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

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

  3. U.C. Marx, K. Adermann, P. Bayer, M. Meyer, W.G. Forssmann, P. Rösch. (1998) Structure-activity relation of NH2-terminal human parathyroid hormone fragments. J Biol Chem 273: 4308-4316.

  4. U.C. Marx, J. Klodt, M. Meyer, H. Gerlach, P. Rösch, W.G. Forssmann, K. Adermann. (1998) One peptide, two topologies: structure and interconversion dynamics of human uroguanylin isomers. J Pept Res 52: 229-240.

  5. A. Schulz, S. Escher, U.C. Marx, M. Meyer, P. Rösch, W.G. Forssmann, K. Adermann. (1998) Carboxy-terminal extension stabilizes the topological stereoisomers of guanylin. J Pept Res 52: 518-525.

  6. A. Schulz, U.C. Marx, Y. Hidaka, Y. Shimonishi, P. Rösch, W.G. Forssmann, K. Adermann. (1999) Role of the prosequence of guanylin. Protein Sci 8: 1850-1859.

  7. M. Weidler, U.C. Marx, G. Seidel, W. Schäfer, E. Hoffmann, A. Esswein, P. Rösch. (1999) The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution. FEBS Lett 444: 239-244.

  8. U.C. Marx, K. Adermann, P. Bayer, W.G. Forssmann, P. Rösch. (2000) 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.

  9. S. Urban, C. Schwarz, U.C. Marx, H. Zentgraf, H. Schaller, G. Multhaup. (2000) Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction. Embo J 19: 1217-1227.

  10. T. Lauber, U.C. Marx, A. Schulz, P. Kreutzmann, P. Rösch, S. Hoffmann. (2001) 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.

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

  12. T. Lauber, P. Neudecker, P. Rösch, U.C. Marx.(2003) Solution structure of human proguanylin: the role of a hormone prosequence. J Biol Chem 278: 24118-24124.

  13. T. Lauber, A. Schulz, K. Schweimer, K. Adermann, U.C. Marx. (2003) 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.

  14. U.C. Marx, M.L. Korsinczky, H.J. Schirra, A. Jones, B. Condie, L. Otvos, Jr., D.J. Craik. (2003) 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.

  15. J. Ziegler, H. Sticht, U.C. Marx, W. Muller, P. Rösch, S. Schwarzinger. (2003) 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.

  16. A. Jayakumar, Y. Kang, K. Mitsudo, Y. Henderson, M.J. Frederick, M. Wang, A.K. El-Naggar, U.C. Marx, K. Briggs, G.L. Clayman. (2004) 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.

  17. T. Lauber, A. Schulz, P. Rösch, and U.C. Marx. (2004) Role of disulfide bonds for the structure and folding of proguanylin. Biochemistry 43: 10050-10057.

  18. H. Tidow, T. Lauber, K. Vitzithum, C.P. Sommerhoff, P. Rösch, U.C. Marx. (2004) The solution structure of a chimeric LEKTI domain reveals a chameleon sequence.Biochemistry 43: 11238-11247.

  19. T. Egelrud, M. Brattsand, P. Kreutzmann, M. Walden, K. Vitzithum, U.C. Marx, W.G. Forssmann, H.J. Mägert. (2005) hK5 and hK7, two serine proteinases abundant in human skin, are inhibited by LEKTI domain 6. Br J Dermatol 153: 1200-1203.

  20. T. Lauber, U.C. Marx. (2005) Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin. Protein Pept Lett 12: 153-158.

  21. A. Schulz, U.C. Marx, N. Tidten, T. Lauber, Y. Hidaka, K. Adermann. (2005) Side chain contributions to the interconversion of the topological isomers of guanylin-like peptides. J Pept Sci 11: 319-330.

  22. U.C. Marx, N.L. Daly, D.J. Craik. (2005) NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids. Magn Reson Chem 44: S41-50.

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

  24. K. Vitzithum, T. Lauber, P. Kreutzmann, A. Schulz, C.P. Sommerhoff, P. Rösch, U.C. Marx. LEKTI Domain 15 is a Functional Kazal-Type Proteinase Inhibitor, Protein Expression and Purification In Press, Accepted Manuscript.