Acute targeting of pre-amyloid seeds in transgenic mice reduces Alzheimer-like pathology later in life
Open accessAbstract
Amyloid-β (Aβ) deposits are a relatively late consequence of Aβ aggregation in Alzheimer's disease. When pathogenic Aβ seeds begin to form, propagate and spread is not known, nor are they biochemically defined. We tested various antibodies for their ability to neutralize Aβ seeds before Aβ deposition becomes detectable in Aβ precursor protein-transgenic mice. We also characterized the different antibody recognition profiles using immunoprecipitation of size-fractionated, native, mouse and human brain-derived Aβ assemblies. At least one antibody, aducanumab, after acute administration at the pre-amyloid stage, led to a significant reduction of Aβ deposition and downstream pathologies 6 months later. This demonstrates that therapeutically targetable pathogenic Aβ seeds already exist during the lag phase of protein aggregation in the brain. Thus, the preclinical phase of Alzheimer's disease-currently defined as Aβ deposition without clinical symptoms-may be a relatively late manifestation of a much earlier pathogenic seed formation and propagation that currently escapes detection in vivo.
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
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?
CSF p-tau231 becomes abnormal first and seems the principal p-tau candidate to identify early Aβ seeds in the pre-amyloid phase, which is currently seen as the optimal period for therapeutic intervention.
“Specifically, CSF p-tau231 becomes abnormal first and seems the principal p-tau candidate to identify early Aβ seeds in the recently proposed “pre-amyloid phase”,32 which is currently seen as the optimal period for therapeutic intervention.”
From Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease (2022) · cites this paper as [32]
The Abstract and Discussion describe a pre-amyloid phase with targetable Aβ seeds and propose intervention before detectable deposition, based on a mouse model. They do not establish that CSF p-tau231 becomes abnormal first or is the principal marker of those seeds; the Discussion also says the efficacy of early seed removal in humans has not been established. (LLM, conf=0.88)
Experimental — accuracy not yet measuredEarly removal of Aβ seeds, before Aβ deposition becomes detectable, led to a significant reduction of Aβ accumulation and downstream pathologies in transgenic mice.
“a recent study in transgenic mice suggests that early removal of Aβ seeds, before Aβ deposition becomes detectable, led to a significant reduction of Aβ accumulation and downstream pathologies.32”
From Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease (2022) · cites this paper as [32]
Increases in CSF p-tau231 are related to early Aβ seeds and could act as a key biomarker for the pre-amyloid phase of AD, which occurs before the Aβ deposition threshold.
“Thus, one could propose that increases in CSF p-tau231 are related to early Aβ seeds and could act as a key biomarker for the recently described “pre-amyloid phase” of AD, which occurs before Aβ deposition threshold.32”
From Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease (2022) · cites this paper as [32]
mAducanumab treatment induces overexpression of genes in synapse organization, regulation of membrane potential, and neurotransmitter transport pathways in aged APPswe mouse hippocampus.
“Treatment with mAducanumab induced an overexpression of genes involved in synapse organization (GO:0050808), regulation of membrane potential (GO:0042391) and neurotransmitter transport (GO:0006836; Extended Data Fig. 8k) pathways, which might be attributed to the enhanced clearance of soluble Aβ seeds28 from the brain of aged APPswe mice.”
From Meningeal lymphatics affect microglia responses and anti-Aβ immunotherapy (2021) · cites this paper as [28]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
NIA‐AA Research Framework: Toward a biological definition of Alzheimer's disease
Jack, C. R., Bennett, D. A., Blennow, K., Carrillo, M. C., Dunn, B., Haeberlein, S. B., Holtzman, D. M., Jagust, W., Jessen, F., Karlawish, J., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.02.018 · Cited by 10,537 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Alzheimer Disease: An Update on Pathobiology and Treatment Strategies
Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204 · see citing works
The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · see citing works
Self-citationStages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years
Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194 · see citing works
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178 · see citing works
The Amyloid State of Proteins in Human Diseases
Eisenberg, D. S., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,732 · see citing works
Self-citationTwo amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works
Self-citationDeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298 · see citing works
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · see citing works
Self-citationDominantly Inherited Alzheimer Network, Preische, O., Schultz, S. A., Apel, A., Kuhle, J., Kaeser, S. A., Barro, C., Gräber, S., Kuder-Buletta, E., LaFougere, C., et al. (2019) · Nature Medicine · doi:10.1038/s41591-018-0304-3 · Cited by 927 · see citing works
Self-citationSperling, R. A., Jack, C. R., Black, S. E., Frosch, M. P., Greenberg, S. M., Hyman, B. T., Scheltens, P., Carrillo, M. C., Thies, W., Bednar, M. M., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.05.2351 · Cited by 857 · see citing works
