Affiliation:
1. Department of Neurology (address for correspondence) and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.
Abstract
Bovine spongiform encephalopathy (BSE) and human Creutzfeldt-Jakob disease (CJD) are among the most notable central nervous system degenerative disorders caused by prions. CJD may present as a sporadic, genetic, or infectious illness. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrP
Sc
). The normal, cellular prion protein (PrP
C
) is converted into PrP
Sc
through a posttranslational process during which it acquires a high β-sheet content. It is thought that BSE is a result of cannibalism in which faulty industrial practices produced prion-contaminated feed for cattle. There is now considerable concern that bovine prions may have been passed to humans, resulting in a new form of CJD.
Publisher
American Association for the Advancement of Science (AAAS)
Reference177 articles.
1. Prions are defined as proteinaceous infectious particles that lack nucleic acid. PrP C is the cellular prion protein; PrP Sc is the pathologic isoform. Amino-terminal truncation during limited proteolysis of PrP Sc produces PrP 27–30 (so named because this protease-resistant core of PrP Sc migrates at ∼27 to 30 kD).
2. Molecular Biology of Prion Diseases
3. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
4. Meyer R. K., et al., ibid. 83, 2310 (1986).
5. Oesch B., et al., Cell 40, 735 (1985).
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