@article{MuschallikMolinnusBongaertsetal.2017,
  author    = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten},
  title     = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme},
  series = {Journal of Biotechnology},
  volume    = {258},
  journal   = {Journal of Biotechnology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2017.07.020},
  pages     = {41 -- 50},
  year      = {2017},
  abstract  = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.},
  language  = {en}
}
@article{MerschenzQuackHemmerlingWunderlich2004,
  author    = {Merschenz-Quack, Angelika and Hemmerling, Hans-J{\"o}rg and Wunderlich, Hartmut},
  title     = {1,2-Deoxygenation of vic-Dihydroxyindenoimidazoles: Optimization of a Novel Deoxygenation Reagent. I. / Hemmerling, Hans-J{\"o}rg ; Merschenz-Quack, Angelika ; Wunderlich, Hartmut},
  series = {Zeitschrift f{\"u}r Naturforschung B. 59 (2004), H. 10},
  journal   = {Zeitschrift f{\"u}r Naturforschung B. 59 (2004), H. 10},
  isbn      = {0932-0776},
  pages     = {1143 -- 1152},
  year      = {2004},
  language  = {en}
}
@article{MangKricheldorf1981,
  author    = {Mang, Thomas and Kricheldorf, Hans R.},
  title     = {13-C-NMR Sequence Analysis 20. Stereospecificity of the polymerization of D,L-Leu-NCA and D,L-Val-NCA / Kricheldorf, Hans R. ; Mang, Thomas},
  series = {Die makromolekulare Chemie. 182 (1981), H. 11},
  journal   = {Die makromolekulare Chemie. 182 (1981), H. 11},
  isbn      = {1022-1352},
  pages     = {3077 -- 3098},
  year      = {1981},
  language  = {en}
}
@article{MangKricheldorf1982,
  author    = {Mang, Thomas and Kricheldorf, Hans R.},
  title     = {13-C-NMR sequence analysis. 21. Stereoselectivity of oligopeptide syntheses / Kricheldorf, Hans R. ; Mang, Thomas},
  series = {Die makromolekulare Chemie. 183 (1982), H. 9},
  journal   = {Die makromolekulare Chemie. 183 (1982), H. 9},
  isbn      = {1022-1352},
  pages     = {2093 -- 2111},
  year      = {1982},
  language  = {en}
}
@article{MangKricheldorf1982,
  author    = {Mang, Thomas and Kricheldorf, Hans R.},
  title     = {13-C-NMR sequence analysis. 22. Stereoselectivity of the polymerization of D,L-leucine and D,L-valine N-thiocarboxy anhydrides / Kricheldorf, Hans R. ; Mang, Thomas},
  series = {Die makromolekulare Chemie. 183 (1982), H. 9},
  journal   = {Die makromolekulare Chemie. 183 (1982), H. 9},
  isbn      = {1022-1352},
  pages     = {2113 -- 2129},
  year      = {1982},
  language  = {en}
}
@article{SelmerYuBlaseretal.2006,
  author    = {Selmer, Thorsten and Yu, Lihua and Blaser, Martin and Andrei, Paula I.},
  title     = {4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of glycyl radical enzyme systems / Yu, L. ; Blaser, M. ; Andrei, PI. ; Pierik, AJ. Selmer, T.},
  series = {Biochemistry. 31 (2006), H. 45},
  journal   = {Biochemistry. 31 (2006), H. 45},
  pages     = {9584 -- 9592},
  year      = {2006},
  language  = {en}
}
@misc{BanowskiWaldmannLaueWadleetal.2004,
  author    = {Banowski, Bernhard and Waldmann-Laue, Marianne and Wadle, Armin and Siegert, Petra and S{\"a}ttler, Andreas},
  title     = {5-Lipoxigenase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen / Den Hague},
  pages     = {1 -- 12},
  year      = {2004},
  language  = {de}
}
@article{BrabandYegenPaulssenetal.2005,
  author    = {Braband, Henrik and Yegen, Eda and Paulßen, Elisabeth and Abram, Ulrich},
  title     = {[{ReN(PMe2Ph)3}{ReO3N}]2 - Structural Evidence for the Nitridotrioxorhenate(VII) Anion, [ReO3N]2-},
  series = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry},
  volume    = {631},
  journal   = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry},
  number    = {12},
  issn      = {1521-3749},
  doi       = {10.1002/zaac.200500240},
  pages     = {2408 -- 2410},
  year      = {2005},
  language  = {en}
}
@article{BiselliNollMuehlsiepenetal.2000,
  author    = {Biselli, Manfred and Noll, Thomas and M{\"u}hlsiepen, Heinz and Engels, Ralf},
  title     = {A cell-culture reactor for the on-line evaluation of radiopharmaceuticals : evaluation of the lumped constant of FDG in human glioma cells / Noll, Thomas ; M{\"u}hlensiepen, Heinz ; Engels, Ralf ; Hamacher, Kurt ; Papaspyrou, Manfred ; Langen, Karl-Josef ; Bi},
  series = {Journal of Nuclear Medicine. 41 (2000), H. 3},
  journal   = {Journal of Nuclear Medicine. 41 (2000), H. 3},
  isbn      = {0022-3123},
  pages     = {556 -- 564},
  year      = {2000},
  language  = {en}
}
@article{ScheerWilson2016,
  author    = {Scheer, Nico and Wilson, Ian D.},
  title     = {A comparison between genetically humanized and chimeric liver humanized mouse models for studies in drug metabolism and toxicity},
  series = {Drug Discovery Today},
  volume    = {21},
  journal   = {Drug Discovery Today},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1359-6446},
  doi       = {10.1016/j.drudis.2015.09.002},
  pages     = {250 -- 263},
  year      = {2016},
  abstract  = {Mice that have been genetically humanized for proteins involved in drug metabolism and toxicity and mice engrafted with human hepatocytes are emerging and promising in vivo models for an improved prediction of the pharmacokinetic, drug-drug interaction and safety characteristics of compounds in humans. The specific advantages and disadvantages of these models should be carefully considered when using them for studies in drug discovery and development. Here, an overview on the corresponding genetically humanized and chimeric liver humanized mouse models described to date is provided and illustrated with examples of their utility in drug metabolism and toxicity studies. We compare the strength and weaknesses of the two different approaches, give guidance for the selection of the appropriate model for various applications and discuss future trends and perspectives.},
  language  = {en}
}