Heat shock proteins (Hsps) are conserved molecules whose main role is to facilitate folding
of other proteins. Most Hsps are generally stress-inducible as they play a particularly …

Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Heat causes protein misfolding and aggregation and, in eukaryotic cells, triggers
aggregation of proteins and RNA into stress granules. We have carried out extensive …

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

Bacteria often encounter temperature fluctuations in their natural habitats and must adapt to
survive. The molecular response of bacteria to sudden temperature upshift or downshift is …

Protein aggregation occurs as a consequence of perturbations in protein homeostasis that
can be triggered by environmental and cellular stresses. The accumulation of protein …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

Composed of up to 1,000 phospho-anhydride bond-linked phosphate monomers, inorganic
polyphosphate (polyP) is one of the most ancient, conserved, and enigmatic molecules in …

Cells are faced with the task of folding thousands of different polypeptides into a wide range
of conformations. For many proteins, the folding process requires the action of molecular …