In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

Journal of Cell Biology

Volumn 143, Issue 4, 1998, Pages 901-910

  Obermann, Wolfgang M J ^a   Sondermann, Holger ^a   Russo, Alicia A ^b   Pavletich, Nikola P ^b   Hartl, F Ulrich ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

Geldanamycin; Heat shock protein 90; Molecular chaperone; Nucleotide binding; p23

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; DNA TOPOISOMERASE (ATP HYDROLYSING); HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; HUMAN; HUMAN CELL; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; SEQUENCE HOMOLOGY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BENZOQUINONES; CELL DIVISION; CHAPERONINS; CRYSTALLOGRAPHY; DNA TOPOISOMERASES, TYPE II; ENZYME INHIBITORS; FUNGAL PROTEINS; GENE EXPRESSION REGULATION, FUNGAL; HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; LACTAMS, MACROCYCLIC; MAGNESIUM; MUTAGENESIS; PROTEIN STRUCTURE, TERTIARY; QUINONES; SACCHAROMYCES CEREVISIAE PROTEINS; YEASTS;

ANIMALIA; ESCHERICHIA COLI; EUKARYOTA;

EID: 0032538995     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.4.901     Document Type: Article

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