ArticleMolecular cell2010
The mechanism of prion inhibition by HET-S.
Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 95 citations in OpenAlex.
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Amyloids in bacterial antiphage defence.Nature microbiology · 2025Article
- Characterization of an amyloid-based antiphage defence system in Escherichia coli.Nature microbiology · 2025Article
- Expanding the Landscape of Amyloid Sequences with CARs-DB: A Database of Polar Amyloidogenic Peptides from Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- Emergence of the fungal immune system.iScience · 2023Review
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- In Silico Predictions of Ecological Plasticity Mediated by Protein Family Expansions in Early-Diverging Fungi.Journal of fungi (Basel, Switzerland) · 2022Article
- Molecular Mechanisms and Evolutionary Consequences of Spore Killers in Ascomycetes.Microbiology and molecular biology reviews : MMBR · 2021Review
- The expanding scope of amyloid signalling.Prion · 2021Article
- NOD-like receptor-mediated plant immunity: from structure to cell death.Nature reviews. Immunology · 2021Review
- Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Ribosomal RNA Modulates Aggregation of theInternational journal of molecular sciences · 2020Article
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- RPW8/HR repeats control NLR activation in Arabidopsis thaliana.PLoS genetics · 2019Article
- Targeting intrinsic cell death pathways to control fungal pathogens.Biochemical pharmacology · 2019Review
- Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly.Journal of molecular biology · 2018Review
- Necroptosis: MLKL Polymerization.Journal of nature and science · 2018Article
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
Abstract
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 of the globular domains of HET-s and HET-S are highly similar, comprising a helical fold, while NMR-based characterizations revealed no differences in the conformations of the PFDs. We conclude that prion inhibition is not encoded by structure but rather in stability and oligomerization properties: when HET-S forms a prion seed or is incorporated into a HET-s fibril via its PFD, the beta-structuring in this domain induces a change in its globular domain, generating a molecular species that is incompetent for fibril growth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.