FDA approves Alzheimer’s drug lecanemab amid safety concerns

Reardon, Sara

doi:10.1038/d41586-023-00030-3

Cited by 182Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchPharmacovigilance and Adverse Drug Reactions

FDA approves Alzheimer’s drug lecanemab amid safety concerns

Reardon, Sara·2023·Nature

DOI 10.1038/d41586-023-00030-3

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1038/d41586-023-00030-3

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Aducanumab was given FDA approval under the expedited approval pathway to treat moderate AD.
“Aducanumab has been given FDA approval under the expedited approval pathway to treat moderate AD [134,135,136].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [136]
Reduction in amyloid-beta brain plaques and encouraging clinical outcomes in one of two pivotal Phase III trials were factors cited for aducanumab's expedited approval.
“The reduction in amyloid-beta brain plaques, a purported surrogate endpoint that indicates the “progression” of AD, and the encouraging clinical outcomes in one of the two pivotal Phase III trials were two of the factors cited for aducanumab’s expedited approval [130,134,135,136].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [136]
Lecanemab is a humanized IgG1 monoclonal antibody specifically targeting aggregated forms of amyloid beta and was given fast approval by the FDA.
“Lecanemab (LEQEMBI, brand name), a different monoclonal antibody known as humanized immunoglobulin G1 (IgG1), which specifically targets aggregated forms of amyloid beta, was also given fast approval by the FDA earlier in the year [134,135,136].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [136]

Lecanemab in early Alzheimer's disease
van Dyck, C. H., Swanson, C. J., Aisen, P., Bateman, R. J., Chen, C., Gee, M., Kanekiyo, M., Li, D., Reyderman, L., Cohen, S., et al. (2023) · New England Journal of Medicine · doi:10.1056/nejmoa2212948 · Cited by 5,678 · see citing works
A randomized, double-blind, phase 2b proof-of-concept clinical trial in early Alzheimer’s disease with lecanemab, an anti-Aβ protofibril antibody
Swanson, C. J., Zhang, Y., Dhadda, S., Wang, J., Kaplow, J., Lai, R. Y. K., Lannfelt, L., Bradley, H., Rabe, M., Koyama, A., et al. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00813-8 · Cited by 847 · see citing works

