The overexpression of RNA chaperones, including several DEAD box RNA helicases, enhances the fitness of mutationally compromised E. coli strains.

NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.

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.

Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.

Cells accumulate damaged proteins during aging and, by compromising the function of chaperones in folding newly synthesized G1 cyclins, proteostasis breakdown inhibits cell-cycle entry and drives yeast cells into senescence.

Mechanistic insight into the chaperone-like activity of NMNAT to phosphorylated Tau reveals a connection between NAD⁺metabolism and Tau homeostasis.

Cytosolic and organellar Hsp90s from higher eukaryotes have evolved a variable, and environmentally responsive N-terminal extension to regulate their activity.

Quantitative dissection of the roles of chaperone binding and phosphorylation in regulating heat shock factor 1 leads to a predictive model of the dynamics of the yeast heat shock response.

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.

The endoplasmic reticulum (ER) folding sensor UGGT1 essentially cooperates with the peptide editor TAPBPR to provide quality control of MHC I molecules in the antigen presentation pathway.