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Structure (London, England : 1993)|November 14, 2002
Periplasmic chaperones--new structural and functional insightsSusanne BehrensCell|June 6, 2003
Periplasmic chaperones--preservers of subunit folding energy for organelle assemblySusanne BehrensInternational Journal of Medical Microbiology : IJMM|May 8, 2010
The role of SurA factor in outer membrane protein transport and virulenceSusanne Behrens-KneipBMC Microbiology|October 6, 2010
PpiD is a player in the network of periplasmic chaperones in Escherichia coliYvonne Matern, Birgitta Barion, Susanne Behrens-KneipALTEX|February 15, 2001
[Development of an in vitro assay for the detection of Botulinum Neurotoxins]Frank Gessler, Susanne Behrens, Petra Loch, et al.Biochemistry|April 23, 2009
Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence studyJian Qu, Susanne Behrens-Kneip, Otto Holst, et al.The Journal of Biological Chemistry|January 2, 2003
Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharidePaula V Bulieris, Susanne Behrens, Otto Holst, et al.Protein Engineering, Design & Selection : PEDS|September 6, 2005
A ToxR-based two-hybrid system for the detection of periplasmic and cytoplasmic protein-protein interactions in Escherichia coli: minimal requirements for specific DNA binding and transcriptional activationFrank Hennecke, Arne Müller, Roland Meister, et al.Journal of Molecular Biology|October 12, 2007
The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactionsJian Qu, Christoph Mayer, Susanne Behrens, et al.Biochemistry|September 29, 2009
The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potentialGeetika J Patel, Susanne Behrens-Kneip, Otto Holst, et al.Pageof 2