Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex (original) (raw)

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Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insights

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A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone

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Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways

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ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)

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Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

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Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

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Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

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The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

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Hsp90 Oligomers Interacting with the Aha1 Cochaperone: An Outlook for the Hsp90 Chaperone Machineries

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N-terminal domain of human Hsp90 triggers binding to the cochaperone p23

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivo

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Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50

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Dynamics of the regulation of Hsp90 by the co-chaperone Sti1

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Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

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Structural and Computational Biology of the Molecular Chaperone Hsp90: From Understanding Molecular Mechanisms to Computer-Based Inhibitor Design

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Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics

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Hsp90: Breaking the Symmetry

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Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

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Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94

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

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GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex

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Conformations of the Nucleotide and Polypeptide Binding Domains of a Cytosolic Hsp70 Molecular Chaperone Are Coupled

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Molecular chaperones: The busy life of Hsp90

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Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone

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Liberation of the intramolecular interaction as the mechanism of heat-induced activation of HSP90 molecular chaperone

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Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

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