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

The role of conformational flexibility in prion propagation and maintenance for Sup35p.

Nature structural biology - 1 Nov 2001

Scheibel T, Lindquist S L

Abstract excerpt

The [PSI(+)] factor of Saccharomyces cerevisiae is a protein-based genetic element (prion) comprised of a heritable altered conformation of the cytosolic translation termination factor Sup35p. In vitro, the prion-determining region (NM) of Sup35p undergoes conformational conversion from a highly flexible soluble state to structured amyloid fibers, with a rate that is greatly accelerated by preformed NM fiber...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis
Share to Oligopeptides
Share to Osmolar Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptide Termination Factors

Share to Pliability

Share to Protein Denaturation

Share to Repetitive Sequences, Amino Acid

Share to Solubility

Source

Identifiers

PMID: 11685242
DOI: 10.1038/nsb1101-958

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of conformational flexibility in prion propagation and maintenance for Sup35p.PMID 11685242Read ↗

Structural insights into a yeast prion illuminate nucleation and strain diversity.Semantic proximity Read ↗

Structural definition is important for the propagation of the yeast [PSI+] prion.Semantic proximity Read ↗

Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotypeSemantic proximity Read ↗

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

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

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

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.Semantic proximity Read ↗

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

Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein.Semantic proximity Read ↗

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.Semantic proximity Read ↗

Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Semantic proximity Read ↗

Conformation preserved in a weak-to-strong or strong-to-weak [PSI+] conversion during transmission to Sup35 prion variants.Semantic proximity Read ↗

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