In vitro evidence that hsp90 contains two independent chaperone sites

FEBS Letters

Volumn 418, Issue 1-2, 1997, Pages 139-143

  Young, Jason C ^a   Schneider, Christine ^a   Hartl, F Ulrich ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Geldanamycin; Hsp90; Human; Molecular chaperone

Indexed keywords

CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90;

ARTICLE; HUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BENZOQUINONES; BINDING SITES; DIMERIZATION; ENZYME INHIBITORS; GLUTATHIONE TRANSFERASE; HSP90 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; LACTAMS, MACROCYCLIC; LUCIFERASES; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; QUINONES; RECOMBINANT FUSION PROTEINS;

EID: 0030862486     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01363-X     Document Type: Article

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