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Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin.

Human molecular genetics - 1 May 2002

Wyttenbach Andreas, Sauvageot Olivier, Carmichael Jenny, Diaz-Latoud Chantal, Arrigo Andre-Patrik, Rubinsztein David C

Abstract excerpt

Neuronal loss and intraneuronal protein aggregates are characteristics of Huntington's disease (HD), which is one of 10 known neurodegenerative disorders caused by an expanded polyglutamine [poly(Q)] tract in the disease protein. N-terminal fragments of mutant huntingtin produce intracellular aggregates and cause toxicity. Several studies have shown that chaperones suppress poly(Q) aggregation and toxicity/cell...

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Identifiers

PMID: 11978772
DOI: 10.1093/hmg/11.9.1137

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin.PMID 11978772Read ↗

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