Cell-based high-throughput screening identifies IBT21 as a chemical chaperone, that inhibits ER protein aggregation and prevents the cell death caused by a proteotoxin, the aggregation-prone prion protein.

Lab-evolved 'super Spy' chaperones show enhanced flexibility, which allows them to bind to and stabilize proteins more effectively than natural chaperones.

Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.

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.

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

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

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.

A dedicated structural element facilitates chaperone and antigenic peptide selector function of TAP-associated glycoprotein, a major quality assurance auditor in adaptive immunity.

A combined NMR and kinetic study demonstrates how the dynamic transition of a molecular chaperone between different oligomerization states can modulate its activity by altering the binding kinetics and energetics of non-native proteins.

SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.