The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Genetic influence on the structural variations of the abnormal prion protein
Open accessAbstract
Prion diseases are characterized by the presence of the abnormal prion protein PrP Sc , which is believed to be generated by the conversion of the α-helical structure that predominates in the normal PrP isoform into a β-sheet structure resistant to proteinase K (PK). In human prion diseases, two major types of PrP Sc , type 1 and 2, can be distinguished based on the difference in electrophoretic migration of the PK-resistant core fragment. In this study, protein sequencing was used to identify the PK cleavage sites of PrP Sc in 36 cases of prion diseases. We demonstrated two primary cleavage sites at residue 82 and residue 97 for type 1 and type 2 PrP Sc , respectively, and numerous secondary cleavages distributed along the region spanning residues 74–102. Accordingly, we identify three regions in PrP Sc : one N-terminal (residues 23–73) that is invariably PK-sensitive, one C-terminal (residues 103–231) that is invariably PK-resistant, and a third variable region (residues 74–102) where the site of the PK cleavage, likely reflecting the extent of the β-sheet structure, varies mostly as a function of the PrP genotype at codon 129.
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Cites
Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., & Hill, A. F. (1996) · Nature · doi:10.1038/383685a0 · Cited by 1,735
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Cited by
Ma, J., & Lindquist, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011578098 · Cited by 294
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Belay, E. D., Maddox, R. A., Williams, E. S., Miller, M. W., Gambetti, P., & Schonberger, L. B. (2004) · Emerging Infectious Diseases · doi:10.3201/eid1006.031082 · Cited by 257
Self-citationPhenotypic variability in human prion diseases
Ironside, J. W., Ritchie, D. L., & Head, M. W. (2005) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2005.00697.x · Cited by 58
Self-citationDistinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease
Kim, C., Haldiman, T., Kang, S.-G., Hromadkova, L., Han, Z. Z., Chen, W., Lissemore, F., Lerner, A., de Silva, R., Cohen, M. L., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg0253 · Cited by 55
Metadata
- Authors
- Parchi, P., Zou, W., Wang, W., Brown, P., Capellari, S., Ghetti, B., Kopp, N., Schulz-Schaeffer, W. J., Kretzschmar, H. A., Head, M. W., Ironside, J. W., Gambetti, P., & Chen, S. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-08-29
- Volume
- 97
- Issue
- 18
- Pages
- 10168-10172
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2089569305
- Cited by
- 330
- References
- 1
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- green
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- Parchi, P., Zou, W., Wang, W., Brown, P., Capellari, S., Ghetti, B., Kopp, N., Schulz-Schaeffer, W. J., Kretzschmar, H. A., Head, M. W., Ironside, J. W., Gambetti, P., & Chen, S. G. (2000). Genetic influence on the structural variations of the abnormal prion protein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.18.10168
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