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Peer-reviewed publications at MBG - 2025

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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

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

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

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

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

Toft, S., Cuende, E., Olesen, A. L., Mathiesen, A., Meisner Larsen, M. & Jensen, K. (2019). Food and specific macronutrient limitation in an assemblage of predatory beetles. Oikos, 128(10), 1467-1477. https://doi.org/10.1111/oik.06479

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.

Thuillet, A.-C., Bru, D., David, J., Roumet, P., Santoni, S., Sourdille, P. & Bataillon, T. (2002). Direct estimation of mutation rate for 10 microsatellite loci in durum wheat, Triticum turgidum (L.) Thell. ssp durum desf. Molecular Biology and Evolution, 19(1), 122-5.

Thuillet, A.-C., Bataillon, T., Sourdille, P. & David, J. L. (2004). Factors affecting polymorphism at microsatellite loci in bread wheat [ Triticum aestivum (L.) Thell]: effects of mutation processes and physical distance from the centromere. Theoretical and Applied Genetics, 108(2), 368-77. https://doi.org/10.1007/s00122-003-1443-5

Thuillet, A. C., Bataillon, T., Poirier, S., Santoni, S. & David, J. L. (2005). Estimation of long-term effective population sizes through the history of durum wheat using microsatellite data. Genetics, 169(3), 1589-1599. https://doi.org/10.1534/genetics.104.029553

Thorslund, T., Sunesen, M., Bohr, V. & Stevnsner, T. (2002). Repair of 8-oxoG is slower in endogenous nuclear genes than in mitochondrial DNA and is without strand bias. D N A Repair, 1, 261-273.

Thorslund, T., von Kobbe, C., Harrigan, J. A., Indig, F. E., Christiansen, M., Stevnsner, T. V. & Bohr, V. (2005). Cooperation of the Cockayne syndrome group B protein and poly (ADP-ribose) polymerase 1 in the response to oxidative stress. Molecular and Cellular Biology, 25, 7625-7236.

Thorsen, K., Schepeler, T., Øster, B., Rasmussen, M. H., Vang, S., Wang, K., Hansen, K. Q., Lamy, P., Pedersen, J. S., Eller, A. Ø., Mansilla, F., Laurila, K., Wiuf, C. H., Laurberg, S., Dyrskjot, L., Orntoft, T. F. & Andersen, C. L. (2011). Tumor-specific usage of alternative transcription start sites in colorectal cancer identified by genome-wide exon array analysis. B M C Genomics, 12(1), 505. https://doi.org/10.1186/1471-2164-12-505

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