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 pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling.

PloS one - 1 Jan 2017

Nuvolone Mario, Paolucci Marta, Sorce Silvia, Kana Veronika, Moos Rita, Matozaki Takashi, Aguzzi Adriano

Abstract excerpt

Prion diseases are neurodegenerative conditions caused by misfolding of the prion protein, leading to conspicuous neuronal loss and intense microgliosis. Recent experimental evidence point towards a protective role of microglia against prion-induced neurodegeneration, possibly through elimination of prion-containing apoptotic bodies. The molecular mechanisms by which microglia recognize and eliminate apoptotic...

Read the complete abstract on PubMed

Topics

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

Share to Disease Progression
Share to Gene Expression Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microglia

Share to Phagocytosis

Share to Prion Diseases

Share to Prion Proteins

Share to Receptors, Immunologic

Source

Open in PubMed Open full text

Identifiers

PMID: 28545141
DOI: 10.1371/journal.pone.0177876
PMCID: PMC5435345

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

Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling.PMID 28545141Read ↗

SIRPα polymorphisms, but not the prion protein, control phagocytosis of apoptotic cells.Semantic proximity Read ↗

Absence of Apolipoprotein E is associated with exacerbation of prion pathology and promotes microglial neurodegenerative phenotype.Semantic proximity Read ↗

Microglia in the degenerating brain are capable of phagocytosis of beads and of apoptotic cells, but do not efficiently remove PrPSc, even upon LPS stimulation.Semantic proximity Read ↗

Microglia in prion diseases.Semantic proximity Read ↗

RNA-seq and network analysis reveal unique glial gene expression signatures during prion infectionSemantic proximity Read ↗

Atypical inflammation in the central nervous system in prion diseaseSemantic proximity Read ↗

Transcriptomic Determinants of Scrapie Prion Propagation in Cultured Ovine Microglia.Semantic proximity Read ↗

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

LPS-induced systemic inflammation reveals an immunomodulatory role for the prion protein at the blood-brain interface.Semantic proximity Read ↗

Systemic Inflammation Accelerates Changes in Microglial and Synaptic Markers in an Experimental Model of Chronic NeurodegenerationSemantic proximity Read ↗

Prion Infection of Mouse Brain Reveals Multiple New Upregulated Genes Involved in Neuroinflammation or Signal TransductionSemantic proximity Read ↗

Unaltered prion disease in mice lacking developmental endothelial locus-1 (Del-1)Semantic proximity Read ↗

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