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Volumn 267, Issue 19, 1992, Pages 13728-13734
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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 activity and repression of intrinsic DNA binding activity
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Author keywords
[No Author keywords available]
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Indexed keywords
AROMATIC HYDROCARBON RECEPTOR;
DIOXIN;
GLUTATHIONE TRANSFERASE;
HEAT SHOCK PROTEIN;
LIGAND;
ANIMAL CELL;
ARTICLE;
BINDING AFFINITY;
CROSS LINKING;
DNA BINDING;
DRUG METABOLISM;
GENE TRANSLOCATION;
HEAT STROKE;
HEPATOMA CELL;
LIGAND BINDING;
MOUSE;
NONHUMAN;
PRIORITY JOURNAL;
SIGNAL TRANSDUCTION;
TRANSCRIPTION REGULATION;
AFFINITY LABELS;
ANIMAL;
CELL NUCLEUS;
CROSS-LINKING REAGENTS;
DNA;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
HEAT-SHOCK PROTEINS;
LIGANDS;
MICE;
RECEPTORS, ARYL HYDROCARBON;
RECEPTORS, DRUG;
SODIUM CHLORIDE;
SUPPORT, NON-U.S. GOV'T;
SUPPORT, U.S. GOV'T, P.H.S.;
TEMPERATURE;
TETRACHLORODIBENZODIOXIN;
TUMOR CELLS, CULTURED;
TRITICUM AESTIVUM;
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EID: 0026631538
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
Times cited : (204)
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References (0)
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