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

Structural insights into a yeast prion illuminate nucleation and strain diversity.

Nature - 9 Jun 2005

Krishnan Rajaraman, Lindquist Susan L

Abstract excerpt

Self-perpetuating changes in the conformations of amyloidogenic proteins play vital roles in normal biology and disease. Despite intense research, the architecture and conformational conversion of amyloids remain poorly understood. Amyloid conformers of Sup35 are the molecular embodiment of the yeast prion known as [PSI], which produces heritable changes in phenotype through self-perpetuating changes in protein...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Cysteine
Share to Peptide Termination Factors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Prions

Share to Protein Folding

Share to Protein Structure, Quaternary

Share to Protein Subunits

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 15944694
DOI: 10.1038/nature03679
PMCID: PMC1405905

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural insights into a yeast prion illuminate nucleation and strain diversity.PMID 15944694Read ↗

Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.Semantic proximity Read ↗

Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].Semantic proximity Read ↗

How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypesSemantic proximity Read ↗

Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.Semantic proximity Read ↗

The physical basis of how prion conformations determine strain phenotypes.Semantic proximity Read ↗

W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme.Semantic proximity Read ↗

Exposed Hsp70-binding site impacts yeast Sup35 prion disaggregation and propagationSemantic proximity Read ↗

Emerging Principles of Conformation-Based Prion InheritanceSemantic proximity Read ↗

Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.Semantic proximity Read ↗

Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation.Semantic proximity Read ↗

Prions, protein homeostasis, and phenotypic diversity.Semantic proximity Read ↗

Fungal prions: structure, function and propagation.Semantic proximity Read ↗

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