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Structure, Function, and Mechanism of the Hsp90 Molecular Chaperone
British Library Online Contents | 2002| -
Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism
British Library Online Contents | 2016| -
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system
British Library Online Contents | 2013| -
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system
British Library Online Contents | 2013| -
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| -
Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90
British Library Online Contents | 2013| -
Crystal structure of the Hsp90-nucleotide-Sba1 closed chaperone complex
British Library Conference Proceedings | 2006| -
Inhibition of Hsp90 with Resorcylic Acid Macrolactones: Synthesis and Binding Studies
British Library Online Contents | 2010| -
Structure and assembly of Hsp90-Cdc37-protein kinase complexes
British Library Conference Proceedings | 2006| -
Inhibition of Hsp90 with Synthetic Macrolactones: Synthesis and Structural and Biological Evaluation of Ring and Conformational Analogs of Radicicol
British Library Online Contents | 2006| -
X-RAY AND ENZYMATIC STUDIES ON MUTANT HUMAN LYSOZYMES
Online Contents | 1997|Contributors: Prodromou, C. -
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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