Cited by 971Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

Open access

Meyer-Luehmann, Melanie, Coomaraswamy, Janaky, Bolmont, Tristan, Kaeser, Stephan, Schaefer, Claudia, Kilger, Ellen, Neuenschwander, Anton, Abramowski, Dorothee, Frey, Peter, Jaton, Anneliese L., Vigouret, Jean-Marie, Paganetti, Paolo, Walsh, Dominic M., Mathews, Paul M., Ghiso, Jorge, Staufenbiel, Matthias, Walker, Lary C., Jucker, Mathias·2006·Science

DOI 10.1126/science.1131864

Open this paper in CoChat — free account

Abstract

Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-β (Aβ)–containing brain extracts from humans with Alzheimer's disease or β-amyloid precursor protein (APP) transgenic mice induced cerebral β-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by Aβ immunodepletion, protein denaturation, or by Aβ immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Aβ strains with varying biological activities reminiscent of prion strains.

Integrity signals

Registry

Crossref · 10.1126/science.1131864

Cites

31 of 31 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?

1 retracted

RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
Retracted
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Self-citation
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
Self-citation
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Two 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
Self-citation

Flagged first, then by citations

Show all 31 references

Research works printed but not linked: 1

C. G. Glabe, R. Kayed, Neurology66, S74 (2006).

Sorted by citations

Items 901–970 of 970

A Neuroinflammatory View of Alzheimer’s Disease
Anisman, H., Hayley, S. P., & Kusnecov, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23565-8.00005-3
References
(2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23565-8.09996-8
Could Blood Transfusion Increase the Risk of Alzheimer’s Disease? A Narrative Review
Li, X., Pei, R., Fei, Z., Chen, Z., Lin, F., Sun, P., & Cao, H. (2025) · Healthcare · doi:10.3390/healthcare13050452
Transmissible Spongiform Encephalopathies (Creutzfeldt-Jakob Disease, Gerstmann-Sträussler-Scheinker Disease, Kuru, Fatal Familial Insomnia, New Variant Creutzfeldt-Jakob Disease, Sporadic Fatal Insomnia, Variably Protease Sensitive Prionopathy)
Britt, W. J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-82763-8.00211-9
In vivo and in silico alpha-synuclein propagation dynamics: The role of genotype, epicentre, and connectivityPreprint
Tullo, S., Park, J., Rahayel, S., Gallino, D., Park, M., Mar, K., Zheng, Y., del Cid‐Pellitero, E., Fon, E. A., Luo, W., et al. (2025) · eLife · doi:10.1101/2025.07.18.665565 · Cited by 1
Prions and the Transmissible Spongiform Encephalopathies
Wiggins, R. C. (2008) · Springer eBooks · doi:10.1007/978-0-387-79112-8_23
Physiological function of FUS: An RNA binding protein in motor neuron disease
Yang, L. (2015) · UKnowledge (University of Kentucky)
Additional file 1 of Peripheral administration of SOD1 aggregates does not transmit pathogenic aggregation to the CNS of SOD1 transgenic mice
Keskin, I., Ekhtiari Bidhendi, E., Marklund, M., Andersen, P. M., Brännström, T., Marklund, S. L., & Nordström, U. (2021) · Figshare · doi:10.6084/m9.figshare.14826085
Additional file 1 of Evaluating the inter-species transmission risk of amyloid beta peptide aggregates via ingestion
Raine, J., Tolwinski, N. S., Gruber, J., & Mathuru, A. S. (2024) · Figshare · doi:10.6084/m9.figshare.25996956
Additional file 1 of Transformation of non-neuritic into neuritic plaques during AD progression drives cortical spread of tau pathology via regenerative failure
Tsering, W., Hery, G. P., Phillips, J. L., Lolo, K., Bathe, T., Villareal, J. A. B., Ruan, I. Y., & Prokop, S. (2024) · Figshare · doi:10.6084/m9.figshare.26648013
Additional file 1 of Infusion of blood from mice displaying cerebral amyloidosis accelerates amyloid pathology in animal models of Alzheimer’s disease
Morales, R., Duran-Aniotz, C. A., Bravo-Alegria, J. B., Estrada, L. D., Shahnawaz, M., Hu, P.-P., Kramm, C., Morales‐Scheihing, D., Urayama, A., & Soto, C. (2020) · Figshare · doi:10.6084/m9.figshare.13346964
Additional file 5 of Modeling the early stages of Alzheimer’s disease by administering intracerebroventricular injections of human native Aβ oligomers to rats
