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

Mutant prion proteins are partially retained in the endoplasmic reticulum.

The Journal of biological chemistry - 9 Nov 2001

Ivanova L, Barmada S, Kummer T, Harris D A

Abstract excerpt

Familial prion diseases are linked to point and insertional mutations in the prion protein (PrP) gene that are presumed to favor conversion of the cellular isoform of PrP to the infectious isoform. In this report, we have investigated the subcellular localization of PrP molecules carrying pathogenic mutations using immunofluorescence staining, immunogold labeling, and PrP-green fluorescent protein chimeras. To...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Cricetinae
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Antibody Technique

Share to Golgi Apparatus

Share to Prions

Share to Sindbis Virus

Share to Virus Replication

Source

Identifiers

PMID: 11527974
DOI: 10.1074/jbc.M106928200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutant prion proteins are partially retained in the endoplasmic reticulum.PMID 11527974Read ↗

GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice.Semantic proximity Read ↗

Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases.Semantic proximity Read ↗

Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein.Semantic proximity Read ↗

Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes.Semantic proximity Read ↗

Prion neurotoxicity: insights from prion protein mutants.Semantic proximity Read ↗

Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum: implications for prion propagation and neurotoxicity.Semantic proximity Read ↗

Transgenic mice recapitulate the phenotypic heterogeneity of genetic prion diseases without developing prion infectivity: Role of intracellular PrP retention in neurotoxicity.Semantic proximity Read ↗

Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation.Semantic proximity Read ↗

Misfolding leads the way to unraveling signaling pathways in the pathophysiology of prion diseases.Semantic proximity Read ↗

Selective processing and metabolism of disease-causing mutant prion proteins.Semantic proximity Read ↗

Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein.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 ↗

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