List of Publications Prof. Dr. Thomas Brüser

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Berthelmann, F., & Brüser, T. (2004). Localization of the Tat translocon components in Escherichia coli. FEBS Letters, 569(1-3), 82-88.


Brüser, T., & Sanders, C. (2003). An alternative model of the twin arginine translocation system. Microbiological Research, 158(1), 7-17.

Brüser, T., Yano, T., Brune, D. C., & Daldal, F. (2003). Membrane targeting of a folded and cofactor-containing protein. European Journal of Biochemistry, 270(6), 1211-1221.

Kipping, M., Lilie, H., Lindenstrauß, U., Andreesen, J. R., Griesinger, C., Carlomagno, T., & Brüser, T. (2003). Structural studies on a twin-arginine signal sequence. FEBS Letters, 550(1-3), 18-22.


Rose, R. W., Brüser, T., Kissinger, J. C., & Pohlschröder, M. (2002). Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Molecular Microbiology, 45(4), 943-950.


Brüser, T., Selmer, T., & Dahl, C. (2000). 'ADP sulfurylase' from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases. Journal of Biological Chemistry, 275(3), 1691-1698.


Brüser, T., Deutzmann, R., & Dahl, C. (1998). Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli. FEMS Microbiology Letters, 164(2), 329-336.

Reinartz, M., Tschäpe, J., Brüser, T., Trüper, H. G., & Dahl, C. (1998). Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum. Archives of Microbiology, 170(1), 59-68.


Brüser, T., Trüper, H. G., & Dahl, C. (1997). Cloning and sequencing of the gene encoding the high potential iron-sulfur protein (HiPIP) from the purple sulfur bacterium Chromatium vinosum. Biochimica et Biophysica Acta - Gene Structure and Expression, 1352(1), 18-22.


Strange, R. W., Dodd, F. E., Abraham, Z. H. L., Grossmann, J. G., Brüser, T., Eady, R. R., Smith, B. E., & Hasnain, S. S. (1995). The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase. Nature Structural Biology, 2(4), 287-292.


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