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Prions as adaptive conduits of memory and inheritance
Abstract
Changes in protein conformation drive most biological processes, but none have seized the imagination of scientists and the public alike as have the self-replicating conformations of prions. Prions transmit lethal neurodegenerative diseases by means of the food chain. However, self-replicating protein conformations can also constitute molecular memories that transmit genetic information. Here, we showcase definitive evidence for the prion hypothesis and discuss examples in which prion-encoded heritable information has been harnessed during evolution to confer selective advantages. We then describe situations in which prion-enciphered events might have essential roles in long-term memory formation, transcriptional memory and genome-wide expression patterns.
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“Moreover, the templated modification of protein structure also subserves the transfer and storage of useful biological information in systems ranging from microbes to mammals107-110.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [107]
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Metadata
- Authors
- Shorter, J., & Lindquist, S.
- Affiliations
- Whitehead Institute for Biomedical Research (US)
- Corresponding author
- Shorter, James
- Lindquist, Susan
- ORCID
- Shorter, James
- Venue
- Nature Reviews Genetics
- Published
- 2005-06
- Volume
- 6
- Issue
- 6
- Pages
- 435-450
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- OpenAlex
- W2141566674
- Cited by
- 555
- References
- 160
- Citations by year
- 2026: 15 · 2025: 15 · 2024: 15 · 2023: 16 · 2022: 15 · 2021: 28 · 2020: 27 · 2019: 18 · 2018: 23 · 2017: 26 · 2016: 27 · 2015: 30 · 2014: 21 · 2013: 33 · 2012: 38
- FWCI
- 2.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Charles A. King Trust
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- prions, protein conformation, prion hypothesis, molecular memory, evolution, neurodegenerative diseases, long-term memory, transcriptional memory, gene expression patterns
- MeSH terms
- Amyloid, Animals, Biological Evolution, Humans, Memory, Peptide Termination Factors, Prions, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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