Nucleated conformational conversion and the replication of conformational information by a prion determinant.

@article{Serio2000NucleatedCC,
  title={Nucleated conformational conversion and the replication of conformational information by a prion determinant.},
  author={Tricia R Serio and Anil Cashikar and Anthony S. Kowal and George Sawicki and Javid J. Moslehi and Louise C. Serpell and Morton F. Arnsdorf and Susan L. Lindquist},
  journal={Science},
  year={2000},
  volume={289 5483},
  pages={1317-21}
}
Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these… CONTINUE READING
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