Contact information
CV
Academic education
| 2014 - 2020 | Graduate studies in Biology/Genetics, supervisor: Prof. Dr. Hamid Kashkar, University of Cologne, Germany |
| 2011 - 2014 | Studies in Biology (M. Sc.), University of Cologne, Germany |
| 2012 | Internship in the Gyrd-Hansen Lab during Masters, University of Copenhagen, Denmark |
| 2007 - 2011 | Studies in Biology (B. Sc.), University of Cologne, Germany |
Scientific degrees
| 2020 | Ph.D in Genetics, supervisor: Prof. H. Kashkar, University of Cologne, Germany |
Scientific career
| 2022 - present | Junior Research Group Leader, Cancer Research Center Cologne Essen (CCCE), Institute for Molecular Immunology, University of Cologne, Germany |
| 2020 - 2022 | Postdoctoral Research Fellow. Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Germany |
Honors/ Awards/ Memberships
| 2025 - present | Member of the Editorial Advisory Board of The FEBS Journal |
| 2019 - present | Supervisor Master-module “Cell Death in Inflammation, Immunity and Disease”, University of Cologne, Germany |
Publications
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Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis
Caspase-8 is the initiator caspase of extrinsic apoptosis1,2 and inhibits necroptosis mediated by RIPK3 and MLKL. Accordingly, caspase-8 deficiency in mice causes embryonic lethality3, which can be rescued by deletion of either Ripk3 or Mlkl4,5,6. Here we show that the expression of enzymatically…
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Mitochondrial respiration controls neoangiogenesis during wound healing and tumour growth
The vasculature represents a highly plastic compartment, capable of switching from a quiescent to an active proliferative state during angiogenesis. Metabolic reprogramming in endothelial cells (ECs) thereby is crucial to cover the increasing cellular energy demand under growth conditions. Here we…
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Proteolytic activation of executioner caspase-3 and -7 regulates different physiological processes in mice
Caspase-3 (CASP3) and caspase-7 (CASP7) are the two major executioner caspases that are proteolytically activated by upstream initiator caspases. They possess almost indistinguishable activity, which has led to the overall view that these caspases have functionally redundant roles. Here, we generate…