Department of Molecular Biology and Genetics

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Peer-reviewed publications at MBG - 2025

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Tzivelekidis, T., Jank, T., Pohl, C., Schlosser, A., Rospert, S., Knudsen, C. R., Rodnina, M., Belyi, Y. & Aktories, K. (2011). Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases. PLoS One, 6(12), e29525. https://doi.org/10.1371/journal.pone.0029525
Turyna, B., Osyczka, A., Kostrzewa, A., Blicharski, W., Enghild, J. J. & Froncisz, W. (1998). Preparation and electron paramagnetic resonance characterization of spin labeled monoderivatives of horse cytochrome c. BBA General Subjects, 1386(1), 50-8.
Turtola, M., Manav, C. M., Kumar, A., Tudek, A., Mroczek, S., Krawczyk, P. S., Dziembowski, A., Schmid, M., Passmore, L. A., Casanal, A. & Jensen, T. H. (2021). Three-layered control of mRNA poly(A) tail synthesis in Saccharomyces cerevisiae. Genes and Development, 35(17-18), 1290-1303. https://doi.org/10.1101/GAD.348634.121
Turpaev, K., Hartmann, R. & Justesen, J. (1999). 2′-Adenylated derivatives of Ap3A activate RNase L. FEBS Letters, 457, 9-12.
Turpaev, K., Hartmann, R., Kisselev, L. & Justesen, J. (1997). Ap3A and Ap4A is primers for oligoadenylate synthesis catalyzed by interferon-inducible 2-5A synthetase. FEBS Letters, 408, 177-181.
Tudek, A., Schmid, M. & Jensen, T. H. (2017). Nuclear Decay Factors Crack Up mRNA. Molecular Cell, 65(5), 775-776. https://doi.org/10.1016/j.molcel.2017.02.014
Tudek, A., Schmid, M., Makaras, M., Barrass, J. D., Beggs, J. D. & Jensen, T. H. (2018). A Nuclear Export Block Triggers the Decay of Newly Synthesized Polyadenylated RNA. Cell Reports, 24(9), 2457-2467.e7. https://doi.org/10.1016/j.celrep.2018.07.103
Tudek, A., Lloret-Llinares, M. & Jensen, T. H. (2018). The multitasking polyA tail: nuclear RNA maturation, degradation and export. Philosophical Transactions of the Royal Society B: Biological Sciences, 373(1762), Article 20180169. https://doi.org/10.1098/rstb.2018.0169
Tudek, A., Schmid, M. & Jensen, T. H. (2019). Escaping nuclear decay: the significance of mRNA export for gene expression. Current Genetics, 65(2), 473-476. https://doi.org/10.1007/s00294-018-0913-x
Tudek, A., Krawczyk, P. S., Mroczek, S., Tomecki, R., Turtola, M., Matylla-Kulińska, K., Jensen, T. H. & Dziembowski, A. (2021). Global view on the metabolism of RNA poly(A) tails in yeast Saccharomyces cerevisiae. Nature Communications, 12, Article 4951. https://doi.org/10.1038/s41467-021-25251-w
Tu, Y., Peng, F., André, A. A. M., Men, Y., Srinivas, M. & Wilson, D. A. (2017). Biodegradable Hybrid Stomatocyte Nanomotors for Drug Delivery. ACS Nano, 11(2), 1957-1963. https://doi.org/10.1021/acsnano.6b08079
Tsochatzis, E., Berggreen, I. E., Tedeschi, F., Ntrallou, K., Gika, H. & Corredig, M. (2021). Gut microbiome and degradation product formation during biodegradation of expanded polystyrene by mealworm larvae under different feeding strategies. Molecules, 26(24), Article 7568. https://doi.org/10.3390/molecules26247568
Tsitsikli, M., Simonsen, B., Luu, T. B., Larsen, M. M., Andersen, C. G., Gysel, K., Lironi, D., Krönauer, C., Rübsam, H., Hansen, S. B., Bærentsen, R., Wulff, J. L., Johansen, S. H., Sezer, G., Stougaard, J., Andersen, K. R. & Radutoiu, S. (2025). Two residues reprogram immunity receptors for nitrogen-fixing symbiosis. Nature. Advance online publication. https://doi.org/10.1038/s41586-025-09696-3
Tsikou, D., Ramirez, E. E., Psarrakou, I. S., Wong, J. E., Jensen, D. B., Isono, E., Radutoiu, S. & Papadopoulou, K. K. (2018). A Lotus japonicus E3 ligase interacts with the Nod Factor Receptor 5 and positively regulates nodulation. BMC Plant Biology, 18(1), Article 217. https://doi.org/10.1186/s12870-018-1425-z
Tsikou, D., Yan, Z., Holt, D. B., Abel, N. B., Reid, D. E., Madsen, L. H., Bhasin, H., Sexauer, M., Stougaard, J. & Markmann, K. (2018). Systemic control of legume susceptibility to rhizobial infection by a mobile microRNA. Science, 362(6411), 233-236. https://doi.org/10.1126/science.aat6907
