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13. Abstracts

Author

Kaatsch, Hans-Jürgen, Püschel, K., Heinemann, A., Klaas, Jakob, Graß, Hildegard, Staak, Michael, Benthaus, S., Vock, R., Brinkmann, B., Temme, O., Daldrup, T., Dilger, M., Fink, T., Rittner, Ch., Thali, Michael J., Braun, M., Brueschweiler, W., Kneubuehl, B. P., Vock, P., Wirth, J., Dirnhofer, R., Bohnert, M., Berger, H., Buck, U., Pollak, S., Gotta, J. C., Erdmann, F., Riße, M., Schütz, H., Weiler, G., Pragst, F., Auwärter, V., Sporkcrt, F., Roewer, L., Willuweit, S., Kayser, M., Nagy, M., de Knijff, P., Geserick, G., Augustin, C., Betz, A., Carracedo, A., Corach, D., Dupuy, B. M., Gusmaõ, L., Henke, L., Hidding, M., Kärgel, H. J., Lessig, R., Liebeherr, E., Parson, W., Pascali, V. L., Rolf, B., Schneider, P. M., Dobosz, T., Teifel-Greding, J., Krawczak, M., Bauer, M., Patzelt, D., Kuznik, J., Bondy, B., Eisenmenger, W., Möller, H. -J., Zehner, R., Niess, C., Amendt, J., Krettek, R., Weinmann, W., Görner, M., Goerke, R., Mahler, H., Fowinkel, C., Haarhoff, K., Schmidt, P., Schmolke, C., Mußhoff, F., Menzen, M., Prohaska, C., Madea, B., Kauert, G., Gleicher, S., Drasch, G., von Meyer, L., Roider, G., Quitterer, D., Kröner, L., Toennes, S. W., Jurowich, S., Käferstein, H., Sticht, G., Gilg, T., Priemer, F., Jocham, N., Fechner, G., Ortmann, Ch., Schulte, T., Nieschalk, M., Weirich, V., Rummel, J., Rentsch, D., Wegener, R., Berehaus, G., Graß, H., Grellner, W., Rettig-Stürmer, A., Kühn-Becker, H., Georg, T., Möller, M., Wilske, J., Kemmerling, R., Sachs, H., Menting, T., Musshoff, F., Schoenemeier, S., Bürrig, K. -F., Jacob, B., Bonte, W., Maeda, H., Zhu, B. -L., Fujita, M. Q., Quan, L., Ishida, K., Taniguchi, M., Böhme, B., Rauch, E., Penning, R., Amberg, R., Blackwell, C. C., Pelz, K., Meier, V., Saternus, K. -S., Gessler, F., Böhnel, H., Bouska, I., Toupalík, P., Klir, P., Kleemann, W. J., Ast, F., Beck, U., Debertin, S., Giebe, B., Heide, S., Sperhake, J., Poets, C. F., Weis, C., Schlaud, M., Bajanowski, T., Wedekind, H., Breithardt, G., Debertin, A. S., Tönjes, H., Tschernig, T., Pabst, R., Tröger, H. D., Krill, A., Hame, M., Bouška, I., Ježková, J., Kernbach-Wighton, G., Wense, A. v. d., Kijewski, H., Goeke, M., Weber, B., Staak, M., Dettmeyer, R., Driever, F., Becker, A., Wiestler, O. D., Verhoff, M. A., Woenckhaus, J., Hauri-Bionda, R., Strehler, M., Bär, W., Ohshima, T., Takayasu, T., Kondo, T., Sato, Y., Tarbah, Fuad A., Mahler, Hellmut, Temme, Oliver, Daldrup, Thomas, Pötsch, Lucia, Emmerich, Patricia, Skopp, Gisela, Andresen, H., Schmoldt, A., Thurau, K., Vogt, S., Große-Perdekamp, M., Pufal, E., Sykutera, M., Rochholz, G., Lis, G., Sliwka, K., Zörntlein, S., Röhrich, J., Pötsch, L., Becker, J., Mattern, Rainer, Yamamoto, Yoshiko, Hayase, Tamaki, Yamamoto, Keiichi, Piette, Michel H. A., De Letter, Els A., Cordonnier, Jan, Schultes, A., Pluisch, F., Darok, M., Kollroser, M., Mannweiler, S., Babel, B., Magerl, H., Mahfoud, B., Stein, S., Iwersen-Bergmann, S., Risser, D., Hönigschnabl, S., Stichenwirth, M., Sebald, D., Kaff, A., Schneider, B., Vycudilik, W., Bauer, G., Reitz, E., Kimont, H. -G., Molnár, A., Jeszenszky, E., Benkó, A., Száz, E., Varga, T., Mayr, N. P., Schmidbauer, S., Hallfeldt, K., Bank, A., Iffland, R., Schuff, A., Fischer, T., Weingarten, Y., Alt, A., Janda, I., Wurst, F. M., Seidl, S., Seitler, C., Haag-Dawoud, Munira, Beike, J., Vennemann, B., Köhler, H., Hendreich, F. -I., Giebe, W., Reimann, I