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

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms.

Biological chemistry - 1 May 2003

Hundt Christoph, Gauczynski Sabine, Leucht Christoph, Riley M Louise, Weiss Stefan

Abstract excerpt

Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogeneous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric. The PrP/PrP interaction was confirmed in Semliki Forest virus-RNA transfected BHK cells co-expressing FLAG- and oligohistidine-tagged human PrP. The yeast two-hybrid system...

Read the complete abstract on PubMed

Topics

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

Share to Animals, Genetically Modified
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to PrPC Proteins

Share to Recombinant Fusion Proteins

Share to Saccharomyces cerevisiae Proteins

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 12817476
DOI: 10.1515/BC.2003.088

Genes

GSS

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

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms.PMID 12817476Read ↗

Recombinant human prion protein mutants huPrP D178N/M129 (FFI) and huPrP+9OR (fCJD) reveal proteinase K resistance.Semantic proximity Read ↗

The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrPScSemantic proximity Read ↗

Natural and Pathogenic Protein Sequence Variation Affecting Prion-Like Domains Within and Across Human ProteomesSemantic proximity Read ↗

Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion.Semantic proximity Read ↗

Aggregation of cellular prion protein is initiated by proximity-induced dimerization.Semantic proximity Read ↗

Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein.Semantic proximity Read ↗

Prion protein gene variation among primates.Semantic proximity Read ↗

Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans.Semantic proximity Read ↗

Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.Semantic proximity Read ↗

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.Semantic proximity Read ↗

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

Genetic predictions of prion disease susceptibility in carnivore species based on variability of the prion gene coding region.Semantic proximity Read ↗

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