Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53

Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone

(2011) Timothy O. Street et al.   MOLECULAR CELL

The client protein p53 adopts a molten globule–like state in the presence of Hsp90

(2011) Sung Jean Park et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

ATP Binding to Hsp90 Is Sufficient for Effective Chaperoning of p53 Protein

(2010) Dawid Walerych et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Charge-Rich Regions Modulate the Anti-Aggregation Activity of Hsp90

(2010) Natalie Wayne et al.   JOURNAL OF MOLECULAR BIOLOGY

SEDVIEW, Real-time Sedimentation Analysis

(2010) David B. Hayes et al.   MACROMOLECULAR BIOSCIENCE

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

(2010) Marco Retzlaff et al.   MOLECULAR CELL

The HADDOCK web server for data-driven biomolecular docking

(2010) Sjoerd J de Vries et al.   Nature Protocols

BclxL Changes Conformation upon Binding to Wild-type but Not Mutant p53 DNA Binding Domain

(2009) Franz Hagn et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

(2009) Martin Hessling et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Hsp90 Chaperone Machinery

(2008) Sebastian Karl Wandinger et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Conserved Conformational Changes in the ATPase Cycle of Human Hsp90

(2008) Klaus Richter et al.   JOURNAL OF BIOLOGICAL CHEMISTRY