Inhibition of ClpB, the bacterial representative of the heat-shock protein 100 family that is
associated with virulence of several pathogens, could be an effective strategy to develop …

This review focuses on the molecular chaperone ClpB that belongs to the Hsp100/Clp
subfamily of the AAA+ ATPases and its biological function in selected bacterial pathogens …

Bacterial survival within a mammalian host is contingent upon sensing environmental
perturbations and initiating an appropriate counter-response. To achieve this, sophisticated …

The ClpB–DnaK bichaperone system reactivates aggregated cellular proteins and is
essential for survival of bacteria, fungi, protozoa, and plants under stress. AAA+ ATPase …

The ClpB heat-shock protein is necessary for the survival of Escherichia coli cells upon
sudden increase of temperature. Using a PCR-based genomic walking method, the …

ClpL is a member of the HSP100 family of AAA+ chaperones that is widely present in Gram-
positive but surprisingly absent in Gram-negative bacteria. ClpL is involved in various …

Hsp100/Clp proteins are key players in the protein quality control network of prokaryotic
cells and function in the degradation and refolding of misfolded or aggregated proteins …

The ClpC ATPase is a subfamily of HSP100/Clp molecular chaperones–regulators of
proteolysis. By screening a library of loss of function mutants for the ability to survive …

In prokaryotic cells and eukaryotic organelles, the ClpP protease plays an important role in
proteostasis. The disruption of the ClpP function has been shown to influence the infectivity …

Eubacteria synthesize a full-length (ClpB95) and a N-terminally truncated (ClpB80) version
of the ClpB disaggregase owing to the presence of a translation initiation site within the clpB …