Flagged first, then by citations

Sorted by citations

Tracking neuroinflammatory biomarkers in Alzheimer’s disease: a strategy for individualized therapeutic approaches?
Lista, S., Imbimbo, B. P., Grasso, M., Fidilio, A., Emanuele, E., Minoretti, P., López-Ortiz, S., Martín-Hernández, J., Gabelle, A., Caruso, G., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03163-y · Cited by 81 · see citing works
Brain uptake pharmacokinetics of albiglutide, dulaglutide, tirzepatide, and DA5-CH in the search for new treatments of Alzheimer’s and Parkinson’s diseases
Rhea, E. M., Babin, A., Thomas, P., Omer, M., Weaver, R., Hansen, K., Banks, W. A., & Talbot, K. (2024) · Tissue Barriers · doi:10.1080/21688370.2023.2292461 · Cited by 81 · see citing works
Alzheimer’s disease and neuroinflammation: will new drugs in clinical trials pave the way to a multi-target therapy?
Melchiorri, D., Merlo, S., Micallef, B., Borg, J.-J., & Dráfi, F. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1196413 · Cited by 72 · see citing works
Alzheimer blood biomarkers: practical guidelines for study design, sample collection, processing, biobanking, measurement and result reporting
Zeng, X., Chen, Y., Sehrawat, A., Lee, J., Lafferty, T. K., Kofler, J., Berman, S. B., Sweet, R. A., Tudorascu, D., Klunk, W. E., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00711-1 · Cited by 73 · see citing works
The Amyloid-Beta Clearance: From Molecular Targets to Glial and Neural Cells
Cai, W., Wu, T., & Chen, N. (2023) · Biomolecules · doi:10.3390/biom13020313 · Cited by 65 · see citing works
Initial Experience with Lecanemab and Lessons Learned in 71 Patients in a Regional Medical Center
Shields, L. B. E., Hust, H. S., Cooley, S. D., Cooper, G. E., Hart, R. N., Dennis, B. C., Freeman, S. W., Cain, J., Shang, W. Y., Wasz, K. M., et al. (2024) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2024.159 · Cited by 57 · see citing works
Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease
Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works
“Lecanemab (LEQEMBI, brand name), a different monoclonal antibody known as humanized immunoglobulin G1 (IgG1), which specifically targets aggregated forms of amyloid beta, was also given fast approval by the FDA earlier in the year [134–136].”
BackgroundResult
Molecular insights into the pathogenic impact of vitamin D deficiency in neurological disorders
Anwar, M. J., Alenezi, S. K., & Alhowail, A. H. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114718 · Cited by 60 · see citing works
Decreased Cerebrospinal Fluid Amyloid β 38, 40, 42, and 43 Levels in Sporadic and Hereditary Cerebral Amyloid Angiopathy
de Kort, A. M., Kuiperij, H. B., Marques, T. M., Jäkel, L., van den Berg, E., Kersten, I., van Berckel‐Smit, H. E. P., Duering, M., Stoops, E., Abdo, W. F., et al. (2023) · Annals of Neurology · doi:10.1002/ana.26610 · Cited by 49 · see citing works
Natural Alkaloids as Multi-Target Compounds towards Factors Implicated in Alzheimer’s Disease
Vrabec, R., Blunden, G., & Cahlíková, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054399 · Cited by 46 · see citing works
In 2024, the amyloid-cascade-hypothesis still remains a working hypothesis, no less but certainly no more
Behl, C. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1459224 · Cited by 48 · see citing works
Enhancing the Therapeutic Effect in Alzheimer's Disease Drugs: The role of Polypharmacology and Cholinesterase inhibitors
Martins, M. M., Branco, P. S., & Ferreira, L. M. (2023) · ChemistrySelect · doi:10.1002/slct.202300461 · Cited by 45 · see citing works
A Nanozyme-Boosted MOF-CRISPR Platform for Treatment of Alzheimer’s Disease
Yang, J., Qin, G., Liu, Z., Zhang, H., Du, X., Ren, J., & Qu, X. (2024) · Nano Letters · doi:10.1021/acs.nanolett.4c02272 · Cited by 42 · see citing works
Gut-brain axis: gut dysbiosis and psychiatric disorders in Alzheimer’s and Parkinson’s disease
Denman, C. R., Park, S. M., & Jo, J. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1268419 · Cited by 43 · see citing works
The multiple roles of chronic stress and glucocorticoids in Alzheimer's disease pathogenesis
