Dr. Ute Marx

Bruker BioSpin
Fax: 49-721-516-1297
Email: [email protected]

Ute Marx



Keller, M.D., Pollitt, C.C., Marx, U.C. Nuclear magnetic resonance-based metabonomic study of early time point laminitis in an oligofructose-overload model. Equine Vet. J. (2011) Mar 15. doi: 10.1111/j.2042-3306.2010.00336.x. [Epub ahead of print].


Spraul, M., Schütz, B., Rinke, P., Koswig, S., Humpfer, E., Schäfer, H., Mörtter, M., Fang, F., Marx, U.C., & Minoja, A. NMR-Based Multi Parametric Quality Control of Fruit Juices: SGF Profiling. Nutrients, 1: 148-155 (2009).
Timmins, M., Zhou, W., Rupprecht, J., Lim, L., Thomas-Hall, S.R., Doebbe, A., Kruse, O., Hankamer, B., Marx, U.C., Smith, S.M., & Schenk, P.M. The Metabolome of Chlamydomonas reinhardtii following Induction of Anaerobic H2 Production by Sulfur Depletion. J. Biol. Chem., 284: 23415-23425 (2009).
Timmins, M., Thomas-Hall, S.R., Darling, A., Zhang, E., Hankamer, B., Marx, U.C., & Schenk, P.M. Phylogenetic and molecular analysis of hydrogen-producing green algae. J. Exp. Bot., 60: 1691-1702 (2009).
Daly, N.L., Chen, Y.K., Rosengren, K.J., Marx, U.C., Phillips, M.L., Waring, A.J., Wang, W., Lehrer, R.I., & Craik, D.J. Retrocyclin-2: a potent anti-HIV theta-defensin that forms a cyclic cystine ladder structural motif. Adv. Exp. Med. Biol., 611: 577-578 (2009).
Lauber, T., Tidten, N., Matecko, I., Zeeb, M., Rösch, P., & Marx, U.C. Design and characterization of a soluble fragment of the extracellular ligand-binding domain of the peptide hormone receptor guanylyl cyclase-C. Protein Eng. Des. Sel., 22: 1-7 (2009).


Vitzithum, K., Lauber, T., Kreutzmann, P., Schulz, A., Sommerhoff, C.P., Rösch, P., & Marx, U.C. LEKTI domain 15 is a functional Kazal-type proteinase inhibitor. Protein Expr. Purif., 57: 45-56 (2008).
Schenk, P., Thomas-Hall, S., Stevens, E., Marx, U., Mussgnug, J., Posten, C., Kruse, O. & Hankamer, B. Second Generation Biofuels: High-efficiency microalgae for biodiesel production. Bioenergy Research, 1: 20-43 (2008).


Daly, N.L., Chen, Y.K., Rosengren, K.J., Marx, U.C., Phillips, M.L., Waring, A.J., Wang, W., Lehrer, R.I., & Craik, D.J. Retrocyclin-2: Structural Analysis of a Potent Anti-HIV theta-Defensin. Biochemistry, 46: 9920-9928 (2007).


Marx, U.C., Daly, N.L., & Craik, D.J. NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids. Magn. Reson. Chem., 44: S41-50 (2006).


Egelrud, T., Brattsand, M., Kreutzmann, P., Walden, M., Vitzithum, K., Marx, U.C., Forssmann, W.G., & Mägert, H.J. hK5 and hK7, two serine proteinases abundant in human skin, are inhibited by LEKTI domain 6. Br. J. Dermatol., 153: 1200-1203 (2005).
Lauber, T., & Marx, U.C. Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin. Protein Pept. Lett., 12: 153-158 (2005).
Schulz, A., Marx, U.C., Tidten, N., Lauber, T., Hidaka, Y., & Adermann, K. Side chain contributions to the interconversion of the topological isomers of guanylin-like peptides. J. Pept. Sci., 11: 319-330 (2005).


