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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Open accessAbstract
For several decades scientists have speculated that the key to understanding age-related neurodegenerative disorders may be found in the unusual biology of the prion diseases. Recently, owing largely to the advent of new disease models, this hypothesis has gained experimental momentum. In a remarkable variety of diseases, specific proteins have been found to misfold and aggregate into seeds that structurally corrupt like proteins, causing them to aggregate and form pathogenic assemblies ranging from small oligomers to large masses of amyloid. Proteinaceous seeds can therefore serve as self-propagating agents for the instigation and progression of disease. Alzheimer's disease and other cerebral proteopathies seem to arise from the de novo misfolding and sustained corruption of endogenous proteins, whereas prion diseases can also be infectious in origin. However, the outcome in all cases is the functional compromise of the nervous system, because the aggregated proteins gain a toxic function and/or lose their normal function. As a unifying pathogenic principle, the prion paradigm suggests broadly relevant therapeutic directions for a large class of currently intractable diseases.
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In the citing paper
“The recent discovery that specific misfolded and aggregated proteins can propagate and spread in a prion-like fashion has sparked considerable interest (67).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“In Parkinson’s disease and Lewy body disease, α-synuclein aggregates initially spread through the brainstem and olfactory bulb followed by limbic structures, and only thence to the neocortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“In each of these cases, the aggregates initially deposit at the ventral base of the forebrain and midbrain, and then extend rostrally and dorsally to the cortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“While still a contentious topic [46], there is now substantial evidence that also supports the idea that propagation of pathological tau species occurs between cells [47–50].”
From Glial contributions to neurodegeneration in tauopathies (2017) · cites this paper as [50]
In the citing paper
“As aforementioned, the neuropathological lesions of not only AD but also PD/DLB and amyotrophic lateral sclerosis (ALS) are known to spread through the brain in a rather specific pattern, which also serves as a basis for the neuropathological staging of disease severity [203].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [203]
In the citing paper
“Importantly, the spatiotemporal spread of αSyn lesions in PD/DLB is nearly inverted to the spread of Aβ and tau pathology as observed in AD [203].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [203]
In the citing paper
“pathological neurofibrillary Tau aggregates show a pattern of accumulation that starts in the entorhinal cortex and spreads through connected pathways to cortical areas (Jucker and Walker, 2013)”
From Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease (2020) · cites this paper as Jucker and Walker, 2013
In the citing paper
“It has been suggested that alpha-synuclein could act like a prion protein during PD pathogenesis.In this theory pathologic, misfolded alpha-synuclein is an 'infectious' protein spreading pathology by forming a template that seeds misfolding for nearby alpha-synuclein protein, turning the previously healthy protein into a pathogenic protein (Jucker and Walker, 2013;Visanji et al., 2013).”
From The Gut-Brain Axis in Parkinson’s Disease: Possibilities for Food-Based Therapies (2017) · cites this paper as Jucker and Walker, 2013
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Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814
Phases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
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Halpern, M., Brennand, K., & Gregory, J. A. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104562 · Cited by 30
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Han, Y., Li, J., Xia, W., Li, Q., Sun, Z., Zeng, W., Hu, Y., Luk, K. C., Liu, C., Xiang, S., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.03.019 · Cited by 28
Yurinskaya, M. M., Mitkevich, V. A., Kozin, S. A., Evgen’ev, M. B., Makarov, A. А., & Винокуров, М. Г. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.336 · Cited by 27
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Ruan, L., Zhang, X., & Li, R. (2018) · Journal of Cell Science · doi:10.1242/jcs.210831 · Cited by 28
Zhu, X.-H., Lee, B., Tuite, P., Coles, L. D., Sathe, A. G., Chen, C., Cloyd, J. C., Low, W. C., Steer, C. J., & Chen, W. (2021) · Metabolites · doi:10.3390/metabo11030145 · Cited by 27
