Cited by 274Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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The Murine Version of BAN2401 (mAb158) Selectively Reduces Amyloid-β Protofibrils in Brain and Cerebrospinal Fluid of tg-ArcSwe Mice

Tucker, Stina, Möller, Christer, Tegerstedt, Karin, Lord, Anna, Laudon, Hanna, Sjödahl, Johan, Söderberg, Linda, Spens, Erika, Sahlin, Charlotte, Waara, Erik Rollman, Satlin, Andrew, Gellerfors, Pär, Osswald, Gunilla, Lannfelt, Lars·2015·Journal of Alzheimer’s Disease

DOI 10.3233/jad-140741

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Abstract

Amyloid-β (Aβ) immunotherapy for Alzheimer's disease (AD) has good preclinical support from transgenic mouse models and clinical data suggesting that a long-term treatment effect is possible. Soluble Aβ protofibrils have been shown to exhibit neurotoxicity in vitro and in vivo, and constitute an attractive target for immunotherapy. Here, we demonstrate that the humanized antibody BAN2401 and its murine version mAb158 exhibit a strong binding preference for Aβ protofibrils over Aβ monomers. Further, we confirm the presence of the target by showing that both antibodies efficiently immunoprecipitate soluble Aβ aggregates in human AD brain extracts. mAb158 reached the brain and reduced the brain protofibril levels by 42% in an exposure-dependent manner both after long-term and short-term treatment in tg-ArcSwe mice. Notably, a 53% reduction of protofibrils/oligomers in cerebrospinal fluid (CSF) that correlated with reduced brain protofibril levels was observed after long-term treatment, suggesting that CSF protofibrils/oligomers could be used as a potential biomarker. No change in native monomeric Aβ 42 could be observed in brain TBS extracts after mAb158-treatment in tg-ArcSwe mice. By confirming the specific ability of mAb158 to selectively bind and reduce soluble Aβ protofibrils, with minimal binding to Aβ monomers, we provide further support in favor of its position as an attractive new candidate for AD immunotherapy. BAN2401 has undergone full phase 1 development, and available data indicate a favorable safety profile in AD patients.

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Items 201–274 of 274

The Interaction between Oligodendrocytes and Aβ in Alzheimer's Disease
Wang, W., Huang, X., Xu, Z., & Yu, C. (2025) · Current Alzheimer Research · doi:10.2174/0115672050401966250625171338 · Cited by 3
“In addition, Aβ deposition can be significantly reduced by targeting knockdown of BACE1 in OLs, and the effects of this approach are comparable to the efficacy of FDA-approved Aβ antibodies [104, 105].”
Estimating the long-term health outcomes of treatment with lecanemab in early Alzheimer’s disease: a modelling study
Burn, O., Molloy, K., Kanekiyo, M., Parker, C., Rothwell, S. W., Pan, J. J., Trueman, D., & Ritchie, C. W. (2026) · Journal of Medical Economics · doi:10.1080/13696998.2025.2600875 · Cited by 3
Transport pathways across the blood-brain barrier for waste clearance and drug delivery
Gröbner, L. S., & Pietrzik, C. U. (2026) · Fluids and Barriers of the CNS · doi:10.1186/s12987-026-00812-7 · Cited by 4
“An effective Aβ plaque reduction was shown in animal models with a murine variant of lecanemab before [261, 263, 266].”
IGF-1 and Glucocorticoid Receptors Are Potential Target Proteins for the NGF-Mimic Effect of β-Cyclocitral from Lavandula angustifolia Mill. in PC12 Cells
An, C., Gao, L., Xiang, L., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189763 · Cited by 3
“Currently, the primary treatments available drugs for AD contain tacrine, rivastigmine, galantamine, donepezil, huperzine A, and memantine [3], and investigational drugs such as Lecanemab [4] and Donanemab [5] also show promise in clinical trials.”
