@misc{PothMonzonTippkoetteretal.2009,
  author    = {Poth, S. and Monzon, M. and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Fermentation von Hydrolysaten aus Lignocellulose},
  series = {Chemie Ingenieur Technik},
  volume    = {81},
  journal   = {Chemie Ingenieur Technik},
  number    = {8},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.200950243},
  pages     = {1220},
  year      = {2009},
  abstract  = {Die {\"o}konomische Abh{\"a}ngigkeit von fossilen Brennstoffen und der klimatische Wandel durch die Nutzung dieser haben zu einer intensiven Suche nach erneuerbaren Rohstoffen f{\"u}r die Produktion von Chemikalien und Treibstoffen gef{\"u}hrt. Ein viel versprechender Rohstoff in diesem Zusammenhang sind Zucker, die mittels enzymatischer Hydrolyse aus Lignocellulose gewonnen werden k{\"o}nnen. Die Fermentation erfolgt mit Cellulose- bzw. Hemicellulose-Fraktionen, welche durch thermo-chemische Vorbehandlung von Holz gewonnen und anschließend enzymatisch hydrolysiert werden. Die in den Hydrolysaten enthaltenen Zuckermonomere dienen als Kohlenstoffquelle f{\"u}r die Produktion von Ethanol. Da sowohl Glucose als auch Xylose in den unterschiedlichen Fraktionen enthalten sind, wird zur Umsetzung dieser eine Co-Fermentation zweier Hefen durchgef{\"u}hrt. Im Rahmen der Optimierung dieser Fermentationen werden neben der Erg{\"a}nzung der Hydrolysate durch notwendige Salze auch Verfahrenweisen wie Fed-Batch-Fermentationen untersucht. Ein weiterer interessanter Ansatz, welcher in diesem Rahmen gepr{\"u}ft wird, ist die enzymatische Hydrolyse der Lignocellulose-Fraktionen und die simultane Fermentation der dabei entstehenden Zucker in einem Schritt. Des Weiteren wurde die Eignung der Hydrolysate f{\"u}r die Biomasseproduktion anderer Mikroorganismen wie Escherichia coli getestet.},
  language  = {de}
}
@misc{PothMonzonTippkoetteretal.2010,
  author    = {Poth, S. and Monzon, M. and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Lignocellulose-Bioraffinerie: Simultane Verzuckerung und Fermentation},
  series = {Chemie Ingenieur Technik},
  volume    = {82},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  doi       = {10.1002/cite.201050360},
  pages     = {1568},
  year      = {2010},
  abstract  = {Die am h{\"a}ufigsten genutzten Rohstoffe f{\"u}r die Produktion von Treibstoffen und Chemikalien sind fossilen Ursprungs. Da diese limitiert sind, werden im Hinblick auf die Nachhaltigkeit alternative, erneuerbare Rohstoffquellen intensiv untersucht. Vielversprechend in diesem Kontext sind die in Lignocellulose enthaltenen Zucker, die beispielsweise zur Produktion von Ethanol genutzt werden k{\"o}nnen. In der Regel sind f{\"u}r eine Lig-nocellulose-Bioraffinerie mehrere Prozessschritte notwendig: Vorbehandlung, Verzuckerung und Fermentation. Um diesen Prozess einfacher zu gestalten, ist es m{\"o}glich, die Verzuckerung und die Fermentation in einem Schritt durchzuf{\"u}hren (SSF). Als Substrat wird hier Cellulose-Faserstoff verwendet, der durch das Organosolv-Verfahren aufgeschlossen wurde. Die Hydrolyse erfolgt mit kommerziell erh{\"a}ltlichen Enzymen und f{\"u}r die Fermentation zu Ethanol werden zwei Hefen verwendet. Beim SSF-Verfahren konnte, im Vergleich zur entkoppelten Verfahrensweise, trotz bestehender Unterschiede in den Temperatur-Optima von Enzymen und Hefen eine Steigerung in der Ethanol-Ausbeute von 0,15 auf 0,2 gg⁻¹ beobachtet werden. Um wirtschaftliche Ausbeuten und Konzentrationen des Produkts erzielen zu k{\"o}nnen, ist es notwendig den Prozess weiter zu optimieren. Im Einzelfall muss {\"u}berpr{\"u}ft werden, ob diese Verfahrensweise auch f{\"u}r die Produktion anderer interessanter Stoffe (wie Itacons{\"a}ure, Bernsteins{\"a}ure) geeignet ist.},
  language  = {de}
}
@misc{PothMonzonTippkoetteretal.2009,
  author    = {Poth, S. and Monzon, M. and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Enzymatische Hydrolyse von vorbehandelter Lignocellulose},
  series = {Chemie Ingenieur Technik},
  volume    = {81},
  journal   = {Chemie Ingenieur Technik},
  number    = {8},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.200950244},
  pages     = {1049},
  year      = {2009},
  abstract  = {Die {\"o}konomische Abh{\"a}ngigkeit von fossilen Brennstoffen und der klimatische Wandel durch die Nutzung dieser haben zu einer intensiven Suche nach erneuerbaren Rohstoffen f{\"u}r die Produktion von Chemikalien und Treibstoffen gef{\"u}hrt. Ein viel versprechender Rohstoff in diesem Zusammenhang sind Zucker, die mittels enzymatischer Hydrolyse aus Lignocellulose gewonnen und beispielsweise zu Ethanol umgesetzt werden k{\"o}nnen. Dabei ist es notwendig die Hydrolyse in Hinsicht auf das verwendete Substrat und die Verwendung der entstehenden Hydrolysate f{\"u}r die Fermentation von Alkohol zu optimieren. Als Substrat dienen Cellulose- und Hemicellulose-Fraktionen, die durch thermo-chemische Vorbehandlung von Holz gewonnen werden. Die Vorbehandlung erfolgt bei unserem Projektpartner am Johann Heinrich von Th{\"u}nen Institut in Hamburg. Verschiedene kommerziell erh{\"a}ltliche Enzyme, thermostabile eingeschlossen, wurden auf ihre F{\"a}higkeit hin untersucht, diese Fraktionen zu den entsprechenden Zuckern umsetzen zu k{\"o}nnen. Um die Konzentration an fermentierbaren Zuckern zu steigern werden verschiedene Optimierungen durchgef{\"u}hrt, z. B. die Erh{\"o}hung der Substrat- bzw. Enzymkonzentrationen. Ein weiterer interessanter Ansatz, welcher ebenfalls verfolgt wird, ist es die Hydrolyse und die Fermentation in einem Schritt durchzuf{\"u}hren.},
