@article{TippkoetterRoikaewUlberetal.2010,
  author    = {Tippk{\"o}tter, Nils and Roikaew, Wipa and Ulber, Roland and Hoffmann, Alexander and Denzler, Hans-J{\"o}rg and Buchholz, Heinrich},
  title     = {Paracoccus denitrificans for the effluent recycling during continuous denitrification of liquid food},
  series = {Biotechnology Progress},
  volume    = {26},
  journal   = {Biotechnology Progress},
  number    = {3},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {8756-7938},
  doi       = {10.1002/btpr.384},
  pages     = {756 -- 762},
  year      = {2010},
  abstract  = {Nitrate is an undesirable component of several foods. A typical case of contamination with high nitrate contents is whey concentrate, containing nitrate in concentrations up to 25 l. The microbiological removal of nitrate by Paracoccus denitrificans under formation of harmless nitrogen in combination with a cell retention reactor is described here. Focus lies on the resource-conserving design of a microbal denitrification process. Two methods are compared. The application of polyvinyl alcohol-immobilized cells, which can be applied several times in whey feed, is compared with the implementation of a two step denitrification system. First, the whey concentrate's nitrate is removed by ion exchange and subsequently the eluent regenerated by microorganisms under their retention by crossflow filtration. Nitrite and nitrate concentrations were determined by reflectometric color measurement with a commercially available Reflectoquant® device. Correction factors for these media had to be determined. During the pilot development, bioreactors from 4 to 250 mg·L-1 and crossflow units with membrane areas from 0.02 to 0.80 m2 were examined. Based on the results of the pilot plants, a scaling for the exemplary process of denitrifying 1,000 tons per day is discussed.},
  language  = {en}
}
@article{DegeringEggertPulsetal.2010,
  author    = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich},
  title     = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides},
  series = {Applied and environmental microbiology},
  volume    = {76},
  journal   = {Applied and environmental microbiology},
  number    = {19},
  publisher = {American Society for Microbiology},
  address   = {Washington, DC},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  doi       = {10.1128/AEM.01146-10},
  pages     = {6370 -- 6378},
  year      = {2010},
  abstract  = {Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.},
  language  = {en}
}
@article{WernerKrumbeSchumacheretal.2011,
  author    = {Werner, Frederik and Krumbe, Christoph and Schumacher, Katharina and Groebel, Simone and Spelthahn, Heiko and Stellberg, Michael and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Keusgen, Michael and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor},
  series = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  journal   = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1862-6319},
  pages     = {1340 -- 1344},
  year      = {2011},
  language  = {en}
}
@article{MartinsBlaserFeliksetal.2011,
  author    = {Martins, Berta M. and Blaser, Martin and Feliks, Mikolaj and Ullmann, Matthias G. and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme},
  series = {Journal of the American Chemical Society},
  journal   = {Journal of the American Chemical Society},
  publisher = {ACS Publications},
  address   = {Washington, DC},
  pages     = {1 -- 33},
  year      = {2011},
  language  = {en}
}
@article{SchiffelsBaumannSelmer2011,
  author    = {Schiffels, Johannes and Baumann, Marcus and Selmer, Thorsten},
  title     = {Facile analysis of short-chain fatty acids as 4-nitrophenyl esters in complex anaerobic fermentation samples by high performance liquid chromatography},
  series = {Journal of Chromatography A. 1218 (2011), H. 34},
