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

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Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

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Pathways towards and Away from Alzheimer’s Disease

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Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

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MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins

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Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology

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Oligomeric amyloid-β induces early and widespread changes to the proteome in human iPSC-derived neurons

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Propagation of the Prion Phenomenon: Beyond the Seeding Principle

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Amyloid by default

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Seeding, maturation and propagation of amyloid β-peptide aggregates in Alzheimer’s disease

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The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models

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HSA targets multiple Aβ42 species and inhibits the seeding-mediated aggregation and cytotoxicity of Aβ42 aggregates

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Synaptic Protein Alterations in Parkinson’s Disease

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PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions

Barron, R. M., King, D., Jeffrey, M., McGovern, G., Agarwal, S., Gill, A. C., & Piccardo, P. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1594-5 · Cited by 30

Protein Misfolding in Prion and Prion-Like Diseases: Reconsidering a Required Role for Protein Loss-of-Function

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Infusion of blood from mice displaying cerebral amyloidosis accelerates amyloid pathology in animal models of Alzheimer’s disease

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The amyloid state of proteins: A boon or bane?

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Aβ and tau prions feature in the neuropathogenesis of Down syndrome

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Biochemical and strain properties of CJD prions: complexity versus simplicity

Haı̈k, S., & Brandel, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07399.x · Cited by 29

Alzheimer's Disease and Prion Protein

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In vitro screen of prion disease susceptibility genes using the scrapie cell assay

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Thy1-ApoE4/C/EBPβ double transgenic mice act as a sporadic model with Alzheimer’s disease

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Zinc-induced heterodimer formation between metal-binding domains of intact and naturally modified amyloid-beta species: implication to amyloid seeding in Alzheimer’s disease?

Mezentsev, Y. V., Medvedev, A. E., Kechko, O. I., Makarov, A. А., Ivanov, A. S., Mantsyzov, A. B., & Kozin, S. A. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1113890 · Cited by 29

Protein aggregation and prionopathies

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Role of cellular prion protein in interneuronal amyloid transmission

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Clearance of amyloid β-protein and its role in the spreading of Alzheimer's disease pathology

Thal, D. R. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00025 · Cited by 28

Convergent molecular defects underpin diverse neurodegenerative diseases

Tofaris, G. K., & Buckley, N. J. (2018) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-316988 · Cited by 30

Outcome of cell suspension allografts in a patient with Huntington's disease

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Prion-Like Behavior of Amyloid-β

Kim, J., & Holtzman, D. M. (2010) · Science · doi:10.1126/science.1198314 · Cited by 27

Early-onset Formation of Parenchymal Plaque Amyloid Abrogates Cerebral Microvascular Amyloid Accumulation in Transgenic Mice

Xu, F., Kotarba, A. E., Ou-Yang, M.-H., Fu, Z., Davis, J., Smith, S. O., & Nostrand, W. E. V. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.536565 · Cited by 26

Recent insights into the cellular and molecular determinants of aging

Ruan, L., Zhang, X., & Li, R. (2018) · Journal of Cell Science · doi:10.1242/jcs.210831 · Cited by 28

Physical and toxicological profiles of human IAPP amyloids and plaques

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In vivo localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease

Jean, L., Brimijoin, S., & Vaux, D. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006230 · Cited by 27

Human amyloid-β enriched extracts: evaluation of in vitro and in vivo internalization and molecular characterization

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Remodeling Alzheimer-amyloidosis models by seeding

Ulm, B. S., Borchelt, D., & Moore, B. D. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00429-4 · Cited by 26

Docking and Molecular Dynamics-Based Identification of Interaction between Various Beta-Amyloid Isoforms and RAGE Receptor

Tolstova, A. P., Adzhubei, A. A., Mitkevich, V. A., Petrushanko, I. Y., & Makarov, A. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911816 · Cited by 26

A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis

Ogawa, M., & Furukawa, Y. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00083 · Cited by 27

Methods and models in neurodegenerative and systemic protein aggregation diseases.