  language  = {de}
}
@article{PothMonzonTippkoetteretal.2011,
  author    = {Poth, Sebastian and Monzon, Magaly and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Lignocellulosic biorefinery: Process integration of hydrolysis and fermentation (SSF process)},
  series = {Holzforschung},
  volume    = {65},
  journal   = {Holzforschung},
  number    = {5},
  publisher = {De Gruyter},
  address   = {Berlin},
  pages     = {633 -- 637},
  year      = {2011},
  abstract  = {The aim of the present work is the process integration and the optimization of the enzymatic hydrolysis of wood and the following fermentation of the products to ethanol. The substrate is a fiber fraction obtained by organosolv pre-treatment of beech wood. For the ethanol production, a co-fermentation by two different yeasts (Saccharomyces cerevisiae and Pachysolen tannophilus) was carried out to convert glucose as well as xylose. Two approaches has been followed: 1. A two step process, in which the hydrolysis of the fiber fraction and the fermentation to product are separated from each other. 2. A process, in which the hydrolysis and the fermentation are carried out in one single process step as simultaneous saccharification and fermentation (SSF). Following the first approach, a yield of about 0.15 g ethanol per gram substrate can be reached. Based on the SSF, one process step can be saved, and additionally, the gained yield can be raised up to 0.3 g ethanol per gram substrate.},
  language  = {en}
}
@inproceedings{PothMonzonTippkoetteretal.2010,
  author    = {Poth, Sebastian and Monzon, Magaly and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Lignocellulosic biorefinery : process integration of hydrolysis and fermentation},
  series = {Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany},
  booktitle = {Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany},
  publisher = {vTi},
  address   = {Hamburg},
  pages     = {65 -- 68},
  year      = {2010},
  language  = {en}
}
@article{PrielmeierHoerstermannGyngelletal.1992,
  author    = {Prielmeier, Franz and H{\"o}rstermann, D. and Gyngell, M. L. and Merboldt, K.-D.},
  title     = {Localized Proton MRS of Acute and Chronic Gyperglycemia in Rat Brain in vivo / D. H{\"o}rstermann, F. Prielmeier , M. L. Gyngell, K.-D. Merboldt, W. H{\"a}nicke, J. Frahm},
  series = {Book of Abstracts, SMRM, 11th Annual Meeting Berlin},
  journal   = {Book of Abstracts, SMRM, 11th Annual Meeting Berlin},
  pages     = {2740},
  year      = {1992},
  language  = {en}
}
@article{PrielmeierLang1988,
  author    = {Prielmeier, Franz and Lang, E. W.},
  title     = {Multinuclear Spin-Lattice Relaxation Time Studies of Supercooled Aqueous LiCl-Solutions / E .W. Lang, F. X. Prielmeier},
  series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 92 (1988)},
  journal   = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 92 (1988)},
  isbn      = {0005-9021},
  pages     = {717},
  year      = {1988},
  language  = {en}
}
@article{PrielmeierLangLuedemann1984,
  author    = {Prielmeier, Franz and Lang, E. W. and L{\"u}demann, H.-D.},
  title     = {Pressure dependence of the self-diffusion in liquid trifluoromethane / F. X. Prielmeier; E. W. Lang; H.-D. L{\"u}demann},
  series = {Molecular Physics. 52 (1984), H. 5},
  journal   = {Molecular Physics. 52 (1984), H. 5},
  isbn      = {0026-8976},
  pages     = {1105 -- 1113},
  year      = {1984},
  language  = {en}
}
@article{PrielmeierLangRadkowitschetal.1987,
  author    = {Prielmeier, Franz and Lang, E. W. and Radkowitsch, H. and L{\"u}demann, H. D.},
  title     = {High Pressure NMR Study of the Molecular Dynamics of Liquid fluoroform and deutero-fluoroform / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; L{\"u}demann, H. D.},
  series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10},
  journal   = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10},
  isbn      = {0005-9021},
  pages     = {1025 -- 1033},
  year      = {1987},
  language  = {en}
}
@article{PrielmeierLangRadkowitschetal.1987,
  author    = {Prielmeier, Franz and Lang, E. W. and Radkowitsch, H. and L{\"u}demann, H.-D.},
  title     = {High Pressure NMR Study of the Molecular Dynamics of Liquid methyl fluoride and deutero-methyl fluoride / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; L{\"u}demann, H. D.},
  series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10},
  journal   = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10},
  isbn      = {0005-9021},
  pages     = {1017 -- 1025},
  year      = {1987},
  language  = {en}
}
@article{PrielmeierLangSpeedyetal.1988,
  author    = {Prielmeier, Franz and Lang, E. W. and Speedy, R. J. and L{\"u}demann, H.-D.},
  title     = {The pressure Dependence of Self Diffusion in Supercooled Light and Heavy Water / F.X. Prielmeier, E .W. Lang, R. J. Speedy, H.-D. L{\"u}demann},
  series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 92 (1988)},
  journal   = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 92 (1988)},
  isbn      = {0005-9021},
  pages     = {1111},
  year      = {1988},
  language  = {en}
}
@article{PrielmeierLangSpeedyetal.1987,
  author    = {Prielmeier, Franz and Lang, E. W. and Speedy, R. J. and L{\"u}demann, H.-D.},
  title     = {Diffusion in supercooled water to 300 MPa},
  series = {Physical Review Letters. 59 (1987), H. 10},
  journal   = {Physical Review Letters. 59 (1987), H. 10},
  isbn      = {0031-9007},
  pages     = {1128 -- 1131},