  journal   = {Journal of Chromatography A. 1218 (2011), H. 34},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {0021-9673},
  pages     = {5848 -- 5851},
  year      = {2011},
  language  = {en}
}
@article{BaeckerDellePoghossianetal.2011,
  author    = {B{\"a}cker, Matthias and Delle, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Wagner, P. and Sch{\"o}ning, Michael Josef},
  title     = {Electrochemical sensor array for bioprocess monitoring},
  series = {Electrochimica Acta (2011)},
  volume    = {56},
  journal   = {Electrochimica Acta (2011)},
  number    = {26},
  publisher = {Elsevier},
  address   = {Amsterdam},
  pages     = {9673 -- 9678},
  year      = {2011},
  language  = {en}
}
@article{AggarwalSinghSinghetal.2011,
  author    = {Aggarwal, Prerna and Singh, Virendra and Singh, Arjun and Scherer, Ulrich W. and Singh, Tejvir and Singla, Madan L. and Srivastava, Alok},
  title     = {Physico-chemical transformations in swift heavy ion modified poly(ethyleneterephthalate)},
  series = {Radiation Physics and Chemistry},
  journal   = {Radiation Physics and Chemistry},
  publisher = {Pergamon Press},
  address   = {Oxford},
  isbn      = {0969-806X},
  pages     = {1 -- 28},
  year      = {2011},
  language  = {en}
}
@article{OosterhuisOehlschlaegerBergetal.2011,
  author    = {Oosterhuis, Koen and {\"O}hlschl{\"a}ger, Peter and Berg, Joost H. van den and Toebes, Mireille and Gomez, Raquel and Schumacher, Ton N. and Haanen, John B.},
  title     = {Preclinical development of highly effective and safe DNA vaccines directed against HPV 16 E6 and E7},
  series = {International Journal of Cancer},
  volume    = {129},
  journal   = {International Journal of Cancer},
  number    = {2},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1097-0215},
  pages     = {397 -- 406},
  year      = {2011},
  language  = {en}
}
@article{OehlschlaegerSpiesAlvarezetal.2011,
  author    = {{\"O}hlschl{\"a}ger, Peter and Spies, Elmar and Alvarez, Gerardo and Quetting, Michael and Groettrup, Marcus},
  title     = {The combination of TLR-9 adjuvantation and electroporation-mediated delivery enhances in vivo antitumor responses after vaccination with HPV-16 E7 encoding DNA},
  series = {International Journal of Cancer. 128 (2011), H. 2},
  journal   = {International Journal of Cancer. 128 (2011), H. 2},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1097-0215},
  pages     = {473 -- 481},
  year      = {2011},
  language  = {en}
}
@article{ManeaLeursOrbanetal.2011,
  author    = {Manea, Marilena and Leurs, Ulrike and Orban, Erika and Baranyai, Zsuzsa and {\"O}hlschl{\"a}ger, Peter and Marquardt, Andreas and Schulcz, Akos and Tejeda, Miguel},
  title     = {Enhanced Enzymatic Stability and Antitumor Activity of Daunorubicin-GnRH-III Bioconjugates Modified in Position 4},
  series = {Bioconjugate Chemistry},
  volume    = {22},
  journal   = {Bioconjugate Chemistry},
  number    = {7},
  publisher = {ACS},
  address   = {Washington, DC},
  isbn      = {1520-4812},
  pages     = {1320 -- 1329},
  year      = {2011},
  language  = {en}
}
@article{SpiessWilfriedAlvarezetal.2011,
  author    = {Spiess, Elmar and Wilfried, Reichardt and Alvarez, Gerardo and Gottrup, Marcus and {\"O}hlschl{\"a}ger, Peter},
  title     = {An Artificial PAP Gene Breaks Self-tolerance and Promotes Tumor Regression in the TRAMP Model for Prostate Carcinoma},
  series = {Molecular Therapy},
  volume    = {20},
  journal   = {Molecular Therapy},
  number    = {3},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {1525-0016},
  pages     = {555 -- 564},
  year      = {2011},
  language  = {en}
}
@article{DeppeBongaertsO'Connelletal.2011,
  author    = {Deppe, Veronika Maria and Bongaerts, Johannes and O'Connell, Timothy and Maurer, Karl-Heinz and Meinhardt, Friedhelm},
  title     = {Enzymatic deglycation of Amadori products in bacteria},
  series = {Applied microbiology and biotechnology},
  volume    = {Vol. 90},
