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ADP-ribosylation: Function, structure and inhibition

My research revolves around ADP-ribosyltransferases, which cleave NAD+ to link ADP-ribose
to their target proteins. This flags these target proteins for specific activities in our cells.
A number of human enzymes, the PARP enzymes, catalyze this reaction. PARP enzymes
are drug targets: Drugs that inhibit PARP activity are already in use today in treatment of
certain forms of cancer. We want to understand enzymatic mechanisms and improve the fit
of PARP inhibitors to their enzymatic pockets. This will lead to more potent, more selective
drugs in the future. Some bacterial toxins, produced by pathogenic bacteria, have the same
activity. We hope to create inhibitors also for their activities, with the aim of creating new
anti-infective drugs. We also study bacterial toxin-antitoxin (TA) systems to understand their

structure and function.

 

Principal investigator: Herwig Schüler