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Molecular chaperones: How J domains turn on Hsp70s

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Published in Current Biology. 1999, vol. 9, no. 8, p. R305-308
Abstract Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.
Keywords Binding SitesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteins/metabolismHeat-Shock Proteins/chemistry/metabolism/physiologyMolecular Chaperones/metabolism/ physiologyProtein BindingProtein Structure, Tertiary
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PMID: 10226023
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KELLEY, William. Molecular chaperones: How J domains turn on Hsp70s. In: Current Biology, 1999, vol. 9, n° 8, p. R305-308. https://archive-ouverte.unige.ch/unige:7377

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Deposited on : 2010-06-21

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