  year      = {1987},
  language  = {en}
}
@article{PrielmeierLuedemann1986,
  author    = {Prielmeier, Franz and L{\"u}demann, H.-D.},
  title     = {Self diffusion in compressed liquid chloromethane, dichloromethane and trichloromethane / F. X. Prielmeier; H.-D. L{\"u}demann},
  series = {Molecular Physics. 58 (1986), H. 3},
  journal   = {Molecular Physics. 58 (1986), H. 3},
  isbn      = {0026-8976},
  pages     = {593 -- 604},
  year      = {1986},
  language  = {en}
}
@article{PrielmeierMerboldtHanickeetal.1993,
  author    = {Prielmeier, Franz and Merboldt, K. D. and Hanicke, W. and Frahm, J.},
  title     = {Dynamic high-resolution MR imaging of brain deoxygenation during transient anoxia in the anesthetized rat},
  series = {Journal of cerebral blood flow and metabolism. 13 (1993), H. 5},
  journal   = {Journal of cerebral blood flow and metabolism. 13 (1993), H. 5},
  isbn      = {0271-678X},
  pages     = {889 -- 894},
  year      = {1993},
  language  = {en}
}
@article{PrielmeierNagatomoFrahm1994,
  author    = {Prielmeier, Franz and Nagatomo, Yasushi and Frahm, Jens},
  title     = {Cerebral blood oxygenation in rat brain during hypoxic hypoxia. Quantitative MRI of effective transverse relaxation rates},
  series = {Magnetic Resonance in Medicine. 31 (1994), H. 6},
  journal   = {Magnetic Resonance in Medicine. 31 (1994), H. 6},
  isbn      = {0740-3194},
  pages     = {678 -- 681},
  year      = {1994},
  language  = {en}
}
@article{PrielmeierNagatomoWicketal.1995,
  author    = {Prielmeier, Franz and Nagatomo, Yasushi and Wick, Markus and Frahm, Jens},
  title     = {Dynamic monitoring of cerebral metabolites during and after transient global ischemia in rats by quantitative proton NMR spectroscopy in vivo / Yasushi Nagatomo, Markus Wick, Franz Prielmeier, Jens Frahm},
  series = {NMR in Biomedicine. 8 (1995), H. 6},
  journal   = {NMR in Biomedicine. 8 (1995), H. 6},
  isbn      = {1099-1492},
  pages     = {265 -- 270},
  year      = {1995},
  language  = {en}
}
@article{PrielmeierRadkowitschLangetal.1986,
  author    = {Prielmeier, Franz and Radkowitsch, H. and Lang, E. W. and L{\"u}demann, H.-D.},
  title     = {Density dependence of the molecular dynamics of fluid CH3F and CF3H studied by NMR / H. Radkowitsch, F. X. Prielmeier, E. W. Lang and H.-D. L{\"u}demann},
  series = {Physica B+C. 139-140 (1986)},
  journal   = {Physica B+C. 139-140 (1986)},
  isbn      = {0921-4526},
  pages     = {96 -- 99},
  year      = {1986},
  language  = {en}
}
@article{PrielmeierSpeedyLuedemann1987,
  author    = {Prielmeier, Franz and Speedy, R. J. and L{\"u}demann, H.-D.},
  title     = {High Pressure NMR Self-Diffusion Studies on Supercooled Water},
  series = {High Pressure Science and Technology Proceeding XI AIRAPT, Kiew. 1},
  journal   = {High Pressure Science and Technology Proceeding XI AIRAPT, Kiew. 1},
  pages     = {75},
  year      = {1987},
  language  = {en}
}
@article{PrielmeierSpeedyVardagetal.1989,
  author    = {Prielmeier, Franz and Speedy, R. J. and Vardag, T. and Lang, E. W.},
  title     = {Diffusion in simple fluids / R. J. Speedy; F. X. Prielmeier; T. Vardag; E. W. Lang; H.-D. L{\"u}demann},
  series = {Molecular Physics. 66 (1989), H. 3},
  journal   = {Molecular Physics. 66 (1989), H. 3},
  isbn      = {0026-8976},
  pages     = {577 -- 590},
  year      = {1989},
  language  = {en}
}
@article{PrielmeierWickNagatomoetal.1995,
  author    = {Prielmeier, Franz and Wick, Markus and Nagatomo, Yasushi and Frahm, Jens},
  title     = {Alteration of Intracellular Metabolite Diffusion in Rat Brain In Vivo During Ischemia and Reperfusion / Markus Wick, Yasushi Nagatomo, Franz Prielmeier, Jens Frahm},
  series = {Stroke. 26 (1995), H. 10},
  journal   = {Stroke. 26 (1995), H. 10},
  isbn      = {0039-2499},
  pages     = {1930 -- 1934},
  year      = {1995},
  language  = {en}
}
@article{PrielmeierWoznyjLuedemann1984,
  author    = {Prielmeier, Franz and Woznyj, M. and L{\"u}demann, H.-D.},
  title     = {Pressure Dependence of the Melting and Self Diffusion in 2,2-Dimethylpropane, 2,2-Dimethylpropionitrile, and 2-Methylpropanol-2 / M. Woznyj, F. X. Prielmeier, H.-D. L{\"u}demann},
  series = {Zeitschrift f{\"u}r Naturforschung A, Journal of Physical Sciences. 39 (1984)},
  journal   = {Zeitschrift f{\"u}r Naturforschung A, Journal of Physical Sciences. 39 (1984)},
  isbn      = {0932-0784},
  pages     = {800},
  year      = {1984},
  language  = {en}
}
@article{RaabKappelKraemeretal.2011,
  author    = {Raab, Monika and Kappel, Sven and Kr{\"a}mer, Andrea and Sanhaji, Mourad and Matthess, Yves and Kurunci-Csacsko, Elisabeth and Calzada-Wack, Julia and Rathkolb, Birgit and Rosman, Jan and Adler, Thure and Busch, Dirk H. and Esposito, Irene and Fuchs, Helmut and Gailus-Durner, Val{\´e}rie and Klingenspor, Martin and Wolf, Eckhard and S{\"a}nger, Nicole and Prinz, Florian and Hrabe de Angelis, Martin and Seibler, Jost and Yuan, Juping and Bergmann, Martin and Knecht, Rainald and Kreft, Bertolt and Strebhardt, Klaus},
  title     = {Toxicity modelling of Plk1-targeted therapies in genetically engineered mice and cultured primary mammalian cells},
  series = {Nature Communications},
  volume    = {2},
  journal   = {Nature Communications},
  number    = {395},
  publisher = {Nature},
  address   = {London},
  issn      = {2041-1723},
  doi       = {10.1038/ncomms1395},
  pages     = {1 -- 11},
  year      = {2011},
  language  = {en}
}
@article{RachingerBauchStrittmatteretal.2013,
