The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Anchorless Prion Protein Results in Infectious Amyloid Disease Without Clinical Scrapie
Abstract
In prion and Alzheimer's diseases, the roles played by amyloid versus nonamyloid deposits in brain damage remain unresolved. In scrapie-infected transgenic mice expressing prion protein (PrP) lacking the glycosylphosphatidylinositol (GPI) membrane anchor, abnormal protease-resistant PrPres was deposited as amyloid plaques, rather than the usual nonamyloid form of PrPres. Although PrPres amyloid plaques induced brain damage reminiscent of Alzheimer's disease, clinical manifestations were minimal. In contrast, combined expression of anchorless and wild-type PrP produced accelerated clinical scrapie. Thus, the PrP GPI anchor may play a role in the pathogenesis of prion diseases.
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Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Self-citation
Cited by
Non–cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
Ilieva, H., Polymenidou, M., & Cleveland, D. W. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908164 · Cited by 1,008
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
The Glycosylphosphatidylinositol Anchor: A Complex Membrane-Anchoring Structure for Proteins
Paulick, M. G., & Bertozzi, C. R. (2008) · Biochemistry · doi:10.1021/bi8006324 · Cited by 600
The activities of amyloids from a structural perspective
Riek, R., & Eisenberg, D. S. (2016) · Nature · doi:10.1038/nature20416 · Cited by 508
Metadata
- Authors
- Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Favara, C., Baron, G., Priola, S., Caughey, B., Masliah, E., & Oldstone, M.
- Venue
- Science
- Published
- 2005-06-03
- Volume
- 308
- Issue
- 5727
- Pages
- 1435-1439
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2158707059
- Cited by
- 652
- References
- 1
- FWCI
- 17.17
- Type
- journal article
- Language
- en
- Open access
- closed
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- Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Favara, C., Baron, G., Priola, S., Caughey, B., Masliah, E., & Oldstone, M. (2005). Anchorless Prion Protein Results in Infectious Amyloid Disease Without Clinical Scrapie. Science. https://doi.org/10.1126/science.1110837
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
