Biology and Genetics of Prions Causing Neurodegeneration
Open accessAbstract
Prions are proteins that acquire alternative conformations that become self-propagating. Transformation of proteins into prions is generally accompanied by an increase in β-sheet structure and a propensity to aggregate into oligomers. Some prions are beneficial and perform cellular functions, whereas others cause neurodegeneration. In mammals, more than a dozen proteins that become prions have been identified, and a similar number has been found in fungi. In both mammals and fungi, variations in the prion conformation encipher the biological properties of distinct prion strains. Increasing evidence argues that prions cause many neurodegenerative diseases (NDs), including Alzheimer's, Parkinson's, Creutzfeldt-Jakob, and Lou Gehrig's diseases, as well as the tauopathies. The majority of NDs are sporadic, and 10% to 20% are inherited. The late onset of heritable NDs, like their sporadic counterparts, may reflect the stochastic nature of prion formation; the pathogenesis of such illnesses seems to require prion accumulation to exceed some critical threshold before neurological dysfunction manifests.
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The general concept of spreading proteinopathy from one cell to another locally arises from the biology of prions and prion diseases.
“The general concept of this kind of spreading proteinopathy from one cell to another, locally, arise from the biology of prions and prion diseases.60”
From Asynchronous, contagious and digital aging (2021) · cites this paper as [60]
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Genome-wide transcriptomics identifies an early preclinical signature of prion infection
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Role of mitochondrial raft-like microdomains in the regulation of cell apoptosis
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Sporadic and Infectious Human Prion DiseasesPreprint
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Aggregation of MBP in chronic demyelination
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- Authors
- Prusiner, S. B.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Prusiner, Stanley B.
- ORCID
- Prusiner, Stanley B.
- Venue
- Annual Review of Genetics
- Publisher
- Annual Reviews
- Published
- 2013-11-23
- Volume
- 47
- Issue
- 1
- Pages
- 601-623
- ISSN
- 0066-4197 (ISSN-L)
- 1545-2948
- PMC
- PMC4010318
- OpenAlex
- W2150555206
- Cited by
- 455
- References
- 207
- Citations by year
- 2026: 12 · 2025: 18 · 2024: 30 · 2023: 22 · 2022: 27 · 2021: 27 · 2020: 36 · 2019: 45 · 2018: 47 · 2017: 55 · 2016: 61 · 2015: 45 · 2014: 28
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Genetics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG010770, P01AG002132, P01AG021601, P01AG010770, AG002132, AG 021601, AG031220, R37AG031220)
- 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
- prions, prion strains, protein conformation, protein aggregation, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, tauopathy, hereditary neurodegeneration, prion pathogenesis, fungi
- MeSH terms
- Animals, Inclusion Bodies, Fungal Proteins, Humans, Mammals, Models, Molecular, Peptide Termination Factors, Prions, Protein Conformation, Transcription Factors, Virulence, Neurofibrillary Tangles, tau Proteins, Prion Diseases, Age of Onset, Neurodegenerative Diseases, Tauopathies, Saccharomyces cerevisiae Proteins, mRNA Cleavage and Polyadenylation Factors, Synucleins, Plaque, Amyloid, Amyloidogenic Proteins
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