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 …

We introduce a nonintrusive method exploiting single-cell variability after cell division to
validate protein localization. We found that Clp proteases, widely reported to form …

The aggregation of proteins as a result of intrinsic or environmental stress may be
cytoprotective, but is also linked to pathophysiological states and cellular ageing. We …

Members of the AAA+ protein superfamily contribute to many diverse aspects of protein
homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic …

A novel class of antibiotic acyldepsipeptides (designated ADEPs) exerts its unique
antibacterial activity by targeting the peptidase caseinolytic protease P (ClpP). ClpP forms …

Protein modifications not only affect protein homeostasis but can also establish new cellular
protein functions and are important components of complex cellular signal sensing and …

Reversible protein phosphorylation is an important and ubiquitous protein modification in all
living cells. Here we report that protein phosphorylation on arginine residues plays a …

Energy-dependent protein degradation is carried out by bipartite assemblies of conserved
architecture. A chaperone ring comprising ATPase domains of the AAA+-type caps both …

Bacterial cells are frequently exposed to dramatic fluctuations in their environment, which
cause perturbation in protein homeostasis and lead to protein misfolding. Bacteria have …