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A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

Host protein homeostasis is a critical force shaping influenza evolution, impacting both the nature of selection on the influenza genome and the accessibility of specific mutational trajectories.

Heat-induced local unfolding allows Hsf1 to form trimers and bind to DNA, which depends on Hsf1 concentration and is promoted, not inhibited, by Hsp90.

ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.

Phosphatidylinositol 3-phosphate interacts with PfHsp70-1 and stabilizes the Plasmodium digestive vacuole under febrile temperatures.

The aging lineage of budding yeast is differentiated by an early-appearing protein deposit that promotes protein quality control.

A multiscale modeling approach reveals how the energy from ATP hydrolysis is used by Hsp70 chaperones to remodel the conformation of their substrates through a novel force-generating mechanism.

Reconstitution of interleukin-1β secretion in non-macrophage cells implicates how this pro-inflammatory cytokine enters into the unconventional pathway of secretion through autophagy.

Chaperones from different families and classes synergistically target different stages of tau aggregation, thus preventing pathological amyloid formation.

Specific and non-specific conformational confinement, via point mutation or cochaperone interaction or macro-molecular crowding, stimulates protein function in Hsp90 by reducing non-productive conformational flexibility.