., Werner, R., Klein, A., Schulz, K., Feischer, D., Erfurt, Ch., Arnold, R., Winnefeld, K., Riepert, T., Iffland, R., Longauer, F., Kardošovå, V., Anders, S., Hildebrand, E., Schulz, F., Möbus, U., Jaroß, W., Wittig, H., Schmidt, U., Hauptmann, K., Krause, D., Prudlow, B., Rohner, T., Molz, G., Früchtnicht, W., Hoppe, B., Henßge, C., Althaus, L., Herbst, J., Preiß, U., Stein, C., Glenewinkel, F., Leinzinger, E. P., Lászik, A., Soós, M., Hubay, M., Sótonyi, P., Schliff, A., Gatternig, R., Hering, S., Edelmann, J., Plate, I., Michael, M., Kuhlisch, E., Szibor, R., von Wurmb, N., Hammer, U., Meissner, D., Kirches, E., Dietzmann, K., Pfeiffer, H., Ortmann, C., Meißner, C., Mohamed, S. A., Warnk, H., Gehlsen-Lorenzen, A., Oehmichen, M., Heidorn, F., Henkel, R., Schulz, M. M., Reichert, W., Mattern, R., Baasner, A., Banaschak, S., Schäfer, C., Benecke, M., Reibe, S., Barksdale, Larry, Sundermeier, Jon, Ratcliffe, Brett C., Lutz, S., Hohoff, C., Schürenkamp, M., Kahle, C., Fieguth, A., Ritz-Timme, S., Laumeier, I., Schütz, H. W., Schulte-Mönting, J., Chaudri, S., Welti, M., Dittmann, V., Olze, A., Schmeling, A., Reisinger, W., Klotzbach, H., Gabriel, P., Demir, T., Huckenbeck, W., Reuhl, J., Schuster, R., Maxeiner, H., Bockholdt, B., Jachau, K., Kuchheuser, W., Försterling, T., Ehrlich, E., Besselmann, M., Du Chesne, A., Albrecht, U. -V., Guan, D. W., Dreßler, J., Voigtmann, K., Müller, E., Vieler, S., Kirchner, A., Humpert, M., Breitmeier, D., Mansouri, F., Wyler, D., Marty, W., Sigrist, Th., Zollinger, U., Meyer, U., Allmen, G. v., Karger, B., Hoekstra, A., Stehmann, B., Schmidt, P. F., Peschel, O., Vollmar, C., Szeimies, U., Rothschild, M. A., Kegel, D., Klatt, A., Klatt, C., Briese, B. -H., Schyma, C., Schyma, P., Angetter, Daniela, Perdekamp, M. Große, Sun, Y., Guttenberge, R., Riede, U. -N., Poetsch, M., Seefeldt, S., Maschke, M., Lignitz, E., Zeller, M., Wehner, H. -D., Czarnetzki, A., Blin, N., Bender, K., Emmerich, P., Pádár, Zs., Egyed, B., Kemény, G., Woller, J., Füredi, S., Balogh, I., Cremer, U., Scheil, H. -G., Schiwy-Bochat, K. -H., Althoff, H., Immel, U. -D., Tatschner, Th., Lang, C., Versmold, D., Reineke, Th., Mall, G., Dahlmann, F., Büttner, A., Hubig, M., Rötzscher, K., Grundmann, C., Oritani, S., Peter, J., Popov, V., Olejnik, V., Khokhlov, V. D., Stiller, D., Romanowski, U., Kleiber, M., Klupp, N., Mortinger, H., Chadová, L., Bouška, I., Toupalik, P., Schnabel, A., Lutz, F. -U., Crivellaro, A., Strauch, H., Dan, Dermengiu, Silvia, Dermengiu, Buda, Octavian, Kandolf, R., Kaiser, R., Eis-Hübinger, A. M., Kobek, M., Jankowski, Z., Rygol, K., Kulikowska, J., Martin, H., Kolbow, K., Keil, W., Wang, Huijun, Ding, Yanqing, Huang, Guangzhao, Wu, Zhongbi, Wehner, F., Subke, J., Zdravkovic, M., Otasevic, V., Rostov, M., Karadzic, R., Kildüschov, E. M., Buromski, I. W., Plaksin, W. O., Wendland, A., Spiridonow, W. A., Sabusow, J. G., Kalinin, J. P., Heide, S., Schmidt, V., Wiegand, P., Kleiber, M., Demmler, G., Zack, F., Reischle, S., Schönpflug, M., Beier, G., Berchtenbreiter, C., Lackner, K., Jendrusch, B., Wolf, H., Buhmann, D., Summa, H., Matschke, J., Stürenburg, H. J., Junge, M., Wischhusen, F., Müldner, C., Schröder, A., Kaiser, E., Lasczkowski, G., Hofbauer, V., Eberl, N., Thomson, H., Tatschner, T., Milz, S., Gazov, E., Trübner, K., Brenner, M., Tsokos, M., Anders, S., Paulsen, F., Reith, K., Bratzke, H., Schapfeld, R., Graefe-Kirci, U., Stiller, D., Trübner, K., and Schäfer, A. Th.

