The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease
Abstract
The incidence of Alzheimer's disease (AD) and that of prion disorders (PrD) could not be more different. One-third of octogenarians succumb to AD, whereas Creutzfeldt-Jakob disease typically affects one individual in a million each year. However, these diseases have many common features impinging on the metabolism of neuronal membrane proteins: the amyloid precursor protein APP in the case of AD, and the cellular prion protein PrP C in PrD. APP begets the Aβ peptide, whereas PrP C begets the malignant prion protein PrP Sc . Both Aβ and PrP Sc are associated with disease, but we do not know what triggers their accumulation and neurotoxicity. A great deal has been learned, however, about protein folding, misfolding, and aggregation; an entirely new class of intramembrane proteases has been identified; and unsuspected roles for the immune system have been uncovered. There is reason to expect that prion research will profit from advances in the understanding of AD, and vice versa.
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Cites
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Aph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex
De Strooper, B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00205-8 · Cited by 965
Cited by
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,440
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
Conformational variations in an infectious protein determine prion strain differences
Tanaka, M., Chien, P., Naber, N., Cooke, R., & Weissman, J. S. (2004) · Nature · doi:10.1038/nature02392 · Cited by 770
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Meisl, G., Kirkegaard, J. B., Arosio, P., Michaels, T. C. T., Vendruscolo, M., Dobson, C. M., Linse, S., & Knowles, T. P. J. (2016) · Nature Protocols · doi:10.1038/nprot.2016.010 · Cited by 767
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
Metadata
- Authors
- Aguzzi, A., & Haass, C.
- Venue
- Science
- Published
- 2003-10-31
- Volume
- 302
- Issue
- 5646
- Pages
- 814-818
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1967800794
- Cited by
- 225
- References
- 3
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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