| Prions and their partners in crime. | |
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MedLine Citation:
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PMID: 17051207 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), have defied full characterization for decades. The dogma has been that prions lack nucleic acids and are composed of a pathological, self-inducing form of the host's prion protein (PrP). Recent progress in propagating TSE infectivity in cell-free systems has effectively ruled out the involvement of foreign nucleic acids. However, host-derived nucleic acids or other non-PrP molecules seem to be crucial. Interactions between TSE-associated PrP and its normal counterpart are also pathologically important, so the physiological functions of normal PrP and how they might be corrupted by TSE infections have been the subject of recent research. |
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Authors:
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Byron Caughey; Gerald S Baron |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Intramural; Review |
Journal Detail:
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Title: Nature Volume: 443 ISSN: 1476-4687 ISO Abbreviation: Nature Publication Date: 2006 Oct |
Date Detail:
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Created Date: 2006-10-19 Completed Date: 2006-11-27 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0410462 Medline TA: Nature Country: England |
Other Details:
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Languages: eng Pagination: 803-10 Citation Subset: IM |
Affiliation:
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National Institute of Allergy and Infectious Disease, National Institutes of Health, Rocky Mountain Laboratories, 903 South 4th Street, Hamilton, Montana 59840, USA. bcaughey@nih.gov |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Copper / metabolism, pharmacology Glycosylphosphatidylinositols / metabolism Humans Ligands Prion Diseases / genetics, metabolism*, pathology, physiopathology* Prions / chemistry, metabolism*, toxicity |
| Chemical | |
Reg. No./Substance:
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0/Glycosylphosphatidylinositols; 0/Ligands; 0/Prions; 7440-50-8/Copper |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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