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Institut for Molekylærbiologi og Genetik

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Publikationer fra instituttet

Tidsskriftsforsider lavet af forskere fra MBG

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Valero Moreno, J., Lohmann, F. & Famulok, M. (2017). Interlocked DNA topologies for nanotechnology. Current Opinion in Biotechnology, 48, 159-167. https://doi.org/10.1016/j.copbio.2017.04.002

Valero Moreno, J., Lohmann, F., Keppner, D. & Famulok, M. (2016). Single‐Stranded Tile Stoppers for Interlocked DNA Architectures. ChemBioChem, 17(12), 1146-1149. https://doi.org/10.1002/cbic.201500685

Valero Moreno, J., Shiraishi, T., de Mendoza, J. & Nielsen, P. E. (2015). Cellular Antisense Activity of PNA-Oligo(bicycloguanidinium) Conjugates Forming Self-Assembled Nanoaggregates. ChemBioChem, 16(11), 1593-1600. https://doi.org/10.1002/cbic.201500172

Valero Moreno, J. & de Mendoza, J. (2013). A tetraguanidinium macrocycle for the recognition and cavity expansion of calix[4]arene tetraoxoanions. Supramolecular Chemistry, 25(9-11), 728-740. https://doi.org/10.1080/10610278.2013.835814

Valero Moreno, J., Escuder, B., Miravet, J. F. & de Mendoza, J. (2012). Anion-responsive diguanidinium-based chiral organogelators. Chemistry, 18(41), 13038-13047. http://europepmc.org/abstract/med/22936304

Valero Moreno, J., Van Gool, M., Pérez-Fernández, R., Castreño, P., Sánchez-Quesada, J., Prados, P. & de Mendoza, J. (2012). Non-peptidic cell-penetrating agents: synthesis of oligomeric chiral bicyclic guanidinium vectors. Organic & Biomolecular Chemistry, 10, 5417-5430. https://doi.org/10.1039/C2OB25467K

Valero, J. & Skugor, M. (2020). Mechanisms, Methods of Tracking and Applications of DNA Walkers: A Review. ChemPhysChem, 21(17), 1971-1988. https://doi.org/10.1002/cphc.202000235

Valero, J. & Famulok, M. (2020). Regeneration of Burnt Bridges on a DNA Catenane Walker. Angewandte Chemie - International Edition, 59(38), 16366-16370. https://doi.org/10.1002/anie.202004447

Valero, J., Civit, L., Dupont, D. M., Selnihhin, D., Reinert, L. S., Idorn, M., Israels, B. A., Bednarz, A. M., Bus, C., Asbach, B., Peterhoff, D., Pedersen, F. S., Birkedal, V., Wagner, R., Paludan, S. R. & Kjems, J. (2021). A serum-stable RNA aptamer specific for SARS-CoV-2 neutralizes viral entry. Proceedings of the National Academy of Sciences, 118(50), Artikel e2112942118. https://doi.org/10.1073/pnas.2112942118

Valen, E., Preker, P., Andersen, P. R., Zhao, X., Chen, Y., Ender, C., Dueck, A., Meister, G., Sandelin, A. G. & Jensen, T. H. (2011). Biogenic mechanisms and utilization of small RNAs derived from human protein-coding genes. Nature Structural and Molecular Biology, 18(9), 1075-82. https://doi.org/10.1038/nsmb.2091

Vajda, Z., Pedersen, M., Füchtbauer, E.-M., Wertz, K., Stodkilde-Jørgensen, H., Sulyok, E., Doczi, T., Neely, N. D., Agre, P., Frokiar, J. & Nielsen, S. (2002). Delayed onset of brain endema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice. Proceedings of the National Academy of Sciences, 99, 13131-13136.

