Prion amyloid structure explains templating: how proteins can be genes.

@article{Wickner2010PrionAS,
  title={Prion amyloid structure explains templating: how proteins can be genes.},
  author={Reed B Wickner and Frank Shewmaker and Herman K. Edskes and Dmitry S Kryndushkin and Julie Nemecek and Ryan P. McGlinchey and David J. Bateman and Chia-Lin Winchester},
  journal={FEMS yeast research},
  year={2010},
  volume={10 8},
  pages={
          980-91
        }
}
The yeast and fungal prions determine heritable and infectious traits, and are thus genes composed of protein. Most prions are inactive forms of a normal protein as it forms a self-propagating filamentous β-sheet-rich polymer structure called amyloid. Remarkably, a single prion protein sequence can form two or more faithfully inherited prion variants, in effect alleles of these genes. What protein structure explains this protein-based inheritance? Using solid-state nuclear magnetic resonance… CONTINUE READING

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Yeast and Fungal Prions.

  • Cold Spring Harbor perspectives in biology
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HIGHLY INFLUENTIAL