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

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.

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

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.

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.

Food overconsumption impairs cellular protein folding through a novel aging-related signaling pathway.

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.

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