On the lag phase in amyloid fibril formation
Arosio, P., Knowles, T. P. J., & Linse, S. S. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp05563b · Cited by 759 · see citing works
The Evolution of Preclinical Alzheimer’s Disease: Implications for Prevention Trials
Sperling, R., Mormino, E., & Johnson, K. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.038 · Cited by 725 · see citing works
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., & Fändrich, M. (2019) · Nature Communications · doi:10.1038/s41467-019-12683-8 · Cited by 593 · see citing works
Self-citationPeripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis
Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568 · see citing works
Self-citationCerebral Hemorrhage After Passive Anti-Aβ Immunotherapy
Pfeifer, M., Boncristiano, S., Bondolfi, L., Stalder, A., Deller, T., Staufenbiel, M., Mathews, P. M., & Jucker, M. (2002) · Science · doi:10.1126/science.1078259 · Cited by 511 · see citing works
Self-citationPropagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0238-6 · Cited by 450 · see citing works
Self-citationBohrmann, B., Baumann, K., Benz, J., Gerber, F., Huber, W., Knoflach, F., Messer, J., Oroszlan, K., Rauchenberger, R., Richter, W. F., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110977 · Cited by 448 · see citing works
A Plaque-Specific Antibody Clears Existing β-amyloid Plaques in Alzheimer's Disease Mice
DeMattos, R. B., Lu, J., Tang, Y., Racke, M. M., DeLong, C. A., Tzaferis, J. A., Hole, J. T., Forster, B. M., McDonnell, P. C., Liu, F., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.10.029 · Cited by 442 · see citing works
Imaging tau and amyloid-β proteinopathies in Alzheimer disease and other conditions
Villemagne, V. L., Doré, V., Burnham, S. C., Masters, C. L., & Rowe, C. C. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2018.9 · Cited by 440 · see citing works
Bacioglu, M., Maia, L. F., Preische, O., Schelle, J., Apel, A., Kaeser, S. A., Schweighauser, M., Eninger, T., Lambert, M., Pilotto, A., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.018 · Cited by 435 · see citing works
Self-citationPrion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β
Nussbaum, J. M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al. (2012) · Nature · doi:10.1038/nature11060 · Cited by 427 · see citing works
Self-citationPalmqvist, S., Mattsson, N., Hansson, O., & Initiative, F. T. A. D. N. (2016) · Brain · doi:10.1093/brain/aww015 · Cited by 400 · see citing works
Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β
Arndt, J. W., Qian, F., Smith, B. A., Quan, C., Kilambi, K. P., Bush, M. W., Walz, T., Pepinsky, R. B., Bussière, T., Hamann, S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-24501-0 · Cited by 364 · see citing works
Self-citationLa Joie, R., Ayakta, N., Seeley, W. W., Borys, E., Boxer, A. L., DeCarli, C., Doré, V., Grinberg, L. T., Huang, E., Hwang, J., et al. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.09.001 · Cited by 317 · see citing works
Adolfsson, O., Pihlgren, M., Toni, N., Varisco, Y., Buccarello, A. L., Antoniello, K., Lohmann, S., Piorkowska, K., Gafner, V., Atwal, J. K., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4742-11.2012 · Cited by 317 · see citing works
Consequence of Aβ immunization on the vasculature of human Alzheimer's disease brain
Boche, D., Zotova, E., Weller, R. O., Love, S., Neal, J. W., Pickering, R. M., Wilkinson, D., Holmes, C., & Nicoll, J. A. R. (2008) · Brain · doi:10.1093/brain/awn261 · Cited by 316 · see citing works
Longitudinal cognitive and biomarker changes in dominantly inherited Alzheimer disease
McDade, E., Wang, G., Gordon, B. A., Hassenstab, J., Benzinger, T. L. S., Buckles, V., Fagan, A. M., Holtzman, D. M., Cairns, N. J., Goate, A. M., et al. (2018) · Neurology · doi:10.1212/wnl.0000000000006277 · Cited by 314 · see citing works
Self-citationSpontaneous Hemorrhagic Stroke in a Mouse Model of Cerebral Amyloid Angiopathy
Winkler, D. T., Bondolfi, L., Herzig, M. C., Jann, L., Calhoun, M. E., Wiederhold, K., Tolnay, M., Staufenbiel, M., & Jucker, M. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-05-01619.2001 · Cited by 287 · see citing works
Self-citationDemattos, R. B., Bales, K. R., Parsadanian, M., O'Dell, M. A., Foss, E. M., Paul, S. M., & Holtzman, D. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00889.x · Cited by 253 · see citing works
Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition
Langer, F., Eisele, Y. S., Fritschi, S. K., Staufenbiel, M., Walker, L. C., & Jucker, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-11.2011 · Cited by 237 · see citing works
Self-citationStop Alzheimer’s before it starts
McDade, E., & Bateman, R. J. (2017) · Nature · doi:10.1038/547153a · Cited by 228 · see citing works
Rasmussen, J., Mahler, J., Beschörner, N., Kaeser, S. A., Häsler, L. M., Baumann, F., Nyström, S., Portelius, E., Blennow, K., Lashley, T., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713215114 · Cited by 228 · see citing works
Self-citationMaia, L. F., Kaeser, S. A., Reichwald, J., Hruscha, M., Martus, P., Staufenbiel, M., & Jucker, M. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006446 · Cited by 204 · see citing works
Self-citationGüntert, A., Döbeli, H., & Bohrmann, B. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.08.027 · Cited by 180 · see citing works
Amyloid‐β immunotherapy for alzheimer disease: Is it now a long shot?
