Publications 2026

ZORA Publication List

Publications

• Kechagia, Z., & Medalia, O. (2026). High-resolution nuclear cell biology by cryo-electron tomography Nucleus, 17, 2675754. https://doi.org/10.1080/19491034.2026.2675754
• Dalle Vedove, A., Cazzanelli, G., D’Agostino, V. G., Vargas Rosales, P. A., Caflisch, A., & Lolli, G. (2026). Unusual backfolded binding poses of BAZ2A bromodomain binders Acta Crystallographica. Section D: Structural Biology, 82, 776–784. https://doi.org/10.1107/S2059798326004596
• Häfliger, A., Briand, S., Furler, S., Dreier, B., & Plückthun, A. (2026). Semi-automated Ribosome Display for High-Throughput DARPin Binder Selection New Biotechnology, online. https://doi.org/10.1016/j.nbt.2026.06.007
• Suomalainen, M., Haenseler, W., Kolibius, J., Plückthun, A., Hearing, P., & Greber, U. F. (2026). Transcriptional transactivation turns human iPSC-derived macrophages into an adenovirus-producing cell state Journal of Virology, 100, e00392-26. https://doi.org/10.1128/jvi.00392-26
• Münick, P., Balourdas, D.-I., Funk, J. S., Yüksel, B., Mavridi, D., Heftel, J., Dreier, B., Schaefer, J. V., Schäfer, B., Knapp, S., Telatar, T., Akgül, B., Plückthun, A., Stiewe, T., Joerger, A. C., & Dötsch, V. (2026). DARPins as pan-reactivators of temperature-sensitive p53 cancer mutants Proceedings of the National Academy of Sciences of the United States of America, 123, e2531747123. https://doi.org/10.1073/pnas.2531747123
• Liu, B., Spalinger, M. R., Invernizzi, A., Gerdes, E., Steglich, B., Schwarzfischer, M., Machicote, A., Pelczar, P., Pöhlmann, D., Nawrocki, M., Böttcher, M., Aleko, A., Velasquez, L. N., Wende, S., Stallbaum, F., Neuendorff, J., Grosshauser, S., Muscate, F., Douilhet, G., … Caflisch, A. (2026). Indirect inhibition of the NLRP3-interleukin-1β axis contributes to the efficacy of JAK1 inhibitors in experimental colitis and human ulcerative colitis Nature Communications, 17, 5429. https://doi.org/10.1038/s41467-026-71808-y
• Ortiz-López, D., Hove, T. T., Huhn, C., Camuso, S., van Gen Hassend, P. M., Sander, B., Campbell, B. F. N., Tyagarajan, S. K., Plückthun, A., Specht, C. G., Maric, H. M., Böttcher, B., & Schindelin, H. (2026). Cryo-EM structures of higher order Gephyrin oligomers reveal principles of inhibitory postsynaptic scaffold organization Nature Communications, 17, 3541. https://doi.org/10.1038/s41467-026-71771-8
• Matter, C. M., & Caflisch, A. (2026). Fine-Tuning a Transformer Model for METTL3 Lead Optimization ACS Bio & Med Chem Au, 6, 160–167. https://doi.org/10.1021/acsbiomedchemau.5c00198
• Corbeski, I., Bedi, R. K., Matter, C. M., Stamm, F., Bochenkova, E., Herok, M., Hartshorn, M. J., & Caflisch, A. (2026). Ligand-Induced Opening of a Cryptic Pocket in METTL14 ACS Bio & Med Chem Au, 6, 130–144. https://doi.org/10.1021/acsbiomedchemau.5c00184
• Ratnayake, D., Galloux, M., Boersma, S., Noerenberg, M., Sizun, C., Sacristan, C., Sourimant, J., Lakerveld, A. J., Gelderloos, A. T., Apperloo, L., Demyanenko, Y., Baars, M. J. D., Banerjee, R., Dreier, B., Furler, S., Mazur, N. I., Bont, L. J., Mohammed, S., Plückthun, A., … Tanenbaum, M. E. (2026). Pre-assembly of biomolecular condensate seeds drives RSV replication Nature, 652, 189–200. https://doi.org/10.1038/s41586-025-10071-5
