ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

EMBO Journal

Volumn 17, Issue 16, 1998, Pages 4829-4836

  Panaretou, Barry ^a   Prodromou, Chrisostomos ^a   Roe, S Mark ^a   O'Brien, Ronan ^a   Ladbury, John E ^a   Piper, Peter W ^a   Pearl, Laurence H ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

ATP; Chaperone; Hsp90; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90;

ARTICLE; CONTROLLED STUDY; ENZYME INHIBITION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BINDING SITES; CALORIMETRY; HSP90 HEAT-SHOCK PROTEINS; HYDROLYSIS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032541344     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.16.4829     Document Type: Article

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