Neurodegenerative Diseases: Expanding the Prion Concept

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DNA methylation age of human tissues and cell types

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Protein Misfolding, Functional Amyloid, and Human Disease

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Prions

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Novel Proteinaceous Infectious Particles Cause Scrapie

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Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade

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Clinical and biomarker changes in dominantly inherited Alzheimer's disease

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Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

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Adapting Proteostasis for Disease Intervention

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RNA-seq and network analysis reveal unique glial gene expression signatures during prion infection

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Neurodegeneration and neuroinflammation are linked, but independent of alpha‐synuclein inclusions, in a seeding/spreading mouse model of Parkinson's disease

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Applying fluid biomarkers to Alzheimer's disease

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Microglia alterations in neurodegenerative diseases and their modeling with human induced pluripotent stem cell and other platforms

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Developing Therapeutics for PrP Prion DiseasesPreprint

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Spatially-extended nucleation-aggregation-fragmentation models for the dynamics of prion-like neurodegenerative protein-spreading in the brain and its connectome

Fornari, S., Schäfer, A., Ellen Kuhl, A., & Goriely, A. (2019) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2019.110102 · Cited by 62

Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits

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Proteopathic Strains and the Heterogeneity of Neurodegenerative Diseases

Walker, L. C. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-034943 · Cited by 60

Prion‐like propagation as a pathogenic principle in frontotemporal dementia

Hock, E., & Polymenidou, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13668 · Cited by 58

Distribution of Misfolded Prion Protein Seeding Activity Alone Does Not Predict Regions of Neurodegeneration

Alibhai, J. D., Blanco, R. A., Barria, M. A., Piccardo, P., Caughey, B. W., Perry, V. H., Freeman, T. C., & Manson, J. C. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002579 · Cited by 58

Prion Protein: The Molecule of Many Forms and Faces

Kovač, V., & Šerbec, V. Č. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031232 · Cited by 55

Identification of protein aggregates in the aging vertebrate brain with prion-like and phase-separation properties

Harel, I., Chen, Y. R., Ziv, I., Singh, P. P., Heinzer, D., Negredo, P. N., Goshtchevsky, U., Wang, W., Astre, G., Moses, E., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2023.112787 · Cited by 56

Multifaceted Role of Sialylation in Prion Diseases

Baskakov, I. V., & Katorcha, E. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00358 · Cited by 54

Aβ seeding potency peaks in the early stages of cerebral β‐amyloidosis

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Tipping points in neurodegeneration

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The in-tissue molecular architecture of β-amyloid pathology in the mammalian brain

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Biosensing: The best alternative for conventional methods in detection of Alzheimer's disease biomarkers

Mobed, A., & Hasanzadeh, M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.257 · Cited by 47

Specification of Physiologic and Disease States by Distinct Proteins and Protein Conformations

Jarosz, D. F., & Khurana, V. (2017) · Cell · doi:10.1016/j.cell.2017.10.047 · Cited by 46

Microglial Turnover in Ageing-Related Neurodegeneration: Therapeutic Avenue to Intervene in Disease Progression

Azam, S., Haque, M. E., Kim, I., & Choi, D. (2021) · Cells · doi:10.3390/cells10010150 · Cited by 46

Targeting α‐synuclein: Therapeutic options

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Differential diagnosis with other rapid progressive dementias

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Alzheimer’s Disease: From Pathogenesis to Mesenchymal Stem Cell Therapy – Bridging the Missing Link

Hu, J., & Wang, X. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.811852 · Cited by 42

Neuronal Oscillations on Evolving Networks: Dynamics, Damage, Degradation, Decline, Dementia, and Death

Goriely, A., Ellen Kuhl, A., & Bick, C. (2020) · Physical Review Letters · doi:10.1103/physrevlett.125.128102 · Cited by 40

Current insights and assumptions on α-synuclein in Lewy body disease

Leak, R. K., Clark, R. N., Abbas, M., Xu, F., Brodsky, J. L., Chen, J., Hu, X., & Luk, K. C. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02781-3 · Cited by 41

Sialylation Controls Prion Fate in Vivo

Srivastava, S., Katorcha, E., Daus, M. L., Lasch, P., Beekes, M., & Baskakov, I. V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768010 · Cited by 39

A new electrochemical immunosensor for sensitive detection of prion based on Prussian blue analogue

Li, J., Yan, X., Li, X., Zhang, X., & Chen, J. (2017) · Talanta · doi:10.1016/j.talanta.2017.12.006 · Cited by 39

