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Article

Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model.

The Journal of biological chemistry - 23 Mar 2007

Schiffer Niclas W, Broadley Sarah A, Hirschberger Thomas, Tavan Paul, Kretzschmar Hans A, Giese Armin, Haass Christian, Hartl F Ulrich, Schmid Bettina

Abstract excerpt

Several neurodegenerative diseases, including Huntington disease (HD), are associated with aberrant folding and aggregation of polyglutamine (polyQ) expansion proteins. Here we established the zebrafish, Danio rerio, as a vertebrate HD model permitting the screening for chemical suppressors of polyQ aggregation and toxicity. Upon expression in zebrafish embryos, polyQ-expanded fragments of huntingtin (htt)...

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PMID: 17170113
DOI: 10.1074/jbc.M607865200

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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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