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Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Open accessAbstract
Many neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, are characterized by the progressive appearance of abnormal proteinaceous assemblies in the nervous system. Studies in experimental systems indicate that the assemblies originate from the prion-like seeded aggregation of specific misfolded proteins that proliferate and amass to form the intracellular and/or extracellular lesions typical of each disorder. The host in which the proteopathic seeds arise provides the biochemical and physiological environment that either supports or restricts their emergence, proliferation, self-assembly, and spread. Multiple mechanisms influence the spatiotemporal spread of seeds and the nature of the resulting lesions, one of which is the cellular uptake, release, and transport of seeds along neural pathways and networks. The characteristics of cells and regions in the affected network govern their vulnerability and thereby influence the neuropathological and clinical attributes of the disease. The propagation of pathogenic protein assemblies within the nervous system is thus determined by the interaction of the proteopathic agent and the host milieu.
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“This triphasic framework is also shared by other NDDs, such as amyotrophic lateral sclerosis [4,5].”
From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [5]
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“The pathogenesis of AD, PD, and HD can conceptually be broken down into three phases: (1) creation of an abnormal protein, (2) aggregation or lack of clearance, and (3) propagation.”
From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [5]
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Metadata
- Authors
- Jucker, M., & Walker, L. C.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Emory University (US)
- Corresponding author
- Jucker, Mathias
- Walker, Lary C.
- Venue
- Nature Neuroscience
- Published
- 2018-09-26
- Volume
- 21
- Issue
- 10
- Pages
- 1341-1349
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC6375686
- OpenAlex
- W2891544369
- Cited by
- 450
- References
- 154
- Citations by year
- 2026: 50 · 2025: 69 · 2024: 41 · 2023: 59 · 2022: 51 · 2021: 70 · 2020: 66 · 2019: 40 · 2018: 4
- FWCI
- 4.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- DZNE Pub (submittedVersion)
- Funders
- National Institutes of Health (P51OD011132)
- National Institute on Aging (P50AG025688)
- 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 › Amyotrophic Lateral Sclerosis Research
- Keywords
- neurodegenerative diseases, protein aggregation, prion-like seeding, protein misfolding, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, seed propagation, neurodegeneration, host-pathogen interaction
- MeSH terms
- Animals, Cell Communication, Humans, Prions, Neurodegenerative Diseases
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