The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity
Abstract
The fundamental event in prion diseases seems to be a conformational change in cellular prion protein (PrP C ) whereby it is converted into the pathologic isoform PrP Sc . In fatal familial insomnia (FFI), the protease-resistant fragment of PrP Sc after deglycosylation has a size of 19 kilodaltons, whereas that from other inherited and sporadic prion diseases is 21 kilodaltons. Extracts from the brains of FFI patients transmitted disease to transgenic mice expressing a chimeric human-mouse PrP gene about 200 days after inoculation and induced formation of the 19-kilodalton PrP Sc fragment, whereas extracts from the brains of familial and sporadic Creutzfeldt-Jakob disease patients produced the 21-kilodalton PrP Sc fragment in these mice. The results presented indicate that the conformation of PrP Sc functions as a template in directing the formation of nascent PrP Sc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformation of PrP Sc .
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Linkage of the Indiana kindred of Gerstmann-Sträussler-Scheinker disease to the prion protein gene
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Cited by
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Self-citationSelf-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Prion Diseases of Humans and Animals: Their Causes and Molecular Basis
Collinge, J. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.519 · Cited by 1,344
Prion-like mechanisms in neurodegenerative diseases
Frost, B., & Diamond, M. I. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2786 · Cited by 776
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Metadata
- Authors
- Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J., Lugaresi, E., Gambetti, P., & Prusiner, S. B.
- Venue
- Science
- Published
- 1996-12-20
- Volume
- 274
- Issue
- 5295
- Pages
- 2079-2082
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2022614447
- Cited by
- 865
- References
- 2
- FWCI
- 13.98
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J., Lugaresi, E., Gambetti, P., & Prusiner, S. B. (1996). Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity. Science. https://doi.org/10.1126/science.274.5295.2079
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