  author    = {Rachinger, Michael and Bauch, Melanie and Strittmatter, Axel and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Daniel, Rolf and Liebl, Wolfgang and Liesegang, Heiko and Ehrenreich, Armin},
  title     = {Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis},
  series = {Journal of biotechnology},
  volume    = {Vol. 164},
  journal   = {Journal of biotechnology},
  number    = {Iss. 4},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  pages     = {365 -- 369},
  year      = {2013},
  language  = {en}
}
@book{Rath1984,
  author    = {Rath, Walter},
  title     = {Umsetzung [alpha,beta]-ungesaettigter Ketone und ihrer Vorprodukte mit Urotropin},
  pages     = {XIV, 209 S. : graph. Darst.},
  year      = {1984},
  language  = {de}
}
@book{RathDzierzynski1995,
  author    = {Rath, Walter and Dzierzynski, Elmar},
  title     = {Solvent-free contact adhesive = L{\"o}sungsmittelfreier Kontaktklebstoff / Rath, Walter ; Dzierzynski, Elmar [Erfinder]},
  publisher = {Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen},
  year      = {1995},
  language  = {en}
}
@book{RathKochReichardt2002,
  author    = {Rath, Walter and Koch, Markus and Reichardt, R{\"u}diger},
  title     = {Composition de polyurethanne et joint d'etancheite pour vitrage = Polyurethanzusammensetzung und Verglasungsdichtungs-Profil / Rath, Walter, Koch, Markus ; Reichardt, R{\"u}diger [Erfinder]},
  publisher = {Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen},
  year      = {2002},
  language  = {de}
}
@misc{RathSeitz1993,
  author    = {Rath, Walter and Seitz, Karsten},
  title     = {Fr{\"u}hregenfeste Dichtmasse auf Basis w{\"a}ssriger Acrylatdispersionen und Verfahren zu ihrer Herstellung},
  publisher = {Deutsches Patent- und Markenamt},
  address   = {M{\"u}nchen},
  year      = {1993},
  language  = {de}
}
@misc{RathSeitz1993,
  author    = {Rath, Walter and Seitz, Karsten},
  title     = {Fr{\"u}hregenfeste Dichtmasse auf Basis w{\"a}ssriger Acrylatdispersionen und Verfahren zu ihrer Herstellung},
  publisher = {Deutsches Patent- und Markenamt},
  address   = {M{\"u}nchen},
  year      = {1993},
  language  = {de}
}
@article{RatkeMilowLisinskietal.2014,
  author    = {Ratke, Lorenz and Milow, Barbara and Lisinski, Susanne and Hoepfner, Sandra},
  title     = {On an effect of fine ceramic particles on the structure of aerogels},
  series = {Microgravity science and technology},
  volume    = {26},
  journal   = {Microgravity science and technology},
  publisher = {Springer Nature},
  address   = {Heidelberg},
  issn      = {0938-0108 ; 1875-0494},
  doi       = {10.1007/s12217-014-9380-2},
  pages     = {103 -- 110},
  year      = {2014},
  language  = {en}
}
@article{RaueWambachGloeggleretal.2014,
  author    = {Raue, Markus and Wambach, M. and Gl{\"o}ggler, S. and Grefen, Dana and Kaufmann, R. and Abetz, C. and Georgopanos, P. and Handge, U. A. and Mang, Thomas and Bl{\"u}mich, B. and Abetz, V.},
  title     = {Investigation of historical hard rubber ornaments of Charles Goodyear},
  series = {Macromolecular chemistry and physics},
  volume    = {Vol. 215},
  journal   = {Macromolecular chemistry and physics},
  number    = {No. 3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1022-1352},
  pages     = {245 -- 254},
  year      = {2014},
  language  = {en}
}
@article{RauppSchmittWalzetal.2018,
  author    = {Raupp, Sebastian M. and Schmitt, Marcel and Walz, Anna-Lena and Diehm, Ralf and Hummel, Helga and Scharfer, Philip and Schabel, Wilhelm},
  title     = {Slot die stripe coating of low viscous fluids},
  series = {Journal of Coatings Technology and Research},
  volume    = {15},
  journal   = {Journal of Coatings Technology and Research},
  number    = {5},
  publisher = {Springer},
  issn      = {1935-3804},
  doi       = {10.1007/s11998-017-0039-y},
  pages     = {899 -- 911},
  year      = {2018},
  abstract  = {Slot die coating is applied to deposit thin and homogenous films in roll-to-roll and sheet-to-sheet applications. The critical step in operation is to choose suitable process parameters within the process window. In this work, we investigate an upper limit for stripe coatings. This maximum film thickness is characterized by stripe merging which needs to be avoided in a stable process. It is shown that the upper limit reduces the process window for stripe coatings to a major extent. As a result, stripe coatings at large coating gaps and low viscosities are only possible for relatively thick films. Explaining the upper limit, a theory of balancing the side pressure in the gap region in the cross-web direction has been developed.},
  language  = {en}
}
@article{ReugelsBoggettiScheeretal.2006,
  author    = {Reugels, Alexander M. and Boggetti, Barbara and Scheer, Nico and Campos-Ortega, Jos{\´e} A.},
  title     = {Asymmetric localization of Numb:EGFP in dividing neuroepithelial cells during neurulation in Danio rerio},
  series = {Developmental Dynamics},
  volume    = {235},
  journal   = {Developmental Dynamics},
  number    = {4},
  issn      = {1097-0177},
  doi       = {10.1002/dvdy.20699},
  pages     = {934 -- 948},
  year      = {2006},
  language  = {en}
}
@article{RibitschHeumannKarletal.2012,
  author    = {Ribitsch, D. and Heumann, S. and Karl, W. and Gerlach, J. and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Siegert, Petra and Lange, J. and Maurer, Karl-Heinz and Berg, G. and Guebitz, G. M. and Schwab, H.},
  title     = {Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {157},
