Marion Schuller

Fulford Junior Research Fellow; Postdoctoral Researcher, Ivan Ahel Lab

Dr Schuller is a biochemist and structural biologist specialising in ADP-ribosylation research and drug discovery for antimicrobial and oncological targets.

Following a BSc and MSc in Pharmaceutical Sciences at the Ludwig Maximilian University, she obtained a DPhil in ‘Systems Approaches to Biomedical Science – Industrial Doctorate Centre’ at the University of Oxford under the supervision of Prof Stefan Knapp and Prof Benedikt Kessler, in collaboration with Novartis.

Dr Schuller investigated strategies to modify PARP14 function through macrodomain inhibition using a combination of biochemistry, structural biology and cell biology approaches. She subsequently joined the Ivan Ahel lab to pursue her interests in the development of inhibitors of ADP-ribosylation recognising modules and to study novel enzyme systems for the reversible ADP-ribosylation of DNA and their role in microbial pathogenicity.


Key Publications include:

Schuller, M., Raggiaschi, R., Mikolcevic, P., Rack, J.G.M., Ariza, A., Zhang, Y., Ledermann, R., Tang, C., Mikoc, A., Ahel, I. (2023) Molecular basis for the reversible ADP-ribosylation of guanosine bases. Molecular Cell 83 (13), P2303-2315;

Schuller, M.,* Correy, G.J.,* Gahbauer, S.,* Fearon, D.,* […], von Delft, F., Shoichet, B.K., Fraser, J.S., Ahel, I. (2021) Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking. Science Advances 7(6); doi:10.1126/sciadv.abf8711

Schuller, M., Butler, R.E., Ariza, A., Tromans-Coia, C., Jankevicius, G., Claridge, T.D.W., Kendall, S.L., Goh, S., Stewart, G.R., Ahel, I. (2021) Molecular basis for DarT ADP-ribosylation of a DNA base. Nature 596, 597–602;

Schuller, M., Riedel, K., Gibbs-Seymour, I., Uth, K., Sieg, Ch., Gehring, A.P., Ahel I, Bracher F., Kessler B.M., Elkins J.M., Knapp S. (2017) Discovery of a Selective Allosteric Inhibitor Targeting Macrodomain 2 of Poly(ADP)-ribose polymerase 14. ACS Chemical Biology 12, 2866-2874;
doi: 10.1021/acschembio.7b00445

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