Baerends, E., Soud, K., Folke, J., Pedersen, A.-K., Henmar, S., Konrad, L., Lycas, M. D., Mori, Y., Pakkenberg, B., Woldbye, D. P. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20501867
Additional file 1 of Pathological changes induced by Alzheimer’s brain inoculation in amyloid-beta plaque-bearing mice
Lam, S., Hérard, A., Boluda, S., Petit, F., Eddarkaoui, S., Cambon, K., Picq, J., Buée, L., Duyckaerts, C. J., Haı̈k, S., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20502025
Additional file 1 of The 3-O sulfation of heparan sulfate proteoglycans contributes to the cellular internalization of tau aggregates
Ferreira, A., Royaux, I. E., Liu, J., Wang, Z., Su, G., Moechars, D., Callewaert, N., & Muynck, L. D. (2024) · Figshare · doi:10.6084/m9.figshare.26557271
Additional file 1 of Transmission of amyloid-beta and tau pathologies is associated with cognitive impairments in a primate
Lam, S., Petit, F., Hérard, A., Boluda, S., Eddarkaoui, S., Guillermier, M., Buée, L., Duyckaerts, C. J., Haı̈k, S., Picq, J., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16800253
Additional file 6 of Modeling the early stages of Alzheimer’s disease by administering intracerebroventricular injections of human native Aβ oligomers to rats
Baerends, E., Soud, K., Folke, J., Pedersen, A.-K., Henmar, S., Konrad, L., Lycas, M. D., Mori, Y., Pakkenberg, B., Woldbye, D. P. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20501870
Additional file 2 of Evaluating the inter-species transmission risk of amyloid beta peptide aggregates via ingestion
Raine, J., Tolwinski, N. S., Gruber, J., & Mathuru, A. S. (2024) · Figshare · doi:10.6084/m9.figshare.25997052
Additional file 1 of Remodeling Alzheimer-amyloidosis models by seeding
Ulm, B. S., Borchelt, D. R., & Moore, B. D. (2021) · Figshare · doi:10.6084/m9.figshare.14037362
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
Additional file 1 of Frontotemporal dementia-like disease progression elicited by seeded aggregation and spread of FUS
Vazquez‐Sanchez, S., Tilkin, B., Gasset-Rosa, F., Zhang, S., Piol, D., McAlonis‐Downes, M., Artates, J. W., Govea-Perez, N., Verresen, Y., Guo, L. E., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26019613
Additional file 3 of Evaluating the inter-species transmission risk of amyloid beta peptide aggregates via ingestion
Raine, J., Tolwinski, N. S., Gruber, J., & Mathuru, A. S. (2024) · Figshare · doi:10.6084/m9.figshare.26730982
The origin of Alzheimer’s disease: Prions?
Yang, D., & Wang, M. (2025) · Neurology Letters · doi:10.61882/nl.4.1.76
The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism
Cali, M. P., Monistrol, J., Strati, F., Schiller, J., Indig, R. Y., Markworth, R., & Landau, M. (2026) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-05273-5_16 · Cited by 4
Amyloid fibrils in Alzheimer's disease differently modulate sleep and cortical oscillations in mice depending on the type of amyloid
Sanagi, T., Okumura, M., Lin, Y., Kanemura, S., Moon, E., Heo, Y., Takahara, K., Lee, Y.-H., & Tsunematsu, T. (2026) · Biophysical Chemistry · doi:10.1016/j.bpc.2026.107599
3D atomic structure reveals evolution of prions in templated amplification in vitroPreprint
Bieschke, J., Wenborn, A., Chatzitheodosiou, I., Jack, K., Batchelor, M., Chen, L., Ahmed, P., Thirlway, G., Manka, S. W., Jackson, G. S., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9083455/v1
Studies on the Role of Cellular Heparan Sulfate on Tau Pathology in Alzheimer's Disease and Related Tauopathies
Sepulveda-Diaz, J. E. (2013) · theses.fr (ABES) · doi:10.70675/56c42bcbz41dfz432bzbb78z77110b373285
Binding and internalization of exogenous protein assemblies by mammalian cells
Ruiz-Arlandis, G. (2015) · theses.fr (ABES) · doi:10.70675/437e0532ze4e1z4966z80e5z340b6fd3c49d
Etude préclinique et clinique de la phase précoce de la maladie d'Alzheimer
Epelbaum, S. (2015) · theses.fr (ABES) · doi:10.70675/ea81e5c2z5032z4474z9f96z59f62125a629
Evaluation expérimentale du risque prion lié aux porteurs asymptomatiques chez l'Homme et le macaque
Rontard, J. (2018) · theses.fr (ABES) · doi:10.70675/ee7dac13zd082z49c7za670z3e9b627c4ab7
Les nanotubes comme nouvelle voie de transfert et de propagation de la protéine Tau pathologique