Vad-Nielsen, J., Jakobsen, K. R., Daugaard, T. F., Thomsen, R., Brügmann, A., Sørensen, B. S. & Nielsen, A. L. (2016). Regulatory dissection of the CBX5 and hnRNPA1 bi-directional promoter in human breast cancer cells reveals novel transcript variants differentially associated with HP1α down-regulation in metastatic cells. B M C Cancer, 16(1), 32. Artikel 32. https://doi.org/10.1186/s12885-016-2059-x

Vader, P., Fens, M. HAM., Sachini, N., van Oirschot, B. A., Andringa, G., Egberts, A. CG., Gaillard, C. AJM., Rasmussen, J. T., van Wijk, R., van Solinge, W. W. & Schiffelers, R. M. (2013). Taxol®-induced phosphatidylserine exposure and microvesicle formation in red blood cells is mediated by its vehicle Cremophor® EL. Nanomedicine, 8(7), 1127-1135. https://doi.org/10.2217/NNM.12.163

Vad, B. S., Thomsen, L. A. H., Bertelsen, K., Franzmann, M., Pedersen, J. M., Nielsen, S. B., Vosegaard, T., Valnickova, Z., Skrydstrup, T., Enghild, J. J., Wimmer, R., Nielsen, N. C. & Otzen, D. (2010). Divorcing folding from function: how acylation affects the membrane-perturbing properties of an antimicrobial peptide. B B A - Proteins and Proteomics, 1804(4), 806-20. https://doi.org/10.1016/j.bbapap.2009.12.006

Vad, B. S., Bertelsen, K., Johansen, C. H., Pedersen, J. M., Skrydstrup, T., Nielsen, N. C. & Otzen, D. E. (2010). Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption. Biophysical Journal, 98(4), 576-85. https://doi.org/10.1016/j.bpj.2009.08.063

Vad, B. S., Balakrishnan, V. S., Nielsen, S. B. & Otzen, D. (2015). Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin. Journal of Membrane Biology, 487-496. https://doi.org/10.1007/s00232-015-9792-y

Urbanski, D. F., Malolepszy, A., Stougaard, J. & Andersen, S. U. (2012). Genome-wide LORE1 retrotransposon mutagenesis and high-throughput insertion detection in Lotus japonicus. Plant Journal, 69(4), 731-741. https://doi.org/10.1111/j.1365-313X.2011.04827.x

Urbanski, D. F., Malolepszy, A., Stougaard, J. & Andersen, S. U. (2013). High-Throughput and Targeted Genotyping of Lotus japonicus LORE1 Insertion Mutants. Methods in Molecular Biology, 1069, 119-146. https://doi.org/10.1007/978-1-62703-613-9_10

Ung, K. L., Alsarraf, H., Kremer, L. & Blaise, M. (2022). MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs. Protein Expression and Purification, 191, Artikel 106014. https://doi.org/10.1016/j.pep.2021.106014

Ung, K. L., Alsarraf, H., Kremer, L. & Blaise, M. (2022). Corrigendum to “MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs” [Protein Expr. Purif. 191 (March 2022) 106014]. Protein Expression and Purification, 195-196, 106088. Artikel 106088. https://doi.org/10.1016/j.pep.2022.106088

Ung, K. L., Winkler, M., Schulz, L., Kolb, M., Janacek, D. P., Dedic, E., Stokes, D. L., Hammes, U. Z. & Pedersen, B. P. (2022). Structures and mechanism of the plant PIN-FORMED auxin transporter. Nature, 609(7927), 605-610. https://doi.org/10.1038/s41586-022-04883-y

Ung, K. L., Schulz, L., Kleine-Vehn, J., Pedersen, B. P. & Hammes, U. Z. (2023). Auxin transport at the endoplasmic reticulum: Roles and structural similarity of PIN-FORMED and PIN-LIKES. Journal of Experimental Botany, 74(22), 6893-6903. https://doi.org/10.1093/jxb/erad192

Ung, K. L., Schulz, L., Stokes, D. L., Hammes, U. Z. & Pedersen, B. P. (2023). Substrate recognition and transport mechanism of the PIN-FORMED auxin exporters. Trends in Biochemical Sciences, 48(11), 937-948. https://doi.org/10.1016/j.tibs.2023.07.006

Ung, K. L., Alsarraf, H. M. A. B., Kremer, L. & Blaise, M. (2020). The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold. Proteins: Structure, Function and Bioinformatics, 88(6), 809-815. https://doi.org/10.1002/prot.25863

Ung, K. L., Kremer, L. & Blaise, M. (2021). Structural analysis of the N-acetyltransferase Eis1 from Mycobacterium abscessus reveals the molecular determinants of its incapacity to modify aminoglycosides. Proteins: Structure, Function and Bioinformatics, 89(1), 94-106. https://doi.org/10.1002/prot.25997

