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Latest peer-reviewed publications at MBG

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Peer-reviewed publications at MBG - all years

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Taschner, M., Vetter, M. M. & Lorentzen, E. (2012). Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proceedings of the National Academy of Sciences (PNAS), 109(48), 19649-19654.
Schulze, W. X., Sanggaard, K. W., Kreuzer, I., Knudsen, A. D., Bemm, F., Thøgersen, I. B., Brautigam, A., Thomsen, L. R., Schliesky, S., Dyrlund, T. F., Escalante-Perez, M., Becker, D., Schultz, J., Karring, H., Weber, A., Højrup, P., Hedrich, R. & Enghild, J. J. (2012). The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. Molecular and Cellular Proteomics, 11(11), 1306-1319. https://doi.org/10.1074/mcp.M112.021006
Hansen, H. G., Schmidt, J. D., Søltoft, C. L., Ramming, T., Geertz-Hansen, H. M., Christensen, B., Sørensen, E. S., Juncker, A. S., Appenzeller-Herzog, C. & Ellgaard, L. (2012). Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. Journal of Biological Chemistry, 287(47), 39513-39523. https://doi.org/10.1074/jbc.M112.405050
Liao, J., Singh, S., Hossain, M. S., Andersen, S. U., Ross, L., Bonetta, D., Zhou, Y., Sato, S., Tabata, S., Stougaard, J., Szczyglowski, K. & Parniske, M. (2012). Negative regulation of CCaMK is essential for symbiotic infection. Plant Journal, 72(4), 572-584. https://doi.org/10.1111/j.1365-313X.2012.05098.x
Mertens, H. D. T., Kjærgaard, M., Mysling, S., Gårdsvoll, H., Jørgensen, T. J. D., Svergun, D. I. & Ploug, M. (2012). A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). Journal of Biological Chemistry, 287(41), 34304-15. https://doi.org/10.1074/jbc.M112.398404
Daniel, C., Venø, M. T., Ekdahl, Y., Kjems, J. & Öhman, M. (2012). A distant cis acting intronic element induces site-selective RNA editing. Nucleic Acids Research, 40(19), 9876-9886. https://doi.org/10.1093/nar/gks691
Valero Moreno, J., Escuder, B., Miravet, J. F. & de Mendoza, J. (2012). Anion-responsive diguanidinium-based chiral organogelators. Chemistry - A European Journal, 18(41), 13038-13047. http://europepmc.org/abstract/med/22936304
Povlsen, L. K., Beli, P., Wagner, S. A., Poulsen, S. L., Sylvestersen, K. B., Poulsen, J. W., Nielsen, M. L., Bekker-Jensen, S., Mailand, N. & Choudhary, C. (2012). Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Nature Cell Biology, 14(10), 1089-1098. https://doi.org/10.1038/ncb2579
Dasgupta, I., Sanglas, L., Enghild, J. J. & Lindberg, I. (2012). The Neuroendocrine Protein 7B2 Is Intrinsically Disordered. Biochemistry, 51(38), 7456–7464. https://doi.org/10.1021/bi300871k
Bjergbæk, L. (2012). DNA repair protocols. (3. ed. / ed.) Humana Press.
Mizuno, N., Taschner, M., Engel, B. D. & Lorentzen, E. (2012). Structural studies of ciliary components. J. Mol. Biol., 422(2), 163-180.
Sztukowska, M., Veillard, F., Potempa, B., Bogyo, M., Enghild, J. J., Thøgersen, I. B., Nguyen, K.-A. & Potempa, J. (2012). Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes. World Journal of Biological Chemistry, 393(9), 971-977. https://doi.org/10.1515/hsz-2012-0175
Hofbauer, S., Gysel, K., Mlynek, G., Kostan, J., Hagmüller, A., Daims, H., Furtmüller, P. G., Djinović-Carugo, K. & Obinger, C. (2012). Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases. B B A - Molecular and Cell Biology of Lipids, 1824(9), 1031-1038. https://doi.org/10.1016/j.bbapap.2012.05.012
Hebelstrup, K., van Zanten, M., Mandon, J., Voesenek, L. A. C. J., Harren, F. J. M., Cristescu, S. M., Møller, I. M. & Mur, L. A. J. (2012). Haemoglobin modulates NO emission and hyponasty under hypoxia-related stress in Arabidopsis thaliana. Journal of Experimental Botany, 63(15), 5581-5591. https://doi.org/10.1093/jxb/ers210
Hossain, M. S., Liao, J., James, E. K., Sato, S., Tabata, S., Jurkiewicz, A., Madsen, L. H., Stougaard, J., Ross, L. & Szczyglowski, K. (2012). Lotus japonicus ARPC1 is required for Rhizobial Infection. Plant Physiology, 160(2), 917-928. https://doi.org/10.1104/pp.112.202572
Sandal, N., Jin, H., Rodriguez-Navarro, D. N., Temprano, F., Cvitanich, C., Brachmann, A., Sato, S., Kawaguchi, M., Tabata, S., Parniske, M., Ruiz-Sainz, J. E., Andersen, S. U. & Stougaard, J. (2012). A Set of Lotus japonicus Gifu x Lotus burttii Recombinant Inbred Lines Facilitates Map-based Cloning and QTL Mapping. D N A Research, 19(4), 317-323. https://doi.org/10.1093/dnares/dss014
Ferreira, J., Mendes, S., Dall´Agnol, M., Sandal, N. N., Sato, S. & Pedrosa-Harand, A. (2012). Comparative analyses in Lotus: the cytogenetic map of Lotus uliginosus Schkuhr. Cytogenetic and Genome Research, 137(1), 42-49. https://doi.org/10.1159/000339617
Manka, S. W., Carafoli, F., Visse, R., Bihan, D., Raynal, N., Farndale, R. W., Murphy, G., Enghild, J. J., Hohenester, E. & Nagase, H. (2012). Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1. Proceedings of the National Academy of Sciences (PNAS), 109(31), 12461-12466. https://doi.org/10.1073/pnas.1204991109
Salmon, D., Vanwalleghem, G., Morias, Y., Denoeud, J., Krumbholz, C., Lhommé, F., Bachmaier, S., Kador, M., Gossmann, J., Dias, F. B. S., De Muylder, G., Uzureau, P., Magez, S., Moser, M., De Baetselier, P., Van Den Abbeele, J., Beschin, A., Boshart, M. & Pays, E. (2012). Adenylate cyclases of Trypanosoma brucei inhibit the innate immune response of the host. Science, 337(6093), 463-466. https://doi.org/10.1126/science.1222753
Lyons, J. A., Aragão, D., Slattery, O., Pisliakov, A. V., Soulimane, T. & Caffrey, M. (2012). Structural insights into electron transfer in caa 3-type cytochrome oxidase. Nature, 487(7408), 514-518. https://doi.org/10.1038/nature11182
Poulsen, J. W., Madsen, C. T., Young, C., Kelstrup, C. D., Grell, H. C., Henriksen, P., Juhl-Jensen, L. & Nielsen, M. L. (2012). Comprehensive profiling of proteome changes upon sequential deletion of deubiquitylating enzymes. Journal of Proteomics, 75(13), 3886-3897. https://doi.org/10.1016/j.jprot.2012.04.055
Ruetz, M., Fedosov, S. & Kräutler, B. (2012). Reconstitution of the B12 Macrocycle by Radical Ring Closure of a Blue Secocorrin. Angewandte Chemie International Edition, 51(27), 6780-6784. https://doi.org/10.1002/anie.201202878