Burke, M. R., Sotiropoulos, I., & Waites, C. L. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2024.08.015 · Cited by 40 · see citing works
Biomarkers for Managing Neurodegenerative Diseases
Cheslow, L., Snook, A. E., & Waldman, S. A. (2024) · Biomolecules · doi:10.3390/biom14040398 · Cited by 40 · see citing works
The Vascular-Immune Hypothesis of Alzheimer’s Disease
Mehta, R. I., & Mehta, R. I. (2023) · Biomedicines · doi:10.3390/biomedicines11020408 · Cited by 39 · see citing works
Prevention and Treatment Strategies for Alzheimer’s Disease: Focusing on Microglia and Astrocytes in Neuroinflammation
Zhang, S.-S., Gao, Z., Feng, L., & Li, M. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s483412 · Cited by 38 · see citing works
Lipid metabolism transcriptomics of murine microglia in Alzheimer’s disease and neuroinflammation
Shippy, D. C., & Ulland, T. K. (2023) · Scientific Reports · doi:10.1038/s41598-023-41897-6 · Cited by 35 · see citing works
Curcumin-derived carbon quantum dots: Dual actions in mitigating tau hyperphosphorylation and amyloid beta aggregation
Lim, J. L., Lin, C., Huang, C., & Chang, L. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113676 · Cited by 34 · see citing works
Photobiomodulation in Alzheimer’s Disease—A Complementary Method to State-of-the-Art Pharmaceutical Formulations and Nanomedicine?
Ailioaie, L. M., Ailioaie, C., & Litscher, G. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030916 · Cited by 37 · see citing works
The 2022 yearbook of Neurorestoratology
Huang, H., Bach, J. R., Sharma, H. S., Saberi, H., Jeon, S. R., Guo, X., Shetty, A. K., Hawamdeh, Z. M., Sharma, A., Wild, K. V., et al. (2023) · Journal of Neurorestoratology · doi:10.1016/j.jnrt.2023.100054 · Cited by 34 · see citing works
Emerging Alzheimer’s disease therapeutics: promising insights from lipid metabolism and microglia-focused interventions
Tobeh, N. S., & Bruce, K. D. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1259012 · Cited by 31 · see citing works
Lecanemab: More Questions Than Answers!
Kaur, U., Reddy, J., Tiwari, A., Chakrabarti, S., & Chakrabarti, S. S. (2023) · Clinical Drug Investigation · doi:10.1007/s40261-023-01331-1 · Cited by 30 · see citing works
HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species
Chen, S., Puri, A., Bell, B., Fritsche, J., Palacios, H. H., Balch, M., Sprunger, M. L., Howard, M. K., Ryan, J. J., Haines, J. N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46538-8 · Cited by 31 · see citing works
The Breakthroughs and Caveats of Using Human Pluripotent Stem Cells in Modeling Alzheimer’s Disease
Bendtsen, K. M., & Hall, V. J. (2023) · Cells · doi:10.3390/cells12030420 · Cited by 27 · see citing works
PCSK9 inhibition attenuates alcohol-associated neuronal oxidative stress and cellular injury
Wagner, J., Park, L. M., Mukhopadhyay, P., Matyas, C., Trojnar, E., Damadzic, R., Jung, J., Bell, A. S., Mavromatis, L. A., Hamandi, A. M., et al. (2024) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2024.04.022 · Cited by 26 · see citing works
Cutting-edge Strategies for Overcoming Therapeutic Barriers in Alzheimer's Disease
Inamdar, A., Gurupadayya, B., Halagali, P., Nandakumar, S., Pathak, R., Singh, H., & Sharma, H. (2024) · Current Pharmaceutical Design · doi:10.2174/0113816128344571241018154506 · Cited by 27 · see citing works
Role of microbial dysbiosis in the pathogenesis of Alzheimer's disease
Susmitha, G., & Kumar, R. K. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109478 · Cited by 26 · see citing works
Monoclonal antibodies and aptamers: The future therapeutics for Alzheimer's disease
Barrera-Ocampo, A. A. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.03.034 · Cited by 27 · see citing works
Neuronanomedicine for Alzheimer’s and Parkinson’s disease: Current progress and a guide to improve clinical translation
Boyton, I., Valenzuela, S. M., Collins‐Praino, L. E., & Care, A. (2023) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2023.11.004 · Cited by 23 · see citing works
Polysaccharides extracted from common buckwheat (Fagopyrum esculentum) attenuate cognitive impairment via suppressing RAGE/p38/NF-κB signaling and dysbiosis in AlCl3-treated rats
