4.6 Review

The Hsp90 chaperone machinery

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S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities

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CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone

Y Miyata et al.

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Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

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Oncogenic mutations reduce the stability of Src kinase

SF Falsone et al.

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O Hainzl et al.

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The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

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N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

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D Picard

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Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc97

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Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40

F Pirkl et al.

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Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

A Chadli et al.

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R Dutta et al.

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