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

Prion strains depend on different endocytic routes for productive infection

25 Jul 2017

Abstract excerpt

Prions are unconventional agents composed of misfolded prion protein that cause fatal neurodegenerative diseases in mammals. Prion strains induce specific neuropathological changes in selected brain areas. The mechanism of strain-specific cell tropism is unknown. We hypothesised that prion strains rely on different endocytic routes to invade and replicate within their target cells. Using prion permissive cells,...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Neurological diseases and metabolism
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28761068
DOI: 10.1038/s41598-017-07260-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Prion strains depend on different endocytic routes for productive infectionPMID 28761068Read ↗

Strain-associated variations in abnormal PrP trafficking of sheep scrapie.Semantic proximity Read ↗

Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In VivoSemantic proximity Read ↗

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

Prion pathogenesis in the absence of Toll‐like receptor signallingSemantic proximity Read ↗

Cell culture models of transmissible spongiform encephalopathies.Semantic proximity Read ↗

The uptake of tau amyloid fibrils is facilitated by the cellular prion protein and hampers prion propagation in cultured cellsSemantic proximity Read ↗

Cell biological studies of the prion protein.Semantic proximity Read ↗

Amyloid-Like Aggregates of the Yeast Prion Protein Ure2 Enter Vertebrate Cells by Specific Endocytotic Pathways and Induce ApoptosisSemantic proximity Read ↗

JC Virus Enters Human Glial Cells by Clathrin-Dependent Receptor-Mediated EndocytosisSemantic proximity Read ↗

Combined pharmacological, mutational and cell biology approaches indicate that p53-dependent caspase 3 activation triggered by cellular prion is dependent on its endocytosis.Semantic proximity Read ↗

Pathogenic prions deviate PrPC signaling in neuronal cells and impair A-beta clearanceSemantic proximity Read ↗

Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo.Semantic proximity Read ↗

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