Liu, Y.-C., Chen, S.-Y., Chen, Y.-Y., Chang, H., Chiang, I., & Yen, G. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133898 · Cited by 24 · see citing works
Emergence of the brain-border immune niches and their contribution to the development of neurodegenerative diseases
Tan, L. Y., Cunliffe, G., Hogan, M. P., Yeo, X. Y., Oh, C., Jin, B., Kang, J., Park, J., Kwon, M., Kim, M., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1380063 · Cited by 22 · see citing works
Quinolinetrione-tacrine hybrids as multi-target-directed ligands against Alzheimer's disease
Uliassi, E., Bergamini, C., Rizzardi, N., Naldi, M., Cores, Á., Bartolini, M., Menéndez, J. C., & Bolognesi, M. L. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117419 · Cited by 23 · see citing works
Food and Drug Administration (FDA) Approvals of Biological Drugs in 2023
Martins, A. C., Oshiro, M. Y., Alberício, F., & de la Torre, B. G. (2024) · Biomedicines · doi:10.3390/biomedicines12091992 · Cited by 25 · see citing works
Immunotherapies Targeting Amyloid and Tau Protein in Alzheimer’s Disease: Should We Move Away from Diseases and Focus on Biological Targets? A Systematic Review and Expert Opinion
Esquer, A., Blanc, F., & Collongues, N. (2023) · Neurology and Therapy · doi:10.1007/s40120-023-00541-1 · Cited by 25 · see citing works
Alzheimer's Disease and Frontotemporal Dementia: A Review of Pathophysiology and Therapeutic Approaches
Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 25 · see citing works
Improved prebiotic-based “shield” equipped probiotics for enhanced colon cancer therapy by polarizing M1 macrophages and regulating intestinal microbiota
Wang, Y., Su, X., Liu, Y., Hu, L., Lin, K., Xu, C., Sun, Z., Sun, C., Guo, H., & Shen, S. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.05.040 · Cited by 21 · see citing works
Changes of tRNA-Derived Fragments by Alzheimer’s Disease in Cerebrospinal Fluid and Blood Serum
Wu, W., Shen, A., Lee, I., Miranda-Morales, E. G., Spratt, H. M., Pappolla, M. A., Fang, X., & Bao, X. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230412 · Cited by 20 · see citing works
Glycolytic dysregulation in Alzheimer’s disease: unveiling new avenues for understanding pathogenesis and improving therapy
Wu, Y., Yang, L., Jiang, W., Zhang, X., & Yao, Z. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00190 · Cited by 19 · see citing works
Advances in PET imaging of protein aggregates associated with neurodegenerative disease
Higuchi, M., Tagai, K., Takahata, K., & Endo, H. (2025) · Nature Reviews Neurology · doi:10.1038/s41582-025-01126-2 · Cited by 19 · see citing works
Recent progress of small-molecule-based theranostic agents in Alzheimer's disease
Gao, F., Chen, J., Zhou, Y., Cheng, L., Hu, M., & Wang, X. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00330b · Cited by 18 · see citing works
Multi-target potential of newly designed tacrine-derived cholinesterase inhibitors: Synthesis, computational and pharmacological study
Jevtić, I. I., Suručić, R. V., Tovilović-Kovačević, G., Zogovic, N. S., Kostić‐Rajačić, S., Andrić, D. B., & Penjišević, J. Z. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117649 · Cited by 18 · see citing works
The efficacy and safety of lecanemab 10 mg/kg biweekly compared to a placebo in patients with Alzheimer’s disease: a systematic review and meta-analysis of randomized controlled trials
Abdelazim, K., Allam, A. A., Afifi, B., Abdulazeem, H. M., & Elbehiry, A. I. (2024) · Neurological Sciences · doi:10.1007/s10072-024-07477-w · Cited by 18 · see citing works
Alzheimer’s disease basics: we all should know
Das, S. K. (2025) · Neurological Research · doi:10.1080/01616412.2025.2529560 · Cited by 19 · see citing works
Δ8-THC Protects against Amyloid Beta Toxicity Modulating ER Stress In Vitro: A Transcriptomic Analysis
Gugliandolo, A., Blando, S., Salamone, S., Caprioglio, D., Pollastro, F., Mazzon, E., & Chiricosta, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076598 · Cited by 17 · see citing works
Prevalence of Cerebral Amyloid Angiopathy Pathology and Strictly Lobar Microbleeds in East-Asian Versus Western Populations: A Systematic Review and Meta-Analysis