Posttranslational modifications define course of prion strain adaptation and disease phenotype

Makarava, N., Chang, J. C., Molesworth, K., & Baskakov, I. V. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138677 · Cited by 39

α-Synuclein aggregation and transmission in Parkinson’s disease: a link to mitochondria and lysosome

Wang, R., Sun, H., Ren, H., & Wang, G. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1756-9 · Cited by 38

Longitudinal structural gray matter and white matter MRI changes in presymptomatic progranulin mutation carriers

Olm, C. A., McMillan, C. T., Irwin, D. J., Deerlin, V. M. V., Cook, P. A., Gee, J. C., & Grossman, M. (2018) · NeuroImage Clinical · doi:10.1016/j.nicl.2018.05.017 · Cited by 37

Ellagic acid can act as a chaperone and suppress the heat-induced amyloid-like aggregation of ovalbumin

Yan, C., & Zhou, Z. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105408 · Cited by 37

Effects of Polyphenols in Aging and Neurodegeneration Associated with Oxidative Stress

Rivas, F., Poblete-Aro, C., Pando, M. E., Allel, M. J., Fernández, V. S., Soto, A., Nova-Baeza, P., & García‐Díaz, D. F. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666211101100632 · Cited by 37

Can the administration of platelet lysates to the brain help treat neurological disorders?

Nebie, O., Buée, L., Blum, D. L., & Burnouf, T. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04397-w · Cited by 37

Alzheimer’s disease seeded tau forms paired helical filaments yet lacks seeding potential

Duan, P., Dregni, A. J., Xu, H. W., Changolkar, L. N., Lee, V. M. ‐., Lee, E. B., & Hong, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107730 · Cited by 36

Temperature-Induced Misfolding in Prion Protein: Evidence of Multiple Partially Disordered States Stabilized by Non-Native Hydrogen Bonds

Chamachi, N. G., & Chakrabarty, S. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01042 · Cited by 36

Optimization of Aryl Amides that Extend Survival in Prion-Infected Mice

Giles, K., Berry, D. B., Condello, C., Dugger, B. N., Li, Z., Oehler, A., Bhardwaj, S., Elepano, M., Guan, S., Silber, B. M., et al. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.116.235556 · Cited by 35

Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions

Cescatti, M., Saverioni, D., Capellari, S., Tagliavini, F., Kitamoto, T., Ironside, J. W., Giese, A., & Parchi, P. (2016) · Journal of Virology · doi:10.1128/jvi.00144-16 · Cited by 34

Intrinsically disordered proteins in the formation of functional amyloids from bacteria to humans

Avni, A., Swasthi, H. M., Majumdar, A., & Mukhopadhyay, S. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.05.005 · Cited by 35

Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone

Petrosyan, R., Patra, S., Rezajooei, N., Garen, C. R., & Woodside, M. T. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010213118 · Cited by 34

Amyloid pathology arrangements in Alzheimer’s disease brains modulate in vivo seeding capability

Duran-Aniotz, C. A., Moreno‐González, I., Gamez, N., Perez-Urrutia, N., Vegas‐Gomez, L., Soto, C. A., & Morales, R. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01155-0 · Cited by 34

N-terminal Prion Protein Peptides (PrP(120–144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways

Wang, Y., Shao, Q., & Hall, C. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744573 · Cited by 33

Aβ seeds and prions: How close the fit?

Rasmussen, J., Jucker, M., & Walker, L. C. (2017) · Prion · doi:10.1080/19336896.2017.1334029 · Cited by 33

Methionine oxidation within the prion protein

Bettinger, J. Q., & Ghaemmaghami, S. (2020) · Prion · doi:10.1080/19336896.2020.1796898 · Cited by 32

Alpha-Synuclein Strain Variability in Body-First and Brain-First Synucleinopathies

Just, M. K., Gram, H., Theologidis, V., Jensen, P. H., Nilsson, K. P. R., Lindgren, M., Knudsen, K., Borghammer, P., & Berge, N. V. D. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.907293 · Cited by 32

Insights into Mechanisms of Chronic Neurodegeneration

Diack, A. B., Alibhai, J. D., Barron, R. M., Bradford, B. M., Piccardo, P., & Manson, J. C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17010082 · Cited by 31

Unravelling the glial response in the pathogenesis of Alzheimer's disease

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Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

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Discontinuous Galerkin methods for Fisher–Kolmogorov equation with application to α -synuclein spreading in Parkinson’s disease

