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Article

Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells.

Molecular and cellular neurosciences - 1 Apr 2008

Gu Yaping, Singh Ajay, Bose Sharmila, Singh Neena

Abstract excerpt

Point mutations M232R (PrP(232R)), M232T (PrP(232T)), and P238S (PrP(238S)) in the glycosylphosphatidylinositol signal peptide (GPI-SP) of the prion protein (PrP(C)) segregate with familial Creutzfeldt-Jakob disease (CJD). However, the mechanism by which these mutations induce cytotoxicity is unclear since the GPI-SP is replaced by a GPI anchor within 5 min of PrP synthesis and translocation into the endoplasmic...

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Source

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Identifiers

PMID: 18325785
DOI: 10.1016/j.mcn.2007.08.018
PMCID: PMC2693044

Genes

GPI

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.

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Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells.PMID 18325785Read ↗

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A point mutation in GPI-attachment signal peptide accelerates the development of prion disease.Semantic proximity Read ↗

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