de Kort, A. M., Verbeek, M. M., Schreuder, F. H. B. M., Klijn, C. J. M., & Jäkel, L. (2024) · Journal of Stroke · doi:10.5853/jos.2023.04287 · Cited by 17 · see citing works
Exploring Peptido‐Nanocomposites in the Context of Amyloid Diseases
Andrikopoulos, N., Tang, H., Wang, Y., Liang, X., Li, Y., Davis, T. P., & Ke, P. C. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202309958 · Cited by 15 · see citing works
A randomized feasibility trial of the modified Atkins diet in older adults with mild cognitive impairment due to Alzheimer’s disease
Buchholz, A. S., Deme, P., Betz, J., Brandt, J., Haughey, N. J., & Cervenka, M. C. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1182519 · Cited by 15 · see citing works
Refining the interactions between microglia and astrocytes in Alzheimer’s disease pathology
Chen, J., Xu, S., Wang, L., Liu, X., Liu, G., Tan, Q., Li, W., Zhang, S., & Du, Y. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.03.033 · Cited by 16 · see citing works
Inhibition of Amyloid β Aggregation and Cytotoxicity by Berbamine Hydrochloride
Dong, L., Xie, H., Jia, L., Hong, L., & Gao, L. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202301865 · Cited by 14 · see citing works
Lecanemab: A hope in the management of Alzheimer’s disease
Thakkar, N., Martis, P. B., Kutikuppala, L. V. S., Kuchana, S. K., & Mohapatra, R. K. (2023) · Brain Circulation · doi:10.4103/bc.bc_10_23 · Cited by 14 · see citing works
Long-term normalization of calcineurin activity in model mice rescues Pin1 and attenuates Alzheimer’s phenotypes without blocking peripheral T cell IL-2 response
Stallings, N. R., O’Neal, M. A., Hu, J., Shen, Z., & Malter, J. S. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01323-5 · Cited by 14 · see citing works
Hesperidin Methyl Chalcone reduces extracellular Aβ(25-35) peptide aggregation and fibrillation and also protects Neuro 2a cells from Aβ(25-35) induced neuronal dysfunction
Jafni, S., Sathya, S., Arunkumar, M., Kiruthiga, C., Jeyakumar, M., Murugesh, E., & Devi, K. P. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117536 · Cited by 14 · see citing works
Structure-based design of multitargeting ChEs-MAO B inhibitors based on phenyl ring bioisosteres: AChE/BChE selectivity switch and drug-like characterization.
Spada, G. L., Miniero, D. V., Rullo, M., Cipolloni, M., Delre, P., Colliva, C., Colella, M., Leonetti, F., Liuzzi, G., Mangiatordi, G., et al. (2024) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2024.116511 · Cited by 14 · see citing works
Targeting Tau Protein with Proximity Inducing Modulators: A New Frontier to Combat Tauopathies
Uliassi, E., Bolognesi, M. L., & Milelli, A. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00733 · Cited by 13 · see citing works
Progress in precision drug delivery systems for neurodegenerative diseases with muscle atrophy
Zhang, G., Hu, F., Zhang, Y., Li, D., Deng, Y., Yang, M., Huang, T., Deng, X., Li, Y., Fu, C., et al. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.111027 · Cited by 12 · see citing works
Non-invasive biomarkers for mild cognitive impairment and Alzheimer's disease
Botello‐Marabotto, M., Martínez‐Bisbal, M. C., Calero, M., Bernardos, A., Pastor, A. B., Medina, M., & Martínez‐Máñez, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106312 · Cited by 12 · see citing works
A case-control study of phosphodiesterase-5 inhibitor use and Alzheimer’s disease and related dementias among male and female patients aged 65 years and older supporting the need for a phase III clinical trial
Henry, D. S., & Pellegrino, R. (2023) · PLoS ONE · doi:10.1371/journal.pone.0292863 · Cited by 12 · see citing works
Dual inhibition of butyrylcholinesterase and p38α mitogen-activated protein kinase: A new approach for the treatment of Alzheimer's disease
Benetik, S. F., Knez, D., Obreza, A., Košak, U., & Gobec, S. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108748 · Cited by 13 · see citing works
Cerebral to Systemic Representations of Alzheimer’s Pathogenesis Stimulated by Polystyrene Nanoplastics
Wang, Y., Liang, X., Andrikopoulos, N., Zheng, S., Li, Y., & Ke, P. C. (2025) · Environment & Health · doi:10.1021/envhealth.5c00160 · Cited by 12 · see citing works
