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

Disease-Associated Q159X Mutant Prion Protein Is Sufficient to Cause Fatal Degenerative Disease in Mice.

Molecular neurobiology - 1 Dec 2024

Zhang Yan, Yan Runchuan, Zhang Xiangyi, Ma Jiyan

Abstract excerpt

PRNP Q160X is one of the five dominantly inheritable nonsense mutations causing familial prion diseases. Till now, it remains unclear how this type of nonsense mutations causes familial prion diseases with unique clinical and pathological characteristics. Human prion protein (PrP) Q160X mutation is equivalent to Q159X in mouse PrP, which produces the mutant fragment PrP1-158. Through intracerebroventricular...

Read the complete abstract on PubMed

Topics

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

Share to Animals, Newborn
Share to Brain
Share to Gliosis

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

Share to Mice, Inbred C57BL

Share to Mutant Proteins

Share to Prion Diseases

Share to Prion Proteins

Share to Prions

Source

Identifiers

PMID: 38743210
DOI: 10.1007/s12035-024-04224-2

Genes

PRNP

Variants

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disease-Associated Q159X Mutant Prion Protein Is Sufficient to Cause Fatal Degenerative Disease in Mice.PMID 38743210Read ↗

New Drosophila models to uncover the intrinsic and extrinsic factors mediating the toxicity of the human prion proteinSemantic proximity Read ↗

Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration.Semantic proximity Read ↗

Prion protein with Y145STOP mutation induces mitochondria-mediated apoptosis and PrP-containing deposits in vitro.Semantic proximity Read ↗

Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategySemantic proximity Read ↗

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease model.Semantic proximity Read ↗

The N-terminal, polybasic region is critical for prion protein neuroprotective activity.Semantic proximity Read ↗

Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Semantic proximity Read ↗

A naturally occurring variant of the human prion protein completely prevents prion disease.Semantic proximity Read ↗

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

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

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease modelSemantic proximity Read ↗

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