Madl Group

Medical University Graz

Integrated Structural Biology & Metabolism Research

Who we are

Tobias Madl and his team at the Gottfried Schatz Research Center at the Medical University of Graz investigate the molecular mechanisms of how disordered proteins mediate intracellular transport and phase separation of RNA-binding proteins via protein interactions and post-translational modifications. He employs metabolomics and integrative structural biology, molecular modeling, and biophysical methods. T. Madl has studied nuclear export complexes (PMID: 21442693 & 20972448), discovered a novel nuclear import mechanism (PMID: 23333309), discovered links between import cargo recognition, arginine methylation and disease (PMID: 22968170 & 26895297), and found that the importins transportin-1 and transportin-3 can act as molecular chaperones suppressing phase separation and that these mechanisms are regulated by arginine methylation (PMID: 29677514 & 32234784).

Moreover, Tobias Madl has made important contributions to the field of disordered proteins, integrative structural biology and signal transduction over the past years. He was the first to show that surface accessibility data obtained from paramagnetic relaxation enhancements can be used for structure determination of proteins (PMID 27560616 & 28710477 & 31297688). This led him to propose to use NMR surface accessibility data for various aspects of biomolecular structure determination, which is becoming a well-accepted concept in integrative structural biology. With the toolbox of methodology in his hands, he addressed several key biological research questions related to the (patho)physiology of dynamic regulatory processes (PMID 24581495 & 30876805 & 27723736 & 29662162 & 28281558 & 25851214).

At the Integrative Metabolism Research Center (founded by TM), T. Madl and his team established untargeted NMR-based metabolomics for a plethora of biological systems ranging from cell-based assays to in vivo model systems and patients (PMID 31471173 & 30122555 & 30279548 & 31043697). This allows him to bridge the gap between molecular details of metabolic pathways and patient and vice versa and to obtain new insights into disease mechanisms and diagnosis.

His work has been recognized by several awards, including the Research Price of the Styrian Government (2017), and the Science Award (2012) of the Austrian Chemical Society, the most prestigious award for young scientists across all Chemistry disciplines in Austria.

Why/How are we going Green

We want to reduce our ecological footprint by reducing and recycling our plastic waste, choosing more sustainable products where possible and lowering the energy consumption of the lab by raising the temperature of our -80°C freezers to -70°C.

Group Page