Insights into Hsp90 mechanism and in vivo functions learned from studies in the yeast, Saccharomyces cerevisiae

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Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

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Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone

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

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Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi

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Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

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Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1

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The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains

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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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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches

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Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

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Heat-shock protein hsp90 governs the activity of pp60v-src kinase.

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Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease

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Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

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A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways

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Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor

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Chaperone Function of Hsp90-Associated Proteins

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Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23

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<i>In vivo</i> functions of the <i>Saccharomyces cerevisiae</i> Hsp90 chaperone

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The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo

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The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37

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Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

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Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms

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Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.

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Mechanisms of Hsp90 regulation

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p50cdc37 Acting in Concert with Hsp90 Is Required for Raf-1 Function

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

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Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins

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In Vivo Analysis of the Hsp90 Cochaperone Sti1 (p60)

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The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules

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Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

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Post-translational modifications of Hsp90 and translating the chaperone code

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

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Isolation of Hsp90 mutants by screening for decreased steroid receptor function.

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Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase

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Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

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Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code

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A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

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Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis

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Threonine 22 Phosphorylation Attenuates Hsp90 Interaction with Cochaperones and Affects Its Chaperone Activity

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Substrate Transfer from the Chaperone Hsp70 to Hsp90

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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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p23 and HSP20/α‐crystallin proteins define a conserved sequence domain present in other eukaryotic protein families

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The Plasticity of the Hsp90 Co-chaperone System

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Dynamic Tyrosine Phosphorylation Modulates Cycling of the HSP90-P50CDC37-AHA1 Chaperone Machine

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Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor

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Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

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Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis

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Asymmetric Hsp90 N Domain SUMOylation Recruits Aha1 and ATP-Competitive Inhibitors

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Hsp90 activator Aha1 drives production of pathological tau aggregates

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The Middle Domain of Hsp90 Acts as a Discriminator between Different Types of Client Proteins

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Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties

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Dimerization of Hsp90 Is Required for in Vivo Function

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Functional and physical interaction between yeast Hsp90 and Hsp70

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches

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An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. Huber

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Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast

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Yeast Rvb1 and Rvb2 are ATP-Dependent DNA Helicases that Form a Heterohexameric Complex

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Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7ΔCells

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Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance

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Latent Effects of Hsp90 Mutants Revealed at Reduced Expression Levels

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Comprehensive fitness maps of Hsp90 show widespread environmental dependence

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