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

Determinants of the in Vivo Folding of the Prion Protein

1 Apr 2003

Abstract excerpt

Misfolding of the mammalian prion protein (PrP) is implicated in the pathogenesis of prion diseases. We analyzed wild type PrP in comparison with different PrP mutants and identified determinants of the in vivo folding pathway of PrP. The complete N terminus of PrP including the putative transmembrane domain and the first beta-strand could be deleted without interfering with PrP maturation. Helix 1, however,...

Read the complete abstract on PubMed

Topics

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

Share to Monoclonal and Polyclonal Antibodies Research
Share to Prion Diseases and Protein Misfolding
Share to RNA regulation and disease

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 12556465
DOI: 10.1074/jbc.m209942200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Determinants of the in Vivo Folding of the Prion ProteinPMID 12556465Read ↗

Loss of the first β-strand of human prion protein generates an aggregation-competent partially “open” formSemantic proximity Read ↗

Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor.Semantic proximity Read ↗

Functionally relevant domains of the prion protein identified in vivo.Semantic proximity Read ↗

Polar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Semantic proximity Read ↗

Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: a critical role for the putative transmembrane domain.Semantic proximity Read ↗

A structural overview of the vertebrate prion proteins.Semantic proximity Read ↗

A transmembrane form of the prion protein in neurodegenerative disease.Semantic proximity Read ↗

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathiesSemantic proximity Read ↗

[Prion protein structure and its relationships with pathogenesis].Semantic proximity Read ↗

Loss of glycosylation associated with the T183A mutation in human prion disease.Semantic proximity Read ↗

Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding.Semantic proximity Read ↗

Membrane topology influences N-glycosylation of the prion protein.Semantic proximity Read ↗

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