  journal   = {Journal of biotechnology},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2011.09.025},
  pages     = {140 -- 147},
  year      = {2012},
  abstract  = {A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3. From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.},
  language  = {en}
}
@article{RibitschKarlBirnerGruenbergeretal.2010,
  author    = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.},
  title     = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {150},
  journal   = {Journal of biotechnology},
  number    = {3},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2010.09.947},
  pages     = {408 -- 416},
  year      = {2010},
  abstract  = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.},
  language  = {en}
}
@article{RieplPettrakFaulstichetal.2010,
  author    = {Riepl, Herbert Matthias and Pettrak, J{\"u}rgen and Faulstich, Martin and Herrmann, Wolfgang Anton},
  title     = {Self metathesis of fatty alcohols and amines to provide monomers for polyester and polyamide products},
  series = {Macromolecular Symposia},
  volume    = {293},
  journal   = {Macromolecular Symposia},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-3900 (eISSN)},
  doi       = {10.1002/masy.200900041},
  pages     = {39 -- 42},
  year      = {2010},
  abstract  = {Self metathesis of oleochemicals offers a variety of bifunctional compounds, that can be used as monomer for polymer production. Many precursors are in huge scales available, like oleic acid ester (biodiesel), oleyl alcohol (tensides), oleyl amines (tensides, lubricants). We show several ways to produce and separate and purify C18-α,ω-bifunctional compounds, using Grubbs 2nd Generation catalysts, starting from technical grade educts.},
  language  = {en}
}
@article{RossPlummerRodeetal.2010,
  author    = {Ross, Jillian and Plummer, Simon M. and Rode, Anja and Scheer, Nico and Bower, Conrad C. and Vogel, Ortwin and Henderson, Colin J. and Wolf, C. Roland and Elcombe, Clifford R.},
  title     = {Human constitutive androstane receptor (CAR) and pregnane X receptor (PXR) support the hypertrophic but not the hyperplastic response to the murine nongenotoxic hepatocarcinogens phenobarbital and chlordane in vivo},
  series = {Toxicological Sciences},
  volume    = {116},
  journal   = {Toxicological Sciences},
  number    = {2},
  publisher = {Oxford University Press},
  address   = {Oxford},
  issn      = {1096-0929},
  doi       = {10.1093/toxsci/kfq118},
  pages     = {452 -- 466},
  year      = {2010},
  abstract  = {Mouse nongenotoxic hepatocarcinogens phenobarbital (PB) and chlordane induce hepatomegaly characterized by hypertrophy and hyperplasia. Increased cell proliferation is implicated in the mechanism of tumor induction. The relevance of these tumors to human health is unclear. The xenoreceptors, constitutive androstane receptors (CARs), and pregnane X receptor (PXR) play key roles in these processes. Novel "humanized" and knockout models for both receptors were developed to investigate potential species differences in hepatomegaly. The effects of PB (80 mg/kg/4 days) and chlordane (10 mg/kg/4 days) were investigated in double humanized PXR and CAR (huPXR/huCAR), double knockout PXR and CAR (PXRKO/CARKO), and wild-type (WT) C57BL/6J mice. In WT mice, both compounds caused increased liver weight, hepatocellular hypertrophy, and cell proliferation. Both compounds caused alterations to a number of cell cycle genes consistent with induction of cell proliferation in WT mice. However, these gene expression changes did not occur in PXRKO/CARKO or huPXR/huCAR mice. Liver hypertrophy without hyperplasia was demonstrated in the huPXR/huCAR animals in response to both compounds. Induction of the CAR and PXR target genes, Cyp2b10 and Cyp3a11, was observed in both WT and huPXR/huCAR mouse lines following treatment with PB or chlordane. In the PXRKO/CARKO mice, neither liver growth nor induction of Cyp2b10 and Cyp3a11 was seen following PB or chlordane treatment, indicating that these effects are CAR/PXR dependent. These data suggest that the human receptors are able to support the chemically induced hypertrophic responses but not the hyperplastic (cell proliferation) responses. At this time, we cannot be certain that hCAR and hPXR when expressed in the mouse can function exactly as the genes do when they are expressed in human cells. However, all parameters investigated to date suggest that much of their functionality is maintained.},
  language  = {en}
}
@misc{RossJonesTeumerCapitainetal.2018,
  author    = {Ross-Jones, J. and Teumer, T. and Capitain, C. and Tippk{\"o}tter, Nils and Krause, M. J. and Methner, F.-J. and R{\"a}dle, M.},
  title     = {Analytical methods for in-line characterization of beer haze},
  series = {Trends in Brewing},
  journal   = {Trends in Brewing},
  year      = {2018},
  abstract  = {In most beers, producers strive to minimize haze to maximize visual appeal. To detect the formation of particulates, a measurement system for sub-micron particles is required. Beer haze is naturally occurring, composed of protein or polyphenol particles; in their early stage of growth their size is smaller than 2 µm. Microscopy analysis is time and resource intensive; alternatively, backscattering is an inexpensive option for detecting particle sizes of interest.},
  language  = {en}
}
@inproceedings{RothMoehringTippkoetter2016,
  author    = {Roth, J. and M{\"o}hring, S. and Tippk{\"o}tter, Nils},
