Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.

Cell division imposes a limit on proteostasis capacity by reducing chaperone accumulation, but chaperone-substrate interactions reverse these events to allow clearance of even chronically misfolded protein amyloids.

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

Native state dynamics of mouse prion protein were measured, and these motions were shown to be having a role in initiation of aggregation.

The small molecule EMD 57033 is one of a new class of pharmacological chaperones that stabilize, enhance the activity of, and correct stress-induced misfolding of myosin proteins.

Biophysical modeling, performed in silico, can predict the abundance, metabolic stability, and function of MLH1 inside living cells.

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

The mechanism is revealed that connects the protein degradation machinery to cellular membrane-bound compartments during proteostasis stress in mammalian cells.

The mechanism identified here that mediates olanzapine-induced b-cell dysfunction should be considered, along with weight gain, in mitigating adverse side effects when patients with schizophrenia are prescribed olanzapine.