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Article

The mechanism of prion inhibition by HET-S.

Molecular cell - 25 Jun 2010

Greenwald Jason, Buhtz Carolin, Ritter Christiane, Kwiatkowski Witek, Choe Senyon, Maddelein Marie-Lise, Ness Frederique, Cescau Sandra, Soragni Alice, Leitz Dominik, Saupe Sven J, Riek Roland

Abstract excerpt

HET-S (97% identical to HET-s) has an N-terminal globular domain that exerts a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation. We show that HET-S fails to form fibrils in vitro and that it inhibits HET-s PFD fibrillization in trans. In vivo analyses indicate that beta-structuring of the HET-S PFD is required for HET-S activity. The crystal structures...

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Identifiers

PMID: 20620958
DOI: 10.1016/j.molcel.2010.05.019
PMCID: PMC3507513

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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