Researcher Portfolio
Jukna, Sarah
Research Group Biospheric Theory and Modelling, Dr. A. Kleidon, Max Planck Institute for Biogeochemistry
Researcher Profile
Position: Research Group Biospheric Theory and Modelling, Dr. A. Kleidon, Max Planck Institute for Biogeochemistry
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons191714
Publications
(1 - 25 of 240)
: Ghosh Dastidar, N., Freyer, N. S., Petrychenko, V., de A. P. Schwarzer, A. C., Peng, B.-Z., Samatova, E., Kothe, C., Schmidt, M., Peske, F., Politi, A. Z., Urlaub, H., Fischer, N., Rodnina, M. V., & Wohlgemuth, I. (2025). Selective silencing of antibiotic-tethered ribosomes as a resistance mechanism against aminoglycosides. Nature Communications, 16: 9568. doi:10.1038/s41467-025-65298-7. [PubMan] : Poulis, P., & Rodnina, M. V. (2025). Mechanisms and Determinants of −1 Ribosome Frameshifting and Bypassing. Cold Spring Harbor Perspectives in Biology. doi:10.1101/cshperspect.a041946. [PubMan] : Wang, S., Bitran, A., Samatova, E., Shakhnovich, E. I., & Rodnina, M. V. (2025). Cotranslational protein folding through non-native structural intermediates. Science Advances, 11(36): eady2211. doi:10.1126/sciadv.ady2211. [PubMan] : Lee, J. H., Rabl, L., Gamerdinger, M., Goyal, V., Khakzar, K. M., Barbosa, N. M., Abramovich, J., Morales-Polanco, F., Köhler, A.-K., Samatova, E., Rodnina, M. V., Deuerling, E., & Frydman, J. (2025). NAC controls nascent chain fate through tunnel sensing and chaperone action. bioRxiv. doi:10.1101/2025.07.27.667080. [PubMan] : Ford, J. J., Santos-Aberturas, J., Hems, E. S., Sallmen, J. W., Bögeholz, L. A. K., Polturak, G., Osbourn, A., Wright, J. A., Rodnina, M. V., Vereecke, D., Francis, I. M., & Truman, A. W. (2025). Identification of the lydiamycin biosynthetic gene cluster in a plant pathogen guides structural revision and identification of molecular target. Proceedings of the National Academy of Sciences of the United States of America, 122(21): e2424388122. doi:10.1073/pnas.2424388122. [PubMan] : Weller, C., Bartok, O., McGinnis, C. S., Palashati, H., Chang, T.-G., Malko, D., Shmueli, M. D., Nagao, A., Hayoun, D., Murayama, A., Sakaguchi, Y., Poulis, P., Khatib, A., Erlanger Avigdor, B., Gordon, S., Cohen Shvefel, S., Zemanek, M. J., Nielsen, M. M., Boura-Halfon, S., Sagie, S., Gumpert, N., Yang, W., Alexeev, D., Kyriakidou, P., Yao, W., Zerbib, M., Greenberg, P., Benedek, G., Litchfield, K., Petrovich-Kopitman, E., Nagler, A., Oren, R., Ben-Dor, S., Levin, Y., Pilpel, Y., Rodnina, M. V., Cox, J., Merbl, Y., Satpathy, A. T., Carmi, Y., Erhard, F., Suzuki, T., Buskirk, A. R., Olweus, J., Ruppin, E., Schlosser, A., & Samuels, Y. (2025). Translation dysregulation in cancer as a source for targetable antigens. Cancer Cell, 43(5), 823-840.e18. doi:10.1016/j.ccell.2025.03.003. [PubMan] : Thongdee, N., Alaniz, M. M., Samatova, E., Zhong, A., Esnault, C., Zhang, H., Dale, R. K., Rodnina, M. V., & Storz, G. (2025). Modulation of protein activity by small RNA base pairing internal to coding sequences. Molecular Cell, 85(9), 1824-1837.e7. doi:10.1016/j.molcel.2025.03.014. [PubMan] : Petrychenko, V., Yi, S.-H., Liedtke, D., Peng, B.-Z., Rodnina, M. V., & Fischer, N. (2025). Structural basis for translational control by the human 48S initiation complex. Nature Structural & Molecular Biology, 32, 62-72. doi:10.1038/s41594-024-01378-4. [PubMan] : Ford, J. J., Santos-Aberturas, J., Hems, E. S., Sallmen, J. W., Bögeholz, L. A. K., Polturak, G., Osbourn, A., Wright, J. A., Rodnina, M. V., Vereecke, D., Francis, I. M., & Truman, A. W. (2024). Discovery of lydiamycin A biosynthetic gene cluster in the plant pathogen Rhodococcus fascians guides structural revision and identification of molecular target. bioRxiv. doi:10.1101/2024.11.13.623425. [PubMan] : Mudryi, V., Frister, J. O., Peng, B.-Z., Wohlgemuth, I., Peske, F., & Rodnina, M. V. (2024). Kinetic mechanism and determinants of EF-P recruitment to translating ribosomes. Nucleic Acids Research, 52(19), 11870-11883. doi:10.1093/nar/gkae815. [PubMan] : Filipek, K., Blanchet, S., Molestak, E., Zaciura, M., Wu, C.