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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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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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