  journal   = {Applied microbiology and biotechnology},
  number    = {Iss. 2},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {399 -- 406},
  year      = {2011},
  language  = {en}
}
@article{DeppeKlatteBongaertsetal.2011,
  author    = {Deppe, Veronika Maria and Klatte, Stephanie and Bongaerts, Johannes and Maurer, Karl-Heinz and O'Connell, Timothy and Meinhardt, Friedhelm},
  title     = {Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR},
  series = {Applied and environmental microbiology},
  volume    = {Vol. 77},
  journal   = {Applied and environmental microbiology},
  number    = {No. 9},
  publisher = {American Society of Mechanical Engineers (ASME)},
  address   = {New York},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  pages     = {2839 -- 2846},
  year      = {2011},
  language  = {en}
}
@article{BongaertsEsserLorbachetal.2011,
  author    = {Bongaerts, Johannes and Esser, Simon and Lorbach, Volker and Al-Momani, L{\´o}ay and M{\"u}ller, Michael A. and Franke, Dirk and Grondal, Christoph and Kurutsch, Anja and Bujnicki, Robert and Takors, Ralf and Raeven, Leon and Wubbolts, Marcel and Bovenberg, Roel and Nieger, Martin and Sch{\"u}rmann, Melanie and Trachtmann, Natalie and Kozak, Stefan and Sprenger, Georg A. and M{\"u}ller, Michael},
  title     = {Diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis},
  series = {Angewandte Chemie International Edition},
  volume    = {Vol. 50},
  journal   = {Angewandte Chemie International Edition},
  number    = {Iss. 34},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1521-3773 (E-Journal); 0570-0833 (Print); 1433-7851 (Print)},
  pages     = {7781 -- 7786},
  year      = {2011},
  language  = {en}
}
@article{NiehausGaborWielandetal.2011,
  author    = {Niehaus, F. and Gabor, E. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Eck, J.},
  title     = {Enzymes for the laundry industries: tapping the vast metagenomic pool of alkaline proteases},
  series = {Microbial biotechnology},
  volume    = {Vol. 4},
  journal   = {Microbial biotechnology},
  number    = {Iss. 6},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {767 -- 776},
  year      = {2011},
  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{HasegawaKapelyukhTaharaetal.2011,
  author    = {Hasegawa, Maki and Kapelyukh, Yury and Tahara, Harunobu and Seibler, Jost and Rode, Anja and Krueger, Sylvia and Lee, Dongtao N. and Wolf, C. Roland and Scheer, Nico},
  title     = {Quantitative prediction of human pregnane X receptor and cytochrome P450 3A4 mediated drug-drug interaction in a novel multiple humanized mouse line},
  series = {Molecular Pharmacology},
  volume    = {80},
  journal   = {Molecular Pharmacology},
  number    = {33},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/mol.111.071845},
  pages     = {518 -- 528},
  year      = {2011},
  language  = {en}
}
@article{JordanKruegerWillmesetal.2011,
  author    = {Jordan, Sabine D. and Kr{\"u}ger, Markus and Willmes, Diana M. and Redemann, Nora and Wunderlich, F. Thomas and Br{\"o}nneke, Hella S. and Merkwirth, Carsten and Kashkar, Hamid and Olkkonen, Vesa M. and B{\"o}ttger, Thomas and Braun, Thomas and Seibler, Jost and Br{\"u}ning, Jens C.},
  title     = {Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism},
  series = {Nature Cell Biology},
  volume    = {13},
  journal   = {Nature Cell Biology},
  number    = {4},
  publisher = {Nature},
  address   = {New York},
  issn      = {1465-7392},
  doi       = {10.1038/ncb2211},
  pages     = {434 -- 446},
  year      = {2011},