Panza, F., Lozupone, M., Seripa, D., & Imbimbo, B. P. (2019) · Annals of Neurology · doi:10.1002/ana.25410 · Cited by 178 · see citing works
Upadhaya, A. R., Kosterin, I., Kumar, S., Arnim, C. A. F. V., Yamaguchi, H., Fändrich, M., Walter, J., & Thal, D. R. (2014) · Brain · doi:10.1093/brain/awt362 · Cited by 165 · see citing works
New roles for Fc receptors in neurodegeneration-the impact on Immunotherapy for Alzheimer's Disease
Fuller, J. P., Stavenhagen, J. B., & Teeling, J. L. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00235 · Cited by 154 · see citing works
Self-citationAnalysis of Amyloid Aggregates Using Agarose Gel Electrophoresis
Bagriantsev, S. N., Kushnirov, V. V., & Liebman, S. W. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)12003-0 · Cited by 149 · see citing works
Memory decline accompanies subthreshold amyloid accumulation
Landau, S. M., Horng, A., Jagust, W. J., & Initiative, A. D. N. (2018) · Neurology · doi:10.1212/wnl.0000000000005354 · Cited by 145 · see citing works
Frost, J. L., Le, K. X., Cynis, H., Ekpo, E., Kleinschmidt, M., Palmour, R. M., Ervin, F. R., Snigdha, S., Cotman, C. W., Saido, T. C., et al. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.05.005 · Cited by 132 · see citing works
Self-citationAβ and tau prion-like activities decline with longevity in the Alzheimer’s disease human brain
Aoyagi, A., Condello, C., Stöhr, J., Yue, W., Rivera, B. M., Lee, J. C., Woerman, A. L., Halliday, G. M., van Duinen, S. G., Ingelsson, M., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat8462 · Cited by 130 · see citing works
Maier, F. C., Wehrl, H. F., Schmid, A. M., Mannheim, J. G., Wiehr, S., Lerdkrai, C., Calaminus, C., Stahlschmidt, A., Ye, L., Burnet, M. W. M., et al. (2014) · Nature Medicine · doi:10.1038/nm.3734 · Cited by 123 · see citing works
Self-citationEvidence for Age-Dependent in Vivo Conformational Rearrangement within Aβ Amyloid Deposits
Nyström, S., Psonka-Antonczyk, K. M., Ellingsen, P. G., Johansson, L. B. G., Reitan, N. K., Handrick, S., Prokop, S., Heppner, F. L., Wegenast‐Braun, B. M., Jucker, M., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb4000376 · Cited by 111 · see citing works
Self-citationRyan, D. A., Narrow, W. C., Federoff, H. J., & Bowers, W. J. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.05.001 · Cited by 97 · see citing works
Multiple Factors Contribute to the Peripheral Induction of Cerebral -Amyloidosis
Eisele, Y. S., Fritschi, S. K., Hamaguchi, T., Obermüller, U., Füger, P., Skodras, A., Schafer, C., Odenthal, J., Heikenwälder, M. F., Staufenbiel, M., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1608-14.2014 · Cited by 93 · see citing works
Self-citationAβ oligomers trigger and accelerate Aβ seeding
Katzmarski, N., Ziegler‐Waldkirch, S., Scheffler, N., Witt, C. C., Abou‐Ajram, C., Nuscher, B., Prinz, M., Haass, C., & Meyer‐Luehmann, M. (2019) · Brain Pathology · doi:10.1111/bpa.12734 · Cited by 85 · see citing works
Michno, W., Nyström, S., Wehrli, P. M., Lashley, T., Brinkmalm, G., Guérard, L., Syvänen, S., Sehlin, D., Kaya, I., Brinet, D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006604 · Cited by 73 · see citing works
Persistence of Aβ seeds in APP null mouse brain
Ye, L., Fritschi, S. K., Schelle, J., Obermüller, U., Degenhardt, K., Kaeser, S. A., Eisele, Y. S., Walker, L. C., Baumann, F., Staufenbiel, M., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4117 · Cited by 58 · see citing works
Self-citationThal, D. R., Beach, T. G., Zanette, M., Lilja, J., Heurling, K., Chakrabarty, A., Ismail, A., Farrar, G., Buckley, C. J., & Smith, A. P. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1897-9 · Cited by 55 · see citing works
Aβ seeding potency peaks in the early stages of cerebral β‐amyloidosis
Ye, L., Rasmussen, J., Kaeser, S. A., Marzesco, A., Obermüller, U., Mahler, J., Schelle, J., Odenthal, J., Krüger, C., Fritschi, S. K., et al. (2017) · EMBO Reports · doi:10.15252/embr.201744067 · Cited by 53 · see citing works
Self-citationIncreased CSF Aβ during the very early phase of cerebral Aβ deposition in mouse models
