About Ute
Research Focus
Dr. Ute C. Marx has over 16 years experience in high-resolution NMR (nuclear magnetic
resonance) spectroscopy, and completed her PhD (1996) and "Habilitation" (2003) in
biophysical chemistry. The main focus of her research is protein structure determination
and metabonomics, where she is specialised in the determination of metabolic variations
associated with different phenotypes. The international standard of her research is
reflected by 21 entries in the protein data bank (PDB), 30 publications in peer-reviewed
international scientific journals, as well as 5 book contributions and numerous oral and
poster presentations on international conferences. In August 2008 Dr. Marx joined the
company Bruker BioSpin GmbH, the leading global developer and manufacturer of NMR
systems and solutions. One focus of her work is Metabonomics. Metabonomics is the
study of biofluids in order to identify subtle metabolic changes related to altered
phenotype. Data acquisition is mainly carried out with NMR spectroscopy and followed
by statistical/chemometric data analysis.
Key Projects
Within the Solar Bio Fuel Consortium we harness the technique of NMR based
Metabonomics to identify metabolite differences between different phases of algal
growth (aerobic, anaerobic, microoxic) within one strain, and to compare algal strains
with different H2 producing capabilities. Furthermore, we use NMR spectroscopy to
monitor the metabolite flows from water and carbohydrates to hydrogen. This research
will allow the identification of the metabolic pathways involved and will assist in the
determination of the bottlenecks of hydrogen production. The gained knowledge will
facilitate targeted metabolic engineering of H2 production by engineering critical end
point and regulatory genes.
Publications
2011
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].
2009
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).
2008
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).
2007
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).
2006
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).
2005
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).
2004
Jayakumar, A., Kang, Y., Mitsudo, K., Henderson, Y., Frederick, M.J., Wang, M., ElNaggar, 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).
2003
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).
2002
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).
2001
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).
2000
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).
1999
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 nearphysiological solution. FEBS Lett., 444: 239-244 (1999).
1998
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 stabilizes the topological stereoisomers of
guanylin. J. Pept. Res., 52: 518-525 (1998).
1997
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).
1995
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).