  abstract  = {The contribution of altered post-transcriptional gene silencing to the development of insulin resistance and type 2 diabetes mellitus so far remains elusive. Here, we demonstrate that expression of microRNA (miR)-143 and 145 is upregulated in the liver of genetic and dietary mouse models of obesity. Induced transgenic overexpression of miR-143, but not miR-145, impairs insulin-stimulated AKT activation and glucose homeostasis. Conversely, mice deficient for the miR-143-145 cluster are protected from the development of obesity-associated insulin resistance. Quantitative-mass-spectrometry-based analysis of hepatic protein expression in miR-143-overexpressing mice revealed miR-143-dependent downregulation of oxysterol-binding-protein-related protein (ORP) 8. Reduced ORP8 expression in cultured liver cells impairs the ability of insulin to induce AKT activation, revealing an ORP8-dependent mechanism of AKT regulation. Our experiments provide direct evidence that dysregulated post-transcriptional gene silencing contributes to the development of obesity-induced insulin resistance, and characterize the miR-143-ORP8 pathway as a potential target for the treatment of obesity-associated diabetes.},
  language  = {en}
}
@article{InagakiSleddensLinkelsWassenaaretal.2011,
  author    = {Inagaki, Akiko and Sleddens-Linkels, Esther and Wassenaar, Evelyne and Ooms, Marja and Cappellen, Wiggert A. van and Hoeijmakers, Jan H. J. and Seibler, Jost and Vogt, Thomas F. and Shin, Myung K. and Grootegoed, J. Anton and Baarends, Willy M.},
  title     = {Meiotic functions of RAD18},
  series = {Journal of Cell Science},
  volume    = {124},
  journal   = {Journal of Cell Science},
  number    = {16},
  publisher = {Company of Biologists Limited},
  address   = {Cambridge},
  issn      = {1477-9137},
  doi       = {10.1242/jcs.081968},
  pages     = {2837 -- 2850},
  year      = {2011},
  language  = {en}
}
@article{SiekerNeunerDimitrovaetal.2011,
  author    = {Sieker, Tim and Neuner, Andreas and Dimitrova, Darina and Tippk{\"o}tter, Nils and Muffler, Kai and Bart, Hans-J{\"o}rg and Heinzle, Elmar and Ulber, Roland},
  title     = {Ethanol production from grass silage by simultaneous pretreatment, saccharification and fermentation: First steps in the process development},
  series = {Engineering in Life Sciences},
  volume    = {11},
  journal   = {Engineering in Life Sciences},
  number    = {4},
  publisher = {Wiley},
  address   = {Weinheim},
  doi       = {10.1002/elsc.201000160},
  pages     = {436 -- 442},
  year      = {2011},
  abstract  = {Grass silage provides a great potential as renewable feedstock. Two fractions of the grass silage, a press juice and the fiber fraction, were evaluated for their possible use for bioethanol production. Direct production of ethanol from press juice is not possible due to high concentrations of organic acids. For the fiber fraction, alkaline peroxide or enzymatic pretreatment was used, which removes the phenolic acids in the cell wall. In this study, we demonstrate the possibility to integrate the enzymatic pretreatment with a simultaneous saccharification and fermentation to achieve ethanol production from grass silage in a one-process step. Achieved yields were about 53 g ethanol per kg silage with the alkaline peroxide pretreatment and 91 g/kg with the enzymatic pretreatment at concentrations of 8.5 and 14.6 g/L, respectively. Furthermore, it was shown that additional supplementation of the fermentation medium with vitamins, trace elements and nutrient salts is not necessary when the press juice is directly used in the fermentation step.},
  language  = {en}
}
@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}
}
@incollection{HahnKellyMuffleretal.2011,
  author    = {Hahn, Thomas and Kelly, Svenja and Muffler, Kai and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Extraction of lignocellulose and algae for the production of bulk and fine chemicals},
  series = {Industrial scale natural products extraction},
  booktitle = {Industrial scale natural products extraction},
  editor    = {Hans-J{\"o}rg, Bart and Pilz, Stephan},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  isbn      = {978-3-527-32504-7 (Print)},
  doi       = {10.1002/9783527635122},
  pages     = {221 -- 245},
