Protein inheritance (prions) based on parallel in‐register β‐sheet amyloid structures
書誌事項
- 公開日
- 2008-09-17
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1002/bies.20821
- 公開者
- Wiley
この論文をさがす
説明
<jats:title>Abstract</jats:title><jats:p>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 [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>] of yeast are disease agents of <jats:italic>Saccharomyces cerevisiae</jats:italic> while [Het‐s] of <jats:italic>Podospora anserina</jats:italic> 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. © 2008 Wiley Periodicals, Inc.</jats:p>
収録刊行物
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- BioEssays
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BioEssays 30 (10), 955-964, 2008-09-17
Wiley