Lauber T - Search Results

1

On the seeding and oligomerization of pGlu-amyloid peptides (in vitro).

Schilling S, Lauber T, Schaupp M, Manhart S, Scheel E, Böhm G, Demuth HU. Schilling S, et al. Among authors: lauber t. Biochemistry. 2006 Oct 17;45(41):12393-9. doi: 10.1021/bi0612667. Biochemistry. 2006. PMID: 17029395

2

Detection of amyloid-beta oligomers in human cerebrospinal fluid by flow cytometry and fluorescence resonance energy transfer.

Santos AN, Torkler S, Nowak D, Schlittig C, Goerdes M, Lauber T, Trischmann L, Schaupp M, Penz M, Tiller FW, Böhm G. Santos AN, et al. Among authors: lauber t. J Alzheimers Dis. 2007 Mar;11(1):117-25. doi: 10.3233/jad-2007-11114. J Alzheimers Dis. 2007. PMID: 17361040

3

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

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

4

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: lauber t. Biochemistry. 2004 Sep 7;43(35):11238-47. doi: 10.1021/bi0492399. Biochemistry. 2004. PMID: 15366933

This chimeric protein was constructed to investigate the reasons for differences in the folds of the homologous LEKTI domains 1 and 6 [Lauber, T., et al. (2003) J. Mol. Biol. 328, 205-219]. In Dom1PI, two adjacent phenylalanine residues (F28 and F29) of domain 1 wer …

This chimeric protein was constructed to investigate the reasons for differences in the folds of the homologous LEKTI domains 1 and 6 [La …

5

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. Biochemistry. 2002 Dec 10;41(49):14602-12. doi: 10.1021/bi026434j. Biochemistry. 2002. PMID: 12463760

6

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

Lauber T, Neudecker P, Rösch P, Marx UC. Lauber T, et al. 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.

7

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

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

8

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: lauber t. 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

9

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. Protein Expr Purif. 2001 Jun;22(1):108-12. doi: 10.1006/prep.2001.1415. Protein Expr Purif. 2001. PMID: 11388807

10

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. J Mol Biol. 2003 Apr 18;328(1):205-19. doi: 10.1016/s0022-2836(03)00245-6. J Mol Biol. 2003. PMID: 12684009

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