Maia, L. F., Kaeser, S. A., Reichwald, J., Lambert, M., Obermüller, U., Schelle, J., Odenthal, J., Martus, P., Staufenbiel, M., & Jucker, M. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505026 · Cited by 53 · see citing works
Self-citationComparing the efficacy and neuroinflammatory potential of three anti-abeta antibodies
Fuller, J. P., Stavenhagen, J. B., Christensen, S., Kartberg, F., Glennie, M. J., & Teeling, J. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1484-2 · Cited by 44 · see citing works
Self-citationNoncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.Preprint
Westermark, G., Fändrich, M., Lundmark, K., & Westermark, P. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024323 · Cited by 44 · see citing works
Amyloid precursor protein truncated at any of the ?-secretase sites is not cleaved to ?-amyloid
Paganetti, P., Lis, M., Klafki, H.-W., & Staufenbiel, M. (1996) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19961101)46:3 · Cited by 39 · see citing works
Self-citationAlzheimer Lesions in the Autopsied Brains of People 30 to 50 Years of Age
Pletniková, O., Rudow, G. L., Hyde, T. M., Kleinman, J. E., Ali, S. Z., Bharadwaj, R. A., Gangadeen, S., Crain, B. J., Fowler, D. R., Rubio, A. I., et al. (2015) · Cognitive and Behavioral Neurology · doi:10.1097/wnn.0000000000000071 · Cited by 39 · see citing works
Das, P., Verbeeck, C., Minter, L. M., Chakrabarty, P., Felsenstein, K. M., Kukar, T. L., Maharvi, G. M., Fauq, A. H., Osborne, B. A., & Golde, T. E. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-39 · Cited by 35 · see citing works
Karlnoski, R., Rosenthal, A., Kobayashi, D. T., Pons, J., Alamed, J., Mercer, M., Li, Q., Gordon, M. N., Gottschall, P. E., & Morgan, D. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4560-08.2009 · Cited by 34 · see citing works
Early Aβ reduction prevents progression of cerebral amyloid angiopathy
Schelle, J., Wegenast‐Braun, B. M., Fritschi, S. K., Kaeser, S. A., Jährling, N., Eicke, D., Skodras, A., Beschörner, N., Obermueller, U., Häsler, L. M., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25562 · Cited by 20 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Plasma p-tau231: a new biomarker for incipient Alzheimer’s disease pathology.
Ashton, N. J., Pascoal, T. A., Karikari, T. K., Benedet, A. L., Lantero-Rodriguez, J., Brinkmalm, G., Snellman, A., Schöll, M., Troakes, C., Hye, A., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02275-6 · Cited by 719 · see citing works
Meningeal lymphatics affect microglia responses and anti-Aβ immunotherapy
Da Mesquita, S., Papadopoulos, Z., Dykstra, T., Brase, L., Farias, F. G., Wall, M., Jiang, H., Kodira, C. D., de Lima, K. A., Herz, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03489-0 · Cited by 431 · see citing works
Alzheimer's disease: From immunotherapy to immunoprevention
Jucker, M., & Walker, L. C. (2023) · Cell · doi:10.1016/j.cell.2023.08.021 · Cited by 353 · see citing works
Self-citationBorghammer, P. (2021) · Journal of Parkinson's Disease · doi:10.3233/jpd-202481 · Cited by 259 · see citing works
Tolar, M., Hey, J., Power, A., & Abushakra, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126355 · Cited by 246 · see citing works
Mouse Models of Alzheimer’s Disease
Yokoyama, M., Kobayashi, H., Tatsumi, L., & Tomita, T. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.912995 · Cited by 213 · see citing works
Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease
Ashton, N. J., Benedet, A. L., Pascoal, T. A., Karikari, T. K., Lantero-Rodriguez, J., Brum, W. S., Mathotaarachchi, S., Therriault, J., Savard, M., Chamoun, M., et al. (2022) · eBioMedicine · doi:10.1016/j.ebiom.2022.103836 · Cited by 184 · see citing works
Morenas‐Rodríguez, E., Li, Y., Nuscher, B., Franzmeier, N., Xiong, C., Suárez‐Calvet, M., Fagan, A. M., Schultz, S., Gordon, B. A., Benzinger, T. L. S., et al. (2022) · The Lancet Neurology · doi:10.1016/s1474-4422(22)00027-8 · Cited by 177 · see citing works
Self-citationZha, X., Liu, X., Wei, M., Huang, H., Cao, J., Liu, S., Bian, X., Zhang, Y., Xiao, F., Xie, Y., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.10.006 · Cited by 169 · see citing works
Haass, C., & Selkoe, D. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001694 · Cited by 145 · see citing works
The case for low-level BACE1 inhibition for the prevention of Alzheimer disease
McDade, E., Voytyuk, I., Aisen, P. S. S., Bateman, R. J., Carrillo, M. C., Strooper, B. D., Haass, C., Reiman, E. M., Sperling, R. A., Tariot, P. N., et al. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00545-1 · Cited by 143 · see citing works
Schlepckow, K., Morenas‐Rodríguez, E., Hong, S. Y., & Haass, C. (2023) · The Lancet Neurology · doi:10.1016/s1474-4422(23)00247-8 · Cited by 121 · see citing works
Staging of Alzheimer’s disease: past, present, and future perspectives
Therriault, J., Zimmer, E. R., Benedet, A. L., Pascoal, T. A., Gauthier, S. G., & Rosa‐Neto, P. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.05.008 · Cited by 114 · see citing works
Medin co-aggregates with vascular amyloid-β in Alzheimer’s disease
Wagner, J., Degenhardt, K., Veit, M., Louros, N. N., Konstantoulea, K., Skodras, A., Wild, K., Liu, P., Obermüller, U., Bansal, V., et al. (2022) · Nature · doi:10.1038/s41586-022-05440-3 · Cited by 106 · see citing works
Self-citationCombating deleterious phase transitions in neurodegenerative disease
Darling, A. L., & Shorter, J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118984 · Cited by 85 · see citing works
Walker, L. C. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-3025 · Cited by 95 · see citing works
Self-citationAlzheimer’s Disease: A Brief History of Immunotherapies Targeting Amyloid β
Vogt, A. S., Jennings, G. T., Mohsen, M. O., Vogel, M., & Bachmann, M. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043895 · Cited by 86 · see citing works
Early diagnosis and treatment of Alzheimer’s disease by targeting toxic soluble Aβ oligomers
Habashi, M., Vutla, S., Tripathi, K. K., Senapati, S., Chauhan, P. S., Haviv‐Chesner, A., Richman, M., Mohand, S.-A., Dumulon‐Perreault, V., Mulamreddy, R., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210766119 · Cited by 80 · see citing works
Zhao, Y., Zheng, Q., Hong, Y., Gao, Y., Hu, J., Lang, M., Zhang, H., Zhou, Y., Luo, H., Zhang, X., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01352-1 · Cited by 84 · see citing works
Vaccination against β-Amyloid as a Strategy for the Prevention of Alzheimer’s Disease
Mantile, F., & Prisco, A. (2020) · Biology · doi:10.3390/biology9120425 · Cited by 56 · see citing works
Targeting MicroRNA-485-3p Blocks Alzheimer’s Disease Progression
Koh, H., Lee, S., Lee, H., Min, J.-W., Iwatsubo, T., Teunissen, C. E., Cho, H., & Ryu, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313136 · Cited by 54 · see citing works
Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils
Muschol, M., & Hoyer, W. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1120416 · Cited by 55 · see citing works
Knockdown of Amyloid Precursor Protein: Biological Consequences and Clinical Opportunities
Gabriele, R. M. C., Abel, E., Fox, N. C., Wray, S., & Arber, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.835645 · Cited by 44 · see citing works
Cankar, N., Beschörner, N., Tsopanidou, A., Qvist, F. L., Colaço, A. R., Andersen, M., Kjærby, C., Delle, C., Lambert, M., Mundt, F., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114977 · Cited by 42 · see citing works
Self-citationProtein nanoparticles as drug delivery systems for cancer theranostics
Hua, Y., Qin, Z., Gao, L., Zhou, M., Xue, Y., Li, Y., & Xie, J. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.06.004 · Cited by 42 · see citing works
MicroRNA-195 liposomes for therapy of Alzheimer's disease
Su, D., Chen, Z., An, X., Yang, J., Yang, J., Wang, X., Qu, Y., Chen, G., Chai, Y.-N., Liu, X., et al. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.12.003 · Cited by 38 · see citing works
Aducanumab and Its Effects on Tau Pathology: Is This the Turning Point of Amyloid Hypothesis?
Silvestro, S., Valeri, A., & Mazzon, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042011 · Cited by 35 · see citing works
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) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01236-3 · Cited by 35 · see citing works
Senapati, S., Tripathi, K. K., Awad, K., & Rahimipour, S. (2024) · Small · doi:10.1002/smll.202311670 · Cited by 38 · see citing works
Aβ and tau prions feature in the neuropathogenesis of Down syndrome
Condello, C., Maxwell, A. M., Castillo, E., Aoyagi, A., Graff, C., Ingelsson, M., Lannfelt, L., Bird, T. D., Keene, C. D., Seeley, W. W., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2212954119 · Cited by 27 · see citing works
Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae
Rother, C., Uhlmann, R. E., Müller, S. A., Schelle, J., Skodras, A., Obermüller, U., Häsler, L. M., Lambert, M., Baumann, F., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34538-5 · Cited by 28 · see citing works
Self-citationMitochondrial Deficits With Neural and Social Damage in Early-Stage Alzheimer’s Disease Model Mice
Misrani, A. A., Tabassum, S., Huo, Q., Tabassum, S., Jiang, J., Ahmed, A., Chen, X., Zhou, J., Zhang, J., Liu, S., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.748388 · Cited by 29 · see citing works
Experimental modeling of Alzheimer's disease: Translational lessons from cross‐taxon analyses
Yenkoyan, K. B., Kotova, M. M., Apukhtin, K. V., Galstyan, D. S., Amstislavskaya, T. G., Strekalova, T. V., de Abreu, M. S., Chavushyan, V. A., Lim, L. W., Yang, L., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70273 · Cited by 29 · see citing works
Could drugs prevent Alzheimer’s? These trials aim to find out
Abbott, A. (2022) · Nature · doi:10.1038/d41586-022-00651-0 · Cited by 27 · see citing works
Efficient amyloid-β degradation in Alzheimer’s disease using SPYTACs
Teng, F., Liu, J., Cui, T., Tan, X., Liu, K., Hou, Z., (54356), L. Z., Xie, Y., Li, R., Li, D., et al. (2026) · Cell · doi:10.1016/j.cell.2026.01.034 · Cited by 24 · see citing works
Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice
Ruiz‐Riquelme, A., Mao, A., Barghash, M. M., Lau, H. H. C., Stuart, E., Kovács, G. G., Nilsson, K. P. R., Fraser, P. E., Schmitt‐Ulms, G., & Watts, J. C. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01187-6 · Cited by 23 · see citing works
The prion principle and Alzheimer’s disease
Walker, L. C., & Jucker, M. (2024) · Science · doi:10.1126/science.adq5252 · Cited by 27 · see citing works
Self-citationBarendrecht, S., Schreurs, A., Geißler, S., Sabanov, V., Ilse, V., Rieckmann, V., Eichentopf, R., Künemund, A., Hietel, B., Wussow, S., et al. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01144-y · Cited by 22 · see citing works
Self-citationTolar, M., Hey, J. A., Power, A., & Abushakra, S. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052727 · Cited by 22 · see citing works
Frustrated peptide chains at the fibril tip control the kinetics of growth of amyloid-β fibrils
Xu, Y., Knapp, K., Le, K. N., Schafer, N. P., Safari, M. S., Davtyan, A., Wolynes, P. G., & Vekilov, P. G. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110995118 · Cited by 19 · see citing works
Transmission of Cerebral β-Amyloidosis Among Individuals
Hamaguchi, T., Ono, K., & Yamada, M. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03566-4 · Cited by 17 · see citing works
A glance through the effects of CD4 + T cells, CD8 + T cells, and cytokines on Alzheimer's disease
Afsar, A., Chen, M., Xuan, Z., & Li, Z. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.10.058 · Cited by 19 · see citing works
Amyloid‐β in Alzheimer's disease: Structure, toxicity, distribution, treatment, and prospects
Yu, Y., Yu, S., Battaglia, G., & Tian, X. (2024) · Ibrain · doi:10.1002/ibra.12155 · Cited by 19 · see citing works
Bao, J., Liang, Z., Gong, X., Yu, J. H., Xiao, Y., Liu, W. D., Wang, X., Wang, J., & Shu, X. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215299 · Cited by 16 · see citing works
Cope, Z. A., Murai, T., & Rizzo, S. J. S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.805063 · Cited by 15 · see citing works
N‑terminal Domain of Amyloid‑β Impacts Fibrillation and Neurotoxicity
Shi, J., Li, H., Liu, H., Zhu, L., Guo, Y.-B., Pei, J., An, H., Li, Y., Li, S.-D., Zhang, Z., et al. (2022) · ACS Omega · doi:10.1021/acsomega.2c04583 · Cited by 14 · see citing works
Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer’s Disease
Rosenberry, T. L., Zhou, H., Stagg, S. M., & Paravastu, A. K. (2022) · Molecules · doi:10.3390/molecules27248804 · Cited by 13 · see citing works
Porphyromonas gingivalis Impairs Microglial Aβ Clearance in a Mouse Model
Xie, M., Huang, X., Tang, Q., Yu, S., Zhang, K., Lu, X., Zhang, Y., Wang, J., Zhang, L., & Chen, L. (2025) · Journal of Dental Research · doi:10.1177/00220345241294009 · Cited by 12 · see citing works
Njavro, J. R., Vukicevic, M., Fiorini, E., Dinkel, L., Müller, S. A., Berghofer, A., Bordier, C., Kozlov, S. O., Halle, A., Buschmann, K., et al. (2022) · Cells · doi:10.3390/cells12010079 · Cited by 13 · see citing works
Kiselica, A. M., & Initiative, A. D. N. (2021) · Psychogeriatrics · doi:10.1111/psyg.12697 · Cited by 12 · see citing works
Shifting the balance: soluble ADAM10 as a potential treatment for Alzheimer's disease
Hershkovits, A. S., Gelley, S., Hanna, R., Kleifeld, O., Shulman, A., & Fishman, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1171123 · Cited by 12 · see citing works
Zhao, P., Cheng, P., Wang, J., Zhu, G., & Wang, X. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155639 · Cited by 12 · see citing works
Lu, M., Hao, C., Xu, L., Feng, Y., Jiang, J., Wang, Y., Xu, J., Kuang, H., Xu, C., & Sun, M. (2024) · Science China Chemistry · doi:10.1007/s11426-023-1859-4 · Cited by 9 · see citing works
Damuka, N., Irmen, R. E., Krizan, I. M., Miller, M. D., Gollapelli, K., Bhoopal, B., Deep, O., Bansode, A. H., Lockhart, S. N., Orr, M. E., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.14083 · Cited by 9 · see citing works
Shobo, A., James, N. G., Dai, D., Röntgen, A., Black, C. S., Kwizera, J.-R., Hancock, M. A., Bui, K. H., & Multhaup, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101483 · Cited by 7 · see citing works
Chen, S., Yin, H., Zhang, L., Liu, R., Qi, W. D., He, Z., & Su, R. (2021) · RSC Advances · doi:10.1039/d1ra05397c · Cited by 6 · see citing works
Thal, D. R., & Gawor, K. (2023) · Clinical Neuropathology · doi:10.5414/np301564 · Cited by 5 · see citing works
Song, S., Liu, Q., Chen, R., Chen, P., Tao, M., Li, S., Guo, L., Zhu, X., Liu, Y., Liu, L., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02032-w · Cited by 5 · see citing works
Suppression of amyloid-β fibril growth by drug-engineered polymorph transformation
Mafimoghaddam, S., Xu, Y., Sherman, M. B., Orlova, E. V., Karki, P., Orman, M. A., & Vekilov, P. G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102662 · Cited by 4 · see citing works
Exploring exosomes to provide evidence for the treatment and prediction of Alzheimer’s disease
QUAN, X., MA, X., LI, G., FU, X., LI, J., & ZENG, L. (2023) · Biocell · doi:10.32604/biocell.2023.031226 · Cited by 4 · see citing works
Yang, Z., Wu, Y., Liu, H., Li, H., & Deng, X. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c02035 · Cited by 4 · see citing works
Latina, V., Introna, M. D., Malerba, F., Florio, R., Balzamino, B. O., Natale, G. D., Sciacca, M. F. M., Pappalardo, G., Micera, A., Pignataro, A., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02022-y · Cited by 3 · see citing works
Li, Q., Luo, X., Wei, M., Cui, S., Yang, S., Li, Y., He, S., & Dong, G. (2025) · BMC Psychiatry · doi:10.1186/s12888-025-07419-6 · Cited by 3 · see citing works
Morales, R., Kelley, S., & Perez-Urrutia, N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.340403 · Cited by 3 · see citing works
Zhu, J., Xiao, X., Chen, X., Xiao, H., Tao, Z., Zhang, H., Park, K., Lam, L. Q., Thai, C., Trouson, B., et al. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251352213 · Cited by 3 · see citing works
Ramos, J. M. P., Kviatcovsky, D., & Schwartz, M. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15609 · Cited by 3 · see citing works
Gil, B., Rose, J. L., Demurtas, D., Mancini, G., Sordet‐Dessimoz, J., Sorrentino, V., Rudinskiy, N., Frosch, M. P., Hyman, B. T., Moniatte, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.04.519021 · Cited by 3 · see citing works
Gao, F., Xu, W., Xiao, Y., Jiang, W., Chen, M., Liu, Z., Zhang, P., Yang, T., Qian, Z., & Gao, K. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.157496 · Cited by 2 · see citing works
Amyloid‐β Seeds in Alzheimer's Disease: Research Challenges and Implications
Beschörner, N., Xu, Y., Jucker, M., & Ruiz‐Riquelme, A. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70267 · Cited by 2 · see citing works
Self-citationCreutzfeldt–Jakob disease is an Alzheimer’s disease-related dementia
Watts, J. C., Sigurdson, C. J., Yobs, D., & Soto, C. A. (2026) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2026.03.009 · Cited by 2 · see citing works
Cerebrospinal Fluid Biomarkers of Alzheimer Disease
Васильевна, Н. К., Shpilyukova, Y. A., Шабалина, А. А., Fedotova, E. Y., & Illarioshkin, S. N. (2025) · Annals of Clinical and Experimental Neurology · doi:10.17816/acen.1185 · Cited by 1 · see citing works
Early-Onset Alzheimer’s disease and amyloid precursor protein gene mutations
Varte, V., Ralte, L., & Kumar, N. S. (2025) · Discover Neuroscience · doi:10.1186/s13064-025-00203-y · Cited by 2 · see citing works
Chaulagain, B., Gothwal, A., Mahanta, A. K., Jarajapu, Y. P. R., & Singh, J. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c01009 · Cited by 1 · see citing works
Lyu, H., Ye, Y., Lui, V. C. H., & Wang, B. (2022) · Medical Hypotheses · doi:10.1016/j.mehy.2022.110901 · Cited by 1 · see citing works
O’Brien, K., & Blair, P. (2021) · Springer eBooks · doi:10.1007/978-3-030-78559-8_9 · Cited by 1 · see citing works
Marchi, P. M., Marrone, L., Brasseur, L., Bousset, L., Webster, C. P., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., Marroccella, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.463891
Makovitzky, J. (2025) · Springer eBooks · doi:10.1007/978-3-031-70714-8_8
Adachi, Y., Katori, K., Ishiyama, S., Morikawa, S., Saito, T., Saido, T. C., Ikegaya, Y., & Takeuchi, H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.02.651821
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
Additional file 1 of Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice
Ruiz‐Riquelme, A., Mao, A., Barghash, M. M., Lau, H. H. C., Stuart, E., Kovacs, G. G., Nilsson, K. P. R., Fraser, P. E., Schmitt‐Ulms, G., & Watts, J. C. (2021) · Figshare · doi:10.6084/m9.figshare.14570473
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
DONANEMAB AND THE FUTURE OF ALZHEIMER’S TREATMENT: BETWEEN INNOVATION AND CAUTION
Tomasiczek, W., Tomasiczek, S., Kondyjowska, D., Komuńska, D. M., Bukała, N., Sawiec, Z., Antonowicz, E., & Rogozińska, M. (2025) · International Journal of Innovative Technologies in Social Science · doi:10.31435/ijitss.4(48).2025.4214
Castelot, R. (2024) · theses.fr (ABES) · doi:10.70675/c2a7ce1ez8caaz4593zbb3azae8add8055b5
Kashiwagi‐Hakozaki, M., Uchigami, H., 名嘉, 泰., Kokawa, A., Mano, T., Cho, J., Yamada, K., Miyashita, A., Hara, N., Ikeuchi, T., et al. (2026) · Brain Communications · doi:10.1093/braincomms/fcag188
Mao, A., Ruiz‐Riquelme, A., Barghash, M. M., Silver, N. R. G., Lau, H. H. C., Stuart, E., Zampar, S., Sehlin, D., Syvänen, S., Pollanen, M. S., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02390-z
O’Brien, K., & Blair, P. (2026) · Springer eBooks · doi:10.1007/978-3-032-14521-5_9
Porphyromonas gingivalis Promotes Lipid Droplet–Mediated Microglial Dysfunction
Rajoka, M. S. R., Valladares, K. N., Prairie, C. L., Li, W., King, P. H., Katz, J., Michalek, S. M., & Zhang, P. (2026) · Journal of Dental Research · doi:10.1177/00220345261478558
- Authors
- Uhlmann, R. E., Rother, C., Rasmussen, J., Schelle, J., Bergmann, C., Ullrich Gavilanes, E. M., Fritschi, S. K., Buehler, A., Baumann, F., Skodras, A., Al-Shaana, R., Beschorner, N., Ye, L., Kaeser, S. A., Obermüller, U., Christensen, S., Kartberg, F., Stavenhagen, J. B., Rahfeld, J.-U., Cynis, H., Qian, F., Weinreb, P. H., Bussiere, T., Walker, L. C., Staufenbiel, M., & Jucker, M.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Hertie Institute for Clinical Brain Research (DE)
- Lundbeck (Denmark) (DK)
- Fraunhofer Institute for Cell Therapy and Immunology (DE)
- Biogen (United States) (US)
- Emory University (US)
- Corresponding author
- Jucker, Mathias
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2020-11-16
- Volume
- 23
- Issue
- 12
- Pages
- 1580-1588
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC7783656
- OpenAlex
- W3101507523
- Cited by
- 87
- References
- 60
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 13 · 2023: 14 · 2022: 22 · 2021: 17 · 2020: 2
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Publikationsdatenbank der Fraunhofer-Gesellschaft (Fraunhofer-Gesellschaft) (submittedVersion)
- DZNE Pub (submittedVersion)
- Fraunhofer-Publica (Fraunhofer-Gesellschaft) (submittedVersion)
- Funders
- National Institutes of Health (P51OD011132)
- National Institute on Aging (P50AG025688, P30AG066511)
- 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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta aggregation, aducanumab, antibody therapy, preclinical Alzheimer's disease, transgenic mice, amyloid precursor protein, protein aggregation, amyloid-beta deposition
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Brain Chemistry, Humans, Male, Mice, Inbred C57BL, Mice, Transgenic, Middle Aged, Tissue Extracts, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Neurofilament Proteins, Antibodies, Blocking, Mice, Plaque, Amyloid, Antibodies, Monoclonal, Humanized
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
