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

Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein.

The Journal of biological chemistry - 13 Aug 1999

Zanusso G, Petersen R B, Jin T, Jing Y, Kanoush R, Ferrari S, Gambetti P, Singh N

Abstract excerpt

An amber mutation at codon 145 (Y145stop) of the prion protein gene results in a variant of an inherited human prion disease named Gerstmann-Sträussler-Scheinker syndrome. The characteristic features of this disorder include amyloid deposits of prion protein in cerebral parenchyma and vessels. We have studied the biosynthesis and processing of the prion protein containing the Y145stop mutation (PrP(145)) in...

Read the complete abstract on PubMed

Topics

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

Share to Cell Compartmentation
Share to Codon, Terminator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to Golgi Apparatus

Share to Hydrolysis

Share to Multienzyme Complexes

Share to Prions

Share to Proteasome Endopeptidase Complex

Source

Identifiers

PMID: 10438517
DOI: 10.1074/jbc.274.33.23396

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein.PMID 10438517Read ↗

Mutant prion protein acquires resistance to protease in mouse neuroblastoma cells.Semantic proximity Read ↗

Characterization of a Novel Prion Protein Mutation of Serine to Proline at Residue 245 Linked to VPSPr-like PK-Resistant PrPScSemantic 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 ↗

A novel PRNP-P105S mutation associated with atypical prion disease and a rare PrPSc conformation.Semantic proximity Read ↗

An amber mutation of prion protein in Gerstmann-Sträussler syndrome with mutant PrP plaques.Semantic proximity Read ↗

Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Semantic proximity Read ↗

Mutant prion protein D202N associated with familial prion disease is retained in the endoplasmic reticulum and forms 'curly' intracellular aggregates.Semantic proximity Read ↗

A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.Semantic proximity Read ↗

Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP.Semantic proximity Read ↗

Effect of the E200K mutation on prion protein metabolism. Comparative study of a cell model and human brain.Semantic proximity Read ↗

Involvement of puromycin-sensitive aminopeptidase in proteolysis of tau protein in cultured cells, and attenuated proteolysis of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) mutant tau.Semantic proximity Read ↗

Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop.Semantic proximity Read ↗

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