Publications
Lu, Y. *, Schuller, M. *, Bullen, N.P. *, Mikolcevic, P., Zonjic, I., Raggiaschi, R., Mikoc, A., Whitney, J.C. , Ahel, I. (2025) Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack. Nucleic Acids Research 53, gkaf069; https://doi.org/10.1093/nar/gkaf069
Cihlova, B., Lu, Y., Mikoc, A., Schuller, M. and Ahel, I. (2024) Specificity of DNA ADP-Ribosylation Reversal by NADARs. Toxins 16; https://doi.org/10.3390/toxins16050208
Kar, P., Chatrin, C., Dukic, N., Suyari, O., Schuller, M., Zhu, K., Prokhorova, E., Ahel, J., Clausen, T., Niepel, M., Persons, R., Sanyal, S., Ahel, D., Smith, R., Ahel, I. (2024) PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation. EMBO Journal 43(14); https://doi.org/10.1038/s44318-024-00126-0
Wondisford, A.R., Lee, J., Lu, R., Schuller, M., Groslambert, J., Schmaus-Hayes, S., Opresko, P.L., Pickett, H., Ahel, I., O’Sullivan1, R.J. (2024) Deregulated DNA ADP-Ribosylation impairs telomere replication. Nature Structural & Molecular Biology 31(5); https://doi.org/10.1038/s41594-024-01279-6
Đukić1, N. *, Strømland, Ø*, Damgaard Elsborg, J., Munnur, D., Zhu, K., Schuller, M., Chatrin, C., Kar, P., Duma, L., Suyari, O., et al. (2023) PARP14 is a PARP with both ADP-ribosyltransferase and hydrolase activities. Science Advances 9(37), eadi2687; https://doi.org/10.1126/sciadv.adi2687
Suskiewicz, M.J., Munnur, D., Strømland, Ø., Yang, J., Easton, L.E., Chatrin, C.,Zhu, K., Baretić, D., Goffinont, S., Schuller, M., Wu, W., Elkins, J. M., 5 , Ahel, D., Sanyal, S., Neuhaus, D., and Ahel, I. (2023) Updated protein domain annotation of the PARP protein family sheds new light on biological function. Nucleic Acids Research 51(15), 8217-8236; https://doi.org/10.1093/nar/gkad514
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; https://doi.org/10.1016/j.molcel.2023.06.013
Longarini, E.J., Dauben, H., Locatelli, C., Wondisford, A.R., Smith, R., Muench, C., Kolvenbach, A., Lynskey, M.L., Pope, A., Bonfiglio, J.J., Pinto Jurado, E., Fajka-Boja, R., Colby, T., Schuller, M., Ahel, I., Timinszky, G., J O’sullivan, R., Huet, S., Matic, I. (2023) Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling. Molecular Cell 83, 1743–1760; https://doi.org/10.1016/j.molcel.2023.03.027
Schuller, M., Zarganes-Tzitzikas, T., Bennett, J., De Cesco, S., Fearon, D., von Delft, F., Fedorov, O., E. Brennan, P., Ahel, I. (2023) Discovery and development strategies for SARS-CoV-2 NSP3 macrodomain inhibitors. Pathogens 12 (2), 324; https://doi.org/10.3390/pathogens12020324
Gahbauer, S.*, Correyb, G.J.*, Schuller, M., Ferlad, M.P., Dorukf, Y.U., Rachmana, M., Wug, T., Diolaitif, M., Wangh, S., Neitzi, R.J., et al. (2023). Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 macrodomain of SARS-CoV-2. PNAS 120(2) e2212931120; https://doi.org/10.1073/pnas.2212931120
Hloušek-Kasun, A., Mikolčević, P., Rack, J.G.M., Tromans-Coia, C., Schuller, M., Jankevicius, G., Matković, M., Bertoša, B., Ahel, I., and Mikoč, A. (2022). Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA. Computational and Structural Biotechnological Journal 20, 4337–4350; https://doi.org/10.1016/j.csbj.2022.08.002
Schuller, M. & Ahel, I. (2022) Beyond protein modification: The rise of non-canonical ADP-ribosylation. Review for The Biochemical Journal 479, 463–477; https://doi.org/10.1042/BCJ20210280
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; https://doi.org/10.1038/s41586-021-03825-4
Bajusz, D., Wade, W.S., Satała, G., Bojarski, A.J., Ilaš, J., Ebner, J., Grebien, F., Papp, H., Jakab, F., Douangamath, A., Fearon, D., von Delft, F., Schuller, M., Ahel, I., Wakefield, A., Vajda, S., Gerencsér, J., Pallai, P., Keserű, G.M. (2021) Exploring protein hotspots by optimized fragment pharmacophores. Nature Communication 12(1), 3201; https://doi.org/10.1038/s41467-021-23443-y
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), eabf8711; https://doi.org/10.1126/sciadv.abf8711
Rack, J.G.M., Zorzini, V., Zhu, Z., Schuller, M., Ahel, D., Ahel, I. (2020) Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential. Open Biology 10(11); https://doi.org/10.1098/rsob.200237
Moustakim, M.,* Riedel, K.,* Schuller, M., Gehring, A., Monteiro, O., Martin, S., Fedorov, O., Heer, J., Dixon, D., Elkins, J.M., Knapp, S., Bracher, F., Brennan, P. (2018) Discovery of a novel allosteric inhibitor scaffold for polyadenosine-diphosphateribose polymerase 14 (PARP14) macrodomain 2. Bioorganic and Medicinal Chemistry 26, 2965–2972; https://doi.org/10.1016/j.bmc.2018.03.020
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; https://doi.org/10.1021/acschembio.7b00445
Schuller, M., Höfner, G. & Wanner, K.T. (2017) Simultaneous Multiple MS Binding Assays
Addressing D1 and D2 Dopamine Receptors. ChemMedChem 12(19):1585-1594; https://doi.org/10.1002/cmdc.201700369; highlighted as cover story of this issue.
Froese, D.S.*, Kopec, J.*, Fitzpatrick, F.*, Schuller, M., McCorvie, T.J., Chalk, R., Plessl, T., Fettelschoss, V., Fowler, B., Baumgartner, M.R. & Yue, W.W. (2015) Structural Insights into the MMACHC-MMADHC Protein Complex Involved in Vitamin B12 Trafficking. Journal of Biological Chemistry 290(49): 29167–29177; https://doi.org/10.1074/jbc.M115.683268