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 unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier.

Biochemistry - 15 Sept 2009

Robinson Philip J, Pinheiro Teresa J T

Abstract excerpt

Prion diseases are a group of fatal neurodegenerative disorders that manifest as infectious, sporadic, or familial and are all associated with the misfolding of the prion protein (PrP). Disease-modulating polymorphisms in the PrP amino acid sequence can make an individual more or less susceptible...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Glutamine
Share to Prion Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prion Proteins

Share to Prions

Share to Protein Denaturation

Share to Thermodynamics

Share to Tryptophan

Source

Identifiers

PMID: 19655812
DOI: 10.1021/bi901070t

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19655812-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier.PMID 19655812Read ↗

Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.Semantic proximity Read ↗

Prion proteins with pathogenic and protective mutations show similar structure and dynamics.Semantic proximity Read ↗

The roles of the conserved tyrosine in the β2-α2 loop of the prion protein.Semantic proximity Read ↗

Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.Semantic proximity Read ↗

The elusive intermediate on the folding pathway of the prion protein.Semantic proximity Read ↗

Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes.Semantic proximity Read ↗

Conformational polymorphism of wild-type and mutant prion proteins: Energy landscape analysis.Semantic proximity Read ↗

N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.Semantic proximity Read ↗

Pathological mutations H187R and E196K facilitate subdomain separation and prion protein conversion by destabilization of the native structure.Semantic proximity Read ↗

Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich Dimer.Semantic proximity Read ↗

Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple ways.Semantic proximity Read ↗

A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Semantic proximity Read ↗

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