Jayakumar, A., Kang, Y., Mitsudo, K., Henderson, Y., Frederick, M.J., Wang, M., El-Naggar, A.K., Marx, U.C., Briggs, K., & Clayman, G.L. Expression of LEKTI domains 6-9' in the baculovirus expression system: recombinant LEKTI domains 6-9' inhibit trypsin and subtilisin A. Protein Expr. Purif., 35: 93-101 (2004).
Lauber, T., Schulz, A., Rösch, P., & Marx, U.C. Role of disulfide bonds for the structure and folding of proguanylin. Biochemistry, 43: 10050-10057 (2004).
Tidow, H., Lauber, T., Vitzithum, K., Sommerhoff, C.P., Rösch, P., & Marx, U.C. The solution structure of a chimeric LEKTI domain reveals a chameleon sequence. Biochemistry, 43: 11238-11247 (2004).


Lauber, T., Neudecker, P., Rösch, P., & Marx, U.C. Solution structure of human proguanylin: the role of a hormone prosequence. J. Biol. Chem., 278: 24118-24124 (2003).
Lauber , T., Schulz, A., Schweimer, K., Adermann, K., & Marx, U.C. Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI. J. Mol. Biol., 328: 205-219 (2003).
Marx, U.C., Korsinczky, M.L., Schirra, H.J., Jones, A., Condie, B., Otvos, L., Jr., & Craik, D.J. Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide.J. Biol. Chem., 278: 21782-21789 (2003).
Ziegler, J., Sticht, H., Marx, U.C., Müller, W., Rösch, P., & Schwarzinger, S. CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process. J. Biol. Chem., 278: 50175-50181 (2003).


Lauber, T., Nourse, A., Schulz, A., & Marx, U.C. Native and recombinant proguanylin feature identical biophysical properties and are monomeric in solution. Biochemistry, 41: 14602-14612 (2002).


Lauber, T., Marx, U.C., Schulz, A., Kreutzmann, P., Rösch, P., & Hoffmann S. Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI. Protein Expr. Purif., 22: 108-112 (2001).


Marx, U.C., Adermann, K., Bayer, P., Forssmann, W.G., & Rösch, P. Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37). Biochem. Biophys. Res. Commun., 267: 213-220 (2000).
Urban, S., Schwarz, C., Marx, U.C., Zentgraf, H., Schaller, H., & Multhaup, G. Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction. Embo J., 19: 1217-1227 (2000).


Schulz, A., Marx, U.C., Hidaka, Y., Shimonishi, Y., Rösch, P., Forssmann, W.G., & Adermann, K. Role of the prosequence of guanylin. Protein Sci., 8: 1850-1859 (1999).
Weidler, M., Marx, U.C., Seidel, G., Schäfer, W., Hoffmann, E., Esswein, A., & Rösch P. The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution. FEBS Lett., 444: 239-244 (1999).


Marx, U.C., Adermann, K., Bayer, P., Meyer, M., Forssmann, W.G., & Rösch, P. Structure-activity relation of NH2-terminal human parathyroid hormone fragments.J. Biol. Chem., 273: 4308-4316 (1998).
Marx, U.C., Klodt, J., Meyer, M., Gerlach, H., Rösch, P., Forssmann, W.G., & Adermann K. One peptide, two topologies: structure and interconversion dynamics of human uroguanylin isomers. J. Pept. Res., 52: 229-240 (1998).
Schulz, A., Escher, S., Marx, U.C., Meyer, M., Rösch, P., Forssmann, W.G., & Adermann, K. Carboxy-terminal extension stabilises the topological stereoisomers of guanylin. J. Pept. Res., 52: 518-525 (1998).


Klodt, J., Kuhn, M., Marx, U.C., Martin, S., Rösch, P., Forssmann, W.G., & Adermann, K. Synthesis, biological activity and isomerism of guanylate cyclase C-activating peptides guanylin and uroguanylin. J. Pept. Res., 50: 222-230 (1997).


Marx, U.C., Austermann, S., Bayer, P., Adermann, K., Ejchart, A. ,Sticht, H., Walter, S., Schmid, F.X., Jaenicke, R., Forssmann, W.G., & Rösch P. Structure of human parathyroid hormone 1-37 in solution. J. Biol. Chem., 270: 15194-15202 (1995).