The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
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Quantitative analysis of HSP90-client interactions reveals principles of substrate recognitionIdentification of a novel HSP70-binding cochaperone critical to HSP90-mediated activation of small serine/threonine kinaseGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesCooperative regulation of the interferon regulatory factor-1 tumor suppressor protein by core components of the molecular chaperone machineryTargeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseasesKeep your heart in shape: molecular chaperone networks for treating heart diseaseFunctions of the Hsp90 chaperone system: lifting client proteins to new heightsEnhancement of stress resilience through histone deacetylase 6-mediated regulation of glucocorticoid receptor chaperone dynamics.Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90Functional and molecular features of the calmodulin-interacting protein IQCG required for haematopoiesis in zebrafishMitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cellsStabilization of integrin-linked kinase by the Hsp90-CHIP axis impacts cellular force generation, migration and the fibrotic responseHsp90-dependent assembly of the DBC2/RhoBTB2-Cullin3 E3-ligase complexDevelopment and validation of a high-content screening assay to identify inhibitors of cytoplasmic dynein-mediated transport of glucocorticoid receptor to the nucleus.Human GTSE-1 regulates p21(CIP1/WAF1) stability conferring resistance to paclitaxel treatment.Methylmercury alters the activities of Hsp90 client proteins, prostaglandin E synthase/p23 (PGES/23) and nNOS.Evidence of a Cell Surface Role for Hsp90 Complex Proteins Mediating Neuroblast Migration in the Subventricular Zone.Expression of hsp90 alpha and hsp90 beta during Xenopus laevis embryonic development.Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradationPhosphoproteome dynamics reveal heat-shock protein complexes specific to the Leishmania donovani infectious stage.The stress of protein misfolding: from single cells to multicellular organismsC331A mutant of neuronal nitric-oxide synthase is labilized for Hsp70/CHIP (C terminus of HSC70-interacting protein)-dependent ubiquitination.GAPDH regulates cellular heme insertion into inducible nitric oxide synthaseA chaperone trap contributes to the onset of cystic fibrosis.The heat shock protein 90 inhibitor 17-AAG suppresses growth and induces apoptosis in human cholangiocarcinoma cells.Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseasesFunctional interaction of heat shock protein 90 and Beclin 1 modulates Toll-like receptor-mediated autophagy.Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleftPhase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia.Biochemical reconstitution of steroid receptor•Hsp90 protein complexes and reactivation of ligand bindingModulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitinationNitration of Hsp90 on Tyrosine 33 Regulates Mitochondrial MetabolismFK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stabilityMechanistic Insights into the Antilithiatic Proteins from Terminalia arjuna: A Proteomic Approach in UrolithiasisWild-type EGFR is stabilized by direct interaction with HSP90 in cancer cells and tumors.Ubiquitination of neuronal nitric-oxide synthase in the calmodulin-binding site triggers proteasomal degradation of the protein.
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The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 30 May 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@en
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@nl
type
label
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@en
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@nl
prefLabel
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@en
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@nl
P2093
P2860
P356
P1476
The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
@en
P2093
William B Pratt
Yoichi Osawa
Yoshihiro Morishima
P2860
P304
22885-22889
P356
10.1074/JBC.R800023200
P407
P577
2008-05-30T00:00:00Z