Heat shock response modulators as therapeutic tools for diseases of protein conformation

Sandy D. Westerheide, Richard I. Morimoto*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

367 Scopus citations


The disruption of protein folding quality control results in the accumulation of non-native protein species that can form oligomers, aggregates, and inclusions indicative of neurodegenerative disease. Likewise for over 100 other human diseases of protein conformation, a common feature may be the formation of off-path way folding intermediates that are unstable, self-associate, and with time lead to a chronic imbalance in protein homeostasis with deleterious consequences on cellular function. This has led to a hypothesis that enhancement of components of the cellular quality control machinery, specifically the levels and activities of molecular chaperones, suppress aggregation and toxicity phenotypes to allow cellular function to be restored. This review addresses the regulation of molecular chaperones and components of protein homeostasis by heat shock transcription factor 1 (HSF1), the master stress-inducible regulator, and our current understanding of pharmacologically active small molecule regulators of the heat shock response as a therapeutic strategy for protein conformational diseases.

Original languageEnglish (US)
Pages (from-to)33097-33100
Number of pages4
JournalJournal of Biological Chemistry
Issue number39
StatePublished - Sep 30 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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