Ung, K. L., Alsarraf, H. M. A. B., Olieric, V., Kremer, L. & Blaise, M. (2019). Crystal structure of the aminoglycosides N-acetyltransferase Eis2 from Mycobacterium abscessus. FEBS journal, 286(21), 4342-4355. https://doi.org/10.1111/febs.14975

Underhaug, J., Koldsø, H., Runager, K., Nielsen, J. T., Sørensen, C. S., Kristensen, T., Otzen, D., Karring, H., Malmendal, A., Schiøtt, B., Enghild, J. J. & Nielsen, N. C. (2013). Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization. BBA General Subjects, 1834(12), 2812–2822. https://doi.org/10.1016/j.bbapap.2013.10.008

Underbjerg, M., Kesmodel, U. S., Landrø, N. I., Bakketeig, L. S., Grove, J., Wimberley, T., Kilburn, T. R., Sværke, C., Thorsen, P. & Mortensen, E. L. (2012). The Effects of Low to Moderate Alcohol Consumption and Binge Drinking in Early Pregnancy on Selective and Sustained Attention in Five-Year-Old Children. B J O G, 119(10), 1211-1221. https://doi.org/10.1111/j.1471-0528.2012.03396.x

Umakoshi, H., Persson, J., Kroon, M., Johansson, H. O., Otzen, D. E., Kuboi, R. & Tjerneld, F. (2000). Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems. Journal of Chromatography B: Biomedical Sciences and Applications, 743(1-2), 13-19. https://doi.org/10.1016/S0378-4347(00)00190-0

Ulrich, A., Andersen, K. R. & Schwartz, T. U. (2012). Exponential megapriming PCR (EMP) cloning-seamless DNA insertion into any target plasmid without sequence constraints. PLOS ONE, 7(12), e53360. https://doi.org/10.1371/journal.pone.0053360

Ulleland, M., Eilertsen, I., Quadros, E. V., Rothenberg, S. P., Fedosov, S., Sundrehagen, E. & Ørning, L. (2002). Direct assay for cobalamin bound to transcobalamin (holo-transcobalamin) in serum. Clin. Chem., 48, 526-532.

Uhd, J., Okholm, A., Kjems, J. & Astakhova, K. (2017). Amplification-free liquid biopsy by fluorescence approach. I Biotech, Biomaterials and Biomedical - TechConnect Briefs 2017 (Bind 3, s. 106-109). TechConnect. https://briefs.techconnect.org/wp-content/volumes/TCB2017v3/pdf/762.pdf

Uhd, J., Miotke, L., Ji, H. P., Dunaeva, M., Pruijn, G. J. M., Jørgensen, C. D., Kristoffersen, E. L., Birkedal, V., Yde, C. W., Nielsen, F. C., Hansen, J. & Astakhova, K. (2020). Ultra-fast detection and quantification of nucleic acids by amplification-free fluorescence assay. Analyst, 145(17), 5836-5844. https://doi.org/10.1039/d0an00676a

Ugleholdt, R., Pedersen, J., Bassi, M. R., Füchtbauer, E.-M., Jørgensen, S. M., Kissow, H.-L., Nytofte, N., Poulsen, S. S., Rosenkilde, M. M., Seino, Y., Thams, P., Holst, P. J. & Holst, J. J. (2011). Transgenic Rescue of Adipocyte Glucose-dependent Insulinotropic Polypeptide Receptor Expression Restores High Fat Diet-induced Body Weight Gain. Journal of Biological Chemistry, 286(52), 44632-44645. https://doi.org/10.1074/jbc.M111.311779

Uckert, W., Becker, C., Gladow, M., Klein, D., Kammertoens, T., Pedersen, L. & Blankenstein, T. (2000). Efficient gene transfer into primary human CD8⁺ T Lymphocytes by MuLV-10A1 retrovirus pseudotype. Hum. Gene Ther., 11, 1005-1014.

Uckert, W., Willimsky, G., Pedersen, F. S., Blankenstein, T. & Pedersen, L. (1998). RNA levels of human retrovirus receptors Pit1 and Pit2 do not correlate with infectibility by three retroviral vector pseudotypes. Human Gene Therapy, 9(17), 2619-2627. https://doi.org/10.1089/hum.1998.9.17-2619

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. P L o S 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), Artikel 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, Artikel 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), Artikel 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), Artikel 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

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Lisbeth Heilesen