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.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.

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

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.

Integration of complementary computational approaches reveals an evolutionarily conserved interaction interface between molecular chaperones Hsp70 and Hsp40, rationalizing previous observations.

Environmental conditions strongly impact the fitness effects of Hsp90, resulting in the selection of Hsp90 sequences in nature that are robust to a variety of stressful conditions.

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

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.

Dynamic regulation of the heat shock response depends on a negative feedback loop in which Hsf1 activates expression of Hsp70 and Hsp70 specifically and directly represses Hsf1 transactivation.

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