-C.-C., Horbowicz-Drożdżal, P., Grela, P., Zalewski, M., Kmiecik, S., González-Ibarra, A., Krokowski, D., Latoch, P., Starosta, A. L., Mołoń, M., Shao, Y., Borkiewicz, L., Michalec-Wawiórka, B., Wawiórka, L., Kubiński, K., Socała, K., Wlaź, P., Cunningham, K. W., Green, R., Rodnina, M. V., & Tchórzewski, M. (2024). Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors. EMBO Reports, 25, 5478-5506. doi:10.1038/s44319-024-00297-1. [PubMan] : Bandyra, K. J., Fröhlich, K. S., Vogel, J., Rodnina, M. V., Goyal, A., & Luisi, B. (2024). Cooperation of regulatory RNA and the RNA degradosome in transcript surveillance. Nucleic Acids Research, 52(15), 9161-9173. doi:10.1093/nar/gkae455. [PubMan] : Lewis, K., Lee, R. E., Brötz-Oesterhelt, H., Hiller, S., Rodnina, M. V., Schneider, T., Weingarth, M., & Wohlgemuth, I. (2024). Sophisticated natural products as antibiotics. Nature, 632(8023), 39-49. doi:10.1038/s41586-024-07530-w. [PubMan] : Komar, A., Samatova, E., & Rodnina, M. V. (2024). Translation Rates and Protein Folding. Journal of Molecular Biology, 436(14): 168384. doi:10.1016/j.jmb.2023.168384. [PubMan] : Jäger, N., Pöhlmann, S., Rodnina, M. V., & Ayyub, S. A. (2024). Interferon-Stimulated Genes that Target Retrovirus Translation. Viruses, 16(6): 933. doi:10.3390/v16060933. [PubMan] : Senyushkina, T., Samatova, E., Klimova, M., & Rodnina, M. V. (2024). Kinetics of programmed and spontaneous ribosome sliding along the mRNA. Nucleic Acids Research, 52(11), 6507-6517. doi:10.1093/nar/gkae396. [PubMan] : Haase, N., Holtkamp, W., Christ, S., Heinemann, D., Rodnina, M. V., & Rudorf, S. (2024). Decomposing bulk signals to reveal hidden information in processive enzyme reactions: A case study in mRNA translation. PLOS Computational Biology, 20(3): e1011918. doi:10.1371/journal.pcbi.1011918. [PubMan] : Rodnina, M. V. (2024). Peptidyl-tRNA hydrolase as a key player in the liberation of truncated nascent chains from the ribosomal subunit. Molecular Cell, 84(4), 614-615. doi:10.1016/j.molcel.2024.01.017. [PubMan] : Samatova, E., Komar, A., & Rodnina, M. V. (2024). How the ribosome shapes cotranslational protein folding. Current Opinion in Structural Biology, 84: 102740. doi:10.1016/j.sbi.2023.102740. [PubMan] : Jäger, N., Ayyub, S. A., Peske, F., Liedtke, D., Bohne, J., Hoffmann, M., Rodnina, M. V., & Pöhlmann, S. (2024). The Inhibition of Gag-Pol Expression by the Restriction Factor Shiftless Is Dispensable for the Restriction of HIV-1 Infection. Viruses, 16(4): 583. doi:10.3390/v16040583. [PubMan] : Helm, M., Bohnsack, M., Carell, T., Dalpke, A., Entian, K.-D., Ehrenhofer-Murray, A., Ficner, R., Hammann, C., Höbartner, C., Jäschke, A., Jeltsch, A., Kaiser, S., Klassen, R., Leidel, S., Marx, A., Mörl, M., Meier, J., Meister, G., Rentmeister, A., Rodnina, M. V., Roignant, J.-Y., Schaffrath, R., Stadler, P., & Stafforst, T. (2023). Experience with German Research Consortia in the Field of Chemical Biology of Native Nucleic Acid Modifications. ACS Chemical Biology, 18(12), 2441-2449. doi:10.1021/acschembio.3c00586. [PubMan] : Jain, S., Koziej, L., Poulis, P., Kaczmarczyk, I., Gaik, M., Rawski, M., Ranjan, N., Glatt, S., & Rodnina, M. V. (2023). Modulation of translational decoding by m6A modification of mRNA. Nature Communications, 14: 4784. doi:10.1038/s41467-023-40422-7. [PubMan] : Rodnina, M. V. (2023). Decoding and Recoding of mRNA Sequences by the Ribosome. Annual Review of Biophysics, 52, 161-182. doi:10.1146/annurev-biophys-101922-072452. [PubMan] : Poulis, P., Peske, F., & Rodnina, M. V. (2023). The many faces of ribosome translocation along the mRNA: reading frame maintenance, ribosome frameshifting and translational bypassing. Biological Chemistry, 404(8-9), 755-767. doi:10.1515/hsz-2023-0142. [PubMan] : Han, W., Peng, B.-Z., Wang, C., Townsend II, G. E., Barry, N. A., Peske, F., Goodman, A. L., Liu, J., Rodnina, M. V., & Groisman, E. A. (2023). Gut colonization by Bacteroides requires translation by an EF-G paralog lacking GTPase activity. EMBO Journal, 42(2): e112372. doi:10.15252/embj.2022112372. [PubMan]