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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.
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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]
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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
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Chen, L., Lu, L., Xu, G., Jiang, Z., Guo, Q., Huang, F., Yan, W., Zhang, H., Wu, Y., Xie, Y., et al. (2025) · Fitoterapia · doi:10.1016/j.fitote.2025.106564 · Cited by 3
Fatima, S. J., & Devarakonda, K. P. (2025) · Annals of Neurosciences · doi:10.1177/09727531251356049 · Cited by 6
Gomes, L. S., Schülerb, M. C. G. M., Giannini, G. B., Zapp, E., de Oliveira, A. S., & Nascimento, V. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118447 · Cited by 3
Wozniczka, C. M., & Weaver, D. F. (2026) · NeuroSci · doi:10.3390/neurosci7010013 · Cited by 3
Alimari, A., Seyedalipour, B., Baziyar, P., & Jalalian, E. J. (2026) · Journal of Chemistry · doi:10.1155/joch/8828325 · Cited by 3
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Pandey, J. (2023) · Springer eBooks · doi:10.1007/978-981-99-6038-5_11 · Cited by 3
Alotaibi, B. S., Saleem, U., Farrukh, M., Waseem, S., Chauhdary, Z., Alsharif, I., Al-Qahtani, W. S., Alanzi, A. R., BinMowyna, M. N., Shah, M. A., et al. (2024) · Italian Journal of Food Science · doi:10.15586/ijfs.v36i3.2643 · Cited by 3
Pandey, K., Srivastava, P., Pandey, S. K., Johari, S., Bhatnagar, P., Sonane, M., & Mishra, A. (2024) · Current Molecular Medicine · doi:10.2174/0115665240334785240913071442 · Cited by 3
Kalita, T., Dutta, S., Shakya, A., Ghosh, S. K., Singh, U. P., & Bhat, H. R. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.141577 · Cited by 3
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Patel, R. B., Thakore, S. D., & Patel, M. R. (2017) · Springer eBooks · doi:10.1007/978-3-319-70299-5_14 · Cited by 3
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Yin, Y., Zhang, J., & Zhou, X. (2022) · Highlights in Science Engineering and Technology · doi:10.54097/hset.v11i.1266 · Cited by 3
Salehi, N., Lohrasebi, A., & Bordbar, A. (2023) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2023.108516 · Cited by 3
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Nahar, A., Lukose, A., Ramesh, R. G., Purokayastha, S., Kadiveti, S. H., Thangaraju, S. P., & Rao, N. P. (2017) · Journal of the Indian Institute of Science · doi:10.1007/s41745-017-0051-3 · Cited by 3
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Rajakumar, P. D. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811405-6.00016-5 · Cited by 4
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Sharma, G., Sonu, & Harikumar, S. (2015) · International journal of pharma research and review · Cited by 3
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Mess, E., Witkowicz, M., Ornat, M., Sielski, P., & Klaszczyk, T. (2018) · Archives of Psychiatric Nursing · doi:10.1016/j.apnu.2018.03.008 · Cited by 3
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Liew, C. V., Wooldridge, J. S., Kothari, D. J., & Cronan, T. A. (2014) · Californian Journal of Health Promotion · doi:10.32398/cjhp.v12i1.1557 · Cited by 3
Malone, C., Turk, K. W., Palumbo, R., & Budson, A. E. (2020) · Journal of the International Neuropsychological Society · doi:10.1017/s1355617720000715 · Cited by 3
Nwafor, D. C., Chakraborty, S., Jun, S., Brichacek, A. L., Dransfeld, M., Gemoets, D. E., Dakhlallah, D. A., & Brown, C. M. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112983 · Cited by 3
Digala, L. P., Murala, S., & Bollu, P. C. (2022) · Springer eBooks · doi:10.1007/978-3-031-07897-2_11 · Cited by 3
Halder, A. K., Moura, A. S., & Cordeiro, M. N. D. S. (2018) · Methods in pharmacology and toxicology · doi:10.1007/7653_2018_14 · Cited by 3
Li, B., Yadav, S., Zhou, S. W., Du, Y., Qian, L., Karas, Z., Zhang, Y., Shen, L., Lee, J. J., Vardarajan, B. N., et al. (2023) · medRxiv · doi:10.1101/2023.04.06.23288268 · Cited by 3
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Webb, M. I. (2023) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2846 · Cited by 3
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Negi, M., Amulya, E., Phatale, V., Abraham, N., Hedaoo, A., Srinivasarao, D. A., & Srivastava, S. K. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123155 · Cited by 2
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Deore, A., Kothmire, S., Khade, A., & Bhalerao, S. (2025) · Research Journal of Pharmacognosy and Phytochemistry · doi:10.52711/0975-4385.2025.00036 · Cited by 2
Afify, A. M. R., El-Sayed, E. K., Ismail, A., & Nofal, S. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178411 · Cited by 2
Banu, Z., & Das, N. R. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01759-8 · Cited by 3
Ahn, N.-H., Hong, S.-C., Hong, C. R., Lee, E. H., Lee, J. H., Choi, S.-B., Jung, J., Kim, Y., Kim, J.-S., Park, K., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05680-8 · Cited by 2
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Bortolucci, W. D. C., Trettel, J. R., Bernardi, D. M., Souza, M. M. Q., Lopes, A. D., Lovato, E. C. W., Lívero, F. A. D. R., da SilvaU, G. J., Magalhães, H. M., de Souza, S. G. H., et al. (2020) · Boletin Latinoamericano y del Caribe de plantas Medicinales y Aromaticas · doi:10.37360/blacpma.20.19.5.30 · Cited by 2
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Roy, M., & Dey, S. G. (2022) · Advances in inorganic chemistry · doi:10.1016/bs.adioch.2022.07.003 · Cited by 2
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
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