Associated Papers
Nucleotide exchange is sufficient for Hsp90 functions in vivo.
Reidy M et al.
Nature Communications, 2023
ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.
Walerych D et al.
The Journal of Biological Chemistry, 2010
Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain.
Tsutsumi S et al.
Nature Structural & Molecular Biology, 2009
Cooperative regulation of the interferon regulatory factor-1 tumor suppressor protein by core components of the molecular chaperone machinery.
Narayan V et al.
The Journal of Biological Chemistry, 2009
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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