Protein kinase

The reversible phosphorylation of proteins is a key regulatory mechanism in the control of most cellular actions. More than 500 protein kinases serve as molecular switches that transmit extracellular signals and process information in human cells. Dysregulation of kinase activity plays a pivotal role in many diseases. In the recent years, protein kinase inhibitors have emerged as the most successful class of drugs based on the number of approvals for clinical use. Therefore, the functional characterization of protein kinases and the development of specific inhibitors is a major field of research in pharmacology.

My laboratory is specifically interested in the biochemical and cell biological investigation of the DYRK family of protein kinases, which have been discovered and intensively characterized by our group. The human gene for DYRK1A is localized on chromosome 21 and is overexpressed as consequence of trisomy 21. DYRK1A contributes to the altered brain development in individuals with Down syndrome and neurodegeneration in Alzheimer’s disease. DYRK1B plays an important role in tumor cell quiescence and resistance to cytostatic drugs in cancer therapy. My lab aims to develop selective inhibitors for the DYRK1A and DYRK1B to provide chemical probes for functional studies.


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