Background
Diagnosis and Treatment of Alzheimer’s Disease: Current Update
Yim, Y., & Moon, W. (2025) · Journal of the Korean Society of Radiology · doi:10.3348/jksr.2024.0146 · Cited by 3
Initial Real-World Evidence for Lecanemab in the United States
Brixner, D. I., Zhao, C., Toyosaki, H., Frech, F. H., & Rosenbloom, M. H. (2025) · Drugs & Aging · doi:10.1007/s40266-025-01261-x · Cited by 3
“The molecule selectively targets large soluble protofibrils relative to monomers (> 1000-fold over Aβ monomers), while also interacting with the insoluble fibrils that are a major component of brain amyloid [18–20].”
Longitudinal pharmacokinetic and safety studies of an antibody-erythropoietin fusion protein for Alzheimer's disease
Chang, R., Chandrashekar, D. V., Roules, G. C., Jagadeesan, N., Iwasaki, E., Oyegbesan, A., Davtyan, H., & Sumbria, R. K. (2025) · International Journal of Pharmaceutics X · doi:10.1016/j.ijpx.2025.100459 · Cited by 3
“…dosing resulted in ⁓30 – 40 % reduction in A β load, which, though significant and in line with the reduction seen with the murine analog of Lecane-mab in AD mouse models (Lord et al., 2009; Tucker et al., 2015), is modest compared to the remarkable > 70 % reduction seen in the current study.”
A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils
Grover, S., Pham, T., Jones, A., Pereira, C. S., Maurino, M. V. D., Garrad, E. C., Makoni, N. J., Parks, A., Domalewski, R. J., Riggio, G., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15817 · Cited by 5
“BAN2401 displays selectivity for Aβ protofibrils and fibrils, reduces Aβ protofibril levels in the brain and CSF of an AD transgenic mouse model, and rescues neurons from Aβ- induced death (Englund et al., 2007; Söllvander et al., 2018; Tucker et al., 2015).”
Background
Alzheimer Disease
Waziry, R., & Williams, O. A. (2023) · Neurology Clinical Practice · doi:10.1212/cpj.0000000000200208 · Cited by 4
Lecanemab (Leqembi): an amyloid beta monoclonal antibody approved for the treatment of Alzheimer’s disease
Sang, Z. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23932-8.00035-2 · Cited by 3
Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds
Reyes, F. S. P., Sommerhage, S., Willbold, D., et al. (2025) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.70022 · Cited by 3
Modern Concepts of Alzheimer,s Disease Pathogenesis: Novel Approaches to Pharmacotherapy (Review)
Komleva, Y., Kuvacheva, N. V., Lopatina, O., Gorina, Y., Frolova, O., Teplyashina, E., Petrova, M., & Salmina, A. (2015) · Современные технологии в медицине · doi:10.17691/stm2015.7.3.19 · Cited by 2
Anti-amyloid antibody equilibrium binding to Aβ aggregates from human Alzheimer disease brainPreprint
Butler, P. M., Francis, A., Meunier, A. L., Anderson, A. K., Hennessey, E. L., Miller, M. B., Lemere, C. A., Selkoe, D. J., & Stern, A. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.20.654902 · Cited by 3
Establishment and verification of reference intervals for Alzheimer's disease plasma biomarkers based on evaluation of pre‐analytical procedures: a multicenter study
Jiang, W., Liu, J., Wu, Y., Li, J., Jin, H., Cui, Z., Chen, X., Lian, T., Lv, H., Han, B., et al. (2025) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.70194 · Cited by 2
Brain Amyloid Plaque Levels Affect Clinical Progression in Alzheimer Disease: Assessment of Amyloid PET and Change in CDR ‐ SB Utilizing Semi‐Mechanistic Model
Bhagunde, P. R., Penner, N., Willis, B. A., Bell, R., Charil, A., Irizarry, M. C., Hersch, S. M., & Reyderman, L. (2026) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.70173 · Cited by 2
Lecanemab for treatment of individuals with early Alzheimer’s Disease (AD) who are apolipoprotein E ε4 (ApoE ε4) non-carriers or heterozygotes
Perry, R. J., Kipps, C., Martín, M., Bozzali, M., Logroscino, G., Trafford, S. J., Dhadda, S., Kanekiyo, M., Amanda, G., Hodgkinson, M., et al. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2026.100507 · Cited by 4
“Lecanemab is a novel humanized immunoglobulin G1 monoclonal antibody developed against A β protofibrils, as the ‘Arctic ’ mutation in Swedish subjects with familial AD was found to have an increased propensity for aggregation of A β to form protofibrils [15,16].”
