A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s

FEBS Journal

Volumn 276, Issue 1, 2009, Pages 199-209

  Vaughan, Cara K ^a   Piper, Peter W ^b   Pearl, Laurence H ^a   Prodromou, Chrisostomos ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

ATPase activity; Chaperone; Heat shock protein; Hsp90; N terminal dimerization

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYTOPLASM PROTEIN; HEAT SHOCK PROTEIN 90;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL ANALYSIS; CROSS LINKING; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATASES; CALORIMETRY; CYTOPLASM; DIMERIZATION; HSP90 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 57649215437     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06773.x     Document Type: Article

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