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 structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.

Cellular and molecular life sciences : CMLS - 1 Aug 2010

Lisa Silvia, Meli Massimiliano, Cabello Gema, Gabizon Ruth, Colombo Giorgio, Gasset María

Abstract excerpt

The conversion of the cellular prion protein (PrP(C)) into its disease-associated form (PrP(Sc)) involves a major conformational change and the accumulation of sulfoxidized methionines. Computational and synthetic approaches have shown that this change in the polarity of M206 and M213 impacts the C-terminal domain native alpha-fold allowing the flexibility required for the structural conversion. To test the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Homoserine

Share to Methionine

Share to Prion Diseases

Share to Prions

Share to Protein Conformation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 20454997
DOI: 10.1007/s00018-010-0363-1
PMCID: PMC11115822

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 structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.PMID 20454997Read ↗

Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion.Semantic proximity Read ↗

Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.Semantic proximity Read ↗

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

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

Structural determinants in prion protein folding and stability.Semantic proximity Read ↗

Mechanism of misfolding of the human prion protein revealed by a pathological mutation.Semantic proximity Read ↗

The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc.Semantic proximity Read ↗

Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations.Semantic proximity Read ↗

Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.Semantic proximity Read ↗

Exploring structural and thermodynamic stabilities of human prion protein pathogenic mutants D202N, E211Q and Q217R.Semantic proximity Read ↗

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

Different misfolding mechanisms converge on common conformational changes: human prion protein pathogenic mutants Y218N and E196K.Semantic proximity Read ↗

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