Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.
about
Molecular characterization of two mammalian bHLH-PAS domain proteins selectively expressed in the central nervous systemGenetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesisThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorProtein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complexThe hsp90 molecular chaperone modulates multiple telomerase activities.The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptorTwo parallel pathways mediate cytoplasmic localization of the dioxin (aryl hydrocarbon) receptorTwo distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factorIdentification of functional domains of the aryl hydrocarbon receptorDefinition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificityThe aryl hydrocarbon receptor complex and the control of gene expressionHeat shock protein hsp90 regulates dioxin receptor function in vivo.Ligand displaces heat shock protein 90 from overlapping binding sites within the aryl hydrocarbon receptor ligand-binding domainFunctional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factorHsp90 is required for pheromone signaling in yeast.Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.Ligand promiscuity of aryl hydrocarbon receptor agonists and antagonists revealed by site-directed mutagenesis.Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: expressionvectors with bi-directional promoters for use in Saccharomyces cerevisiae.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 receptorThe role of aryl hydrocarbon receptor and crosstalk with estrogen receptor in response of breast cancer cells to the novel antitumor agents benzothiazoles and aminoflavone.Aryl hydrocarbon nuclear translocator (ARNT) promotes oxygen-independent stabilization of hypoxia-inducible factor-1alpha by modulating an Hsp90-dependent regulatory pathway.Hypoxia-induced activation of HIF-1: role of HIF-1alpha-Hsp90 interaction.A mutation in the aryl hydrocarbon receptor (AHR) in a cultured mammalian cell line identifies a novel region of AHR that affects DNA binding.Aryl hydrocarbon receptor-mediated signal transduction.Transcriptional activation of cytochrome P450 genes by different classes of chemical inducers.Role of the Per/Arnt/Sim domains in ligand-dependent transformation of the aryl hydrocarbon receptor.Mechanisms of ligand-induced aryl hydrocarbon receptor-mediated biochemical and toxic responses.Definition of a dioxin receptor mutant that is a constitutive activator of transcription: delineation of overlapping repression and ligand binding functions within the PAS domain.Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway.Contribution of the Per/Arnt/Sim (PAS) domains to DNA binding by the basic helix-loop-helix PAS transcriptional regulators.Novel DNA binding by a basic helix-loop-helix protein. The role of the dioxin receptor PAS domain.MAGED1 is a novel regulator of a select subset of bHLH PAS transcription factors.The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.A Novel Mechanism for Cross-Adaptation between Heat and Altitude Acclimation: The Role of Heat Shock Protein 90
P2860
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P2860
Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Distinct roles of the molecula ...... ix-loop-helix and PAS domains.
@en
type
label
Distinct roles of the molecula ...... ix-loop-helix and PAS domains.
@en
prefLabel
Distinct roles of the molecula ...... ix-loop-helix and PAS domains.
@en
P2093
P2860
P356
P1476
Distinct roles of the molecula ...... ix-loop-helix and PAS domains.
@en
P2093
Antonsson C
Gustafsson JA
Poellinger L
Whitelaw ML
P2860
P304
P356
10.1128/MCB.15.2.756
P407
P577
1995-02-01T00:00:00Z