We are primarily interested in studying the interactions of proteins and low-molecular substances in the topic of carcinogenesis and bacterial pathogenesis. Currently we realize our own projects involving structural characterization of kinases of essential role cancer, p53 pathway, bacterial proteases of unknown catalytic mechanism and staphylococcal proteases. In parallel to the crystallographic studies we also develop aptamer selection techniques (especially single-stranded DNA) against targets of importance in cancer. In addition to our own research, we are also involved in broad scientific collaboration and cooperation with the industry on other subjects whenever problem scan be solved by X-ray crystallography of proteins. We invite anyone interested in collaboration.

We study different translation control mechanisms, which regulate the production of specific sets of proteins by chemical modifications of tRNA molecules. Every protein in the cell is produced by the ribosome, which uses transfer RNA (tRNA) molecules to translate the sequence information coded in mRNAs into correctly assembled poly-peptide chains. The decoding/translation of genetic information is based on the recognition of a respective codon by its corresponding tRNA anticodon triplet.

The lab is focusing on understanding the molecular mechanisms that lead to the specific base modifications in anticodons of tRNAs. These modifications have a strong influence on the efficiency and accuracy of the codon-anticodon pairing and therefore regulate the translational rates and folding dynamics of protein synthesis. Recent findings have shown that alterations of these modification pathways play important roles in the onset of certain neurodegenerative diseases and cancer.