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Current Opinion in Structural Biology|February 19, 2000
Structure and in vivo function of Hsp90L H Pearl, C ProdromouProteins|August 1, 1996
Expression and crystallization of the yeast Hsp82 chaperone, and preliminary X-ray diffraction studies of the amino-terminal domainC Prodromou, P W Piper, L H PearlNature Structural Biology|June 1, 1997
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperoneC Prodromou, S M Roe, P W Piper, et al.Gene|March 9, 1996
Synthesis of a modified gene encoding human ornithine transcarbamylase for expression in mammalian mitochondrial and universal translation systems: a novel approach towards correction of a genetic defectV C Wheeler, C Prodromou, L H Pearl, et al.Journal of Medicinal Chemistry|February 2, 1999
Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycinS M Roe, C Prodromou, R O'Brien, et al.Cell|July 11, 1997
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperoneC Prodromou, S M Roe, R O'Brien, et al.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.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.Mutation Research|August 18, 2000
Structure and function in the uracil-DNA glycosylase superfamilyL H PearlPageof 7