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

Increasing prion propensity by hydrophobic insertion.

PloS one - 1 Jan 2014

Gonzalez Nelson Aaron C, Paul Kacy R, Petri Michelina, Flores Noe, Rogge Ryan A, Cascarina Sean M, Ross Eric D

Abstract excerpt

Prion formation involves the conversion of proteins from a soluble form into an infectious amyloid form. Most yeast prion proteins contain glutamine/asparagine-rich regions that are responsible for prion aggregation. Prion formation by these domains is driven primarily by amino acid composition, not primary sequence, yet there is a surprising disconnect between the amino acids thought to have the highest...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Asparagine
Share to Glutamine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Mutagenesis

Share to Prions

Share to Saccharomyces cerevisiae Proteins

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 24586661
DOI: 10.1371/journal.pone.0089286
PMCID: PMC3930707

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

Increasing prion propensity by hydrophobic insertion.PMID 24586661Read ↗

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

Generating new prions by targeted mutation or segment duplication.Semantic proximity Read ↗

Manipulating the aggregation activity of human prion-like proteins.Semantic proximity Read ↗

PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid coresSemantic proximity Read ↗

The mutational landscape of a prion-like domainSemantic proximity Read ↗

A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prionsSemantic proximity Read ↗

Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Semantic proximity Read ↗

Aggregation prone regions and gatekeeping residues in protein sequences.Semantic proximity Read ↗

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

The utility of prions.Semantic proximity Read ↗

Dissection and design of yeast prions.Semantic proximity Read ↗

Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.Semantic proximity Read ↗

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