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 physical dimensions of amyloid aggregates control their infective potential as prion particles.

eLife - 7 Sept 2017

Marchante Ricardo, Beal David M, Koloteva-Levine Nadejda, Purton Tracey J, Tuite Mick F, Xue Wei-Feng

Abstract excerpt

Transmissible amyloid particles called prions are associated with infectious prion diseases in mammals and inherited phenotypes in yeast. All amyloid aggregates can give rise to potentially infectious seeds that accelerate their growth. Why some amyloid seeds are highly infectious prion particles while others are less infectious or even inert, is currently not understood. To address this question, we analyzed the...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Amyloidosis
Share to Peptide Termination Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phenotype

Share to Prions

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 28880146
DOI: 10.7554/eLife.27109
PMCID: PMC5589414

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The physical dimensions of amyloid aggregates control their infective potential as prion particles.PMID 28880146Read ↗

Dissection and design of yeast prions.Semantic proximity Read ↗

Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Semantic proximity Read ↗

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

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

A size threshold limits prion transmission and establishes phenotypic diversity.Semantic proximity Read ↗

Conserved features of intermediates in amyloid assembly determine their benign or toxic statesSemantic proximity Read ↗

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

Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.Semantic proximity Read ↗

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

The utility of prions.Semantic proximity Read ↗

Development of a Novel Yeast Cell-Based System for Studying the Aggregation of Alzheimer’s Disease-Associated Aβ Peptides in vivoSemantic proximity Read ↗

Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Semantic proximity Read ↗

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