NDLI: Prions. (Journal: Proceedings of the National Academy of Sciences of the United States of America Volume: 95 Issue: 23)

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Prions. (Journal: Proceedings of the National Academy of Sciences of the United States of America Volume: 95 Issue: 23)

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Prions. (Journal: Proceedings of the National Academy of Sciences of the United States of America Volume: 95 Issue: 23)

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Prusiner, S. B.
Description	Author Affiliation: Prusiner SB ( Departments of Neurology and of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.);
Abstract	Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP). Bovine spongiform encephalopathy (BSE), scrapie of sheep, and Creutzfeldt-Jakob disease (CJD) of humans are among the most notable prion diseases. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular PrP (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta-sheet content. The species of a particular prion is encoded by the sequence of the chromosomal PrP gene of the mammals in which it last replicated. In contrast to pathogens carrying a nucleic acid genome, prions appear to encipher strain-specific properties in the tertiary structure of PrPSc. Transgenetic studies argue that PrPSc acts as a template upon which PrPC is refolded into a nascent PrPSc molecule through a process facilitated by another protein. Miniprions generated in transgenic mice expressing PrP, in which nearly half of the residues were deleted, exhibit unique biological properties and should facilitate structural studies of PrPSc. While knowledge about prions has profound implications for studies of the structural plasticity of proteins, investigations of prion diseases suggest that new strategies for the prevention and treatment of these disorders may also find application in the more common degenerative diseases.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Prion Diseases Prions Physiology Animals Genome, Viral Mice Mutation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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