Malte Gersch accepted to the Young College of the NRW Academy of Sciences, Humanities and the Art
Malte Gersch's team is looking for new ways to develop innovative therapeutic approaches.
The “Junge Kolleg” was founded in 2006 by the North Rhine-Westphalian Academy of Sciences, Humanities and the Arts to promote excellent young researchers. They are supported professionally, financially as well as ideally. In addition, they are given the opportunity to discuss their projects in interdisciplinary working groups and to exchange ideas with renowned members of the Academy. Researchers from all disciplines as well as artists can be appointed to the “Junge Kolleg”. Beyond a doctorate they must meet the following requirements: outstanding academic achievements, must not be older than 36 and must not yet hold a permanent university teaching position.
"I am delighted and thankful to be accepted by the Academy and hope for the chance – depending on common interests - to communicate research more boradly," says Malte Gersch. He studied chemistry and biochemistry at LMU Munich. During a research stay at the Stanford School of Medicine, he got interested in chemical biology, whereupon he did his doctorate at the TU Munich with Stephan Sieber. There he worked on the function and inhibition of the bacterial proteasome ClpP. He was awarded the Hans Fischer Prize, the Friedrich Weygand Prize and the Emil Erlenmeyer Medal for his doctorate. During his postdoc in Cambridge, UK, with David Komander, his research focus was on the regulation and structure of human deubiquitinases. Since December 2018, he has been leading an independent Emmy Noether Junior Research Group at the Technical University Dortmund with a secondary affiliation to the Chemical Genomics Centre at the Max Planck Institute for Molecular Physiology in Dortmund.
Malte’s research team investigates how proteolytic enzymes operate in the ubiquitin system and exploits these insights towards novel therapeutic approaches. A major interest is on specialised proteases termed de-ubiquitinating enzymes, which selectively cleave the isopeptide bond between ubiquitin moieties in chains or between ubiquitin and substrate proteins. Aberrant ubiquitin-dependent signaling has been implicated in the development of cancer, neurodegenerative and inflammatory diseases. Recent efforts to modulate DUB activity with small molecules have shown this to be a powerful strategy, to amplify ubiquitin-dependent signaling and thereby alter key cellular processes, but compounds with high specificity and activity are lacking in many cases. The ultimate goal of the Gersch lab is to connect these proteolytic enzymes to pathologically relevant processes and to develop well-characterised small molecule tools to interrogate protein function in biological systems. To achieve these goals Malte’s Team combines chemical biology, organic chemistry, protein biochemistry, structural biology and cellular assays.