Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery. The initial hsp90·p60·hsp70-dependent step is sufficient for creating the steroid binding conformation

Journal of Biological Chemistry

Volumn 272, Issue 20, 1997, Pages 13047-13054

  Dittmar, Kurt D ^a   Pratt, William B ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GELDANAMYCIN; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MOLYBDIC ACID; PROTEIN P23; PROTEIN P60; TRIAMCINOLONE ACETONIDE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ESCHERICHIA COLI; FIBROBLAST; HORMONE RECEPTOR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; RABBIT; RETICULOCYTE LYSATE; STEROID BINDING;

ANIMALS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; PROTEIN BINDING; PROTEIN FOLDING; RABBITS; RECEPTORS, GLUCOCORTICOID; RETICULOCYTES;

ANIMALIA; ASTEROIDEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

EID: 0030989277     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.20.13047     Document Type: Article

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