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Heat-shock protein 90, a chaperone for folding and regulation

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Published in Cellular and Molecular Life Sciences. 2002, vol. 59, no. 10, p. 1640-1648
Abstract Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.
Keywords Amino Acid SequenceAnimalsBinding SitesCell Cycle/physiologyHSP90 Heat-Shock Proteins/chemistry/metabolismHumansMolecular Chaperones/metabolismProtein FoldingSignal Transduction/physiologySubstrate Specificity
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PMID: 12475174
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PICARD, Didier. Heat-shock protein 90, a chaperone for folding and regulation. In: Cellular and Molecular Life Sciences, 2002, vol. 59, n° 10, p. 1640-1648. https://archive-ouverte.unige.ch/unige:4625

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Deposited on : 2009-12-07

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