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Highly potent intracellular membrane-associated Aβ seeds

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Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds

Madsen, H. B., & Vilhardt, F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010227 · Cited by 26

Structure-specific amyloid precipitation in biofluids

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GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells

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Self-Propagative Replication of Aβ Oligomers Suggests Potential Transmissibility in Alzheimer Disease

Kumar, A., Pate, K. M., Moss, M. A., Dean, D. N., & Rangachari, V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111492 · Cited by 26

Prion-like properties of disease-relevant proteins in amyotrophic lateral sclerosis

Bräuer, S., Zimyanin, V. L., & Hermann, A. (2018) · Journal of Neural Transmission · doi:10.1007/s00702-018-1851-y · Cited by 29

Effect of β-amyloid on blood-brain barrier properties and function

Petrushanko, I. Y., Mitkevich, V. A., & Makarov, A. А. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01052-x · Cited by 28

Infectivity versus Seeding in Neurodegenerative Diseases Sharing a Prion-Like Mechanism

Fernández‐Borges, N., Eraña, H., Elezgarai, S. R., Harrathi, C., Gayosso, M., & Castilla, J. (2013) · International Journal of Cell Biology · doi:10.1155/2013/583498 · Cited by 26

Prion-like disorders and Transmissible Spongiform Encephalopathies: An overview of the mechanistic features that are shared by the various disease-related misfolded proteins

Eraña, H., Venegas, V., Charco, J. M., & Castilla, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.166 · Cited by 26

The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates

Creekmore, B. C., Chang, Y., & Lee, E. B. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab039 · Cited by 28

Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases

Furukawa, Y., & Nukina, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.011 · Cited by 25

Sequence-dependent Internalization of Aggregating Peptides

Couceiro, J. R., Gallardo, R. U., Smet, F. D., Baets, G. D., Baatsen, P., Annaert, W. G., Roose, K., Saelens, X., Schymkowitz, J. W. H., & Rousseau, F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586636 · Cited by 27

Neuron-to-Neuron Transmission of Neurodegenerative Pathology

Hallbeck, M., Nath, S., & Marcusson, J. O. (2013) · The Neuroscientist · doi:10.1177/1073858413494270 · Cited by 24

Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R

Kumar, H., & Udgaonkar, J. B. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.010 · Cited by 25

Alpha-Synuclein Transmission and Mitochondrial Toxicity in Primary Human Foetal Enteric Neurons In Vitro

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Conformational Dynamics of Specific Aβ Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis

Dean, D. N., Pate, K. M., Moss, M. A., & Rangachari, V. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00161 · Cited by 23

Production of seedable Amyloid-β peptides in model of prion diseases upon PrPSc-induced PDK1 overactivation

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Human subiculo-fornico-mamillary system in Alzheimer’s disease: Tau seeding by the pillar of the fornix

Brainbank Neuro-CEB Neuropathology Network, Thierry, M., Boluda, S., Delatour, B., Marty, S., Seilhean, D., Potier, M., & Duyckaerts, C. J. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02108-7 · Cited by 26

Anticoagulants for Treatment of Alzheimer’s Disease

Grossmann, K. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200610 · Cited by 27

N-terminally truncated Aβ4-x proteoforms and their relevance for Alzheimer’s pathophysiology

Rostagno, A. A., Cabrera, E., Lashley, T., & Ghiso, J. A. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00303-3 · Cited by 23

Linking Cerebrovascular Dysfunction to Age-Related Hearing Loss and Alzheimer’s Disease—Are Systemic Approaches for Diagnosis and Therapy Required?

Förster, C. Y., Shityakov, S., Scheper, V., & Lenarz, T. (2022) · Biomolecules · doi:10.3390/biom12111717 · Cited by 30

Molecular drug targets and therapies for Alzheimer’s disease

Singh, D. B., Gupta, M., Kesharwani, R. K., Sagar, M., Dwivedi, S., & Misra, K. (2014) · Translational Neuroscience · doi:10.2478/s13380-014-0222-x · Cited by 25

Hypoxia induces expression of a GPI‐anchorless splice variant of the prion protein

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Lesion of the subiculum reduces the spread of amyloid beta pathology to interconnected brain regions in a mouse model of Alzheimer’s disease

George, S., Rönnbäck, A., Gouras, G. K., Petit, G. H., Grueninger, F., Winblad, B., Graff, C., & Brundin, P. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-17 · Cited by 23

Potential common pathogenesis of several neurodegenerative diseases

Fan, T., Peng, J., Liang, H., Chen, W., Wang, J., & Xu, R. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01054 · Cited by 29

Neurodegenerative lesions: Seeding and spreading

Duyckaerts, C. J. (2013) · Revue Neurologique · doi:10.1016/j.neurol.2013.07.018 · Cited by 24

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

Direct Oral Anticoagulants (DOACs) for Therapeutic Targeting of Thrombin, a Key Mediator of Cerebrovascular and Neuronal Dysfunction in Alzheimer’s Disease

Grossmann, K. (2022) · Biomedicines · doi:10.3390/biomedicines10081890 · Cited by 24

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., The Brainbank Neuro-CEB Neuropathology Network, Letournel, F., Martin‐Négrier, M., Faisant, M., et al. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01410-y · Cited by 29

Harnessing prions as test agents for the development of broad-range disinfectants