  title     = {Characterization and evaluation of lignocellulosic biomass 130 hydrolysates for ABE fermentation},
  series = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  booktitle = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  publisher = {DECHEMA},
  address   = {Frankfurt am Main},
  pages     = {130},
  year      = {2016},
  language  = {en}
}
@misc{RothTippkoetter2016,
  author    = {Roth, J. and Tippk{\"o}tter, Nils},
  title     = {New Approach for Enzymatic Hydrolysis of Lignocellulose with Selective Diffusion Separation of the Monosaccharide Products},
  series = {Chemie Ingenieur Technik},
  volume    = {88},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.201650301},
  pages     = {1237},
  year      = {2016},
  abstract  = {Enzymatic hydrolysis of lignocellulosic material plays an important role in the classical biorefinery approach. Apart from the pretreatment of the raw material, hydrolysis is the basis for the conversion of the cellulose and hemicellulose fraction into fermentable sugars. After hydrolysis, usually a solid-liquid separation takes place, in order to separate the residual plant material from the sugar-rich fraction, which can be subsequently used in a fermentation step. In order to factor out the separation step, the usage of in alginate immobilized crude cellulose fiber beads (CFBs) were evaluated. Pretreated cellulose fibers are incorporated in an alginate matrix together with the relevant enzymes. In doing so, sugars diffuse trough the alginate matrix, allowing a simplified delivery into the surrounding fluid. This again reduces product inhibition of the glucose on the enzyme catalysts. By means of standardized bead production the hydrolysis in lab scale was possible. First results show that liberation of glucose and xylose is possible, allowing a maximum total sugar yield of 75 \%.},
  language  = {en}
}
@article{RothTippkoetter2016,
  author    = {Roth, Jasmine and Tippk{\"o}tter, Nils},
  title     = {Evaluation of lignocellulosic material for butanol production using enzymatic hydrolysate medium},
  series = {Cellulose Chemistry and Technology},
  volume    = {50},
  journal   = {Cellulose Chemistry and Technology},
  number    = {3-4},
  publisher = {Editura Academiei Romane},
  address   = {Bukarest},
  pages     = {405 -- 410},
  year      = {2016},
  abstract  = {Butanol is a promising gasoline additive and platform chemical that can be readily produced via acetone-butanolethanol (ABE) fermentation from pretreated lignocellulosic materials. This article examines lignocellulosic material from beech wood for ABE fermentation, using Clostridium acetobutylicum. First, the utilization of both C₅₋ (xylose) and C₆₋ (glucose) sugars as sole carbon source was investigated in static cultivation, using serum bottles and synthetic medium. The utilization of pentose sugar resulted in a solvent yield of 0.231 g·g_sugar⁻¹, compared to 0.262 g·g_sugar⁻¹ using hexose. Then, the Organosolv pretreated crude cellulose fibers (CF) were enzymatically decomposed, and the resulting hydrolysate medium was analyzed for inhibiting compounds (furans, organic acids, phenolics) and treated with ionexchangers for detoxification. Batch fermentation in a bioreactor using CF hydrolysate medium resulted in a total solvent yield of 0.20 gABE·g_sugar⁻¹.},
  language  = {en}
}
@misc{RothkranzKrafftTippkoetter2022,
  author    = {Rothkranz, Berit and Krafft, Simone and Tippk{\"o}tter, Nils},
  title     = {Media optimization for sustainable fuel production: How to produce biohydrogen from renewable resources with Thermotoga neapolitana},
  series = {Chemie Ingenieur Technik},
  volume    = {94},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.202255305},
  pages     = {1298 -- 1299},
  year      = {2022},
  abstract  = {Hydrogen is playing an increasingly important role in research and politics as an energy carrier of the future. Since hydrogen has commonly been produced from methane by steam reforming, the need for climate-friendly, alternative production routes is emerging. In addition to electrolysis, fermentative routes for the production of so-called biohydrogen are "green" alternatives. The application of microorganisms offers the advantage of sustainable production from renewable resources using easily manageable technologies. In this project, the hyperthermophilic, anaerobic microorganism Thermotoga neapolitana is used for the productio nof biohydrogen from renewable resources. The enzymatically hydrolyzed resources were used in fermentation leading to yield coefficients of 1.8 mole H₂ per mole glucose when using hydrolyzed straw and ryegrass supplemented with medium, respectively. These results are similar to the hydrogen yields when using Thermotoga basal medium with glucose (TBGY) as control group. In order to minimize the supplementation of the hydrolysate and thus increase the economic efficiency of the process, the essential media components were identified. The experiments revealed NaCl, KCl, and glucose as essential components for cell growth as well as biohydrogen production. When excluding NaCl, a decrease of 96\% in hydrogen production occured.},
  language  = {en}
}
@article{RoehlenPilasDahmenetal.2018,
  author    = {R{\"o}hlen, Desiree and Pilas, Johanna and Dahmen, Markus and Keusgen, Michael and Selmer, Thorsten and Sch{\"o}ning, Michael Josef},
  title     = {Toward a Hybrid Biosensor System for Analysis of Organic and Volatile Fatty Acids in Fermentation Processes},
  series = {Frontiers in Chemistry},