Novel drug-like fluorenyl derivatives as selective butyrylcholinesterase and β-amyloid inhibitors for the treatment of Alzheimer’s disease
Pasieka, A., Panek, D., Zaręba, P., Sługocka, E., Gucwa, N., Espargaró, A., Latacz, G., Khan, N., Bucki, A., Sabaté, R., et al. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117333 · Cited by 12 · see citing works
Monoclonal antibodies for the management of central nervous system diseases: clinical success and future strategies
Gautam, A. S., Pandey, S. K., Lasure, V., Dubey, S., & Singh, R. K. (2023) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2023.2227378 · Cited by 12 · see citing works
Clinical Characteristics, Neuroimaging Markers, and Outcomes in Patients with Cerebral Amyloid Angiopathy: A Prospective Cohort Study
Theodorou, A., Palaiodimou, L., Papagiannopoulou, G., Kargiotis, O., Psychogios, K., Safouris, A., Bakola, E., Chondrogianni, M. E., Kotsali-Peteinelli, V., Melanis, K., et al. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12175591 · Cited by 11 · see citing works
Advances in Understanding and Managing Alzheimer's Disease: From Pathophysiology to Innovative Therapeutic Strategies
Rathee, S., Sen, D., Pandey, V., & Jain, S. (2024) · Current Drug Targets · doi:10.2174/0113894501320096240627071400 · Cited by 13 · see citing works
Disrupted mitochondrial response to nutrients is a presymptomatic event in the cortex of the APPSAA knock‐in mouse model of Alzheimer's disease
Norambuena, A., Sagar, V. K., Wang, Z., Raut, P., Feng, Z., Wallrabe, H., Pardo, E., Kim, T., Alam, S. R., Hu, S., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14144 · Cited by 10 · see citing works
Cerebral biomimetic nano-drug delivery systems: A frontier strategy for immunotherapy
Tian, H., Yao, J., Ba, Q., Meng, Y., Cui, Y., Quan, L., Gong, W., Wang, Y., Yang, Y., Yang, M., et al. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.10.058 · Cited by 11 · see citing works
Proteomics revealed an association between ribosome-associated proteins and amyloid beta deposition in Alzheimer's disease
Feng, L., Wang, G., Song, Q., Feng, X., Su, J., Ji, G., & Li, M. (2023) · Metabolic Brain Disease · doi:10.1007/s11011-023-01330-3 · Cited by 11 · see citing works
A real-world pharmacovigilance study of adverse drug reactions associated with lecanemab and aducanumab based on WHO-VigiAccess and FAERS databases
Hu, H., Zhao, Y., Mao, J., He, J., Zhang, Y., Ye, H., & Yang, X. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1561020 · Cited by 10 · see citing works
Deciphering mechanisms of action of ACE inhibitors in neurodegeneration using Drosophila models of Alzheimer’s disease
Ghalayini, J., & Boulianne, G. L. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1166973 · Cited by 10 · see citing works
Novel Development and Prospects in Pathogenesis, Diagnosis, and Therapy of Alzheimer’s Disease
Teng, Z. (2024) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-230130 · Cited by 9 · see citing works
Study on the effect of 40 Hz non-invasive light therapy system. A protocol for a randomized, double-blinded, placebo-controlled clinical trial
Agger, M. P., Horning, M., Carstensen, M. S., Danielsen, E. R., Baandrup, A. O., Nguyen, M., Høgh, P., Miskowiak, K. W., Petersen, P. M., Madsen, K. H., et al. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1250626 · Cited by 9 · see citing works
Protein kinases as therapeutic targets for Alzheimer’s disease: a brief review
Silva, I. M. F., Franco, G. D. R. R., Gontijo, V. S., & Viegas, C. (2024) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2024.00092 · Cited by 9 · see citing works
Derivatives of 9-phosphorylated acridine as butyrylcholinesterase inhibitors with antioxidant activity and the ability to inhibit β-amyloid self-aggregation: potential therapeutic agents for Alzheimer’s disease
Makhaeva, G., Kovaleva, N., Rudakova, E., Boltneva, N., Lushchekina, S., Astakhova, T., Timokhina, E., Serebryakova, O., Shchepochkin, A. V., Averkov, M. A., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1219980 · Cited by 9 · see citing works
