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Article

The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.

Protein science : a publication of the Protein Society - 1 Aug 2016

Fonseca-Ornelas Luis, Zweckstetter Markus

Abstract excerpt

In a group of neurodegenerative diseases, collectively termed transmissible spongiform encephalopathies, the prion protein aggregates into β-sheet rich amyloid-like deposits. Because amyloid structure has been connected to different prion strains and cellular toxicity, it is important to obtain insight into the structural properties of prion fibrils. Using a combination of solution NMR spectroscopy, thioflavin-T...

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Identifiers

PMID: 27184108
DOI: 10.1002/pro.2947
PMCID: PMC4972213

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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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