The AAA+-ATPases are a family of molecular motors which have been seconded into a
plethora of cellular tasks. One subset, the Hsp100 molecular chaperones, are general …

The ring-forming AAA+ protein ClpB cooperates with the DnaK chaperone system to refold
aggregated proteins in Escherichia coli. The M domain, a ClpB-specific coiled-coil structure …

The oligomeric AAA+ chaperones Hsp104 in yeast and ClpB in bacteria are responsible for
the reactivation of aggregated proteins, an activity essential for cell survival during severe …

Large protein machines are tightly regulated through allosteric communication channels.
Here we demonstrate the involvement of ultrafast conformational dynamics in allosteric …

While phosphotyrosine modification is an established regulatory mechanism in eukaryotes,
it is less well characterized in bacteria due to low prevalence. To gain insight into the extent …

Hsp100 chaperones cooperate with the Hsp70 chaperone system to disaggregate and
reactivate heat-denatured aggregated proteins to promote cell survival after heat stress. The …

Non-destructive dissagregation of protein aggregates is a formidable task mediated by the
specialized AAA+ chaperone Hsp104/ClpB in combination with the Hsp70/DnaK chaperone …

It has been recently shown that in some proteins, tertiary‐structure dynamics occur
surprisingly fast, that is on the microsecond or sub‐millisecond time scales. In this State of …

ClpB is a hexameric chaperone that solubilizes and reactivates protein aggregates in
cooperation with the Hsp70/DnaK chaperone system. Each of the identical protein …

Reactivation of intracellular protein aggregates after a severe stress is mandatory for cell
survival. In bacteria, this activity depends on the collaboration between the DnaK system …