Characteristics of infusion-related reactions to lecanemab in early Alzheimer’s disease: A multicenter real-world study in Northwestern China
Liu, P., Liu, J., Wang, J., Du, Y., Liu, Z., Zhang, H., Zhu, A., Zhang, G., Meng, X., Zhao, C., et al. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2026.100542 · Cited by 3
Development of Monoclonal Antibody Therapeutics for Alzheimer's Disease
Takeda, M. (2022) · Taiwanese Journal of Psychiatry · doi:10.4103/tpsy.tpsy_31_22 · Cited by 2
TO MARKET, TO MARKET—2023: MACROMOLECULAR THERAPEUTICS
Lim, S. A., Agard, N. J., Kelly, R. L., Bell, B. N., Chen, S.-J., Gram, A. M., Moench, I., Pance, K., & Petojevic, T. (2024) · Medicinal chemistry reviews · doi:10.1021/mc-2024-vol59.ch20 · Cited by 2
Ectopic expression of Slc1a2 in the prefrontal cortex of sleep-deprived male mice counteracts the glutamate/GABA-glutamine dysfunction
Zhang, F., Yao, L., Jiang, L., Wang, Y., Tang, Y., Ouyang, B., Song, G., Li, X., Quan, X., Li, M., et al. (2025) · BMC Biology · doi:10.1186/s12915-025-02161-7 · Cited by 3
“The samples were then transferred to collection tubes and stored at − 80°C for subsequent ELISA [45].”
The tale of donanemab: God is in the details
Saido, T. C., & Iwata, N. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251371240 · Cited by 2
Pharmacotherapy for Alzheimer’s disease: what’s new on the horizon?
Khoury, R., Gallop, A., Roberts, K., Grysman, N., Lu, J., & Grossberg, G. T. (2022) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2022.2097868 · Cited by 2
“AHEAD3-45 plans to enroll around 1400 participants aged 55–80 years, having a first-degree relatively diagnosed with dementia onset before age 75, possessing at least one APOE4 allele, or elevated amyloid levels in the central nervous system (CNS) demonstrated by previous amyloid PET imaging or CSF measurements.”
BackgroundInfluential
SMPL Synaptic Membranes: Nanodisc-Mediated Synaptic Membrane Mimetics Expand the Toolkit for Drug Discovery and the Molecular Cell Biology of Synapses
Bu, R. L., Clark, J. R., DiChiara, T., Sligar, S. G., & Klein, W. L. (2018) · Neuromethods · doi:10.1007/978-1-4939-8739-9_13 · Cited by 2
Immunotherapy: An Approach to Treat Alzheimer’s Disease and Autism Spectrum Disorder
Maarfi, F., Hasan, Z., Khanam, A., Husain, A., Khan, M. H., & Khan, M. Y. (2021) · Springer eBooks · doi:10.1007/978-981-16-4558-7_11 · Cited by 3
Targeting Soluble Amyloid-Beta Oligomers With a Novel NanobodyPreprint
Haynes, J. R., Whitmore, C. A., Behof, W. J., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-3944211/v1 · Cited by 2
“This antibody binds preferentially to soluble protofibrils over mature, insoluble fibrils but has no affinity for amyloid precursor protein (APP) 35-38 .”
