L. Sohn-Bösser

Ectoine-Induced Proteins in Sinorhizobium meliloti Include an Ectoine ABC-Type Transporter Involved in Osmoprotection and Ectoine Catabolism

E. Bremer, M. Jebbar, L. Sohn-Bösser, 2005, Journal of bacteriology.

Crystal Structures of the Choline/Acetylcholine Substrate-binding Protein ChoX from Sinorhizobium meliloti in the Liganded and Unliganded-Closed States*

E. Bremer, S. Smits, L. Schmitt, 2008, Journal of Biological Chemistry.

Biochemical and Structural Analysis of the Bacillus subtilis ABC Transporter OpuA and Its Isolated Subunits

E. Bremer, L. Schmitt, Carsten Horn, 2006, Journal of Molecular Microbiology and Biotechnology.

Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine.

J. Breed, W. Welte, E. Bremer, 2006, Journal of molecular biology.

Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state.

H. Gohlke, E. Bremer, S. Smits, 2011, Journal of molecular biology.

Crystal structure of the ligand-binding protein EhuB from Sinorhizobium meliloti reveals substrate recognition of the compatible solutes ectoine and hydroxyectoine.

E. Bremer, L. Schmitt, M. Jebbar, 2007, Journal of molecular biology.