J. Sawa

Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins

R. Huber, K. Mechtler, M. Ehrmann, 2008, Proceedings of the National Academy of Sciences.

Structural basis for the regulated protease and chaperone function of DegP

H. Saibil, M. Ehrmann, T. Clausen, 2008, Nature.

The 1.3 Å Crystal Structure of the Flavoprotein YqjM Reveals a Novel Class of Old Yellow Enzymes*

G. Bourenkov, T. Clausen, P. Macheroux, 2005, Journal of Biological Chemistry.

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

H. Saibil, M. Ehrmann, H. Malet, 2011, Nature Structural &Molecular Biology.

Molecular Adaptation of the DegQ Protease to Exert Protein Quality Control in the Bacterial Cell Envelope*

Tim Clausen, M. Ehrmann, H. Malet, 2011, The Journal of Biological Chemistry.

HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues

R. Huber, T. Clausen, T. Krojer, 2010, Nature Structural &Molecular Biology.

Molecular transformers in the cell: lessons learned from the DegP protease-chaperone.

M. Ehrmann, A. Heuck, T. Clausen, 2010, Current opinion in structural biology.

Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress.

R. Kurzbauer, M. Ehrmann, T. Clausen, 2007, Genes & development.