Published
2000
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15. Soybean Yellow Stripe-like7 is a symbiosome membrane peptide transporter essential for nitrogen fixation

Author

Gavrin, A, primary, Loughlin, PC, additional, Brear, EM, additional, Griffith, OW, additional, Bedon, F, additional, Suter Grotemeyer, M, additional, Escudero, V, additional, Reguera, M, additional, Qu, Y, additional, Mohd-Noor, SN, additional, Chen, C, additional, Osorio, MB, additional, Rentsch, D, additional, González-Guerrero, M, additional, Day, DA, additional, and Smith, PMC, additional

Published
2020
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19. Session 15 Cellular transport

Author

Epel, B., Yahalom, A., Katz, A., Kotlizky, G., Cohen, L., Erlanger, M., Levi, R., Levi, N., Van Lent, J., Belyaeva, N., Nasyrova, G., Simchuk, E., Buckhout, Thomas J., Buntukova, E. K., Karimova, F. G., Klochkova, E. E., Driouich, A., Staehelin, La., Frommer, W. B., Fischer, W. N., Hirner, B., Kwart, M., Lauter, F. R., Ninnemann, O., Rentsch, D., Fuks, B., Homble, F., Getz, H. P., Klein, M., Henricson, D., Opanasenko, V. K., Bergstedt, K. -G., Gardeström, P., Samuelsson, G., Janáček, K., Nešpůrková, L., Beneš, I., Metlička, R., Sigler, K., Jordi, W., Stoopen, G. M., Karnauchov, I., Cai, D., Clausmeyer, S., Herrmann, R. G., KlOsgen, R. B., Lyalin, O. O., Ktitorova, I. N., Marichev, G. A., Skobeleva, O. V., Miklós, E., Szöke, L., Kozma, P., Haydu, Zs., Erdei, L., Moshkov, A. V., Batov, A. Y., Petrussa, E., Marci’, F., Zancani, M., Dell’antone, P., Vianello, A., Seedorf, M., Soll, J., Sokolik, A. I., Yurin, V. M., Szakiel, A., Janiszowska, W., Tokarska, M., Spiewla, E., Vicente, J. A. F., Vale, M. G. P., Weig, A., Dolle, L. -O., Franz, J., Komor, E., Zagdańska, B., and Rybka, Z.

Published
1994
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21. Preparation and characterization of water-redispersible nanofibrillated cellulose in powder form

Author

Eyholzer, Ch, Bordeanu, N., Lopez-Suevos, F., Rentsch, D., Zimmermann, T., and Oksman, K.

Subjects
endocrine system
Abstract

Water-redispersible, nanofibrillated cellulose (NFC) in powder form was prepared from refined, bleached beech pulp (RBP) by carboxymethylation (c) and mechanical disintegration (m). Two routes were examined by altering the sequence of the chemical and mechanical treatment, leading to four different products: RBP-m and RBP-mc (route 1), and RBP-c and RBP-cm (route 2). The occurrence of the carboxymethylation reaction was confirmed by FT-IR spectrometry and 13C solid state NMR (13C CP-MAS) spectroscopy with the appearance of characteristic signals for the carboxylate group at 1,595cm−1 and 180ppm, respectively. The chemical modification reduced the crystallinity of the products, especially for those of route 2, as shown by XRD experiments. Also, TGA showed a decrease in the thermal stability of the carboxymethylated products. However, sedimentation tests revealed that carboxymethylation was critical to obtain water-redispersible powders: the products of route 2 were easier to redisperse in water and their aqueous suspensions were more stable and transparent than those from route 1. SEM images of freeze-dried suspensions from redispersed RBP powders confirmed that carboxymethylation prevented irreversible agglomeration of cellulose fibrils during drying. These results suggest that carboxymethylated and mechanically disintegrated RBP in dry form is a very attractive alternative to conventional NFC aqueous suspensions as starting material for derivatization and compounding with (bio)polymers

Published
2018

22. Enzymatic synthesis of lignin-based concrete dispersing agents

Author

Jankowska, D., Heck, T., Schubert, M., Yerlikaya, A., Weymuth, C., Rentsch, D., Schober, I., Richter, M., and Publica

Abstract

Lignin is the most abundant aromatic biopolymer, functioning as an integral component of woody materials. In its unmodified form it shows limited water solubility and is relatively unreactive, so biotechnological lignin valorisation for high-performance applications is greatly underexploited. Lignin can be obtained from the pulp and paper industry as a by-product. To expand its application, a new synthesis route to new dispersing agents for use as concrete additives was developed. The route is based on lignin functionalisation by enzymatic transformation. Screening of lignin-modifying systems resulted in functionalised lignin polymers with improved solubility in aqueous systems. Through grafting of sulfanilic acid or p-aminobenzoic acid by fungal laccases, lignin became soluble in water at pHâ¤4 or pHâ¤7, respectively. Products were analysed and evaluated in miniaturised application tests in cement paste and mortar. Their dispersing properties match the performance criteria of commercially available lignosulfonates. The study provides examples of new perspectives for the use of lignin.

Published
2018

28. Arginine and lysine transporters are essential for Trypanosoma brucei

Author

Mathieu C, Macedo JP, Hürlimann D, Wirdnam C, Haindrich AC, Suter Grotemeyer M, Gonzalez-Salgado A, Schmidt RS, Inbar E, Mäser P, Bütikofer P, Zilberstein D, and Rentsch D

Subjects
bacteria, complex mixtures
Abstract

For Trypanosoma brucei arginine and lysine are essential amino acids and therefore have to be imported from the host. Heterologous expression in Saccharomyces cerevisiae mutants identified cationic amino acid transporters among members of the T. brucei AAAP (amino acid/auxin permease) family. TbAAT5 3 showed high affinity arginine uptake (Km 3.6 ± 0.4 µM) and high selectivity for L arginine. L arginine transport was reduced by a 10 times excess of L arginine homo arginine canavanine or arginine ß naphthylamide while lysine was inhibitory only at 100 times excess and histidine or ornithine did not reduce arginine uptake rates significantly. TbAAT16 1 is a high affinity (Km 4.3 ± 0.5 µM) and highly selective L lysine transporter and of the compounds tested only L lysine and thialysine were competing for L lysine uptake. TbAAT5 3 and TbAAT16 1 are expressed in both procyclic and bloodstream form T. brucei and cMyc tagged proteins indicate localization at the plasma membrane. RNAi mediated down regulation of TbAAT5 and TbAAT16 in bloodstream form trypanosomes resulted in growth arrest demonstrating that TbAAT5 mediated arginine and TbAAT16 mediated lysine transport are essential for T. brucei. Growth of induced RNAi lines could partially be rescued by supplementing a surplus of arginine or lysine respectively while addition of both amino acids was less efficient. Single and double RNAi lines indicate that additional low affinity uptake systems for arginine and lysine are present in T. brucei.

Published
2017

29. Jagdgeschwader 27

Author

Manhart, J., primary, Kozlowski, J., additional, Rentsch, D., additional, Kegler, R., additional, Lindner, I., additional, Meißner, D., additional, and Büttner, A., additional

Published
2016
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30. Reversible hydrogen storage in Mg(BH4)2/carbon nanocomposites

Author

Yan, Y., Au, Y.S., Rentsch, D., Remhof, A., de Jongh, P.E., Züttel, A., Inorganic Chemistry and Catalysis, Sub Inorganic Chemistry and Catalysis, Inorganic Chemistry and Catalysis, and Sub Inorganic Chemistry and Catalysis

Subjects
Nanocomposite, Materials science, Renewable Energy, Sustainability and the Environment, chemistry.chemical_element, Nanotechnology, Aerogel, General Chemistry, Hydrogen storage, chemistry, Chemical engineering, General Materials Science, Dehydrogenation, Chemical stability, Ball mill, Carbon, Chemical decomposition
Abstract

Mg(BH4)2 exhibits a high hydrogen content of 14.9 wt% and thermodynamic stability in the overall decomposition reaction that corresponds to hydrogen desorption at around room temperature. However, the potential applications in hydrogen storage are restricted by high kinetic barriers. In this study, we show the synthesis of Mg(BH4)2/carbon nanocomposites by ball milling of MgH2 nanoparticles supported on carbon aerogel in a B2H6/H2 atmosphere. The nanocomposite exhibits a lower kinetic barrier as compared to bulk Mg(BH4)2. The temperature for major hydrogen desorption is decreased to 160 °C. Furthermore, re-formation of Mg(BH4)2 after full dehydrogenation is achieved under mild conditions (200 °C and 80 to 150 bar H2) in the nanocomposite. This work demonstrates nanoengineering as an effective approach to realize the reversible hydrogen storage of Mg(BH4)2 under mild conditions., Journal of Materials Chemistry A, 1 (37), ISSN:2050-7488, ISSN:2050-7496

Published
2013

31. Synthesis, stability and Li-ion mobility of nanoconfined Li2B12H12.

Author

Yan, Y., Rentsch, D., Battaglia, C., and Remhof, A.

Subjects
*CHEMICAL stability, *LITHIUM ions, *CHEMICAL synthesis
Abstract

This communication presents the first synthesis of nanoconfined Lithium closo-borate, Li2B12H12, using nanoporous SiO2 as scaffold. The yield of Li2B12H12 is up to 94 mol%. The as-synthesized nanoconfined Li2B12H12 exhibits a structural transition around 380 °C and conversion to H-deficiency Li2B12H12−x at 580 °C. [ABSTRACT FROM AUTHOR]

Published
2017
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32. Synthesis, stability and Li-ion mobility of nanoconfined Li2B12H12.

Author

Yan, Y., Rentsch, D., Battaglia, C., and Remhof, A.

Subjects
CHEMICAL stability, LITHIUM ions, CHEMICAL synthesis
Abstract

This communication presents the first synthesis of nanoconfined Lithium closo-borate, Li2B12H12, using nanoporous SiO2 as scaffold. The yield of Li2B12H12 is up to 94 mol%. The as-synthesized nanoconfined Li2B12H12 exhibits a structural transition around 380 °C and conversion to H-deficiency Li2B12H12−x at 580 °C. [ABSTRACT FROM AUTHOR]

Published
2017
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33. Traffic routes and signals for the tonoplast

Author

Pedrazzini E., Komarova N., Rentsch D., and Vitale A.

Subjects
Protein Transport, plant-protein sorting, endoplasmic reticulum quality control, Plant Cells, Vacuoles, Vesicular Transport Proteins, food and beverages, membrane proteins, vesicle traffic, Protein Sorting Signals, Endoplasmic Reticulum, tonoplast, Plant Proteins
Abstract

Tonoplast, the membrane delimiting plant vacuoles, regulates ion, water and nutrient movement between the cytosol and the vacuolar lumen through the activity of its membrane proteins. Correct traffic of proteins from the endoplasmic reticulum (ER) to the tonoplast requires (i) approval by the ER quality control, (ii) motifs for exit from the ER and (iii) motifs that promote sorting to the tonoplast. Recent evidence suggests that this traffic follows different pathways that are protein-specific and could also reflect vacuole specialization for lytic or storage function. The routes can be distinguished based on their sensitivity to drugs such as brefeldin A and C834 as well as using mutant plants that are defective in adaptor proteins of vesicle coats, or dominant-negative mutants of Rab GTPases.

Published
2012

37. Controllable decomposition of Ca(BH4)2 for reversible hydrogen storage.

Author

Yan, Y., Rentsch, D., and Remhof, A.

Abstract

Ca(BH4)2 could reversibly store 9.6 wt% hydrogen based on the overall reaction of Ca(BH4)2→ 1/3CaB6 + 2/3CaH2 + 10/3H2. Formation of CaB6 instead of elemental boron and/or high boranes (e.g. CaB12H12) in the dehydrogenation process is crucial for rehydrogenation. Here, we reported two experimental protocols regarding how to form CaB6 from the decomposition of Ca(BH4)2: (1) decomposition below the melting point, e.g. 350 °C via CaB2H6 to CaB6 and (2) decomposition above the melting point, e.g. 400 °C via elemental boron to CaB6. [ABSTRACT FROM AUTHOR]

Published
2017
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41. Tod in Tüten

Author

Bittorf, A., primary, Thieme, D., additional, Püschel, K., additional, Friedrich, P., additional, Peschel, O., additional, Rentsch, D., additional, and Büttner, A., additional

Published
2012
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