Roles of molecular chaperones in protein misfolding diseases

José M. Barral, Sarah A. Broadley, Gregor Schaffar, F. Ulrich Hartl

    Research output: Contribution to journalReview articlepeer-review

    232 Scopus citations


    Human misfolding diseases result from the failure of proteins to reach their active state or from the accumulation of aberrantly folded proteins. The mechanisms by which molecular chaperones influence the development of these diseases is beginning to be understood. Mutations that compromise the activity of chaperones lead to several rare syndromes. In contrast, the more frequent amyloid-related neurodegenerative diseases are caused by a gain of toxic function of misfolded proteins. Toxicity in these disorders may result from an imbalance between normal chaperone capacity and production of dangerous protein species. Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies.

    Original languageEnglish (US)
    Pages (from-to)17-29
    Number of pages13
    JournalSeminars in Cell and Developmental Biology
    Issue number1
    StatePublished - Feb 2004


    • Amyloid
    • Misfolding diseases
    • Molecular chaperones
    • Polyglutamine diseases
    • Ubiquitin-proteasome system

    ASJC Scopus subject areas

    • Developmental Biology
    • Cell Biology

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