Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains

Keyphrases

• Heat Shock Protein 90 (Hsp90) 100%
• Dioxin Receptor 100%
• Molecular Chaperone 100%
• Receptor Function 100%
• Basic Helix-loop-helix (bHLH) 100%
• Distinct Roles 100%
• Chaperone Hsp90 100%
• Per-ARNT-Sim Domains 100%
• Arnt 85%
• DNA Binding 42%
• Ligand-binding Domain 28%
• Wheat Germ 28%
• Binding Activity 28%
• Lysate 28%
• Dimerization 28%
• Reticulocyte Lysate 28%
• Helix-loop-helix Domain 28%
• Transcription Factor 14%
• Signal Transduction 14%
• Transcription Regulation 14%
• Ligand-independent Activation 14%
• Receptor System 14%
• Ligand Binding 14%
• Receptor-mediated 14%
• Heterodimerization 14%
• Ligand-activated Transcription Factors 14%
• In Vitro Translation 14%
• Dioxins 14%
• Mediated Interaction 14%
• Xenobiotic Response Element 14%
• DNA Binding Affinity 14%
• Bound Form 14%
• Helix-loop-helix Motifs 14%
• Binding Conformation 14%

Biochemistry, Genetics and Molecular Biology

• Chaperone Protein 100%
• Hsp90 100%
• Basic Helix-Loop-Helix 100%
• Aryl Hydrocarbon Receptor 100%
• DNA Binding 50%
• Binding Affinity 50%
• Transcription Factor 25%
• Cell Lysate 25%
• Ligand Binding Domain 25%
• Dimerization 25%
• Reticulocyte Lysate 25%
• Response Element 12%
• Signal Transduction 12%
• Heat Shock Protein 12%
• Conformation 12%
• Ligand Binding 12%
• Xenobiotic Metabolism 12%
• Extract 12%

Neuroscience

• Receptor 100%
• Aryl Hydrocarbon Receptor 100%
• Chaperone 100%
• Basic Helix-Loop-Helix 100%
• Binding Affinity 50%
• DNA Binding 50%
• Ligand Binding 37%
• Transcription Factor 25%
• In Vitro 12%
• Signal Transduction 12%
• Response Element 12%
• Heat Shock Protein 90 12%
• Helix Loop Helix Protein 12%