  journal   = {Frontiers in Chemistry},
  number    = {6},
  publisher = {Frontiers},
  address   = {Lausanne},
  doi       = {10.3389/fchem.2018.00284},
  pages     = {Artikel 284},
  year      = {2018},
  abstract  = {Monitoring of organic acids (OA) and volatile fatty acids (VFA) is crucial for the control of anaerobic digestion. In case of unstable process conditions, an accumulation of these intermediates occurs. In the present work, two different enzyme-based biosensor arrays are combined and presented for facile electrochemical determination of several process-relevant analytes. Each biosensor utilizes a platinum sensor chip (14 × 14 mm²) with five individual working electrodes. The OA biosensor enables simultaneous measurement of ethanol, formate, d- and l-lactate, based on a bi-enzymatic detection principle. The second VFA biosensor provides an amperometric platform for quantification of acetate and propionate, mediated by oxidation of hydrogen peroxide. The cross-sensitivity of both biosensors toward potential interferents, typically present in fermentation samples, was investigated. The potential for practical application in complex media was successfully demonstrated in spiked sludge samples collected from three different biogas plants. Thereby, the results obtained by both of the biosensors were in good agreement to the applied reference measurements by photometry and gas chromatography, respectively. The proposed hybrid biosensor system was also used for long-term monitoring of a lab-scale biogas reactor (0.01 m³) for a period of 2 months. In combination with typically monitored parameters, such as gas quality, pH and FOS/TAC (volatile organic acids/total anorganic carbonate), the amperometric measurements of OA and VFA concentration could enhance the understanding of ongoing fermentation processes.},
  language  = {en}
}
@article{RoehlenPilasSchoeningetal.2017,
  author    = {R{\"o}hlen, Desiree and Pilas, Johanna and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid},
  series = {Applied Biochemistry and Biotechnology},
  volume    = {183},
  journal   = {Applied Biochemistry and Biotechnology},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1559-0291},
  doi       = {10.1007/s12010-017-2578-1},
  pages     = {566 -- 581},
  year      = {2017},
  abstract  = {Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM-1 (L-malate biosensor) and 0.4 μA mM-1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0-10.0 mM with a sensitivity of 0.09 μA mM-1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.},
  language  = {en}
}
@article{RoeschKratzHeringetal.2016,
  author    = {R{\"o}sch, C. and Kratz, F. and Hering, T. and Trautmann, S. and Umanskaya, N. and Tippk{\"o}tter, Nils and M{\"u}ller-Renno, C.M. and Ulber, Roland and Hannig, M. and Ziegler, C.},
  title     = {Albumin-lysozyme interactions: cooperative adsorption on titanium and enzymatic activity},
  series = {Colloids and Surfaces B: Biointerfaces},
  volume    = {149},
  journal   = {Colloids and Surfaces B: Biointerfaces},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  doi       = {10.1016/j.colsurfb.2016.09.048},
  pages     = {115 -- 121},
  year      = {2016},
  abstract  = {The interplay of albumin (BSA) and lysozyme (LYZ) adsorbed simultaneously on titanium was analyzed by gel electrophoresis and BCA assay. It was found that BSA and lysozyme adsorb cooperatively. Additionally, the isoelectric point of the respective protein influences the adsorption. Also, the enzymatic activity of lysozyme and amylase (AMY) in mixtures with BSA was considered with respect to a possible influence of protein-protein interaction on enzyme activity. Indeed, an increase of lysozyme activity in the presence of BSA could be observed. In contrast, BSA does not influence the activity of amylase.},
  language  = {en}
}
@article{SalpatiChuChenetal.2014,
  author    = {Salpati, Laurent and Chu, Xiaoyan and Chen, Liangfu and Prasad, Bhagwat and Dallas, Shannon and Evers, Raymond and Mamaril-Fishman, Donna and Geier, Ethan G. and Kehler, Jonathan and Kunta, Jeevan and Mezler, Mario and Laplanche, Loic and Pang, Jodie and Soars, Matthew G. and Unadkat, Jashvant D. and van Waterschoot, Robert A.B. and Yabut, Jocelyn and Schinkel, Alfred H. and Scheer, Nico and Rode, Anja},
  title     = {Evaluation of organic anion transporting polypeptide 1B1 and 1B3 humanized mice as a translational model to study the pharmacokinetics of statins},
  series = {Drug Metabolism and Disposition},
  volume    = {42},
  journal   = {Drug Metabolism and Disposition},
  number    = {8},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-009X},
  doi       = {10.1124/dmd.114.057976},
  pages     = {1301 -- 1313},
  year      = {2014},