  year      = {2011},
  language  = {en}
}
@incollection{MufflerPothSiekeretal.2011,
  author    = {Muffler, Kai and Poth, Sabastian and Sieker, Tim and Tippk{\"o}tter, Nils and Ulber, Roland and Sell, Dieter},
  title     = {Bio-feedstocks},
  series = {Comprehensive biotechnology : principles and practices in industry, agcriculture, medicine and the environment. Volume 2: Engineering fundamentals of biotechnology},
  booktitle = {Comprehensive biotechnology : principles and practices in industry, agcriculture, medicine and the environment. Volume 2: Engineering fundamentals of biotechnology},
  editor    = {Moo-Young, Murray},
  edition   = {2. edition},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {978-0-444-53352-4},
  doi       = {10.1016/B978-0-08-088504-9.00088-X},
  pages     = {93 -- 101},
  year      = {2011},
  language  = {en}
}
@article{ImmelGrothHuhnetal.2011,
  author    = {Immel, Timo A. and Groth, Ulrich and Huhn, Thomas and {\"O}hlschl{\"a}ger, Peter},
  title     = {Titanium salan complexes displays strong antitumor properties in vitro and in vivo in mice},
  series = {PLoS ONE},
  volume    = {6},
  journal   = {PLoS ONE},
  number    = {3},
  publisher = {Plos},
  address   = {San Francisco, California, US},
  doi       = {10.1371/journal.pone.0017869},
  pages     = {e17869},
  year      = {2011},
  abstract  = {The anticancer activity of titanium complexes has been known since the groundbreaking studies of K{\"o}pf and K{\"o}pf-Maier on titanocen dichloride. Unfortunately, possibly due to their fast hydrolysis, derivatives of titanocen dichloride failed in clinical studies. Recently, the new family of titanium salan complexes containing tetradentate ONNO ligands with anti-cancer properties has been discovered. These salan complexes are much more stabile in aqueous media. In this study we describe the biological activity of two titanium salan complexes in a mouse model of cervical cancer. High efficiency of this promising complex family was demonstrated for the first time in vivo. From these data we conclude that titanium salan complexes display very strong antitumor properties exhibiting only minor side effects. Our results may influence the chemotherapy with metallo therapeutics in the future.},
  language  = {en}
}
@article{LeursMezoOehlschlaegeretal.2012,
  author    = {Leurs, Ulrike and Mezo, Gabor and {\"O}hlschl{\"a}ger, Peter and Orban, Erika and Marquard, Andrea and Manea, Marilena},
  title     = {Design, synthesis, in vitro stability and cytostatic effect of multifunctional anticancer drug-bioconjugates containing GnRH-III as a targeting moiety},
  series = {Peptide Science},
  volume    = {98},
  journal   = {Peptide Science},
  number    = {1},
  publisher = {Wiley},
  address   = {New York, NY},
  issn      = {1097-0282},
  doi       = {10.1002/bip.21640},
  pages     = {1 -- 10},
  year      = {2012},
  abstract  = {Bioconjugates containing the GnRH-III hormone decapeptide as a targeting moiety are able to deliver chemotherapeutic agents specifically to cancer cells expressing GnRH receptors, thereby increasing their local efficacy while limiting the peripheral toxicity. However, the number of GnRH receptors on cancer cells is limited and they desensitize under continuous hormone treatment. A possible approach to increase the receptor mediated tumor targeting and consequently the cytostatic effect of the bioconjugates would be the attachment of more than one chemotherapeutic agent to one GnRH-III molecule. Here we report on the design, synthesis and biochemical characterization of multifunctional bioconjugates containing GnRH-III as a targeting moiety and daunorubicin as a chemotherapeutic agent. Two different drug design approaches were pursued. The first one was based on the bifunctional [4Lys]-GnRH-III (Glp-His-Trp-Lys-His-Asp-Trp-Lys-Pro-Gly-NH2) containing two lysine residues in positions 4 and 