Tardivel, M. (2017) · theses.fr (ABES) · doi:10.70675/0cfcd049z970ez4f2dz8417z195cfabdc00d
Study of the mechanism of Tunneling nanotubes formation and their role in aggregate proteins transfer between cells
Zhu, S. (2017) · theses.fr (ABES) · doi:10.70675/e0cb0a13z36b9z4af5z8fa3zb783ac21e9a9
La protéine prion cellulaire : un relai de neurotoxicité commun aux protéines amyloïdes et aux nanoparticules
Boudet-Devaud, F. (2018) · theses.fr (ABES) · doi:10.70675/111341b9z5eeez4531z8f07zcb44d6f469a0
Etude de mécanismes de type prion impliqués dans la maladie d’Alzheimer sur un modèle de mini-cerveaux humains avec exploration par microscopie 3D
Nassor, F. (2019) · theses.fr (ABES) · doi:10.70675/12cc8581z360ez4d83z8e37z1bf0e6781c4c
Étude de la propagation prion-like de l'alpha-synucléine dans des réseaux de neurones reconstruits
Courte, J. (2019) · theses.fr (ABES) · doi:10.70675/95ccfbd6zedb2z4a1bz8024zb46a3ec60ebf
Déterminants structuraux d’agrégats de Tau distincts : vers de nouveaux outils moléculaires pour discriminer les tauopathies
Caroux, E. (2019) · theses.fr (ABES) · doi:10.70675/35d706bfz0d1bz440ezac4bz7fd4138464f8
Du rôle physiologique de la protéine prion cellulaire à l'infection par les prions : régulation/dérégulation du module de signalisation PDK1/TACE α-secrétase
Ezpeleta, J. (2019) · theses.fr (ABES) · doi:10.70675/4e7ccce5z4f1ez4a57zac28z5380a39dd820
La protéine prion cellulaire : rôles physiologiques et implications croisées dans les maladies neurodégénératives amyloïdes
Baudouin, V. (2020) · theses.fr (ABES) · doi:10.70675/a212ad92z3b22z4eeczb177z417025bff4ef
Structural characterization of amyloid fibrils by solid-state NMR
Shenoy, J. (2020) · doi:10.70675/75b3a59ez2c1ez4544z86e3z8840a9bdd7b2
Physiological and pathological roles of the amyloid precursor protein at the presynapse
Jordá-Siquier, T. (2021) · theses.fr (ABES) · doi:10.70675/3bff9a77z3935z4d28zb02bz5b454bcbc77e
Influences biochimiques, anatomiques et cognitives de la troncation exopeptidasique N-terminale du peptide Aβ
Valverde, A. (2020) · theses.fr (ABES) · doi:10.70675/f1b70734zf4e3z4870z8fbdz950d831642a7
Auto-assemblage du Lanréotide - rôle des sels et des contre-ions
Petcut, C. (2020) · doi:10.70675/c17f8855z9dbbz4580z883cz5a3e5fcbabee
Implication de nouvelles cibles microgliales, Cst7 et Clec7a/Dectin-1, dans le développement et la progression de la maladie d'Alzheimer
Hemonnot-Girard, A.-L. (2021) · theses.fr (ABES) · doi:10.70675/9c8a4775zd774z494ez9bbazf7566faefa8f
Propagation axonale des pathologies Tau et Aβ dans la maladie d'Alzheimer : à la recherche de propagons dans le circuit subiculo-fornico-mamillaire
Thierry, M. (2020) · theses.fr (ABES) · doi:10.70675/d2f36d94zaa16z4617z94c6zabb1ad26f3fb
Early memory deficits and extensive brain network disorganization in the AppNL-F/MAPT double knock-in mouse model of familial Alzheimer's disease
Borcuk, C. (2021) · theses.fr (ABES) · doi:10.70675/c316f2dcz54d3z41cfzb3f5z99c7b2d3cd95 · Cited by 1
Impact of α-synuclein fibrillar strains and ß-amyloid assemblies on cultured mouse cortical neurons endo-lysosomal logistics
Chou, Q.-L. (2021) · theses.fr (ABES) · doi:10.70675/d60d2c8cze696z4500za571zfe56e6cc9082
Modulation des peptides amyloïde-β par des chélates azotés pour la thérapie de la maladie d’Alzheimer
Lelong, E. (2021) · theses.fr (ABES) · doi:10.70675/7cda5a3ez022cz475az9b2bz977814a60663
Transmission of Alzheimer pathology in murine and primate models : from proteinopathies to neuronal and cognitive impairments
Lam, S. (2021) · theses.fr (ABES) · doi:10.70675/60b353ffz56fcz41a2z9e53zf0d9ac078167 · Cited by 1
Rôle de la morphologie neuronale dans la régulation des flux moléculaires de l’ECS du cortex cérébral : un mécanisme potentiel de la neuroprotection dépendante d’IGF
Camus, C. (2023) · theses.fr (ABES) · doi:10.70675/30c3ec29z9149z47f1zb7c1z83c3a6b9a334
The Use of Localized Proteomics to Understand the Pathogenesis of Alzheimer's Disease
Pires, G. (2021) · theses.fr (ABES) · doi:10.70675/45826fd6zd2c8z4b3dz91e0za5080544cb17
Regulation of Alzheimer pathology by amyloid seeds : from toxic effects to therapeutic opportunities, in mouse model of amyloidosis
Célestine, M. (2023) · theses.fr (ABES) · doi:10.70675/873ca377z9a97z43f6z8051zdab4082686ba
