Niko Schenck

This paper investigates how LonP1 protease uses ATP hydrolysis to regulate substrate translocation and proteolytic activation, showing that proteolysis of folded proteins requires ATP-driven unfolding and translocation.

The paper shows that human mitochondrial Lon protease degrades substrates starting from either terminus, with unidirectional processing, and provides structural and biochemical evidence for this mechanism.

This paper shows LonP1 inhibits fibrillar aggregate growth without ATPase activity, localizing chaperone function to its N-domain hexamer.