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Volumn 275, Issue 47, 2000, Pages 37181-37186

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

(5) Marcu, Monica G a Chadli, Ahmed b Bouhouche, Ilham c Catelli, Maria c Neckers, Leonard M a

a NATIONAL CANCER INSTITUTE (United States)

b MAYO GRADUATE SCHOOL (United States)

c Institut Cochin (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; CHAPERONE; DNA TOPOISOMERASE (ATP HYDROLYSING); GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; NOVOBIOCIN; NUCLEOTIDE BINDING PROTEIN; PROTEIN KINASE; PROTEIN P23; RADICICOL; STEROID RECEPTOR;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; DELETION MUTANT; EUKARYOTE; IN VITRO STUDY; IN VIVO STUDY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CHICKENS; ENZYME INHIBITORS; HSP90 HEAT-SHOCK PROTEINS; LACTONES; MACROLIDES; MOLECULAR SEQUENCE DATA; NOVOBIOCIN; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN-TYROSINE KINASES; RABBITS; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 0034711270 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M003701200 Document Type: Article

Times cited : (476)

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