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Article

The presence of valine at residue 129 in human prion protein accelerates amyloid formation.

FEBS letters - 9 May 2005

Baskakov Ilia, Disterer Petra, Breydo Leonid, Shaw Michael, Gill Andrew, James William, Tahiri-Alaoui Abdessamad

Abstract excerpt

The polymorphism at residue 129 of the human PRNP gene modulates disease susceptibility and the clinico-pathological phenotypes in human transmissible spongiform encephalopathies. The molecular mechanisms by which the effect of this polymorphism are mediated remain unclear. It has been shown that the folding, dynamics and stability of the physiological, alpha-helix-rich form of recombinant PrP are not affected by...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15862295
DOI: 10.1016/j.febslet.2005.03.075

Genes

PRNP

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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The presence of valine at residue 129 in human prion protein accelerates amyloid formation.PMID 15862295Read ↗

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Molecular dynamics simulation of local structural models of PrP <sup>Sc</sup> reveals how codon 129 polymorphism affects propagation of PrP <sup>Sc</sup>Semantic proximity Read ↗

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