The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.
Open accessAbstract
By comparing the amino acid sequences of 11 mammalian and 1 avian prion proteins (PrP), structural analyses predicted four alpha-helical regions. Peptides corresponding to these regions of Syrian hamster PrP were synthesized, and, contrary to predictions, three of the four spontaneously formed amyloids as shown by electron microscopy and Congo red staining. By IR spectroscopy, these amyloid peptides exhibited secondary structures composed largely of beta-sheets. The first of the predicted helices is the 14-amino acid peptide corresponding to residues 109-122; this peptide and the overlapping 15-residue sequence 113-127 both form amyloid. The most highly amyloidogenic peptide is AGAAAAGA, which corresponds to Syrian hamster PrP residues 113-120 and is conserved across all species for which the PrP sequence has been determined. Two other predicted alpha-helices corresponding to residues 178-191 and 202-218 form amyloids and exhibit considerable beta-sheet structure when synthesized as peptides. These findings suggest the possibility that the conversion of the cellular isoform of PrP to the scrapie isoform of PrP involves the transition of one or more putative PrP alpha-helices into beta-sheets and that prion diseases are disorders of protein conformation.
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Cites
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
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Molecular Biology of Prion Diseases
Prusiner, S. B. (1991) · Science · doi:10.1126/science.1675487 · Cited by 1,988
Self-citationA cellular gene encodes scrapie PrP 27-30 protein
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Self-citationScrapie prions aggregate to form amyloid-like birefringent rods
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Self-citationCaughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., & Caughey, W. S. (1991) · Biochemistry · doi:10.1021/bi00245a003 · Cited by 822
Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
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Separation and properties of cellular and scrapie prion proteins.
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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-citationPhysiology 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
PATHOLOGIC CONFORMATIONS OF PRION PROTEINS
Cohen, F. E., & Prusiner, S. B. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.793 · Cited by 533
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Self-citationProlines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4
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Metadata
- Authors
- Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J. M., Holtzman, D. M., Cohen, F., Fletterick, R., & Prusiner, S. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-11-15
- Volume
- 89
- Issue
- 22
- Pages
- 10940-10944
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2028469737
- Cited by
- 329
- References
- 39
- FWCI
- 8.02
- Type
- journal article
- Language
- en
- Open access
- green
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- Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J. M., Holtzman, D. M., Cohen, F., Fletterick, R., & Prusiner, S. B. (1992). Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.22.10940
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