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Article

Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants.

The Journal of biological chemistry - 1 Feb 2013

Skora Lukasz, Fonseca-Ornelas Luis, Hofele Romina V, Riedel Dietmar, Giller Karin, Watzlawik Jens, Schulz-Schaeffer Walter J, Urlaub Henning, Becker Stefan, Zweckstetter Markus

Abstract excerpt

Misfolding of the natively α-helical prion protein into a β-sheet rich isoform is related to various human diseases such as Creutzfeldt-Jakob disease and Gerstmann-Sträussler-Scheinker syndrome. In humans, the disease phenotype is modified by a methionine/valine polymorphism at codon 129 of the prion protein gene. Using a combination of hydrogen/deuterium exchange coupled to NMR spectroscopy, hydroxyl radical...

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Identifiers

PMID: 23209282
DOI: 10.1074/jbc.M112.423715
PMCID: PMC3561524

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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.

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