Prion-like mechanisms in neurodegenerative diseases
Open accessAbstract
Many non-infectious neurodegenerative diseases are associated with the accumulation of fibrillar proteins. These diseases all exhibit features that are reminiscent of those of prionopathies, including phenotypic diversity and the propagation of pathology. Furthermore, emerging studies of amyloid-beta, alpha-synuclein and tau--proteins implicated in common neurodegenerative diseases--suggest that they share key biophysical and biochemical characteristics with prions. Propagation of protein misfolding in these diseases may therefore occur through mechanisms similar to those that underlie prion pathogenesis. If this hypothesis is verified in vivo, it will suggest new therapeutic strategies to block propagation of protein misfolding throughout the brain.
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AD and other non-infectious neurodegenerative disorders associated with aggregation of fibrillar proteins exhibit features similar to prion disease.
“Studies propose that AD and other non-infectious neurodegenerative disorders associated with aggregation of fibrillar proteins exhibit features similar to prion disease [55].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [55]
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References 63 · Cited by 776
Research works printed but not linked: 2
- [8]Askanas V Engel WK Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition Neurology 66 S39 48 2006 16432144
- [13]Ibanez P Causal relation between alpha-synuclein gene duplication and familial Parkinson’s disease Lancet 364 1169 71 2004 15451225
- Authors
- Frost, B., & Diamond, M. I.
- Affiliations
- Harvard University (US)
- Washington University in St. Louis (US)
- Corresponding author
- Diamond, Marc I.
- Venue
- Nature Reviews Neuroscience
- Published
- 2009-12-23
- Volume
- 11
- Issue
- 3
- Pages
- 155-159
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- PMC
- PMC3648341
- OpenAlex
- W2011637489
- Cited by
- 776
- References
- 63
- Citations by year
- 2026: 26 · 2025: 46 · 2024: 29 · 2023: 42 · 2022: 54 · 2021: 36 · 2020: 43 · 2019: 60 · 2018: 43 · 2017: 48 · 2016: 52 · 2015: 48 · 2014: 59 · 2013: 62 · 2012: 64
- FWCI
- 3.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Center for Research Resources (UL1RR024992)
- 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 › Amyotrophic Lateral Sclerosis Research
- Keywords
- prion-like mechanisms, neurodegenerative diseases, prionopathies, protein misfolding, amyloid-beta, alpha-synuclein, tau protein, pathogenesis, treatment options
- MeSH terms
- Brain, Humans, Prions, Protein Conformation, Amyloid beta-Peptides, tau Proteins, Disease Progression, Neurodegenerative Diseases, alpha-Synuclein
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