Tschernoster, N., Erger, F., Kohl, S., Reusch, B., Wenzel, A., Walsh, S., Thiele, H., Becker, C., Franitza, M., Bartram, M. P., Kömhoff, M., Schumacher, L., Kukat, C., Borodina, T., Quedenau, C., Nürnberg, P., Rinschen, M. M., Driller, J. H., Pedersen, B. P. ... Altmüller, J. (2023). Long-read sequencing identifies a common transposition haplotype predisposing for CLCNKB deletions. Genome Medicine, 15(1), Article 62. https://doi.org/10.1186/s13073-023-01215-1
Truhlar, S. M. E., Cervantes, C. F., Torpey, J. W., Kjærgaard, M. & Komives, E. A. (2008). Rapid mass spectrometric analysis of 15N-Leu incorporation fidelity during preparation of specifically labeled NMR samples. Protein Science, 17(9), 1636-9. https://doi.org/10.1110/ps.036418.108
Trubetskoy, V., Pardiñas, A. F., Qi, T., Panagiotaropoulou, G., Awasthi, S., Bigdeli, T. B., Bryois, J., Chen, C.-Y., Dennison, C. A., Hall, L. S., Lam, M., Watanabe, K., Frei, O., Ge, T., Harwood, J. C., Koopmans, F., Magnusson, S., Richards, A. L., Sidorenko, J. ... Indonesia Schizophrenia Consortium (2022). Mapping genomic loci implicates genes and synaptic biology in schizophrenia. Nature, 604(7906), 502-508. https://doi.org/10.1038/s41586-022-04434-5
Trolle, C., Nielsen, M. M., Skakkebæk, A., Lamy, P., Vang, S., Hedegaard, J., Nordentoft, I., Ørntoft, T. F., Pedersen, J. S. & Gravholt, C. H. (2016). Widespread DNA hypomethylation and differential gene expression in Turner syndrome. Scientific Reports, 6, Article 34220. https://doi.org/10.1038/srep34220
Troeberg, L., Fushimi, K., Scilabra, S. D., Nakamura, H., Dive, V., Thøgersen, I. B., Enghild, J. J. & Nagase, H. (2009). The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3. Matrix Biology, 28(8), 463-9. https://doi.org/10.1016/j.matbio.2009.07.005
Trist, B. G., Wright, C. J., Rangel, A., Cottle, L., Prasad, A., Jensen, N. M., Gram, H., Dzamko, N., Jensen, P. H. & Kirik, D. (2024). Novel tools to quantify total, phospho-Ser129 and aggregated alpha-synuclein in the mouse brain. npj Parkinson's Disease , 10(1), Article 217. https://doi.org/10.1038/s41531-024-00830-y
Triano, I., Barrera, F. N., Renart, M. L., Molina, M. L., Fernández-Ballester, G., Poveda, J. A., Fernández, A. M., Encinar, J. A., Ferrer-Montiel, A. V., Otzen, D. & González-Ros, J. M. (2010). Occupancy of nonannular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Biochemistry, 49(25), 5397-5404. https://doi.org/10.1021/bi1003712
Trebeschi, S., Drago, S. G., Birkbak, N. J., Kurilova, I., Cǎlin, A. M., Delli Pizzi, A., Lalezari, F., Lambregts, D. M. J., Rohaan, M. W., Parmar, C., Rozeman, E. A., Hartemink, K. J., Swanton, C., Haanen, J. B. A. G., Blank, C. U., Smit, E. F., Beets-Tan, R. G. H. & Aerts, H. J. W. L. (2019). Predicting response to cancer immunotherapy using noninvasive radiomic biomarkers. Annals of Oncology, 30(6), 998-1004. Article mdz108. https://doi.org/10.1093/annonc/mdz108
Torvund-Jensen, J., Steengaard, J., Reimer, L., Fihl, L. B. & Laursen, L. S. (2014). Transport and translation of MBP mRNA is regulated differently by distinct hnRNP proteins. Journal of Cell Science, 127(Pt 7), 1550-1564. https://doi.org/10.1242/jcs.140855
Torvund-Jensen, J., Steengaard, J., Askebjerg, L. B., Kjaer-Sorensen, K. & Laursen, L. S. (2018). The 3’UTRs of myelin basic protein mRNAs regulate transport, local translation and sensitivity to neuronal activity in zebrafish. Frontiers in Molecular Neuroscience, 11, Article 185. https://doi.org/10.3389/fnmol.2018.00185
Torralba, S., Sojat, J. & Hartmann, R. (2008). 2'-5' oligoadenylate synthetase shares active site architecture with the archaeal CCA-adding enzyme. Cellular and Molecular Life Sciences, 65(16), 2613-20. https://doi.org/10.1007/s00018-008-8164-5
Tornaletti, S., Andersen, A. H., Christiansen, K. & Pedrini, A. M. (1992). 8-methoxycaffeine inhibition of Drosophila DNA topoisomerase II. B B A - General Subjects, 1131(1), 30-3.