Structure and function in artificial, zebrafish and human neural networks
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Olm, C. A., Kandel, B. M., Avants, B., Detre, J. A., Gee, J. C., Grossman, M., & McMillan, C. T. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8221-1 · Cited by 29
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Wickner, R. B., Bezsonov, E. E., Son, M., Ducatez, M., DeWilde, M., & Edskes, H. K. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01285 · Cited by 27
Goldstein, L., Fogel‐Grinvald, H., & Steiner, I. (2019) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2019.01.012 · Cited by 27
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Walker, L. C., & Jucker, M. (2024) · Science · doi:10.1126/science.adq5252 · Cited by 27
Self-citationSong, H.-L., Kim, N.-Y., Park, J., Kim, M. I., Jeon, Y.-N., Lee, S.-J., Cho, K., Shim, Y.-L., Lee, K.-H., Mun, Y.-S., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci156537 · Cited by 26
Meyer, V., Holden, M. R., Weismiller, H. A., Eaton, G. R., Eaton, S. S., & Margittai, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.715557 · Cited by 26
Liu, Y., Subedi, K., Baride, A., Romanova, S., Callegari, E. A., Huber, C. C., Wang, X., & Wang, H. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02081-7 · Cited by 26
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Raj, A., Tora, V., Gao, X., Cho, H., Choi, J. Y., Ryu, Y. H., Lyoo, C. H., & Franchi, B. (2021) · Brain Connectivity · doi:10.1089/brain.2020.0841 · Cited by 27
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Chen, M., Vincent, J., Ezeanii, A., Wakade, S. C., Yerigenahally, S. D., & Mor, D. E. (2022) · Life Science Alliance · doi:10.26508/lsa.202201366 · Cited by 28
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Ikegawa, M., Kakuda, N., Miyasaka, T., Toyama, Y., Nirasawa, T., Minta, K., & Hanrieder, J. (2023) · Brain Connectivity · doi:10.1089/brain.2022.0057 · Cited by 26
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Pfeiffer, P. B., Ugrina, M., Schwierz, N., Sigurdson, C. J., Schmidt, M., & Fändrich, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168422 · Cited by 26
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
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Preston, G. M., Guerriero, C. J., Metzger, M. B., Michaelis, S., & Brodsky, J. L. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.016 · Cited by 26
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Mysiris, D. S., Vavougios, G. D., Karamichali, E., Papoutsopoulou, S., Stavrou, V. T., Papayianni, E., Boutlas, S., Mavridis, T., Foka, P., Zarogiannis, S. G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179739 · Cited by 25
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Sampson, T. R. (2023) · FEBS Journal · doi:10.1111/febs.17023 · Cited by 25
Ho, P., Hsieh, T., & Tsai, K. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102441 · Cited by 28
Torbeev, V. Y., Ebert, M., Dolenc, J., & Hilvert, D. (2015) · Journal of the American Chemical Society · doi:10.1021/ja510109p · Cited by 25
Choudhary, S., Save, S. N., & Vavilala, S. L. (2018) · Scientific Reports · doi:10.1038/s41598-018-24079-7 · Cited by 25
Brain insulin response and peripheral metabolic changes in a Tau transgenic mouse model
Leboucher, A., Ahmed, T., Caron, É., Tailleux, A., Raison, S., Joly‐Amado, A., Marciniak, E., Carvalho, K., Hamdane, M., Bantubungi, K., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.01.008 · Cited by 29
Anticoagulants for Treatment of Alzheimer’s Disease
Grossmann, K. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200610 · Cited by 27
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Kaiser, M. (2020) · The MIT Press eBooks · doi:10.7551/mitpress/11980.001.0001 · Cited by 25
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Mehra, S., Ahlawat, S., Kumar, H., Datta, D., Navalkar, A., Singh, N., Patel, K., Gadhe, L. G., Kadu, P., Kumar, R., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167761 · Cited by 25
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Loch, R. A., Wang, H., Perálvarez‐Marín, A., Berger, P., Nielsen, H. M., Chroni, A., & Luo, J. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.01.022 · Cited by 26
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Zhang, L., Qu, J., Ma, H., Chen, T., Liu, T., & Zhu, D. (2024) · Psychoradiology · doi:10.1093/psyrad/kkad033 · Cited by 27
Anti-acetylated-tau immunotherapy is neuroprotective in tauopathy and brain injury
Bravo, C., Krukowski, K., Barker, S., Wang, C., Li, Y., Fan, L., Vázquez‐Rosa, E., Shin, M., Wong, M. Y., McCullough, L. D., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00733-9 · Cited by 26
