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

α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model

12 Sept 2024

Abstract excerpt

The cellular prion protein, PrPC, has been postulated to function as a receptor for α-synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of α-synuclein aggregates in neurodegenerative disorders such as Parkinson's disease. Previously, we generated the "Salt (S)" and "No Salt (NS)" strains of α-synuclein aggregates that cause distinct pathological phenotypes in M83 transgenic mice...

Read the complete abstract on PubMed

Topics

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

Share to Neurological diseases and metabolism
Share to Parkinson's Disease Mechanisms and Treatments
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 39264912
DOI: 10.1371/journal.ppat.1012517

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse modelPMID 39264912Read ↗

α-Synuclein Strain Propagation is Independent of Cellular Prion Protein Expression in Transgenic MiceSemantic proximity Read ↗

The G51D SNCA mutation generates a slowly progressive α-synuclein strain in early-onset Parkinson's disease.Semantic proximity Read ↗

α-Synuclein Amyloids Hijack Prion Protein to Gain Cell Entry, Facilitate Cell-to-Cell Spreading and Block Prion ReplicationSemantic proximity Read ↗

α-Synuclein strain homogeneity in multiple system atrophy clinical subtypesSemantic proximity Read ↗

Comparative analyses of the in vivo induction and transmission of α-synuclein pathology in transgenic mice by MSA brain lysate and recombinant α-synuclein fibrilsSemantic proximity Read ↗

α-Synuclein strains cause distinct synucleinopathies after local and systemic administration.Semantic proximity Read ↗

'Prion-like' propagation of the synucleinopathy of M83 transgenic mice depends on the mouse genotype and type of inoculum.Semantic proximity Read ↗

Templating of Monomeric Alpha-Synuclein Induces Inflammation and SNpc Dopamine Neuron Death in a Genetic Mouse Model of SynucleinopathySemantic proximity Read ↗

Pathogenic Mutations Differentially Regulate Cell-to-Cell Transmission of α-SynucleinSemantic proximity Read ↗

Stochastic Misfolding Drives the Emergence of Distinct α-Synuclein StrainsSemantic proximity Read ↗

Unique seeding profiles and prion-like propagation of synucleinopathies are highly dependent on the host in human α-synuclein transgenic miceSemantic proximity Read ↗

ɑ-Synuclein strains and the variable pathologies of synucleinopathies.Semantic proximity Read ↗

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