• Ghafouri, H., Kadeřávek, P., Melo, A. M., Aspromonte, M. C., Bernadó, P., Cortés, J., Dosztányi, Z., Erdős, G., Feig, M., Janson, G., Lindorff-Larsen, K., Mulder, F. A. A., Nagy, P., Pestell, R., Piovesan, D., Schiavina, M., Schuler, B., Sibille, N., Tesei, G., … Monzon, A. M. (2026). Toward a unified framework for determining conformational ensembles of disordered proteins Nature Methods, 23, 705–719. https://doi.org/10.1038/s41592-026-03003-2
• Andricioaei, I., Best, R. B., Birge, R. R., Boresch, S., Brunger, A., Brooks, B. R., Buck, M., Brüschweiler, R., Caflisch, A., Case, D. A., Cui, Q., Dejaegere, A., Dinner, A. R., Elber, R., Evanseck, J. D., Gao, J., Guo, H., Hubbard, R. E., Kuriyan, J., … et al. (2026). The scientific legacy of Martin Karplus from the perspective of his collaborators Biophysical Journal, online. https://doi.org/10.1016/j.bpj.2026.03.050
• Bedi, R. K., & Caflisch, A. (2026). A DNA-Based Binding Assay for the mA-RNA Reader Proteins Chembiochem, 27, e202500897. https://doi.org/10.1002/cbic.202500897
• Ivanović, M., Holla, A., Nüesch, M. F., Von Roten, V., Schuler, B., & Best, R. B. (2026). Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins JACS Au, 6, 1900–1913. https://doi.org/10.1021/jacsau.5c01753
• Phillips, M., Holla, A., Wojtas, M., Chowdhury, A., Sottini, A., König, S. L. B., Mutter, N., Lamb, N., Huihui, J., Lopko, M., Soranno, A., Nettels, D., Ożyhar, A., Schuler, B., & Ghosh, K. (2026). Mapping Charge Interactions in Intrinsically Disordered Proteins Advanced Science, 13, e14056. https://doi.org/10.1002/advs.202514056
• Ren, L., Zhang, H., Bobileva, O., Nai, F., Bi, H., Chan, A., Baker, G. E., Dong, L., Guarin, D., Hu, W., Li, W., Leite, I., Wang, X., Zhang, X., Xue, M., Wang, H., Qin, H., Wu, X., Ghoda, L. Y., … Caflisch, A. (2026). Targeting the METTL1/m⁷G axis as a therapeutic strategy in myeloid leukemia Blood, 147, 3069–3085. https://doi.org/10.1182/blood.2025030336
• Pelea, O., Tálas, A., Fernández Carrera, J., Mathis, N., van de Venn, L., Yeh, C. D., Kulcsár, P. I., Marquart, K. F., Weber, Y., Gerecke, S. E., Harvey-Seutcheu, I. F., Mailänder, D., Pfleiderer, M. M., Chanez, C., Corn, J. E., Schwank, G., & Jinek, M. (2026). Programmable genome editing in human cells using RNA-guided bridge recombinases Science, 391, eadz1884. https://doi.org/10.1126/science.adz1884
• Vukovic, D., Winkelvoß, D., Udovcic, A., Riermeier, L., Jaime-Figueroa, S., Crews, C. M., & Plückthun, A. (2026). Quantitative Degradation Rate Assessment of bioPROTACs Based on Peptide Degrons, E3 Domains, Adapters and Conjugated Small Molecules ACS Chemical Biology, 21, 62–73. https://doi.org/10.1021/acschembio.5c00569
• Cruz, A. R., Wimmer, B. H., Teo, T. H., Pehau-Arnaudet, G., Winter, J.-M., Gazi, A. D., Lafaye, P., Brier, S., Legrand, A., Dubrovsky-Gaupp, A., Bérard, M., Aymé, G., Sartori-Rupp, A., Medalia, O., & Schnupf, P. (2026). Segmented filamentous bacteria undergo a structural transition at their adhesive tip during unicellular to filament development Nature Communications, 17, 222. https://doi.org/10.1038/s41467-025-66892-5