The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Separation and properties of cellular and scrapie prion proteins.
Open accessAbstract
Purified preparations of scrapie prions contain a sialoglycoprotein of Mr 27,000-30,000, designated PrP 27-30, which is derived from the scrapie prion protein [Mr, 33,000-35,000 (PrP 33-35Sc)] by limited proteolysis. Under these same conditions of proteolysis, a cellular protein of the same size (PrP 33-35C) is completely degraded. Subcellular fractionation of hamster brain showed that both PrP 33-35Sc and PrP 33-35C were found only in membrane fractions. NaCl, EDTA, and osmotic shock failed to release the prion proteins from microsomal membranes. Electron microscopy of these microsomal fractions showed membrane vesicles but not prion amyloid rods. Detergent treatment of scrapie-infected membranes solubilized PrP 33-35C, while PrP 33-35Sc aggregated into amyloid rods; the concentration of PrP 33-35C was similar to that recovered from analogous fractions prepared from uninfected control brains. The apparent amphipathic character of the PrP 33-35Sc may explain the association of scrapie infectivity with both membranes and amyloid filaments.
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Cites
INGRAM, V. M. (1957) · Nature · doi:10.1038/180326a0 · Cited by 978
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-citationScrapie and cellular PrP isoforms are encoded by the same chromosomal gene
Basler, K., Oesch, B., Scott, M., Westaway, D., Wälchli, M., Groth, D. F., McKinley, M. P., Prusiner, S. B., & Weissmann, C. (1986) · Cell · doi:10.1016/0092-8674(86)90662-8 · Cited by 835
Self-citationPredicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.
Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J. M., Holtzman, D. M., Cohen, F., Fletterick, R., & Prusiner, S. B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10940 · Cited by 329
Self-citationPrusiner, S. B., & Hsiao, K. K. (1994) · Annals of Neurology · doi:10.1002/ana.410350404 · Cited by 328
Self-citationRole of microglia in neuronal cell death in prion disease
Giese, A., Brown, D. R., Groschup, M. H., Feldmann, C., Haist, I., & Kretzschmar, H. A. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00167.x · Cited by 239
Metadata
- Authors
- Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A., & Prusiner, S. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1986-04
- Volume
- 83
- Issue
- 8
- Pages
- 2310-2314
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2029440340
- Cited by
- 623
- References
- 1
- FWCI
- 6.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A., & Prusiner, S. B. (1986). Separation and properties of cellular and scrapie prion proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.8.2310
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