The DOI matches its Crossref record; 154 of the 154 references it cites were found in a registry or an index.
The prion hypothesis: from biological anomaly to basic regulatory mechanism
Open accessAbstract
Prions are unusual proteinaceous infectious agents that are typically associated with a class of fatal degenerative diseases of the mammalian brain. However, the discovery of fungal prions, which are not associated with disease, suggests that we must now consider the effect of these factors on basic cellular physiology in a different light. Fungal prions are epigenetic determinants that can alter a range of cellular processes, including metabolism and gene expression pathways, and these changes can lead to a range of prion-associated phenotypes. The mechanistic similarities between prion propagation in mammals and fungi suggest that prions are not a biological anomaly but instead could be a newly appreciated and perhaps ubiquitous regulatory mechanism.
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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 [109]
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1 retracted
RETRACTED: A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen
Nemecek, J. C., Nakayashiki, T., & Wickner, R. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812470106 · Cited by 60
RetractedPrusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R. A., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,279
Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent
Bruce, M. E., Will, R. G., Ironside, J. W., McConnell, I., Drummond, D., Suttie, A., McCardle, L., Chree, A., Hope, J., Birkett, C. R., et al. (1997) · Nature · doi:10.1038/39057 · Cited by 1,963
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845
Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., & Hill, A. F. (1996) · Nature · doi:10.1038/383685a0 · Cited by 1,735
Barnhart, M. M., & Chapman, M. R. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142106 · Cited by 1,289
[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae
Wickner, R. B. (1994) · Science · doi:10.1126/science.7909170 · Cited by 1,216
Nature of the Scrapie Agent: Self-replication and Scrapie
Griffith, J. S. (1967) · Nature · doi:10.1038/2151043a0 · Cited by 1,188
Research works printed but not linked: 4
- Dickinson, A. G. & Outram, G. W. in Virus Nonconventionnels et Affections du Systeme Nerveux Central (eds Court, L. A. & Cathala, F.) 3–16 (Masson, Paris, 1983).
- Dickinson, A. G. & Outram, G. W. in Slow Transmissible Diseases of The Nervous System (eds Prusiner, S. B. & Hadlow, W. J.) 13–31 (Academic Press, New York, 1979).
- Goldfarb, L. et al. Patients wth Creutzfeldt-Jakob disease and kuru lack the mutation in the PRIP gene found in Gerstmann-Sträussler syndrome, but they show a different double-allele mutation in the same gene. Am. J. Hum. Genet. 45, A189 (1989).
- Pattison, I. in NINDB Monograph, No.2: Slow, Latent, and Temperate Virus Infections (eds Gajdusek D. C., Gibbs C. J. Jr & Alpers M. P.)249–257 (US National Institutes of Health, Bethesda, Maryland, 1965).
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Hall, G. F. (2014) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000e133 · Cited by 2
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Cann, A. J. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384939-7.10008-0
Farooq, M., Shah, M. D., Padder, B. A., Sofi, T. A., Masoodi, K. Z., Nabi, A., Hamid, S., & Ahmad, M. (2021) · Research Square · doi:10.21203/rs.3.rs-541535/v1
Pascual, M., & Roa, S. (2013) · SpringerBriefs in genetics · doi:10.1007/978-1-4614-6366-5_3
(2016) · Elsevier eBooks · doi:10.1016/b978-1-78548-216-8.50014-2
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Domingo, E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816331-3.00010-6
Weiss, S. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.12426956.14282057
Santiago, F., & Sindi, S. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010107
Howell-Bray, T., & Byrne, L. J. (2023) · Research Square · doi:10.21203/rs.3.rs-2511186/v1
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Lemarre, P. (2021) · theses.fr (ABES) · doi:10.70675/14ed1979z0e17z4c24z8327z72623f9320c4
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Metadata
- Authors
- Tuite, M. F., & Serio, T. R.
- Affiliations
- University of Kent (GB)
- Brown University (US)
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2010-11-17
- Volume
- 11
- Issue
- 12
- Pages
- 823-833
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC3003427
- OpenAlex
- W1982935057
- Cited by
- 146
- References
- 154
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 5 · 2021: 6 · 2020: 13 · 2019: 2 · 2018: 8 · 2017: 10 · 2016: 7 · 2015: 10 · 2014: 14 · 2013: 11 · 2012: 21
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Kent Academic Repository (University of Kent) (submittedVersion)
- Funders
- Wellcome Trust
- National Institutes of Health
- Biotechnology and Biological Sciences Research Council (BB/H012982/1)
- National Institute of General Medical Sciences (R01GM069802)
- 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 › Molecular Biology › Protein Structure and Dynamics
- Keywords
- prions, fungal prions, epigenetic regulation, prion propagation, neurodegenerative diseases, gene expression regulation
- MeSH terms
- Animals, Cell Physiological Phenomena, Fungi, Gene Expression Regulation, Humans, Models, Biological, Phenotype, Prions, Signal Transduction, Prion Diseases, Epigenesis, Genetic
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