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Article

Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction.

PloS one - 29 Apr 2011

Quaglio Elena, Restelli Elena, Garofoli Anna, Dossena Sara, De Luigi Ada, Tagliavacca Luigina, Imperiale Daniele, Migheli Antonio, Salmona Mario, Sitia Roberto, Forloni Gianluigi, Chiesa Roberto

Abstract excerpt

The cellular pathways activated by mutant prion protein (PrP) in genetic prion diseases, ultimately leading to neuronal dysfunction and degeneration, are not known. Several mutant PrPs misfold in the early secretory pathway and reside longer in the endoplasmic reticulum (ER) possibly stimulating ER stress-related pathogenic mechanisms. To investigate whether mutant PrP induced maladaptive responses, we checked...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 21559407
DOI: 10.1371/journal.pone.0019339
PMCID: PMC3084828

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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