Exploration of the novel phthalimide-hydroxypyridinone derivatives as multifunctional drug candidates against Alzheimer’s disease
Zhu, X., Lv, Y., Fan, M., Guo, J., Zhang, Y., Gao, B., Zhang, C., & Xie, Y. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106817 · Cited by 9 · see citing works
Effects of Serious Games in Older Adults With Mild Cognitive Impairment
Wang, S., Kang, D. W., Um, Y. H., Kim, S., Lee, S., Lee, C. U., & Lim, H. K. (2024) · Psychiatry Investigation · doi:10.30773/pi.2023.0308 · Cited by 9 · see citing works
A Systematic Online Living Evidence Summary of experimental Alzheimer’s disease research
Hair, K., Wilson, E., Maksym, O., Macleod, M. R., & Sena, E. S. (2024) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2024.110209 · Cited by 9 · see citing works
Novel tacrine-based multi-target directed Ligands: Enhancing cholinesterase inhibition, NMDA receptor antagonism, and CNS bioavailability for Alzheimer's disease treatment.
Svobodová, B., Moravcova, Z., Misiachna, A., Nováková, G., Marek, A., Finger, V., Odvarkova, J., Pejchal, J., Karasova, J., Netolicky, J., et al. (2025) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2025.117678 · Cited by 10 · see citing works
Structure-based discovery of forsythoside A as an effective inhibitor to reduce the neurotoxicity of amyloid β
Bai, S., Wang, Y., Ye, W.-L., Wu, S.-Y., Jia, L., Hong, L., Xie, H., & Gao, L. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01587-y · Cited by 8 · see citing works
Bioactivated Glucoraphanin Improves Cell Survival, Upregulating Phospho-AKT, and Modulates Genes Involved in DNA Repair in an In Vitro Alzheimer’s Disease Model: A Network-Transcriptomic Analysis
Minuti, A., Mazzon, E., Iori, R., Chiricosta, L., & Artimagnella, O. (2024) · Nutrients · doi:10.3390/nu16234202 · Cited by 9 · see citing works
Amyloid Imaging–Based Food and Drug Administration Approval of Lecanemab to Treat Alzheimer Disease—What Lasts Long Finally Becomes Good?
Barthel, H. (2023) · Journal of Nuclear Medicine · doi:10.2967/jnumed.123.265667 · Cited by 8 · see citing works
Investigation of Novel Aronia Bioactive Fraction-Alginic Acid Nanocomplex on the Enhanced Modulation of Neuroinflammation and Inhibition of Aβ Aggregation
Jang, B.-K., Shin, S. J., Park, H. H., Kumar, V., Park, Y., Kim, J. Y., Kang, H., Park, S. Y., Kwon, Y., Shin, S.-E., et al. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics17010013 · Cited by 7 · see citing works
Advances of therapeutic strategies for Alzheimer’s disease
Guo, X., Yue, R.-Z., Cui, Z., Wang, S., Jia, T., Li, W., Zhang, W., Shan, L., & Li, C. (2025) · Journal of Neurology · doi:10.1007/s00415-025-13456-8 · Cited by 8 · see citing works
The Role of Bacopa monnieri in Alzheimer’s Disease: Mechanisms and Potential Clinical Use—A Review
Wiciński, M., Fajkiel-Madajczyk, A., Wójcicki, J., Ozorowski, M., & Szambelan, M. (2025) · Nutrients · doi:10.3390/nu17223538 · Cited by 7 · see citing works
P2Y1 receptor in Alzheimer’s disease
Luo, S., Wang, Y., & Hisatsune, T. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-02103 · Cited by 8 · see citing works
Quality by design endorsed fabrication of xanthohumol loaded solid nanostructured lipid carrier based powder for effective treatment of Alzheimer's disease in rats
Khandale, N. B., Birla, D., Alam, M. S., Bashir, B., Vishwas, S., Kumar, A., Potale, Y., Gupta, G., Negi, P., Alam, A., et al. (2025) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2025.106792 · Cited by 7 · see citing works
Therapeutic approaches using natural substances on the streptozotocin-induced animal model of sporadic Alzheimer’s disease: a systematic review
Alexandre-Silva, V., Pereira, G. C., & Ribeiro, A. M. (2023) · Oriental Pharmacy and Experimental Medicine · doi:10.1007/s13596-023-00696-0 · Cited by 7 · see citing works
Probing the interactions between amyloidogenic proteins and bio-membranes
Ma, L., Li, X., Petersen, R. B., Peng, A., & Huang, K. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.106984 · Cited by 7 · see citing works
Targeting Neuroinflammation and Cognitive Decline: First-in-Class Dual Butyrylcholinesterase and p38α Mitogen-Activated Protein Kinase Inhibitors
