Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserina

1 May 2003

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer's disease research and treatments
Share to Prion Diseases and Protein Misfolding
Share to Trace Elements in Health

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 12727874
DOI: 10.1093/emboj/cdg213

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserinaPMID 12727874Read ↗

The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility.Semantic proximity Read ↗

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.Semantic proximity Read ↗

Correlation of structural elements and infectivity of the HET-s prion.Semantic proximity Read ↗

Prions as Protein-Based Genetic ElementsSemantic proximity Read ↗

Prions: infectious proteins with genetic properties.Semantic proximity Read ↗

Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal GenomesSemantic proximity Read ↗

Structural biology of prions.Semantic proximity Read ↗

Structural biology of prions.Semantic proximity Read ↗

Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Semantic proximity Read ↗

Prions of yeast are genes made of protein: amyloids and enzymes.Semantic proximity Read ↗

Theme and variations: evolutionary diversification of the HET-s functional amyloid motifSemantic proximity Read ↗

Yeast prions and their prion-forming domain.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.