Cited by 1,665Alzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis ResearchPrion Diseases and Protein Misfolding

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Pathology of Neurodegenerative Diseases

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Dugger, Brittany N., Dickson, Dennis W.·2017·Cold Spring Harbor Perspectives in Biology

DOI 10.1101/cshperspect.a028035PMC PMC5495060

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Abstract

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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Authors: Dugger, B. N., & Dickson, D. W.
Affiliations: University of California, San Francisco (US)
Mayo Clinic in Florida (US)
ORCID: Dugger, Brittany N.
Dickson, Dennis W.
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)
DOI: 10.1101/cshperspect.a028035
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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