Heat shock protein hsp90 regulates dioxin receptor function in vivo. - Wikidata - awgldk - TriplyDB

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

http://www.wikidata.org/entity/Q34333109

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Overview of AHR functional domains and the classical AHR signaling pathway: induction of drug-metabolizing enzymes Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor Interaction networks in yeast define and enumerate the signaling steps of the vertebrate aryl hydrocarbon receptor The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor Defining the role for XAP2 in stabilization of the dioxin receptor Two distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90 Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor Identification of a highly conserved module in E proteins required for in vivo helix-loop-helix dimerization Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity Characterization of the Ah receptor-associated protein, ARA9 Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein The aryl hydrocarbon receptor complex and the control of gene expression Recombinant expression of aryl hydrocarbon receptor for quantitative ligand-binding analysis cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the aryl hydrocarbon receptor nuclear translocator (Arnt)PAS domains: internal sensors of oxygen, redox potential, and light Characterization of the mouse Cyp1B1 gene. Identification of an enhancer region that directs aryl hydrocarbon receptor-mediated constitutive and induced expression.Mechanistic aspects--the dioxin (aryl hydrocarbon) receptor.Ligand displaces heat shock protein 90 from overlapping binding sites within the aryl hydrocarbon receptor ligand-binding domain Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor The dioxin (aryl hydrocarbon) receptor as a model for adaptive responses of bHLH/PAS transcription factors.Hsp90 is required for pheromone signaling in yeast.2,3,7,8-Tetrachlorodibenzo-p-dioxin-mediated impairment of B cell differentiation involves dysregulation of paired box 5 (Pax5) isoform, Pax5a.The potential role of transcription factor aryl hydrocarbon receptor in downregulation of hepatic cytochrome P-450 during sepsis.Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.Relevance of the aryl hydrocarbon receptor (AhR) for clinical toxicology.The role of hepatic cytochrome P-450 in sepsis.Regulatory interactions among three members of the vertebrate aryl hydrocarbon receptor family: AHR repressor, AHR1, and AHR2.Analysis of Glycogen Synthase Kinase Inhibitors That Regulate Cytochrome P450 Expression in Primary Human Hepatocytes by Activation of β-Catenin, Aryl Hydrocarbon Receptor and Pregnane X Receptor Signaling.Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: expressionvectors with bi-directional promoters for use in Saccharomyces cerevisiae.Expression of the human aryl hydrocarbon receptor complex in yeast. Activation of transcription by indole compounds.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 receptor Regulation of dioxin receptor function by omeprazole.Heat shock proteins and circadian rhythms.Aryl hydrocarbon receptor-mediated signal transduction.Induction of drug-metabolizing enzymes by dioxin.

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P2860

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

http://www.wikidata.org/entity/Q34333109

description

1995 nî lūn-bûn

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1995 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1995 թվականի մայիսին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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type

label

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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prefLabel

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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Heat shock protein hsp90 regulates dioxin receptor function in vivo.

@en

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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PNAS.92.10.4437

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Heat shock protein hsp90 regulates dioxin receptor function in vivo.

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P2093

Gustafsson JA

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McGuire J

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Picard D

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Poellinger L

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Whitelaw ML

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P2860

Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors

In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition

Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor

Cloning and expression of a human Ah receptor cDNA

Improved method for high efficiency transformation of intact yeast cells

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

Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex

The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system

Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action

Consequences of heteromeric interactions among helix-loop-helix proteins

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4437-4441

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