Background
Monoclonal antibody therapy in Alzheimer’s disease: an overview and vision
Bentley, J. H., Bishop, L. E., & Broussard, J. I. (2024) · Brain Network and Modulation · doi:10.4103/bnm.bnm_14_23 · Cited by 2
Recent updates on immunotherapy in neurodegenerative diseases
Salunkhe, J., & Ugale, R. R. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149205 · Cited by 2
Antibodies against Alzheimer's: Pioneering a New Era in Treatment Strategies
Verma, M., Singh, N. K., & Siddique, M. U. M. (2025) · Current Bioactive Compounds · doi:10.2174/0115734072347198241226113039 · Cited by 1
Social Isolation as a Risk Factor for Dementia: Insights from Animal Model Studies
Araki, W. (2025) · Current Alzheimer Research · doi:10.2174/0115672050373522250421054927 · Cited by 1
Prospects for treating Alzheimer’s disease
Васильевна, В. Н., Novikov, D. K., Vekhova, K. A., Zhuk, A. M., Klimanovich, D. L., Isaikin, A. I., & Zakharov, V. V. (2025) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro202512504254 · Cited by 1
Self-assembling ferritin nanoplatform enables amyloid-β-targeted immunotherapy and cognitive rescue in APP/PS1 mice
Liu, J., Zhang, C., Zhao, L., Liu, R., Cao, T., Zhang, D., Liu, Z., Sun, D., Zhang, Y., Yu, X., et al. (2026) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2026.106486 · Cited by 1
Pharmacokinetic/pharmacodynamic analyses of plasma pathophysiology biomarkers in subjects with early Alzheimer's disease following lecanemab treatment
Bhagunde, P. R., Penner, N., Willis, B. A., Bell, R. D., Sachdev, P., Charil, A., Irizarry, M. C., Hersch, S. M., & Reyderman, L. (2026) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.70246 · Cited by 1
Neurotheranostics in Alzheimer's Disease: Current concepts and experimental strategies
Yanagisawa, D., Ohgita, T., Kawashima, H., Yoshikawa, H., Saito, H., Tooyama, I., & Takata, K. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109084 · Cited by 1
[Progress of clinical trials in Alzheimer’s disease drugs].
Peng, Y., Li, P., Li, L., Zhang, Y., Hou, W.-Z., Cui, D.-D., Li, J., Wang, L., Wang, Q., & Wang, X. (2016) · PubMed · Cited by 1
Immunotherapy in Alzheimer’s Disease
Gupta, J., & Hoque, M. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_14 · Cited by 2
Commentaries: Lecanemab: pioneering the way as the first approved drug for Alzheimer’s disease treatment
Zhang, J. (2023) · Inflammation Research · doi:10.1007/s00011-023-01788-y · Cited by 1
A Review of Clinical Biomarker Insights: Advances in Diagnosis and Prognosis of Early Alzheimer
Rajagopalan, R., Hariharan, S., Akshaya, N. R., & Senthamarai, R. (2025) · Global Journal of Medical Pharmaceutical and Biomedical Update · doi:10.25259/gjmpbu_38_2024 · Cited by 1
Aducanumab and lecanemab – two novel antibodies against pathologic species of amyloid beta in the treatment of Alzheimer’s disease
Wojcieszak, J. (2023) · Farmacja Polska · doi:10.32383/farmpol/166243 · Cited by 1
Current and Prospective Treatments for Alzheimer's Disease (and Other Neurodegenerative Diseases)
Pedrini, S., Morici, M., & Martins, R. N. (2019) · Wiley eBooks · doi:10.1002/9781119356752.ch14 · Cited by 1
Identification of Fibrinogen as a Plasma Protein Binding Partner for Lecanemab Biosimilar IgG: Implications for Alzheimer’s Disease TherapyPreprint
Bellier, J., Viera, A. M. R., Christiano, C., Anzai, J. A. U., Moreno, S., Campbell, E. C., Godwin, L., Li, A., Chen, A. Y., Alam, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.01.591892 · Cited by 1
Strategies for Neuroprotection in Alzheimer's Disease
Jasutkar, H. G. (2025) · Wiley eBooks · doi:10.1002/9783527844678.ch5 · Cited by 1
Amyloid-β Protofibrils in Alzheimer´s Disease : Focus on Antibodies, Inflammation and Astrocytes
Söllvander, S. (2015) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Immunotherapeutic Approaches Against Amyloid-β in Drug Discovery for Alzheimer’s Disease
Yang, S., Kim, J., & Kim, Y. S. (2015) · Springer eBooks · doi:10.1007/978-4-431-55763-0_22
Immunotherapy Against Amyloid-β Protofibrils: Opportunities and Challenges
Lannfelt, L. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-3560-4_4
Self-citation
Customer Loyalty in E-Business.
