Marx UC - Search Results

1

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.

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

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

4

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.

5

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.

6

Side chain contributions to the interconversion of the topological isomers of guanylin-like peptides.

Schulz A, Marx UC, Tidten N, Lauber T, Hidaka Y, Adermann K. Schulz A, et al. Among authors: marx uc. J Pept Sci. 2005 Jun;11(6):319-30. doi: 10.1002/psc.625. J Pept Sci. 2005. PMID: 15635659

7

Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI.

Lauber T, Marx UC, Schulz A, Kreutzmann P, Rösch P, Hoffmann S. Lauber T, et al. Among authors: marx uc. Protein Expr Purif. 2001 Jun;22(1):108-12. doi: 10.1006/prep.2001.1415. Protein Expr Purif. 2001. PMID: 11388807

8

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

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

Design and characterization of a soluble fragment of the extracellular ligand-binding domain of the peptide hormone receptor guanylyl cyclase-C.

Lauber T, Tidten N, Matecko I, Zeeb M, Rösch P, Marx UC. Lauber T, et al. Among authors: marx uc. Protein Eng Des Sel. 2009 Jan;22(1):1-7. doi: 10.1093/protein/gzn062. Epub 2008 Nov 5. Protein Eng Des Sel. 2009. PMID: 18987130

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