Benetik, S. F., Proj, M., Knez, D., Košak, U., Meden, A., Krajšek, K., Pišlar, A. H., Horvat, S., Švajger, U., Tešić, N., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00933 · Cited by 6 · see citing works
CRM197-scaffolded vaccines designed by epitope grafting ameliorate cognitive decline in an Alzheimer's disease model
Cui, W., Wang, Y., Tang, X., Liu, S., Duan, Y., Gu, T., Mao, J., Li, W., Bao, J., & Wei, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136477 · Cited by 6 · see citing works
Bisphosphonates and the risk of dementia in patients with osteoporosis or fragility fracture: A population‐based study in Hong Kong
Sing, C., Chan, K., Chiu, P. K. C., Lau, W. C. Y., Zhang, X., Tan, K. C. B., & Cheung, C. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70503 · Cited by 7 · see citing works
Analysis of Costs for Imaging-Assisted Pharmaceutical Intervention in Alzheimer’s Disease with Lecanemab: Snapshot of the First 3 Years
Perron, J., Scramstad, C., & Ko, J. H. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230633 · Cited by 6 · see citing works
Unraveling the dual role of ADAM10: Bridging the gap between cancer and Alzheimer’s disease
Alexandre-Silva, V., & Cominetti, M. R. (2024) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2024.111928 · Cited by 6 · see citing works
Inhibition of FAM19A5 restores synaptic loss and improves cognitive function in mouse models of Alzheimer’s diseasePreprint
Kim, H., Yoo, S., Kwak, H., Ma, S., Kim, R., Lee, M., Ha, N., Pyo, S., Kwon, S.-G., Cho, E.-H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.22.568357 · Cited by 6 · see citing works
Leveraging targeted kinase degradation as a novel therapeutic strategy for Alzheimer's disease
Tassinari, E., & Milelli, A. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00681c · Cited by 5 · see citing works
The identification of a Distinct Astrocyte Subtype that Diminishes in Alzheimer’s Disease
Wei, H., Withrow, J. S., Rakshit, J., Amin, F. U., Nahm, J., Mowry, F. E., Mao, Z., Bhattacharjee, M. B., Zhu, J., Yang, Y., et al. (2024) · Aging and Disease · doi:10.14336/ad.2024.0205-1 · Cited by 5 · see citing works
Identification of a specific APOE transcript and functional elements associated with Alzheimer’s disease
Chen, Q., Aguirre, L., Liang, G., Zhao, H., Dong, T., Borrego, F., de Rojas, I., Hu, Q., Reyes, C., Su, L., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00751-7 · Cited by 5 · see citing works
Effect of Low-Frequency, Low-Energy Pulsed Electromagnetic Fields in Neuronal and Microglial Cells Injured with Amyloid-Beta
Merighi, S., Nigro, M., Travagli, A., Fernández, M., Vincenzi, F., Varani, K., Pasquini, S., Borea, P. A., Salati, S., Cadossi, R., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312847 · Cited by 5 · see citing works
Potential molecular mechanisms of tobacco smoke exposure in Alzheimer’s disease
Xie, Y., Yang, M., Wang, H., Chen, Y., Shi, X., Tang, H., & Sun, Q. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149394 · Cited by 5 · see citing works
Phyto-nanotechnology: A novel beneficial strategy for Alzheimer's disease therapy
Ganguly, S. C., Sangram, S., Paul, S., & Kundu, M. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105868 · Cited by 5 · see citing works

Authors: Reardon, S.
Corresponding author: Reardon, Sara
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2023-01-07
Volume: 613
Issue: 7943
Pages: 227-228
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/d41586-023-00030-3
OpenAlex: W4315434323
Cited by: 180
References: 2
Citations by year: 2026: 16 · 2025: 33 · 2024: 66 · 2023: 65
Type: other
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Pharmacovigilance and Adverse Drug Reactions
Keywords: lecanemab, Alzheimer's disease, drug approval, drug safety, adverse events, anti-amyloid therapy, FDA
MeSH terms: Alzheimer Disease, Humans, United States, United States Food and Drug Administration, Drug Approval, Antibodies, Monoclonal, Humanized, Patient Safety

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

FDA approves Alzheimer’s drug lecanemab amid safety concerns

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks