Gerstmann-sträussler-scheinker disease and anchorless prion protein mice share prion conformational properties diverging from sporadic creutzfeldt-jakob disease

Gianluigi Zanusso, Michele Fiorini, Sergio Ferrari, Kimberly Meade-White, Ilaria Barbieri, Emiliana Brocchi, Bernardino Ghetti, Salvatore Monaco

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Background: Prion strains exhibit distinct physical and biochemical repertoires, aggregation propensity, and biological properties. Results: A biochemical approach is developed for defining the conformational features of prions with or without glycosylphosphatidylinositol (GPI)-anchor. Conclusion: GPI anchorless prions are detected in human genetic prion diseases, but not in sporadic forms. Significance: Unveiling the structure of GPI anchorless prions to predict pathological properties.

Original languageEnglish (US)
Pages (from-to)4870-4881
Number of pages12
JournalJournal of Biological Chemistry
Volume289
Issue number8
DOIs
StatePublished - Feb 21 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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