Torarinsson, E., Yao, Z., Wiklund, E. D., Bramsen, J. B., Hansen, C. A., Kjems, J., Tommerup, N., Ruzzo, W. L. & Gorodkin, J. (2008). Comparative genomics beyond sequence-based alignments: RNA structures in the ENCODE regions. Genome Research, 18(2), 242-251. https://doi.org/10.1101/gr.6887408
Tong, T., Ozsvar, A., Hou, W.-H., Capogna, M. & Korshøj, A. R. (2023). OS10.6.A GLIOBLASTOMA CELLS IMITATE NEURON’S EXCITABILITY IN ACUTE AND ORGANOTYPIC HUMAN BRAIN SLICES. Neuro-Oncology, 25(Supplement 2), ii22-ii23. https://doi.org/10.1093/neuonc/noad137.066
Tonami, K., Hata, S., Ojima, K., Ono, Y., Kurihara, Y., Amano, T., Sato, T., Kawamura, Y., Kurihara, H. & Sorimachi, H. (2013). Calpain-6 deficiency promotes skeletal muscle development and regeneration. PLoS Genetics, 9(8), e1003668. https://doi.org/10.1371/journal.pgen.1003668
Tomecki, R., Kristiansen, M. S., Lykke-Andersen, S., Chlebowski, A., Larsen, K. M., Szczesny, R. J., Drazkowska, K., Pastula, A., Andersen, J. S., Stepien, P. P., Dziembowski, A. & Jensen, T. H. (2010). The human core exosome associates with differentially localized processive ribonucleases: hDIS3 and hDIS3L. E M B O Journal, 29(14), 2342-2357.
Tomassoni-Ardori, F., Hong, Z., Fulgenzi, G. & Tessarollo, L. (2020). Generation of Functional Mouse Hippocampal Neurons. Bio-protocol, 10(15), Article e3702. https://doi.org/10.21769/bioprotoc.3702
Tomasiak, T. M., Pedersen, B. P., Chaudhary, S., Rodriguez, A., Colmanares, Y. R., Roe-Zurz, Z., Thamminana, S., Tessema, M. & Stroud, R. M. (2014). General qPCR and Plate Reader Methods for Rapid Optimization of Membrane Protein Purification and Crystallization Using Thermostability Assays. Current Protocols in Protein Science, 77, 29.11.1-29.11.14. https://doi.org/10.1002/0471140864.ps2911s77
Tolomeo, D., Traversa, D., Venuto, S., Ebbesen, K., Garcia Rodriguez, J. L., Tamma, G., Ranieri, M., Simonetti, G., Ghetti, M., Paganelli, M., Visci, G., Liso, A., Kok, K., Muscarella, L. A., Fabrizio, F. P., Frassanito, M. A., Lamanuzzi, A., Saltarella, I., Solimando, A. G. ... Storlazzi, C. T. (2023). circPVT1 and PVT1/AKT3 show a role in cell proliferation, apoptosis, and tumor subtype-definition in Small Cell Lung Cancer. Genes, Chromosomes & Cancer, 62(7), 377-391. https://doi.org/10.1002/gcc.23121
Todt, D., François, C., Anggakusuma, U., Behrendt, P., Engelmann, M., Knegendorf, L., Vieyres, G., Wedemeyer, H., Hartmann, R., Pietschmann, T., Duverlie, G. & Steinmann, E. (2016). Antiviral Activities of Different Interferon Types and Subtypes against Hepatitis E Virus Replication. Antimicrobial Agents and Chemotherapy, 60(4), 2132-2139. https://doi.org/10.1128/AAC.02427-15
Tiwari, M. K., Leinisch, F., Sahin, C., Møller, I. M., Otzen, D., Davies, M. J. & Bjerrum, M. J. (2018). Early events in copper-ion catalyzed oxidation of α-synuclein. Free Radical Biology & Medicine, 121, 38-50. https://doi.org/10.1016/j.freeradbiomed.2018.04.559
Tiwari, M. K., Hägglund, P. M., Møller, I. M., Davies, M. J. & Bjerrum, M. J. (2019). Copper ion / H2O2 oxidation of Cu/Zn-Superoxide dismutase: Implications for enzymatic activity and antioxidant action. Redox Biology, 26, Article 101262. https://doi.org/10.1016/j.redox.2019.101262
Tirichine, L., James, E., Sandal, N. N. & Stougaard, J. (2006). Spontaneous root nodule formation in the model legume Lotus japonicus: A novel class of mutants nodulates in the absence of Rhizobia. MPMI, 19, 373-382.
