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Article

The key-role of tyrosine 155 in the mechanism of prion transconformation as highlighted by a study of sheep mutant peptides.

Peptides - 1 Jul 2008

Bertho Gildas, Bouvier Guillaume, Hoa Gaston Hui Bon, Girault Jean-Pierre

Abstract excerpt

Prion protein is a strongly conserved and ubiquitous glycoprotein. The conformational conversion of the non-pathogenic cellular prion isoform (PrP(C)) into a pathogenic scrapie isoform (PrP(Sc)) is a fundamental event in the onset of transmissible spongiform encephalopathies (TSE). During this conversion, helix H1 and its two flanking loops are known to undergo a conformational transition into a beta-like...

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Identifiers

PMID: 18455265
DOI: 10.1016/j.peptides.2008.03.014

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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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