The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
Open accessAbstract
The transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases characterized by amyloid formation in the brain. The major amyloid protein is the prion protein (PrP). PrP and the beta-amyloid protein of Alzheimer disease share a similar sequence that, in both cases, may be responsible for the initiation of protein aggregation in vivo. We report here that a peptide based on this sequence in PrP (PrP96-111M) forms amyloid fibrils. The existence of a kinetic barrier to amyloid formation by this peptide was demonstrated, suggesting that formation of an ordered nucleus is the rate-determining step for aggregation. Seeding was demonstrated to occur with PrP96-111M amyloid fibrils but not with amyloid fibrils of a related peptide. This effect is consistent with the proposal that the aggregation of PrP, which characterizes TSE, involves a nucleation event analogous to the seeding of a crystallization.
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Cites
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
Some Speculations about Prions, Amyloid, and Alzheimer's Disease
Prusiner, S. B. (1984) · New England Journal of Medicine · doi:10.1056/nejm198403083101021 · Cited by 213
Cited by
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Self-citationConway, K. A., Lee, S.-J., Rochet, J.-C., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,541
Self-citationChi, E. Y., Krishnan, S., Randolph, T. W., & Carpenter, J. F. (2003) · Pharmaceutical Research · doi:10.1023/a:1025771421906 · Cited by 1,379
Advanced glycation end products contribute to amyloidosis in Alzheimer disease
Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K., & Cerami, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4766 · Cited by 806
Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537
Metadata
- Authors
- Come, J. H., Fraser, P. E., & Lansbury, P. T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-07
- Volume
- 90
- Issue
- 13
- Pages
- 5959-5963
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2094337931
- Cited by
- 394
- References
- 2
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- green
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- Come, J. H., Fraser, P. E., & Lansbury, P. T. (1993). A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.13.5959
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