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Pathology of Neurodegenerative Diseases
Open accessAbstract
Neurodegenerative disorders are characterized by progressive loss of selectively vulnerable populations of neurons, which contrasts with select static neuronal loss because of metabolic or toxic disorders. Neurodegenerative diseases can be classified according to primary clinical features (e.g., dementia, parkinsonism, or motor neuron disease), anatomic distribution of neurodegeneration (e.g., frontotemporal degenerations, extrapyramidal disorders, or spinocerebellar degenerations), or principal molecular abnormality. The most common neurodegenerative disorders are amyloidoses, tauopathies, α-synucleinopathies, and TDP-43 proteinopathies. The protein abnormalities in these disorders have abnormal conformational properties. Growing experimental evidence suggests that abnormal protein conformers may spread from cell to cell along anatomically connected pathways, which may in part explain the specific anatomical patterns observed at autopsy. In this review, we detail the human pathology of select neurodegenerative disorders, focusing on their main protein aggregates.
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“The presence of NFTs in the brain triggers a complex cascade of biochemical and cellular processes that result in neurodegeneration and neuronal loss [2].”
From Diffusion tensor imaging reveals whole-brain microstructural changes in the P301L mouse model of tauopathy. (2020) · cites this paper as [2]
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“AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations (19, 65).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]
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“Both 3R- and 4R-tau isoforms were detected with no noticeable difference in the 3R to 4R ratio between LOAD and HC 3D-CNs, consistent with the concept that AD is a mixed 3R/4R tauopathy (65, 66) (Fig. 3D).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]
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Metadata
- Authors
- Dugger, B. N., & Dickson, D. W.
- Affiliations
- University of California, San Francisco (US)
- Mayo Clinic in Florida (US)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2017-01-06
- Volume
- 9
- Issue
- 7
- Pages
- a028035
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC5495060
- OpenAlex
- W2570634615
- Cited by
- 1,665
- References
- 159
- Citations by year
- 2026: 161 · 2025: 265 · 2024: 319 · 2023: 334 · 2022: 233 · 2021: 210 · 2020: 98 · 2019: 21 · 2018: 14 · 2017: 7
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Henry M. Jackson Foundation
- CurePSP
- Daiichi-Sankyo
- National Institutes of Health (AG016574, NS084974, AG002132, NS072187, AG037491)
- National Institute on Aging (P01AG002132, R01AG037491, P50AG016574)
- National Institute of Neurological Disorders and Stroke (P01NS084974, P50NS072187)
- Daiichi Sankyo Europe
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- neurodegenerative diseases, proteinopathies, amyloidosis, tauopathy, synucleinopathies, TDP-43 proteinopathy, protein aggregation, protein conformation, prion-like spread, selective neuronal loss, dementia, parkinsonism, motor neuron disease, frontotemporal lobar degeneration, extrapyramidal disorders, spinocerebellar degeneration
- MeSH terms
- Humans, Protein Conformation, Neurodegenerative Diseases, Protein Aggregates
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