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The EMBO Journal|August 26, 1998
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivoB Panaretou, C Prodromou, S M Roe, et al.
Oncogene|December 3, 2013
Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsJ R Smith, E de Billy, S Hobbs, et al.
The EMBO Journal|August 16, 2000
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domainsC Prodromou, B Panaretou, S Chohan, et al.
The EMBO Journal|February 2, 1999
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperonesC Prodromou, G Siligardi, R O'Brien, et al.
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