520-9 · Cited by 20
Naseer, A., Mir, S. S., Takács‐Vellai, K., & Nazir, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212263 · Cited by 22
Formica, C., Bonanno, L., Giambò, F. M., Maresca, G., Latella, D., Marra, A., Cucinotta, F., Bonanno, C., Lombardo, M., Tomarchio, O., et al. (2023) · Journal of Personalized Medicine · doi:10.3390/jpm13091386 · Cited by 20
Cereblon suppresses the formation of pathogenic protein aggregates in a p62-dependent manner
Zhou, L., Hao, Z., Wang, G., & Xu, G. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx433 · Cited by 19
Pfeffer, A., Munder, T., Schreyer, S., Klein, C., Rasińska, J., Winter, Y., & Steiner, B. (2018) · Behavioural Brain Research · doi:10.1016/j.bbr.2018.03.030 · Cited by 20
Tundis, R., Loizzo, M. R., Nabavi, S. M., Orhan, İ. E., Skalicka‐Woźniak, K., D’Onofrio, G., & Aiello, F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809593-5.00003-3 · Cited by 19
Jamal, S., Goyal, S., Shanker, A., & Grover, A. (2015) · PLOS ONE · doi:10.1371/journal.pone.0129370 · Cited by 19
Ali, A. A., Khalil, M. G., El‐latif, D. M. A., Okda, T. M., Abdelaziz, A. I., Abu‐Elfotuh, K., Kamal, M. M., & Wahid, A. M. (2021) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2021.104557 · Cited by 18
Current Drug Targets in Alzheimer’s Associated Memory Impairment: A Comprehensive Review
Chandrashekar, K. S., Mathew, A., Vignesh Balaji, E., Pai, K. S. R., Kishore, A., Pai, V., & Pemmireddy, R. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666220401124719 · Cited by 18
Abosharaf, H. A., Elsonbaty, Y., Tousson, E., & Mohamed, T. M. (2023) · Journal of Neuroendocrinology · doi:10.1111/jne.13356 · Cited by 19
Sen, D., Rathee, S., Pandey, V., Jain, S., & Patil, U. K. (2024) · Current Alzheimer Research · doi:10.2174/0115672050309057240404075003 · Cited by 19
Detection of Novel Biomarker Genes of Alzheimer’s Disease Using Gene Expression Data
Perera, S., Hewage, K. P., Gunarathne, C., Navarathna, R., Herath, D., & Ragel, R. (2020) · Moratuwa Engineering Research Conference (MERCon) · doi:10.1109/mercon50084.2020.9185336 · Cited by 18
Szałaj, N., Godyń, J., Jończyk, J., Pasieka, A., Panek, D., Wichur, T., Więckowski, K., Zaręba, P., Bajda, M., Pišlar, A. H., et al. (2020) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2020.1835882 · Cited by 17
The Role of Gene Editing in Neurodegenerative Diseases
Fan, H.-C., Chi, C.-S., Lee, Y.-J., Tsai, J., Lin, S., & Harn, H.-J. (2018) · Cell Transplantation · doi:10.1177/0963689717753378 · Cited by 18
Habibi, F., Ghaderkhani, S., Shokoohi, M., Banari, T., Morsali, M., Abadi, R. N. S., & Kiamehr, H. (2025) · AI and Ethics · doi:10.1007/s43681-025-00673-0 · Cited by 19
Memorcise and Alzheimer’s disease
Loprinzi, P. D., Frith, E., & Ponce, P. (2018) · The Physician and Sportsmedicine · doi:10.1080/00913847.2018.1445932 · Cited by 17
Juybari, K. B., Hosseinzadeh, A., & Sharifi, A. M. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2018.1557206 · Cited by 17
Ngo, F. Y., Wang, W., Chen, Q., Zhao, J., Chen, H., Gao, J., & Rong, J. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5780703 · Cited by 17
Alzheimer's Disease THErapy With NEuroaid (ATHENE): A Randomized Double-Blind Delayed-Start Trial
Chen, C., Lu, Q., Moorakonda, R. B., Kandiah, N., Tan, B. Y., Villaraza, S. G., Cano, J., & Venketasubramanian, N. (2021) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2021.10.018 · Cited by 16
Rombouts, F. J. R., Alexander, R., Cleiren, E., Groot, A. D., Carpentier, M., Dijkmans, J., Fierens, K., Masure, S., Moechars, D., Palomino‐Schätzlein, M., et al. (2017) · ACS Omega · doi:10.1021/acsomega.6b00482 · Cited by 17
Liu, X., Lv, M., Huang, M., Yu-qiu, S., Gao, P., & Li, D. (2019) · Journal of Food Biochemistry · doi:10.1111/jfbc.12955 · Cited by 18
Maity, D., Rahi, V., Dorai, S. T., Chandrashekharappa, S., & Kaundal, R. K. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00886 · Cited by 15
Quinuclidine-Based Carbamates as Potential CNS Active Compounds
Matošević, A., Kastelić, A. R., Mikelić, A., Zandona, A., Katalinić, M., Primožič, I., Bosak, A., & Hrenar, T. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13030420 · Cited by 16
A review of therapeutic failures in late-stage clinical trials
Jain, R., Subramanian, J., & Rathore, A. S. (2022) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2022.2161366 · Cited by 18
Jain, U., Johari, S., & Srivastava, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03671-7 · Cited by 16
Rodent Models of Alzheimer’s Disease: Past Misconceptions and Future Prospects
Collins, H. M., & Greenfield, S. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116222 · Cited by 21
Bhatt, A., Bhardwaj, H., & Srivastava, P. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.07.019 · Cited by 19
Similarity search combined with docking and molecular dynamics for novel hAChE inhibitor scaffolds
Borges, N. M., Sartori, G., Ribeiro, J. F. R., da Rocha, J. R., Martins, J. B. L., Montanari, C. A., & Gargano, R. (2018) · Journal of Molecular Modeling · doi:10.1007/s00894-017-3548-9 · Cited by 16
de Matos, A. M., Martins, A., Man, T., Evans, D. A. P., Walter, M. W., Oliveira, M. C., López, Ó., Fernández‐Bolaños, J. G., Dätwyler, P., Ernst, B., et al. (2019) · Pharmaceuticals · doi:10.3390/ph12020098 · Cited by 18
Metadata
- Authors
- Yiannopoulou, K. G., & Papageorgiou, S. G.
- Affiliations
- Laiko General Hospital of Athens (GR)
- National and Kapodistrian University of Athens (GR)
- Venue
- Therapeutic Advances in Neurological Disorders
- Publisher
- SAGE Publications
- Published
- 2012-10-15
- Volume
- 6
- Issue
- 1
- Pages
- 19-33
- ISSN
- 1756-2856 (ISSN-L)
- 1756-2864
- PMC
- PMC3526946
- OpenAlex
- W1987204546
- Cited by
- 677
- References
- 83
- Citations by year
- 2026: 35 · 2025: 55 · 2024: 66 · 2023: 70 · 2022: 84 · 2021: 81 · 2020: 83 · 2019: 61 · 2018: 45 · 2017: 37 · 2016: 27 · 2015: 9 · 2014: 9 · 2013: 14
- FWCI
- 6.86
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Therapeutic Advances in Neurological Disorders (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- 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
- Alzheimer's disease, cholinesterase inhibitors, memantine, disease-modifying therapy, symptomatic treatment, amyloid plaques, neurofibrillary tangles, oxidative stress, neuroinflammation, cholesterol metabolism, NMDA receptor antagonists, clinical trials
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