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Berry, D. B., Giles, K., Oehler, A., Bhardwaj, S., DeArmond, S. J., & Prusiner, S. B. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu656 · Cited by 25
Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils
Yagi, H., Mizuno, A., So, M., Hirano, M., Adachi, M., Ogawa, Y., Hagihara, Y., Ikenoue, T., Lee, Y., Kawata, Y., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.12.014 · Cited by 25
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Smith, J., Rha, A. K., Mehta, A., & Lynn, D. G. (2014) · Life · doi:10.3390/life4040887 · Cited by 25
Lou, Z., Wang, B., Guo, C., Wang, K., Zhang, H., & Xu, B. (2015) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2015.07.053 · Cited by 25
Bondy, S. C. (2016) · Toxicology · doi:10.1016/j.tox.2016.01.007 · Cited by 25
sFRP-mediated Wnt sequestration as a potential therapeutic target for Alzheimer’s disease
Warrier, S. R., Marimuthu, R., Sekhar, S. C., Bhuvanalakshmi, G., Arfuso, F., Das, A. K., Bhonde, R. R., Martins, R. N., & Dharmarajan, A. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.04.002 · Cited by 25
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Powell, F., Tosun, D., Sadeghi, R., Weiner, M., & Raj, A. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170798 · Cited by 27
Kumar, H., & Udgaonkar, J. B. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.010 · Cited by 25
Concha‐Marambio, L., Shahnawaz, M., & Soto, C. A. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9124-2_4 · Cited by 25
Drobny, A., Ngo, P. A., Neurath, M. F., Zunke, F., & López-Posadas, R. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.655123 · Cited by 24
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Tkemaladze, J. (2026) · Longevity Horizon · doi:10.65649/3hm9b025 · Cited by 24
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Ma, Y., Huang, R., Qi, W. D., Su, R., & He, Z. (2019) · Journal of Materials Chemistry B · doi:10.1039/c8tb02964d · Cited by 24
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Bécot, A., Volgers, C., & van Niel, G. (2020) · Biomedicines · doi:10.3390/biomedicines8080272 · Cited by 25
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Self-citationHuman cystatin C monomer, dimer, oligomer, and amyloid structures are related to health and disease
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Angelov, B., & Angelova, A. (2017) · Nanoscale · doi:10.1039/c7nr03454g · Cited by 24
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Pluta, R. M., Ułamek-Kozioł, M., Januszewski, S., & Czuczwar, S. J. (2018) · Biomarkers in Medicine · doi:10.2217/bmm-2018-0034 · Cited by 25
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Peraza, L. R., Díaz‐Parra, A., Kennion, O., Moratal, D., Taylor, J., Kaiser, M., Bauer, R., & Initiative, A. D. N. (2019) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2018.12.004 · Cited by 24
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Heinemann, S. D., Posimo, J. M., Mason, D. M., Hutchison, D. F., & Leak, R. K. (2016) · Hippocampus · doi:10.1002/hipo.22580 · Cited by 24
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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
Kassubek, J., & Müller, H. (2016) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2016.1146590 · Cited by 23
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Graw, J. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.11.006 · Cited by 23
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Metadata
- Authors
- Jucker, M., & Walker, L. C.
- Affiliations
- Hertie Institute for Clinical Brain Research (DE)
- Emory University (US)
- Corresponding author
- Jucker, Mathias
- Walker, Lary C.
- Venue
- Nature
- Published
- 2013-09-04
- Volume
- 501
- Issue
- 7465
- Pages
- 45-51
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3963807
- OpenAlex
- W2034147064
- Cited by
- 1,663
- References
- 126
- Citations by year
- 2026: 82 · 2025: 113 · 2024: 114 · 2023: 111 · 2022: 119 · 2021: 161 · 2020: 140 · 2019: 153 · 2018: 131 · 2017: 166 · 2016: 147 · 2015: 119 · 2014: 101 · 2013: 6
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DZNE Pub (submittedVersion)
- Funders
- National Institutes of Health (P51OD011132)
- National Institute on Aging (R21AG040589)
- National Center for Research Resources (P51RR165, P51RR000165)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- protein aggregation, seeded aggregation, neurodegenerative diseases, prion disease, Alzheimer's disease, Parkinson's disease, Creutzfeldt-Jakob disease, protein misfolding, amyloid, oligomers, proteinopathies, disease models, neurodegeneration therapy
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Humans, Prions, tau Proteins, Prion Diseases, Neurodegenerative Diseases, alpha-Synuclein
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