Marx UC - Search Results

1

Solution structure of human proguanylin: the role of a hormone prosequence.

Lauber T, Neudecker P, Rösch P, Marx UC. Lauber T, et al. Among authors: marx uc. J Biol Chem. 2003 Jun 27;278(26):24118-24. doi: 10.1074/jbc.M300370200. Epub 2003 Apr 21. J Biol Chem. 2003. PMID: 12707255 Free article.

2

Native and recombinant proguanylin feature identical biophysical properties and are monomeric in solution.

Lauber T, Nourse A, Schulz A, Marx UC. Lauber T, et al. Among authors: marx uc. Biochemistry. 2002 Dec 10;41(49):14602-12. doi: 10.1021/bi026434j. Biochemistry. 2002. PMID: 12463760

3

CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.

Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S. Ziegler J, et al. Among authors: marx uc. J Biol Chem. 2003 Dec 12;278(50):50175-81. doi: 10.1074/jbc.M305234200. Epub 2003 Sep 2. J Biol Chem. 2003. PMID: 12952977 Free article.

4

Role of disulfide bonds for the structure and folding of proguanylin.

Lauber T, Schulz A, Rösch P, Marx UC. Lauber T, et al. Among authors: marx uc. Biochemistry. 2004 Aug 10;43(31):10050-7. doi: 10.1021/bi049667e. Biochemistry. 2004. PMID: 15287732 Free article.

5

The solution structure of a chimeric LEKTI domain reveals a chameleon sequence.

Tidow H, Lauber T, Vitzithum K, Sommerhoff CP, Rösch P, Marx UC. Tidow H, et al. Among authors: marx uc. Biochemistry. 2004 Sep 7;43(35):11238-47. doi: 10.1021/bi0492399. Biochemistry. 2004. PMID: 15366933

6

Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin.

Lauber T, Marx UC. Lauber T, et al. Among authors: marx uc. Protein Pept Lett. 2005 Feb;12(2):153-8. doi: 10.2174/0929866053005836. Protein Pept Lett. 2005. PMID: 15723641 Review.

7

Structure-activity relation of NH2-terminal human parathyroid hormone fragments.

Marx UC, Adermann K, Bayer P, Meyer M, Forssmann WG, Rösch P. Marx UC, et al. J Biol Chem. 1998 Feb 20;273(8):4308-16. doi: 10.1074/jbc.273.8.4308. J Biol Chem. 1998. PMID: 9468478 Free article.

8

Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI.

Lauber T, Schulz A, Schweimer K, Adermann K, Marx UC. Lauber T, et al. Among authors: marx uc. J Mol Biol. 2003 Apr 18;328(1):205-19. doi: 10.1016/s0022-2836(03)00245-6. J Mol Biol. 2003. PMID: 12684009

9

LEKTI domain 15 is a functional Kazal-type proteinase inhibitor.

Vitzithum K, Lauber T, Kreutzmann P, Schulz A, Sommerhoff CP, Rösch P, Marx UC. Vitzithum K, et al. Among authors: marx uc. Protein Expr Purif. 2008 Jan;57(1):45-56. doi: 10.1016/j.pep.2007.08.012. Epub 2007 Sep 5. Protein Expr Purif. 2008. PMID: 17936012

10

Structure of human parathyroid hormone 1-37 in solution.

Marx UC, Austermann S, Bayer P, Adermann K, Ejchart A, Sticht H, Walter S, Schmid FX, Jaenicke R, Forssmann WG, et al. Marx UC, et al. J Biol Chem. 1995 Jun 23;270(25):15194-202. doi: 10.1074/jbc.270.25.15194. J Biol Chem. 1995. PMID: 7797503 Free article.

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