List of Publications Prof. Dr. Thomas Brüser
2018
Ringel, M. T., Dräger, G., & Brüser, T. (2018). PvdO is required for the oxidation of dihydropyoverdine as the last step of fluorophore formation in Pseudomonas fluorescens. Journal of Biological Chemistry, 293(7), 2330-2341.
Ringel, M. T., & Brüser, T. (2018). The biosynthesis of pyoverdines. Microbial Cell, 5(10), 424-437.
2017
Rathmann, C., Schlösser, A. S., Schiller, J., Bogdanov, M., & Brüser, T. (2017). Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid. FEBS letters, 591(18), 2848-2858.
Ringel, M. T., Dräger, G., & Brüser, T. (2017). The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to α-ketoglutaric acid. Journal of Biological Chemistry, 292(45), 18660-18671.
Thurotte, A., Brüser, T., Mascher, T., & Schneider, D. (2017). Membrane Chaperoning by Members of the PspA/IM30 Protein Family. Communicative & Integrative Biology, [e1264546].
2016
Ringel, M. T., Dräger, G., & Brüser, T. (2016). PvdN enzyme catalyzes a periplasmic pyoverdine modification. Journal of Biological Chemistry, 291(46), 23929-23938.
Stolle, P., Hou, B., & Brüser, T. (2016). The Tat substrate CueO is transported in an incomplete folding state. Journal of Biological Chemistry, 291(26), 13520-13528.
2015
Osadnik, H., Schöpfel, M., Heidrich, E., Mehner, D., Lilie, H., Parthier, C., Risselada, H. J., Grubmüller, H., Stubbs, M. T., & Brüser, T. (2015). PspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteins. Molecular Microbiology, 98(4), 743-759.
Taubert, J., Hou, B., Risselada, H. J., Mehner, D., Lünsdorf, H., Grubmüller, H., & Brüser, T. (2015). TatBC-Independent TatA/Tat substrate interactions contribute to transport efficiency. PLOS ONE, 10(3), [0119761].
2014
Behrendt, J., & Brüser, T. (2014). The TatBC complex of the Tat protein translocase in Escherichia coli and its transition to the substrate-bound TatABC complex. Biochemistry, 53(14), 2344-2354.