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Chaperoned ubiquitylation-Structure of the CHIP E3 ubiquitin ligase and a CHIP-Uev1a complex
British Library Conference Proceedings | 2006| -
ATPase catalytic center within the N-terminal domain of hsp90 is needed for essential in vivo functions of this chaperone
British Library Conference Proceedings | 1998| -
X-Ray and Enzymatic Studies on Mutant Human Lysozymes
British Library Conference Proceedings | 1997| -
Crystal structure of the Hsp90-nucleotide-Sba1 closed chaperone complex
British Library Conference Proceedings | 2006| -
Structure and assembly of Hsp90-Cdc37-protein kinase complexes
British Library Conference Proceedings | 2006| -
Mutational analysis of Hsp90 reveals an ATPase-coupled "clamp" mechanism involving transient dimerization of the N-terminal domain
British Library Conference Proceedings | 2000|
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