Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23

EMBO Journal

Volumn 19, Issue 21, 2000, Pages 5930-5940

  Young, J C ^a   Hartl, F U ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

ATP; Glucocorticoid receptor; Hsp90; Molecular chaperones; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; GELDANAMYCIN; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 90; POLYPEPTIDE; PROTEIN P23;

ARTICLE; BINDING SITE; DISSOCIATION; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

EID: 0034329452     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.21.5930     Document Type: Article

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