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.

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.

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

Human cells adapt to chronic mild stresses, such as slightly elevated temperature, by getting larger in a process that couples increased translation to increased cell size in an Hsp90-dependent manner.

An exploration of the unanswered questions in how the molecular chaperone Hsp90 supports protein homeostasis, and how single-molecule techniques could drive future breakthroughs in answering them.

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.

Protein biosynthesis and protein quality control jointly determine protein production costs.

Unique integrate stress response sensors differentially trigger pro-survival versus pro-apoptotic responses in cells confronted with Hsp70 inhibitor-associated proteotoxic challenges.

Direct modification by endogenous peroxide of a conserved cysteine in the molecular chaperone BiP decouples its ATPase and peptide-binding activities, allowing for enhanced polypeptide holdase activity during oxidative stress.

Quantitative time-resolved crosslinking mass spectrometry is developed to monitor protein interactions and dynamics inside molecular condensates and used to identify misfolding of the RNA-binding domain of FUS as a key driver of condensate-aging.