Tirichine, L., Imaizumi-Anraku, H., Yoshida, S., Murakami, Y., Madsen, L. H., Miwa, H., Nakagawa, T., Sandal, N. N., Kawaguchi, M., Albrektsen, A. S., Downie, A., Sato, S., Tabata, S., Kouchi, H., Parniske, M., Kawazaki, S. & Stougaard, J. (2006). Deregulation of a Ca2+/calmodulin dependent kinase leads to spontaneous nodule development. Nature, 441, 1153-1156.
Tirichine, L., Sandal, N. N., Madsen, L. H., Radutoiu, E. S., Albrektsen, A. S., Sato, S., Asamizu, E., Tabata, S. & Stougaard, J. (2007). A gain-of-function mutation in a cytokinine receptor triggers spontaneous root nodule organogenesis. Science, 315, 104-107.
Timcenko, M., Lyons, J. A., Januliene, D., Ulstrup, J. J., Dieudonné, T., Montigny, C., Ash, M. R., Karlsen, J. L., Boesen, T., Kühlbrandt, W., Lenoir, G., Moeller, A. & Nissen, P. (2019). Structure and autoregulation of a P4-ATPase lipid flippase. Nature, 571(7765), 366-370. https://doi.org/10.1038/s41586-019-1344-7
Timcenko, M., Dieudonné, T., Montigny, C., Boesen, T., Lyons, J. A., Lenoir, G. & Nissen, P. (2021). Structural Basis of Substrate-Independent Phosphorylation in a P4-ATPase Lipid Flippase. Journal of Molecular Biology, 433(16), Article 167062. https://doi.org/10.1016/j.jmb.2021.167062
Tian, J. Y., Sørensen, E. S., Butler, W. T., Lopez, C. A., Sy, M. S., Desai, N. K. & Denhardt, D. T. (2000). Regulation of no synthesis induced by inflammatory mediators in RAW264.7 cells: collagen prevents inhibition by osteopontin. Cytokine, 12, 450-457.
Tian, P., Boomsma, W., Wang, Y., Otzen, D., Jensen, M. H. & Lindorff-Larsen, K. (2015). Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation. Journal of the American Chemical Society, 137(1), 22-25. https://doi.org/10.1021/ja5093634
Tian, P., Lindorff-Larsen, K., Boomsma, W., Jensen, M. H. & Otzen, D. E. (2016). A Monte Carlo Study of the Early Steps of Functional Amyloid Formation. PLoS One, 11(1), Article e0146096. https://doi.org/10.1371/journal.pone.0146096
Thykjaer, T., Danielsen, D., She, Q. & Stougaard, J. (1997). Organization and expression of genes in the genomic region surrounding the glutamine synthetase gene Gln1 from Lotus japonicus. Molecular Genetics and Genomics, 255(6), 628-36.
Thykjaer, T., Stiller, J., Handberg, K., Jones, J. & Stougaard, J. (1995). The maize transposable element Ac is mobile in the legume Lotus japonicus. Plant Molecular Biology, 27(5), 981-93.
Thurgood, L. A., Cook, A. F., Sørensen, E. S. & Ryall, R. L. (2010). Face-specific incorporation of osteopontin into urinary and inorganic calcium oxalate monohydrate and dihydrate crystals. Urological Research, 38(5), 357-376.
Thurgood, L. A., Sørensen, E. S. & Ryall, R. L. (2012). The effect of intracrystalline and surface-bound osteopontin on the attachment of calcium oxalate dihydrate crystals to Mandin-Darby canine kidney (MDCK) cells in ultrafiltered human urine. B J U International (Print), 109(7), 1100-1109. https://doi.org/10.1111/j.1464-410X.2011.10530.x
Thurgood, L. A., Sørensen, E. S. & Ryall, R. L. (2012). The effect of intracrystalline and surface-bound osteopontin on the degradation and dissolution of calcium oxalate dihydrate crystals in MDCKII cells. Urological Research, 40, 1-15.

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Lisbeth Heilesen