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The shape of things to come: structural insights into how prion proteins encipher heritable information

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  • Glenn C. Telling

    (Colorado State University)

Abstract

The prion hypothesis embodies the radical concept that prion proteins contain the necessary information for infectious replication within their shape, thus obviating the requirement for genomic material. Two elegant papers by Hoyt et al. and Manka et al. describing high-resolution structures of infectious prions bring us closer to answering the long-standing question of how different prion conformations produce heritably distinct diseases.

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  • Glenn C. Telling, 2022. "The shape of things to come: structural insights into how prion proteins encipher heritable information," Nature Communications, Nature, vol. 13(1), pages 1-3, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31460-8
    DOI: 10.1038/s41467-022-31460-8
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    1. Forrest Hoyt & Heidi G. Standke & Efrosini Artikis & Cindi L. Schwartz & Bryan Hansen & Kunpeng Li & Andrew G. Hughson & Matteo Manca & Olivia R. Thomas & Gregory J. Raymond & Brent Race & Gerald S. B, 2022. "Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    2. Szymon W. Manka & Wenjuan Zhang & Adam Wenborn & Jemma Betts & Susan Joiner & Helen R. Saibil & John Collinge & Jonathan D. F. Wadsworth, 2022. "2.7 Å cryo-EM structure of ex vivo RML prion fibrils," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
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