Corti, M., Bonizzoni, F., Dede’, L., Quarteroni, A. M., & Antonietti, P. F. (2023) · Computer Methods in Applied Mechanics and Engineering · doi:10.1016/j.cma.2023.116450 · Cited by 30

The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis

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Oxidative Stress in Alzheimer’s Disease: The Shortcomings of Antioxidant Therapies

Pappolla, M. A., Martins, R. N., Poeggeler, B., Omar, R. A., & Perry, G. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-240659 · Cited by 29

Exploring Protein Misfolding and Aggregate Pathology in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Interventions

Johnson, J. T., Fila, W. A., & Anumudu, C. K. (2025) · Applied Sciences · doi:10.3390/app151810285 · Cited by 29

Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery

Chernova, T. A., Chernoff, Y. O., & Wilkinson, K. D. (2019) · Molecules · doi:10.3390/molecules24183388 · Cited by 29

On the role of the cellular prion protein in the uptake and signaling of pathological aggregates in neurodegenerative diseases

Legname, G., & Scialò, C. (2020) · Prion · doi:10.1080/19336896.2020.1854034 · Cited by 29

Gut–Brain Axis in Focus: Polyphenols, Microbiota, and Their Influence on α-Synuclein in Parkinson’s Disease

Riegelman, E., Xue, K. S., Wang, J.-S., & Tang, L. (2024) · Nutrients · doi:10.3390/nu16132041 · Cited by 29

Membrane Trafficking Illuminates a Path to Parkinson’s Disease

Hasegawa, T., Sugeno, N., Kikuchi, A., Baba, T., & Aoki, M. (2017) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.242.63 · Cited by 29

Therapeutic applicability of cannabidiol and other phytocannabinoids in epilepsy, multiple sclerosis and Parkinson's disease and in comorbidity with psychiatric disorders

Sampaio, M. D. F. D. S., de Paiva, Y. B., Sampaio, T. B., Pereira, M. G., & Coimbra, N. C. (2024) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13997 · Cited by 28

Cellular Biology of Tau Diversity and Pathogenic Conformers

Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29

Two alternative pathways for generating transmissible prion disease de novo

Makarava, N., Savtchenko, R. S., & Baskakov, I. V. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0248-5 · Cited by 27

Dendrimers in the context of targeting central nervous system disorders

Palan, F., & Chatterjee, B. (2022) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2022.103474 · Cited by 26

Transfer of disrupted-in-schizophrenia 1 aggregates between neuronal-like cells occurs in tunnelling nanotubes and is promoted by dopamine

Zhu, S., Abounit, S., Korth, C., & Zurzolo, C. (2017) · Open Biology · doi:10.1098/rsob.160328 · Cited by 26

Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates

Caughey, B. W., & Kraus, A. (2019) · Viruses · doi:10.3390/v11111044 · Cited by 26

Aβ Assemblies Promote Amyloidogenic Processing of APP and Intracellular Accumulation of Aβ42 Through Go/Gβγ Signaling

Antonino, M., Marmo, P., Freites, C. L., Quassollo, G., Sánchez, M. F., Lorenzo, A., & Bignante, E. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.852738 · Cited by 24

Communicability distance reveals hidden patterns of Alzheimer’s disease

Lella, E., & Estrada, E. (2020) · Network Neuroscience · doi:10.1162/netn_a_00143 · Cited by 24

Longitudinal diffusion tensor imaging resembles patterns of pathology progression in behavioral variant frontotemporal dementia (BVFTD)

Kassubek, J., Müller, H.-P., Del Tredici, K., Hornberger, M., Schroeter, M. L., Müller, K., Anderl-Straub, S., Uttner, I., Grossman, M., Braak, H., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00047 · Cited by 23

Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease

Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23

Types and Strains: Their Essential Role in Understanding Protein Aggregation in Neurodegenerative Diseases

Wemheuer, W. M., Wrede, A., & Schulz‐Schaeffer, W. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00187 · Cited by 23

Shedding light on prion disease

Glatzel, M., Linsenmeier, L., Dohler, F., Krasemann, S., Puig, B., & Altmeppen, H. C. (2015) · Prion · doi:10.1080/19336896.2015.1065371 · Cited by 22

Familial human prion diseases associated with prion protein mutations Y226X and G131V are transmissible to transgenic mice expressing human prion protein

Race, B., Williams, K., Hughson, A. G., Jansen, C., Parchi, P., Rozemüller, A. J. M., & Chesebro, B. W. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0516-2 · Cited by 22

Calling α-synuclein a prion is scientifically justifiable

Watts, J. C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02058-0 · Cited by 22

Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice

Chesebro, B. W., Striebel, J. F., Rangel, A., Phillips, K. L., Hughson, A. G., Caughey, B. W., & Race, B. (2015) · mBio · doi:10.1128/mbio.01419-15 · Cited by 21

A Comprehensive Review on Preclinical Evidence-based Neuroprotective Potential of Bacopa monnieri against Parkinson's Disease

Goyal, A., Gopika, S., Kumar, A., & Garabadu, D. (2022) · Current Drug Targets · doi:10.2174/1389450123666220316091734 · Cited by 20

Stimulations of the Culture Medium of Activated Microglia and TNF-Alpha on a Scrapie-Infected Cell Line Decrease the Cell Viability and Induce Marked Necroptosis That Also Occurs in the Brains from the Patients of Human Prion Diseases

Ma, Y., Shi, Q., Xiao, K., Wang, J., Chen, C., Gao, L., Gao, C., & Dong, X. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00354 · Cited by 20

NLRP3 inflammasome activation is involved in trimethyltin-induced neuroinflammation

Long, J., Wang, Q., He, H., Sui, X. Y., Lin, G.-D., Wang, S., Yang, J., You, P., Luo, Y., & Wang, Y. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.003 · Cited by 20

Is Multiple System Atrophy a Prion-like Disorder?

Jellinger, K. A., Wenning, G. K., & Stefanova, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810093 · Cited by 19

Puzzles, challenges, and information reservoir of SARS-CoV-2 quasispecies

Domingo, E., Martínez‐González, B., García‐Crespo, C., Somovilla, P., de Ávila, A. I., Soria, M. E., Durán‐Pastor, A., & Perales, C. (2023) · Journal of Virology · doi:10.1128/jvi.01511-23 · Cited by 19

Seeding and cross‐seeding fibrillation of N‐terminal prion protein peptides PrP(120–144)

Wang, Y., & Hall, C. K. (2018) · Protein Science · doi:10.1002/pro.3421 · Cited by 19

Emerging links between cell competition and Alzheimer's disease

Coelho, D. S., & Moreno, E. (2019) · Journal of Cell Science · doi:10.1242/jcs.231258 · Cited by 19

Differential Effects of Parkinson’s Disease on Interneuron Subtypes within the Human Anterior Olfactory Nucleus

Úbeda‐Bañón, I., Flores‐Cuadrado, A., Saiz‐Sánchez, D., & Martı́nez-Marcos, A. (2017) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2017.00113 · Cited by 19

secHsp70 as a tool to approach amyloid-β42 and other extracellular amyloids

de Mena, L., Chhangani, D., Fernández-Fúnez, P., & Rincón-Limas, D. E. (2017) · Fly · doi:10.1080/19336934.2017.1291104 · Cited by 19

The Prion 2018 round tables (II): Aβ, tau, α-synuclein… are they prions, prion-like proteins, or what?

Eraña, H. (2019) · Prion · doi:10.1080/19336896.2019.1569451 · Cited by 19

Personalised regional modelling predicts tau progression in the human brain

Chaggar, P., Vogel, J. W., Binette, A. P., Thompson, T., Strandberg, O. T., Mattsson, N., Karlsson, L., Stomrud, E., Jbabdi, S., Magon, S., et al. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003241 · Cited by 19

Reduction of NF-κB (p65) in Scrapie-Infected Cultured Cells and in the Brains of Scrapie-Infected Rodents

Ma, Y., Shi, Q., Wang, J., Xiao, K., Sun, J. F., Lv, Y., Guo, M., Zhou, W., Chen, C., Chen, G., et al. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00273 · Cited by 18

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

Structure and Aggregation Mechanisms in Amyloids

Almeida, Z. L., & Brito, R. M. M. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamolscs.1.2020.9 · Cited by 17

Metal Toxicity and Dementia Including Frontotemporal Dementia: Current State of Knowledge

Gorini, F., & Tonacci, A. (2024) · Antioxidants · doi:10.3390/antiox13080938 · Cited by 17

Cellular Prion Protein and Amyloid-β Oligomers in Alzheimer’s Disease—Are There Connections?

Fułek, M., Hachiya, N., Gachowska, M., Beszłej, J. A., Bartoszewska, E., Kurpas, D., Kurpiński, T., Adamska, H., Poręba, R., Urban, S., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052097 · Cited by 17

Combining molecular dynamics simulations and experimental analyses in protein misfolding

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Lipids and α-Synuclein: adding further variables to the equation

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