The International Max Planck Research School for Chemical and Molecular Biology (IMPRS-CMB) is a collaboration between the Max Planck Institute of Molecular Physiology and three universities, the Technical University Dortmund (TU Dortmund), the Ruhr University Bochum (RUB) and the University of Duisburg-Essen (DUE).

All four institutes are located in the Ruhr Metropolitan Area of Germany, an extremely vibrant and culturally interconnected region. The same spirit is reflected in the science of our program: research groups, with different and often complementary approaches, combine their efforts to study at the molecular level basic cell physiology.

Below you can find all the research groups that are part of IMPRS-CMB, in alphabetical order. You can also search groups by name, topic or technique.

Read about OUR SCIENCE by visiting the webpages of our Faculty Members.


Prof. Dr. Markus Kaiser

Current Position: Full professor at the University of Duisburg-Essen, Essen, Germany.
Group Leader:
Independent Group Leader at the Chemical Genomics Centre of the Max-Planck-Society, Dortmund, Germany.
with Dr. M.-P. Teulade-Fichou and Prof. Dr. J.-M. Lehn, Collège de France, Paris, France.
with Prof. Dr. L. Moroder, Max-Planck-Institute of Biochemistry, Martinsried, Germany.

Research Interest
Our group is interested in elucidating the mode-of-action of bioactive compounds, in particular of natural products. To this end, we use preparative organic chemistry as well as chemical proteomics to synthesize, rationally modify and finally to identify the targets of natural products.

Natural product synthesis, (chemical) proteomics, activity-based protein profiling (ABPP), protein expression, enzyme assays

Selected Reading
Groll M, Schellenberg B, Bachmann AS, Archer CR, Huber R, Powell TK, Lindow S, Kaiser M, Dudler R. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature 2008, 452, 755-758.

Clerc J, Groll M, Illich DJ, Bachmann AS, Huber R, Schellenberg B, Dudler R, Kaiser M. Synthetic and structural studies on Syringolin A and B reveal critical determinants for selectivity and potency of proteasome inhibition. Proc Natl Acad Sci USA 2009, 106, 6507-6512.

Kaschani F, Clerc J, Krahn D, Bier D, Hong TN, Ottmann C, Niessen S, Colby T, van der Hoorn RA, Kaiser M. Identification of a selective, activity-based probe for GAPDHs. Angew Chem Int Ed 2012, 51, 5230-5233.

Stolze SC, Deu E, Kaschani F, Li N, Florea BI, Richau KH, Colby T, van der Hoorn RA, Overkleeft HS, Bogyo M, Kaiser M. The antimalarial natural product symplostatin 4 is a nanomolar inhibitor of the food vacuole falcipains. Chem Biol 2012, 19, 1546-1555.

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