Wagenführ, K., & Beekes, M. (2012) · Prion · doi:10.4161/pri.6.1.18556 · Cited by 23

Same causes, same cures

Zhang, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.086 · Cited by 23

Cells and prions: A license to replicate

Nuvolone, M., Aguzzi, A., & Heikenwälder, M. F. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.06.014 · Cited by 23

De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers

Sharma, J., Wisniewski, B. T., Paulson, E. J., Obaoye, J. O., Merrill, S. J., & Manogaran, A. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-00135-6 · Cited by 23

Analysis of Amyloid Beta Aggregation Kinetics Using Sym‐Triazine β‐Sheet Inhibitors

Veloso, A. J., Hung, V. W. S., Cheng, X. R., & Kerman, K. (2012) · Electroanalysis · doi:10.1002/elan.201200216 · Cited by 22

Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β

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Thiophene‐Based Ligands: Design, Synthesis and Their Utilization for Optical Assignment of Polymorphic‐Disease‐Associated Protein Aggregates

Björk, L., Klingstedt, T., & Nilsson, K. P. R. (2023) · ChemBioChem · doi:10.1002/cbic.202300044 · Cited by 24

Switching On/Off Amyloid Plaque Formation in Transgenic Animal Models of Alzheimer’s Disease

Kozin, S. A., Kechko, O. I., Adzhubei, A. A., Makarov, A. А., & Mitkevich, V. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010072 · Cited by 21

Prions: A Piece of the Puzzle?

Lahiri, D. K. (2012) · Science · doi:10.1126/science.337.6099.1172-a · Cited by 22

A new approach for the separation, characterization and testing of potential prionoid protein aggregates through hollow-fiber flow field-flow fractionation and multi-angle light scattering

Marassi, V., Beretti, F., Roda, B., Alessandrini, A., Facci, P., Maraldi, T., Zattoni, A., Reschiglian, P., & Portolani, M. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.08.003 · Cited by 21

The prion-like nature of amyotrophic lateral sclerosis

McAlary, L., Yerbury, J. J., & Cashman, N. R. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.002 · Cited by 21

Kinetic Modulation of Amyloid-β (1–42) Aggregation and Toxicity by Structure-Based Rational Design

Im, D., Heo, C. E., Son, M. K., Park, C. R., Kim, H. I., & Choi, J. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c10173 · Cited by 21

Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective

Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25

A rapid dual staining procedure for the quantitative discrimination of prion amyloid from tissues reveals how interactions between amyloid and lipids in tissue homogenates may hinder the detection of prions

Hervé, R., Collin, R., Pinchin, H. E., Secker, T. J., & Keevil, C. W. (2009) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2009.01.017 · Cited by 21

Discovery of Chemicals to Either Clear or Indicate Amyloid Aggregates by Targeting Memory‐Impairing Anti‐Parallel Aβ Dimers

Lee, J. C., Kim, H. Y., Lee, S., Shin, J., Kim, H. V., Kim, K., Baek, S., Lee, D.-H., Jeon, H., Kim, D.-W., et al. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202002574 · Cited by 21

Amyloid-beta peptide Aβp3-42 affects early aggregation of full-length Aβ1-42

Sanders, H. M., Lust, R. M., & Teller, J. K. (2009) · Peptides · doi:10.1016/j.peptides.2009.01.027 · Cited by 21

Induction et propagation de la pathologie par la protéine tau chez un modèle murin de la maladie d’Alzheimer

Clavaguera, F., Goedert, M., & Tolnay, M. (2010) · médecine/sciences · doi:10.1051/medsci/2010262121 · Cited by 22

Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero‐oligomers of unique secondary structure

Goldblatt, G., Cilenti, L., Matos, J. O., Lee, B., Ciaffone, N., Wang, Q. X., Tétard, L., Teter, K., & Tatulian, S. A. (2017) · FEBS Journal · doi:10.1111/febs.14058 · Cited by 21

Direct Evidence for Self-Propagation of Different Amyloid-β Fibril Conformations

Spirig, T., Ovchinnikova, O. Y., Vagt, T., & Glockshuber, R. (2014) · Neurodegenerative Diseases · doi:10.1159/000363623 · Cited by 20

Impact of endolysosomal dysfunction upon exosomes in neurodegenerative diseases

Izco, M., Carlos, E., & Alvarez‐Erviti, L. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105651 · Cited by 18

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. (2022) · BMC Molecular and Cell Biology · doi:10.1186/s12860-022-00462-1 · Cited by 24

Linear and conformation specific antibodies in aged beagles after prolonged vaccination with aggregated Abeta

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Countering amyloid polymorphism and drug resistance with minimal drug cocktails

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