Associated Papers
Nucleotide exchange is sufficient for Hsp90 functions in vivo.
Reidy M et al.
Nature Communications, 2023
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1.
Xu W et al.
Nature Communications, 2019
ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.
Walerych D et al.
The Journal of Biological Chemistry, 2010
Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.
Jiang Y et al.
The Journal of Biological Chemistry, 2010
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
Obermann WM et al.
The Journal of Cell Biology, 1998
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