Raggad, B. G., & Lawler, J. E. (2003) · International Conference on Enterprise Information Systems
Innovative Therapeutic Development Programme for the Treatment of Early Alzheimer's Disease: Lecanemab (BAN2401)
Cummings, J. L. (2021) · touchREVIEWS in Neurology · doi:10.17925/usn.2021.17.2.70
Piecing Together the Alzheimer’s Puzzle: Lecanemab’s Role in Treatment
Ashraf, D. A., Tariq, H., Hassan, F. S., Kamran, F., Khosa, W. M., & Khosa, M. M. (2023) · Neurodegenerative Disease Management · doi:10.2217/nmt-2023-0026
Médicaments modificateurs de la maladie d’Alzheimer: implications pour la population canadienne
Watt, J. A., Isaranuwatchai, W., Grossman, L., & Straus, S. E. (2024) · Canadian Medical Association Journal · doi:10.1503/cmaj.230595-f
Major Neurocognitive Disorders Due to Alzheimer’s Disease
Joshi, P., Patel, N., & Gopalakrishna, G. (2024) · Springer eBooks · doi:10.1007/978-3-031-55711-8_1
Recent Updates on Immunotherapy in Neurodegenerative DiseasesPreprint
Salunkhe, J., & Ugale, R. R. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4854723
Therapeutic antibodies as a Wright Brothers' airplane: Clinical proof-of-concept
Saido, T. C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-28979-8.00015-2
The calcium channel blocker Cav2.1 combined with amyloid beta monoclonal antibodies may reduce the occurrence of ARIA-E
An, D., Li, X., & Xu, Y. Y. (2025) · Medical Hypotheses · doi:10.1016/j.mehy.2025.111576
Multiple Ischemic Strokes in a Patient Treated with Lecanemab: A Case ReportPreprint
Alammar, H., & Llano, D. A. (2025) · Research Square · doi:10.21203/rs.3.rs-5845699/v1
Aβ-HMGB1 complex is a pathogenic molecule at the advanced stage of Alzheimer’s diseasePreprint
Tanaka, H., Homma, H., Yoshioka, Y., Fujita, K., Yamada, S., Furukawa, K., Ishiki, A., Atsuta, N., Waragai, M., Mano, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.12.659430
Amyloid- and Tau-Targeted Therapies in Alzheimer’s Disease
Rajic, A. J., Galasko, D. R., & Tuszynski, M. H. (2025) · Springer eBooks · doi:10.1007/978-3-031-89307-0_17
Prospects for the Treatment of Alzheimer’s Disease
Васильевна, В. Н., Novikov, D. K., Vekhova, K. A., Zhuk, A. M., Klimanovich, D. L., Isaikin, A. I., & Zakharov, V. V. (2025) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-025-01882-0
“Therefore, an additional study (ENVISION) is currently under way to evaluate the ef ﬁ cacy of the drug [35].”
