Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ayk Waldow"'
Autor:
Edward N. Schmidt, Dimitra Lamprinaki, Kelli A. McCord, Maju Joe, Mirat Sojitra, Ayk Waldow, Jasmine Nguyen, John Monyror, Elena N. Kitova, Fahima Mozaneh, Xue Yan Guo, Jaesoo Jung, Jhon R. Enterina, Gour C. Daskhan, Ling Han, Amanda R. Krysler, Christopher R. Cromwell, Basil P. Hubbard, Lori J. West, Marianne Kulka, Simonetta Sipione, John S. Klassen, Ratmir Derda, Todd L. Lowary, Lara K. Mahal, Meghan R. Riddell, Matthew S. Macauley
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Abstract Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands. Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing the complex behaviors of glycolipids in a membrane. Throug
Externí odkaz:
https://doaj.org/article/1b849c2f9a814c4e9507f12b5f5f0d43
Autor:
Ayk Waldow, Laura-Sophie Beier, Janine Arndt, Simon Schallenberg, Claudia Vollbrecht, Philip Bischoff, Martí Farrera-Sal, Florian N. Loch, Christian Bojarski, Michael Schumann, Lars Winkler, Carsten Kamphues, Lukas Ehlen, Jörg Piontek
Publikováno v:
Pharmaceutics, Vol 15, Iss 7, p 1980 (2023)
Claudins regulate paracellular permeability, contribute to epithelial polarization and are dysregulated during inflammation and carcinogenesis. Variants of the claudin-binding domain of Clostridium perfringens enterotoxin (cCPE) are highly sensitive
Externí odkaz:
https://doaj.org/article/dd7af9b4ff8a4d9d825bc64bed3e2388
Autor:
Laura‐Sophie Beier, Ayk Waldow, Saeed Khomeijani Farahani, Roman Mannweiler, Sabine Vidal‐Y‐Sy, Johanna M. Brandner, Jörg Piontek, Dorothee Günzel
Publikováno v:
Annals of the New York Academy of Sciences. 1517:251-265
Tight junction (TJ) formation is vital for epidermal barrier function. We aimed to specifically manipulate TJ barriers in the reconstructed human epidermis (RHE) by claudin-1 and -4 knockdown (KD) and by claudin-binding fusion proteins of glutathione
Publikováno v:
ChemCatChem. 10:407-414
Recently, the enzyme family of oleate hydratases (OHs: EC 4.2.1.53) have gained a rising scientific and economic interest, as these FAD-binding bacterial enzymes do not require cofactor recycling and feature high thermal and pH stability. Their produ
Publikováno v:
ChemCatChem. 10:336-336