Roles of molecular chaperones in protein misfolding diseases.

Abstract	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.
Authors	José M Barral, Sarah A Broadley, Gregor Schaffar, F Ulrich Hartl
Journal	Seminars in cell & developmental biology (Semin Cell Dev Biol) Vol. 15 Issue 1 Pg. 17-29 (Feb 2004) ISSN: 1084-9521 [Print] England
PMID	15036203 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References	Amyloid Chaperonin 60 Eye Proteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Heat-Shock Proteins Intracellular Signaling Peptides and Proteins MKKS protein, human Membrane Proteins Molecular Chaperones Multienzyme Complexes Proteins RP2 protein, human SACS protein, human TBCE protein, human Ubiquitins alpha-Crystallins Cysteine Endopeptidases Proteasome Endopeptidase Complex Chaperonins GTP-Binding Proteins Group II Chaperonins
Topics	Amyloid (chemistry, physiology) Chaperonin 60 (genetics, physiology) Chaperonins (physiology) Cysteine Endopeptidases (physiology) Cytosol (physiology) Disease (etiology) Endoplasmic Reticulum (physiology) Eye Proteins (genetics, physiology) GTP-Binding Proteins Group II Chaperonins HSP70 Heat-Shock Proteins (physiology) HSP90 Heat-Shock Proteins (physiology) Heat-Shock Proteins (genetics, physiology) Humans Intracellular Signaling Peptides and Proteins Membrane Proteins Models, Biological Molecular Chaperones (genetics, physiology) Multienzyme Complexes (physiology) Mutation Proteasome Endopeptidase Complex Protein Folding Proteins (chemistry, physiology) Ubiquitins (physiology) alpha-Crystallins (genetics, physiology)

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