Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90
molecular chaperone for in vivo function. Although Hsp90 is required for ligand binding in …

A set of software tools for building and distributing models of macromolecular assemblies
uses an integrative structure modeling approach, which casts the building of models as a …

We present an efficient pipeline enabling high-throughput analysis of protein structure in
solution with small angle X-ray scattering (SAXS). Our SAXS pipeline combines automated …

Protein folding in the cell relies on the orchestrated action of conserved families of molecular
chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …

The ubiquitous molecular chaperone Hsp90 makes up 1–2% of cytosolic proteins and is
required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety …

Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential
role in many cellular processes including cell cycle control, cell survival, hormone and other …

The HSP90 molecular chaperone is involved in the activation and cellular stabilization of a
range of 'client'proteins, of which oncogenic protein kinases and nuclear steroid hormone …