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Article

Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity.

The Journal of biological chemistry - 25 Jun 2010

Harrison Christopher F, Lawson Victoria A, Coleman Bradley M, Kim Yong-Sun, Masters Colin L, Cappai Roberto, Barnham Kevin J, Hill Andrew F

Abstract excerpt

Prion diseases are associated with the misfolding of the endogenously expressed prion protein (designated PrP(C)) into an abnormal isoform (PrP(Sc)) that has infectious properties. The hydrophobic domain of PrP(C) is highly conserved and contains a series of glycine residues that show perfect conservation among all species, strongly suggesting it has functional and evolutionary significance. These glycine...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20356832
DOI: 10.1074/jbc.M109.093310
PMCID: PMC2888434

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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