Journal
BIOESSAYS
Volume 30, Issue 10, Pages 955-964Publisher
WILEY
DOI: 10.1002/bies.20821
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Funding
- Intramural NIH HHS [ZIA DK024950-04] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK024949] Funding Source: NIH RePORTER
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Most prions (infectious proteins) are self-propagating amyloids (filamentous protein multimers), and have been found in both mammals and fungal species. The prions [URE3] and [PSI+] of yeast are disease agents of Saccharomyces cerevisiae while [Het-s] of Podospora anserina may serve a normal cellular function. The parallel in-register beta-sheet structure shown by prion amyloids makes possible a templating action at the end of filaments which explains the faithful transmission of variant differences in these molecules. This property of self-reproduction, in turn, allows these proteins to act as de facto genes, encoding heritable information. BioEssays 30:955-964, 2008. (C) 2008 Wiley Periodicals, Inc.
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