Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine

(2009) Christian Graf et al.   EMBO JOURNAL

Hsp90 is regulated by a switch point in the C-terminal domain

(2009) Marco Retzlaff et al.   EMBO REPORTS

The Charged Linker Region Is an Important Regulator of Hsp90 Function

(2009) Otmar Hainzl et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Modular Control of Cross-oligomerization

(2009) Natalie Wayne et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain

(2009) Shinji Tsutsumi et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

(2009) Moritz Mickler et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

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

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

Modeling Signal Propagation Mechanisms and Ligand-Based Conformational Dynamics of the Hsp90 Molecular Chaperone Full-Length Dimer

(2009) Giulia Morra et al.   PLoS Computational Biology

Apo-Hsp90 coexists in two open conformational states in solution

(2008) Patrick Bron et al.   BIOLOGY OF THE CELL

Vernakalant Hydrochloride for Rapid Conversion of Atrial Fibrillation

(2008) Denis Roy et al.   CIRCULATION

The Hsp90 Chaperone Machinery

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

Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90

(2008) Kristin A. Krukenberg et al.   STRUCTURE