Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Tabea C. Fricke"'
Autor:
Ruth A. Pumroy, Anna D. Protopopova, Tabea C. Fricke, Iris U. Lange, Ferdinand M. Haug, Phuong T. Nguyen, Pamela N. Gallo, Bárbara B. Sousa, Gonçalo J. L. Bernardes, Vladimir Yarov-Yarovoy, Andreas Leffler, Vera Y. Moiseenkova-Bell
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
A non-selective calcium channel transient receptor potential vanilloid 2 (TRPV2) is a potential drug target. Here, the authors employ cryo-electron microscopy, in silico docking, and electrophysiology to identify a binding site for an activator 2-ami
Externí odkaz:
https://doaj.org/article/d877302583004e29b65b3ecd87afcb21
Autor:
Tabea C. Fricke, Sebastian Pantke, Bjarne Lüttmann, Frank G. Echtermeyer, Christine Herzog, Mirjam J. Eberhardt, Andreas Leffler
Publikováno v:
British Journal of Pharmacology.
Autor:
Tabea C. Fricke, Frank Echtermeyer, Johannes Zielke, Jeanne de la Roche, Milos R. Filipovic, Stéphane Claverol, Christine Herzog, Makoto Tominaga, Ruth A. Pumroy, Vera Y. Moiseenkova-Bell, Peter M. Zygmunt, Andreas Leffler, Mirjam J. Eberhardt
Publikováno v:
Proc Natl Acad Sci U S A
Thermosensitive transient receptor potential (TRP) ion channels detect changes in ambient temperature to regulate body temperature and temperature-dependent cellular activity. Rodent orthologs of TRP vanilloid 2 (TRPV2) are activated by nonphysiologi
Gating of the capsaicin receptor TRPV1 by UVA-light and oxidants are mediated by distinct mechanisms
Publikováno v:
Cell Calcium. 96:102391
Redox-sensitivity is a common property of several transient receptor potential (TRP) ion channels. Oxidants and UVA-light activate TRPV2 by oxidizing methionine pore residues which are conserved in the capsaicin-receptor TRPV1. However, the redox-sen