Synthesis and conformational analysis of peptidomimetic foldamers containing diaza-peptide units : application in protein-protein interactions
Shi, C. (2022) · theses.fr (ABES) · doi:10.70675/1f5ac7fdz098fz4bf5z9333z19213aedfbe2
Etude des mécanismes physiοpathοlοgiques de la maladie d'Alzheimer : appοrt de l'étude des variants du gène SΟRL1
Castelot, R. (2024) · theses.fr (ABES) · doi:10.70675/c2a7ce1ez8caaz4593zbb3azae8add8055b5
Preclinical Models of Neurodegenerative Diseases
Cendelín, J., & Tuma, J. (2026) · Contemporary clinical neuroscience · doi:10.1007/978-3-032-18296-8_3
Iatrogenic Cerebral Amyloid Angiopathy
Zedde, M., Kaushik, K., Wermer, M. J. H., Piazza, F., & Pascarella, R. (2026) · Springer eBooks · doi:10.1007/978-3-032-23618-0_13
Catch, dock, unravel, and lock
Bieschke, J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2611975123
Cellular prion protein and its derived peptides: multifaceted roles in neurodegenerative diseases and potential as biomarkers
Mari, E., Aventaggiato, M., Paldino, E., Ceccarelli, S., Mucci, N., Bellomo, G., Mantuano, E., Dugheri, S., Martellucci, S., & Mattei, V. (2026) · Cell & Bioscience · doi:10.1186/s13578-026-01609-9
Prion-like transmission and propagation of human β-amyloid to the bank vole rodent model
Bari, M. A. D., Bruno, R., Riccardi, G., Vanni, I., D’Agostino, C., Nonno, R., Cecco, E. D., Burato, A., Legname, G., Cardone, F., et al. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03041-2
Soluble high-molecular-weight amyloid-β species derived from amyloid-β-laden brains induce cerebral β-amyloidosis
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
De novo formation of familial Alzheimer’s disease-relevant Aβ strains occurs exclusively in the human brain
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
Proteomic comparison of hippocampal neurofibrillary tangles in PART, intermediate Alzheimer’s disease and advanced Alzheimer’s disease
Thierry, M., Leitner, D., Balcomb, K., Kavanagh, T., Tang, L., Kanshin, E., William, C. M., Oakley, D., Hyman, B. T., Ueberheide, B. M., et al. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03064-9
Iatrogenic cerebral amyloid angiopathy: a scoping review
Ikeda, S., Hamaguchi, T., Hirano, T., Yagita, Y., Koga, M., Ihara, M., Nakajima, M., Itabashi, R., Shindo, A., Kudo, K., et al. (2026) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2026-339381
From pathology to network failure: a Question–Model–Outcome framework for interpreting animal models of AD-related and dementia-relevant mechanisms
Şimşekçi, U., & Cesaretli, Y. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1882211
The neuroscience of Alzheimer’s disease
Spires‐Jones, T. L. (2026) · Oxford University Press eBooks · doi:10.1093/9780198995296.003.0003
Perinatal lead (Pb) exposure and alterations to amyloid beta and metabolic profiles in the brain
Morgan, R. K., Matei, E. K., Pan, J., Ishikawa, T., Polemi, K. M., Bergin, I., Ferris, S. P., Wang, H., Dolinoy, D. C., Bakulski, K. M., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71791
Amyloid-β plaque diversity across brain regions in Alzheimer’s disease and its relation to major clinicopathological traits
Neubauer, A., Feyen, P., Pekrun, S., Roeber, S., Ruf, V., Strübing, F., & Herms, J. W. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03096-1
Nanomaterial modulation of lysosomal homeostasis in neurodegenerative proteinopathies: from pathological-protein degradation to re-release and seeding
Song, M.-R., Bu, N., Wei, L., & Chen, J. (2026) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2026.1997252
When brain networks crash: connectivity, slow-wave activity and neural replay in Alzheimer's disease
Pini, L., Campuzano, C., Zhang, L., Imbimbo, B. P., & Allegra, M. (2026) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2026.107053
Probing Isoforms of the Prion Protein through Tyrosine Nitration
Lennon, C. W. (2007) · The Mathematics Enthusiast
Amyloid-β Transmissibility
Duran-Aniotz, C. A., Morales, R., Moreno‐González, I., & Soto, C. A. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_6
Probing Structural Differences of Recombinant Prion Isoforms Using Fluorescence Spectroscopy
Gilbert, J. L. (2008) · The Mathematics Enthusiast

