Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Peter Mühlhahn"'
Autor:
Laura Snaidr, Peter Mühlhahn, Claudia Beimfohr, Christian Kreuzer, Carolin Richly, Jiri Snaidr
Publikováno v:
Frontiers in Microbiology, Vol 15 (2024)
This study introduces an optimized integration of flow cytometry and fluorescence in situ hybridization (Flow-FISH) as an approach for the specific enumeration of gram-positive bacteria in probiotic products, overcoming the limitations of conventiona
Externí odkaz:
https://doaj.org/article/8eaf522563f94132bfd9e0c54764403e
Autor:
T.A. Holak, Julia Georgescu, Christian Renner, J. Bernhagen, Michael Czisch, R. Bucala, Alfred Ross, Peter Mühlhahn
Publikováno v:
Protein Science. 5:2095-2103
Human macrophage migration inhibitory factor is a 114 amino acid protein that belongs to the family of immunologic cytokines. Assignments of 1H, 15N, and 13C resonances have enabled the determination of the secondary structure of the protein, which c
Autor:
Bianca Habermann, Robert Morenweiser, Richard A. Engh, Peter Mühlhahn, Tad A. Holak, Christian P. Sommerhoff, Michael Czisch, Ennes A. Auerswald
Publikováno v:
FEBS Letters. 355:290-296
The three-dimensional solution structure of the leech derived tryptase inhibitor form C (LDTI-C), an inhibitor of 46 amino acids which contains 3 disulfide bridges, has been determined using 2D NMR spectroscopy. The 3D structure was determined on the
Autor:
Stefan Palme, Wojciech Zeslawski, Friederike Hesse, Silke Hansen, Wolfgang Voelter, Mariusz Kamionka, Christian Klein, Raphael Stoll, Anja Belling, Peter Mühlhahn, Till Rehm, Christian Renner, Ralf Schumacher, Richard A. Engh, Tad A. Holak, Kaluza Brigitte
Publikováno v:
Biochemistry. 40(2)
The oncoprotein MDM2 inhibits the tumor suppressor protein p53 by binding to the p53 transactivation domain. The p53 gene is inactivated in many human tumors either by mutations or by binding to oncogenic proteins. In some tumors, such as soft tissue
Autor:
Tad A. Holak, Markus Zweckstetter, Martin Lanzendörfer, Cornelia Ciosto, Michael Baier, Peter Mühlhahn, Dorothee Ambrosius, Christian Renner, Kurt Lang, Reinhard Kurth, Julia Georgescu
Publikováno v:
Nature Structural and Molecular Biology
The structure of a folded core of IL-16 is similar to that of intracellular protein modules called PDZ domains. IL-16 is thus the first extracellular protein found to have a PDZ-like fold. However, it does not exhibit normal peptide binding propertie