  abstract  = {Organic anion transporting polypeptide (Oatp) 1a/1b knockout and OATP1B1 and -1B3 humanized mouse models are promising tools for studying the roles of these transporters in drug disposition. Detailed characterization of these models will help to better understand their utility for predicting clinical outcomes. To advance this approach, we carried out a comprehensive analysis of these mouse lines by evaluating the compensatory changes in mRNA expression, quantifying the amounts of OATP1B1 and -1B3 protein by liquid chromatography-tandem mass spectrometry, and studying the active uptake in isolated hepatocytes and the pharmacokinetics of some prototypical substrates including statins. Major outcomes from these studies were 1) mostly moderate compensatory changes in only a few genes involved in drug metabolism and disposition, 2) a robust hepatic expression of OATP1B1 and -1B3 proteins in the respective humanized mouse models, and 3) functional activities of the human transporters in hepatocytes isolated from the humanized models with several substrates tested in vitro and with pravastatin in vivo. However, the expression of OATP1B1 and -1B3 in the humanized models did not significantly alter liver or plasma concentrations of rosuvastatin and pitavastatin compared with Oatp1a/1b knockout controls under the conditions used in our studies. Hence, although the humanized OATP1B1 and -1B3 mice showed in vitro and/or in vivo functional activity with some statins, further characterization of these models is required to define their potential use and limitations in the prediction of drug disposition and drug-drug interactions in humans.},
  language  = {en}
}
@incollection{SamuelssonScheerWilsonetal.2017,
  author    = {Samuelsson, K. and Scheer, Nico and Wilson, I. and Wolf, C.R. and Henderson, C.J.},
  title     = {Genetically Humanized Animal Models},
  series = {Comprehensive Medicinal Chemistry III. 3rd Edition},
  booktitle = {Comprehensive Medicinal Chemistry III. 3rd Edition},
  editor    = {Chackalamannil, Samuel},
  publisher = {Elsevier},
  address   = {Saint Louis},
  isbn      = {978-0-12-803201-5},
  doi       = {10.1016/B978-0-12-409547-2.12376-5},
  pages     = {130 -- 149},
  year      = {2017},
  abstract  = {Genetically humanized mice for proteins involved in drug metabolism and toxicity and mice engrafted with human hepatocytes are emerging as promising in vivo models for improved prediction of the pharmacokinetic, drug-drug interaction, and safety characteristics of compounds in humans. This is an overview on the genetically humanized and chimeric liver-humanized mouse models, which are illustrated with examples of their utility in drug metabolism and toxicity studies. The models are compared to give guidance for selection of the most appropriate model by highlighting advantages and disadvantages to be carefully considered when used for studies in drug discovery and development.},
  language  = {en}
}
@article{ScheeleBongaertsMaureretal.2009,
  author    = {Scheele, S. and Bongaerts, Johannes and Maurer, K.-H. and Freudl, R.},
  title     = {Sekretion einer Kofaktor-haltigen Oxidase durch Corynebacterium glutamicum},
  series = {Chemie - Ingenieur - Technik (CIT)},
  volume    = {Vol. 81},
  journal   = {Chemie - Ingenieur - Technik (CIT)},
  number    = {Iss. 8},
  issn      = {1522-2640 (E-Journal); 0009-286X (Print)},
  pages     = {1309},
  year      = {2009},
  language  = {de}
}
@article{ScheeleOertelBongaertsetal.2013,
  author    = {Scheele, Sandra and Oertel, Dan and Bongaerts, Johannes and Evers, Stefan and Hellmuth, Hendrik and Maurer, Karl-Heinz and Bott, Michael and Freudl, Roland},
  title     = {Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum},
  series = {Microbial biotechnology},
  journal   = {Microbial biotechnology},
  publisher = {Wiley-Blackwell},
  address   = {Oxford},
  issn      = {1751-7915},
  pages     = {202 -- 206},
  year      = {2013},
  language  = {en}
}
@article{ScheerBalimaneHaywardetal.2012,
  author    = {Scheer, Nico and Balimane, Praveen and Hayward, Michael D. and Buechel, Sandra and Kauselmann, Gunther and Wolf, C. Roland},
  title     = {Generation and Characterization of a Novel Multidrug Resistance Protein 2 Humanized Mouse Line},
  series = {Drug Metabolism and Disposition},
  volume    = {40},
  journal   = {Drug Metabolism and Disposition},
  number    = {11},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/dmd.112.047605},
  pages     = {2212 -- 2218},
  year      = {2012},
  abstract  = {The multidrug resistance protein (MRP) 2 is predominantly expressed in liver, intestine, and kidney, where it plays an important role in the excretion of a range of drugs and their metabolites or endogenous compounds into bile, feces, and urine. Mrp knockout [Mrp2(-/-)] mice have been used recently to study the role of MRP2 in drug disposition. Here, we describe the first generation and initial characterization of a mouse line humanized for MRP2 (huMRP2), which is nulled for the mouse Mrp2 gene and expresses the human transporter in the organs and cell types where MRP2 is normally expressed. Analysis of the mRNA expression for selected cytochrome P450 and transporter genes revealed no major changes in huMRP2 mice compared with wild-type controls. We show that human MRP2 is able to compensate functionally for the loss of the mouse transporter as demonstrated by comparable bilirubin levels in the humanized mice and wild-type controls, in contrast to the hyperbilirubinemia phenotype that is observed in MRP2(-/-) mice. The huMRP2 mouse provides a model to study the role of the human transporter in drug disposition and in assessing the in vivo consequences of inhibiting this transporter by compounds interacting with human MRP2.},
  language  = {en}
}
@article{ScheerCamposOrtega1999,
  author    = {Scheer, Nico and Campos-Ortega, Jos{\´e} A.},
  title     = {Use of the Gal4-UAS technique for targeted gene expression in the zebrafish},
  series = {Mechanism of Development},
  volume    = {80},
  journal   = {Mechanism of Development},
  number    = {2},
  issn      = {0925-4773},
  doi       = {10.1016/S0925-4773(98)00209-3},
  pages     = {153 -- 158},
  year      = {1999},
  language  = {en}
}