Authors: Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., Vigouret, J.-M., Paganetti, P., Walsh, D. M., Mathews, P. M., Ghiso, J., Staufenbiel, M., Walker, L. C., & Jucker, M.
Affiliations: Department of Cellular Neurology, Hertie-Institute for Clinical Brain Research, University of Tübingen, D-72076 Tübingen, Germany.
University College Dublin (IE)
Corresponding author: Coomaraswamy, Janaky
Bolmont, Tristan
Walker, Lary C.
Jucker, Mathias
ORCID: Bolmont, Tristan
Kaeser, Stephan
Kilger, Ellen
Paganetti, Paolo
Walsh, Dominic M.
Mathews, Paul M.
Ghiso, Jorge
Walker, Lary C.
Jucker, Mathias
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2006-09-22
Volume: 313
Issue: 5794
Pages: 1781-1784
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1131864
OpenAlex: W2098022922
Cited by: 971
References: 31
Citations by year: 2026: 22 · 2025: 18 · 2024: 34 · 2023: 31 · 2022: 52 · 2021: 50 · 2020: 47 · 2019: 59 · 2018: 67 · 2017: 57 · 2016: 63 · 2015: 64 · 2014: 73 · 2013: 71 · 2012: 65
FWCI: 21.65
Type: journal article
Language: en
Open access: green
infoscience.epfl.ch
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
Funders: Wellcome Trust
National Institute of Neurological Disorders and Stroke (R21NS045357, NS45357)
National Center for Research Resources (RR-00 165, P51RR000165)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid-beta, Alzheimer's disease, brain extracts, protein aggregation, immunodepletion, immunization, host-pathogen interaction
MeSH terms: Aged, Aged, 80 and over, Aging, Alzheimer Disease, Amyloidosis, Animals, Brain, Brain Chemistry, Brain Diseases, Female, Hippocampus, Humans, Male, Mice, Transgenic, Protein Denaturation, Time Factors, Tissue Extracts, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Mice

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

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks