Prion strains and amyloid polymorphism influence phenotypic variation
[...]variation in amyloid-chaperone sites of interaction is likely a major determinant of the phenotypic differences caused by prion strains. [...]one conformation being uniquely thermodynamically stable above all other combinations seems unrealistic simply in terms of probability. [...]elucidatin...
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Veröffentlicht in: | PLoS pathogens 2014-09, Vol.10 (9), p.e1004328-e1004328 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: |
[...]variation in amyloid-chaperone sites of interaction is likely a major determinant of the phenotypic differences caused by prion strains. [...]one conformation being uniquely thermodynamically stable above all other combinations seems unrealistic simply in terms of probability. [...]elucidating the complex interplay of variables that affect the formation and maintenance of polymorphic structures remains a nontrivial, even crucial, task to gain a full understanding of pathological variability and the etiology of protein conformational disorders. |
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ISSN: | 1553-7374 1553-7366 1553-7374 |
DOI: | 10.1371/journal.ppat.1004328 |