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Ingrid Fleming

Institute for vascular Signalling
Goethe University, Frankfurt
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Research Interests
Ingrid Fleming (born in Northern Ireland) obtained her BSc in Biochemistry and Pharmacology at Aston University in England and her PhD at the Louis Pasteur University in Strasbourg, France. She is currently Chair of the Institute for Vascular Signalling at the Johann Wolfgang Goethe University in Frankfurt, Germany. Research focuses on the elucidation of signal transduction mechanisms in the vessel wall, in particular in the endothelium and on the generation of several “autacoids”; including nitric oxide (NO) and cytochrome P450-derived lipid mediators. Current work addresses changes in eNOS phosphorylation associated with the development of type 2 diabetes.

Selected Recent Publications

  • Fisslthaler, B., Fleming, I., Keserü, B., Walsh, K. & Busse, R. (2007). Fluid shear stress and NO decrease the activity of the hydroxy-methylglutaryl coenzyme A reductase in endothelial cells via the AMP-activated protein kinase and FoxO1. Circ Res 100, e12-e21.
  • Fisslthaler, B., Loot, A. E., Mohamed, A., Busse, R. & Fleming, I. (2008). Inhibition of endothelial nitric oxide synthase activity by proline-rich tyrosine kinase 2 in response to fluid shear stress and insulin. Circ Res 102, 1520-1528.
  • Loot, A. E., Schreiber, J. G., Fisslthaler, B. & Fleming, I. (2009). Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase. J Exp Med 206, 2889-2896.
  • Randriamboavonjy, V., Isaak, J., Fromel, T., Viollet, B., Fisslthaler, B., Preissner, K. T. & Fleming, I. (2010). AMPK a2 subunit is involved in platelet signaling, clot retraction, and thrombus stability. Blood 116, 2134-2140.
  • Bess, E., Fisslthaler, B., Frömel, T. & Fleming, I. (2011). Nitric oxide-induced activation of the AMP-activated protein kinase a2 subunit attenuates IkB kinase activity and inflammatory responses in endothelial cells. PLoS ONE 6, e20848.




POLICY STATEMENT: Biomedicine and Molecular Biosciences Action BM1005 is funded by COST, through its implementing agent the European Science Foundation.