Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activ
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HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signalingThe aryl hydrocarbon receptor: a perspective on potential roles in the immune systemCooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingGenetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesisThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorIn vitro analysis of Ah receptor domains involved in ligand-activated DNA recognitionProtein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complexLigand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptorIdentification of a novel mechanism of regulation of Ah (dioxin) receptor functionIdentification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)Interaction networks in yeast define and enumerate the signaling steps of the vertebrate aryl hydrocarbon receptorActivation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factorTransformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90 kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachlorodibenzo-p-dioxinMolecular mechanism of inhibition of estrogen-induced cathepsin D gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in MCF-7 cellsAh Receptor Pathway Intricacies; Signaling Through Diverse Protein Partners and DNA-MotifsThe aryl hydrocarbon receptor complex and the control of gene expressionDietary chemoprevention strategies for induction of phase II xenobiotic-metabolizing enzymes in lung carcinogenesis: A reviewPAS domains: internal sensors of oxygen, redox potential, and lightTryptamine serves as a proligand of the AhR transcriptional pathway whose activation is dependent of monoamine oxidases.Use of natural AhR ligands as potential therapeutic modalities against inflammatory disorders.Distinct roles for aryl hydrocarbon receptor nuclear translocator and ah receptor in estrogen-mediated signaling in human cancer cell lines.A steroid receptor coactivator acts as the DNA-binding partner of the methoprene-tolerant protein in regulating juvenile hormone response genes.Heat shock protein hsp90 regulates dioxin receptor function in vivo.Heat Shock Protein 70 and 90 Genes in the Harmful Dinoflagellate Cochlodinium polykrikoides: Genomic Structures and Transcriptional Responses to Environmental StressesNuclear receptors in the multidrug resistance through the regulation of drug-metabolizing enzymes and drug transporters.Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factorDown-regulation of nuclear aryl hydrocarbon receptor DNA-binding and transactivation functions: requirement for a labile or inducible factor.Isolation of Hsp90 mutants by screening for decreased steroid receptor function.Hsp90 is required for pheromone signaling in yeast.Ligand promiscuity of aryl hydrocarbon receptor agonists and antagonists revealed by site-directed mutagenesis.A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.Multiple roles of ligand in transforming the dioxin receptor to an active basic helix-loop-helix/PAS transcription factor complex with the nuclear protein Arnt.Role of the PAS domain in regulation of dimerization and DNA binding specificity of the dioxin receptorDistinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.Definition of a novel ligand binding domain of a nuclear bHLH receptor: co-localization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor.Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation.Distinct functions of the 90 kDa heat-shock protein (hsp90) in oestrogen and mineralocorticosteroid receptor activity: effects of hsp90 deletion mutants.Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha.The activation mechanism of the aryl hydrocarbon receptor (AhR) by molecular chaperone HSP90.The Hsp90 chaperone complex A potential target for cancer therapy?
P2860
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P2860
Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activ
description
1992 nî lūn-bûn
@nan
1992 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Dual roles of the 90-kDa heat ...... both for ligand binding activ
@nl
type
label
Dual roles of the 90-kDa heat ...... both for ligand binding activ
@nl
prefLabel
Dual roles of the 90-kDa heat ...... both for ligand binding activ
@nl
P2093
P1476
Dual roles of the 90-kDa heat ...... intrinsic DNA binding activity
@en
P2093
I Pongratz
L Poellinger
P304
P407
P577
1992-07-05T00:00:00Z