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Beate Fisslthaler
Researcher at Goethe University Frankfurt
Publications - 85
Citations - 12773
Beate Fisslthaler is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Endothelial stem cell & Endothelium. The author has an hindex of 47, co-authored 84 publications receiving 12131 citations. Previous affiliations of Beate Fisslthaler include St. Vincent's Institute of Medical Research.
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Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Stefanie Dimmeler,Ingrid Fleming,Beate Fisslthaler,Corinna Hermann,Rudi Busse,Andreas M. Zeiher +5 more
TL;DR: It is demonstrated that the serine/threonine protein kinase Akt/PKB mediates the activation of eNOS, leading to increased NO production, and represents a novel Ca2+-independent regulatory mechanism for activation ofeNOS.
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Cytochrome P450 2C is an EDHF synthase in coronary arteries
Beate Fisslthaler,Rüdiger Popp,Ladislau Kiss,Michael Potente,David R. Harder,Ingrid Fleming,Rudi Busse +6 more
TL;DR: It is shown that the induction of cytochrome P450 (CYP) 2C8/34 in native porcine coronary artery endothelial cells by β-naphthoflavone enhances the formation of 11,12-epoxyeicosatrienoic acid, as well as EDHF-mediated hyperpolarization and relaxation.
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Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity.
TL;DR: It is suggested that the dual phosphorylation of Ser1177 and Thr495 determines the activity of eNOS in agonist-stimulated endothelial cells.
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Nitric Oxide Modulates the Expression of Monocyte Chemoattractant Protein 1 in Cultured Human Endothelial Cells
TL;DR: No modulates MCP-1 expression and monocyte chemotactic activity secreted by human umbilical vein endothelial cells (HUVECs) in culture, and the activation of NF-kappa B-like transcriptional regulatory proteins by inhibition of NO suggests a molecular link between an oxidant-sensitive transcriptional Regulatory mechanism and NO synthesis in HUV ECs.
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Endothelium-Derived Hyperpolarizing Factor Synthase (Cytochrome P450 2C9) Is a Functionally Significant Source of Reactive Oxygen Species in Coronary Arteries
Ingrid Fleming,U. Ruth Michaelis,Daniel Bredenkötter,Beate Fisslthaler,Faramarz Dehghani,Ralf P. Brandes,Rudi Busse +6 more
TL;DR: The results suggest that a CYP isozyme homologous to CYP 2C9 is a physiologically relevant generator of ROS in coronary endothelial cells and modulates both vascular tone and homeostasis.