The DOI matches its Crossref record; 160 of the 160 references it cites were found in a registry or an index.
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]
Citations
Cites
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Research works printed but not linked: 3
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Jablonka, E., & Raz, G. (2009) · The Quarterly Review of Biology · doi:10.1086/598822 · Cited by 1,701
Epigenetics and the biological definition of gene×environment interactions
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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
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