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Ufniarska, M., Ufniarski, T., Piech, A., Pasierb, K., Poplicha, K., Grodzińska, M., Siuzdak, B., Moszkowicz, J., Sobkiewicz, P., Kardasz, P., et al. (2025) · International Journal of Innovative Technologies in Social Science · doi:10.31435/ijitss.3(47).2025.3751
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Ueda-Martinez, E., & Ding, Y. (2025) · Environmental Disease · doi:10.4103/ed.ed_10_25
Use of rodent models in drug discovery for Alzheimer’s disease
Barrett, J. E., Mathiasen, J. R., & McGonigle, P. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-30008-0.00018-1
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Gustavsson, T., Metzendorf, N. G., Wik, E., Roshanbin, S., Julku, U. H., Chourlia, A., Nilsson, P., Andersson, K. G., Laudon, H., Hultqvist, G., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22735597
Self-citation
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Swanson, C. J., Zhang, Y., Dhadda, S., Wang, J., Kaplow, J. M., Lai, R. Y. K., Lannfelt, L., Bradley, H., Rabe, M. P., Koyama, A., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14444875
Self-citation
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Rofo, F., Buijs, J., Falk, R., Honek, K., Lannfelt, L., Lilja, A. M., Metzendorf, N. G., Gustavsson, T., Sehlin, D., Söderberg, L., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16689644
Self-citation
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McDade, E., Cummings, J. L., Dhadda, S., Swanson, C. J., Reyderman, L., Kanekiyo, M., Koyama, A., Irizarry, M. C., Kramer, L. D., & Bateman, R. J. (2023) · Figshare · doi:10.6084/m9.figshare.22603849
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Gustavsson, T., Metzendorf, N. G., Wik, E., Roshanbin, S., Julku, U. H., Chourlia, A., Nilsson, P., Andersson, K. G., Laudon, H., Hultqvist, G., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22735600
Self-citation
NEW DISEASE-MODIFYING THERAPIES IN ALZHEIMER’S DISEASE: A CLINICAL REVIEW OF LECANEMAB AND DONANEMAB
Ollik, K., Harenza, K., Taranowicz, M., Kowalczyk, O., Zdobylak, D., Kowalska, M., Zieba, A., Domin, M., Całka, J., & Ścibisz, K. (2026) · International Journal of Innovative Technologies in Social Science · doi:10.31435/ijitss.1(49).2026.4885
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Albanese, A., Natu, M. M., & Seidler, P. M. (2026) · Biophysica · doi:10.3390/biophysica6020031
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Strohl, W. R. (2026) · Antibody Therapeutics · doi:10.1093/abt/tbag027 · Cited by 6
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Mitsuoka, Y., Morimoto, T., Bando, K., Hara, S., Fujita, K., & Nishida, K. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06200
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Chatterjee, S., Gayen, S., & Roy, S. (2026) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9798898815646126010012
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Ferrer, A., & Moon, J. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261470042
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Passive immunotherapy in Alzheimer’s disease: biomarkers, biological staging, and emerging therapeutic strategies
Surhan, A., Oad, J., Kumar, B., Memon, S. N., Essrani, C., Muhammad, F., Kashif, S. N., Abbas, S. M. I., Ameen, T. B., Sauleh, A., et al. (2026) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-026-01263-5

Authors: Tucker, S., Möller, C., Tegerstedt, K., Lord, A., Laudon, H., Sjödahl, J., Söderberg, L., Spens, E., Sahlin, C., Waara, E. R., Satlin, A., Gellerfors, P., Osswald, G., & Lannfelt, L.
Affiliations: BioArctic Neuroscience (Sweden) (SE)
Eisai (United States) (US)
Uppsala University (SE)
ORCID: Sjödahl, Johan
Satlin, Andrew
Osswald, Gunilla
Lannfelt, Lars
Venue: Journal of Alzheimer’s Disease
Publisher: SAGE Publications
Published: 2014-11-21
Volume: 43
Issue: 2
Pages: 575-588
ISSN: 1387-2877 (ISSN-L)
1875-8908
DOI: 10.3233/jad-140741
OpenAlex: W1664338907
Cited by: 272
References: 0
Citations by year: 2026: 21 · 2025: 47 · 2024: 41 · 2023: 55 · 2022: 19 · 2021: 21 · 2020: 15 · 2019: 12 · 2018: 15 · 2017: 9 · 2016: 10 · 2015: 6
FWCI: 5.54
Type: journal article
Language: en
Open access: closed
Licence: journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)
Locations: Journal of Alzheimer s Disease (publishedVersion)
PubMed (publishedVersion)
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
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
MeSH terms: Alzheimer Disease, Analysis of Variance, Animals, Antibodies, Monoclonal, Brain, Disease Models, Animal, Dose-Response Relationship, Drug, Enzyme-Linked Immunosorbent Assay, Humans, Immunologic Factors, Mice, Inbred C57BL, Mice, Transgenic, Protein Binding, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Immunoprecipitation, Mice, Presenilin-1, Plaque, Amyloid

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The Murine Version of BAN2401 (mAb158) Selectively Reduces Amyloid-β Protofibrils in Brain and Cerebrospinal Fluid of tg-ArcSwe Mice

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