Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
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A hallmark event in neurodegenerative diseases (NDs) is the misfolding, aggregation, and accumulation of proteins, leading to cellular dysfunction, loss of synaptic connections, and brain damage. Despite the involvement of distinct proteins in different NDs, the process of protein misfolding and aggregation is remarkably similar. A recent breakthrough in the field was the discovery that misfolded protein aggregates can self-propagate through seeding and spread the pathological abnormalities between cells and tissues in a manner akin to the behavior of infectious prions in prion diseases. This discovery has vast implications for understanding the mechanisms involved in the initiation and progression of NDs, as well as for the design of novel strategies for treatment and diagnosis. In this Review, we provide a critical discussion of the role of protein misfolding and aggregation in NDs. Commonalities and differences between distinct protein aggregates will be highlighted, in addition to evidence supporting the hypothesis that misfolded aggregates can be transmissible by the prion principle. We will also describe the molecular basis and implications for prion-like conformational strains, cross-interaction between different misfolded proteins in the brain, and how these concepts can be applied to the development of novel strategies for therapy and diagnosis.
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Once a seed is formed, aggregates attract monomers of the same protein and other proteins that may be preferentially bound and entrapped.
“Once a seed is formed, the aggregates attract monomers of the same protein, as well as other proteins which may be preferentially bound and entrapped (60).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [60]
Aggregation-prone proteins include amyloid-β in Alzheimer disease; phosphorylated tau in frontotemporal dementia, chronic traumatic encephalopathy, and Alzheimer's; α-synuclein in Parkinson's, Lewy body disease, and multisystem atrophies; mutant huntingtin in Huntington's disease; and TDP-43 in ALS and frontotemporal dementia.
“These aggregation-prone proteins include amyloid-ß in Alzheimer Disease; phosphorylated tau in frontotemporal dementia (FTD) and chronic traumatic encephalopathy, as well as in Alzheimer’s; α-synuclein in Parkinson’s, Lewy body disease, and the multisystem atrophies; mutant huntingtin in Huntington’s disease, and TDP-43 in ALS and FTD (60).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [60]
Although specific protein species differ across neurodegenerative disorders, in most cases their aggregates are formed in part by interactions of intermolecular β-sheet-rich strands.
“Although the specific protein species differ in the different neurodegenerative disorders, in most cases their protein aggregates are formed in part by the interactions of intermolecular β-sheet-rich strands.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [60]
Several studies have highlighted the critical role of oligomers as both directly toxic and as niduses for macromolecular aggregation.
“several studies have highlighted the critical role of oligomers as both directly toxic, and as niduses for macromolecular aggregation.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [60]
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- Authors
- Soto, C., & Pritzkow, S.
- Corresponding author
- Soto, Claudio
- Venue
- Nature Neuroscience
- Published
- 2018-09-24
- Volume
- 21
- Issue
- 10
- Pages
- 1332-1340
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC6432913
- OpenAlex
- W2890247534
- Cited by
- 1,180
- References
- 148
- Citations by year
- 2026: 140 · 2025: 174 · 2024: 160 · 2023: 171 · 2022: 173 · 2021: 166 · 2020: 123 · 2019: 70 · 2018: 1
- FWCI
- 8.83
- 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)
- Funders
- National Institute on Aging (R56AG061878, R42AG049562, R42AG058333)
- National Institute of Allergy and Infectious Diseases (R01AI132695, P01AI077774)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- protein misfolding, protein aggregation, neurodegenerative diseases, conformational strain, prion-like propagation, seeding, prion hypothesis, prion disease, disease transmission, neurodegeneration therapy, neurodegenerative disease diagnosis
- MeSH terms
- Animals, Humans, Protein Conformation, Protein Folding, Neurodegenerative Diseases, Protein Aggregation, Pathological
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