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

A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons.

The Journal of biological chemistry - 22 Apr 2005

Stewart Richard S, Harris David A

Abstract excerpt

(Ctm)PrP is a transmembrane version of the prion protein that has been proposed to be a neurotoxic intermediate underlying prion-induced pathogenesis. In previous studies, we found that PrP molecules carrying mutations in the N-terminal signal peptide (L9R) and the transmembrane domain (3AV) were synthesized exclusively in the (Ctm)PrP form in transfected cell lines. To characterize the properties of (Ctm)PrP in...

Read the complete abstract on PubMed

Topics

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

Share to Epitopes
Share to Golgi Apparatus
Share to Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mice, Transgenic

Share to Mutation

Share to Neurons

Share to Prions

Share to Sequence Analysis, Protein

Source

Identifiers

PMID: 15671025
DOI: 10.1074/jbc.M412298200

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

A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons.PMID 15671025Read ↗

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

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

Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α(2)δ-1 Subunit.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 ↗

(Ctm)PrP and ER stress: a neurotoxic mechanism of some special PrP mutants.Semantic proximity Read ↗

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

A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicity.Semantic proximity Read ↗

The C-terminal globular domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum.Semantic proximity Read ↗

Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.Semantic proximity Read ↗

Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain.Semantic proximity Read ↗

Mutant prion proteins are partially retained in the endoplasmic reticulum.Semantic proximity Read ↗

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