8, whose ϵ-amino groups were used for the coupling of daunorubicin. In the second drug design, the native GnRH-III (Glp-His-Trp-Ser-His-Asp-Trp-Lys-Pro-Gly-NH2) was used as a scaffold; an additional lysine residue was coupled to the ϵ-amino group of 8Lys in order to generate two free amino groups available for conjugation of daunorubicin. The in vitro stability/degradation of all synthesized compounds was investigated in human serum, as well as in the presence of rat liver lysosomal homogenate. Their cellular uptake was determined on human breast cancer cells and the cytostatic effect was evaluated on human breast, colon and prostate cancer cell lines. Compared with a monofunctional compound, both drug design approaches resulted in multifunctional bioconjugates with increased cytostatic effect.},
  language  = {en}
}
@article{BaeckerRaueSchusseretal.2012,
  author    = {B{\"a}cker, Matthias and Raue, Markus and Schusser, Sebastian and Jeitner, C. and Breuer, L. and Wagner, P. and Poghossian, Arshak and F{\"o}rster, Arnold and Mang, Thomas and Sch{\"o}ning, Michael Josef},
  title     = {Microfluidic chip with integrated microvalves based on temperature- and pH-responsive hydrogel thin films},
  series = {Physica Status Solidi (a)},
  volume    = {209},
  journal   = {Physica Status Solidi (a)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201100763},
  pages     = {839 -- 845},
  year      = {2012},
  abstract  = {Two types of microvalves based on temperature-responsive poly(N-isopropylacrylamide) (PNIPAAm) and pH-responsive poly(sodium acrylate) (PSA) hydrogel films have been developed and tested. The PNIPAAm and PSA hydrogel films were prepared by means of in situ photopolymerization directly inside the fluidic channel of a microfluidic chip fabricated by combining Si and SU-8 technologies. The swelling/shrinking properties and height changes of the PNIPAAm and PSA films inside the fluidic channel were studied at temperatures of deionized water from 14 to 36 °C and different pH values (pH 3-12) of Titrisol buffer, respectively. Additionally, in separate experiments, the lower critical solution temperature (LCST) of the PNIPAAm hydrogel was investigated by means of a differential scanning calorimetry (DSC) and a surface plasmon resonance (SPR) method. Mass-flow measurements have shown the feasibility of the prepared hydrogel films to work as an on-chip integrated temperature- or pH-responsive microvalve capable to switch the flow channel on/off.},
  language  = {en}
}
@article{AggarwalDhimanKumaretal.2012,
  author    = {Aggarwal, P. and Dhiman, S. and Kumar, G. and Scherer, Ulrich W. and Singla, M. L. and Srivastava, A.},
  title     = {Optical study of poly(ethyleneterephthalate) modified by different ionizing radiation dose},
  series = {Indian Journal of Pure and Applied Physics},
  volume    = {50},
  journal   = {Indian Journal of Pure and Applied Physics},
  number    = {2},
  issn      = {0019-5596},
  pages     = {129 -- 132},
  year      = {2012},
  abstract  = {Thin films of poly(ethyleneterephthalate) [PET]were exposed to radiation dose ranging from 10 to 30 kGy by using gamma rays in the range 12.8-177.8 MGy using swift light ions of hydrogen. There was no effect of the radiation dose on the optical behaviour of PET as a result of exposure to radiation dose up to 30 kGy brought about by gamma rays but a significant decrease in the optical band gap values was observed when PET was exposed to swift light ions of hydrogen. The data obtained are discussed in terms of optical studies carried out on PET using swift heavy ions.},
  language  = {en}
}
@article{WernerGroebelKrumbeetal.2012,
  author    = {Werner, Frederik and Groebel, Simone and Krumbe, Christoph and Wagner, Torsten and Selmer, Thorsten and Yoshinobu, Tatsuo and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Nutrient concentration-sensitive microorganism-based biosensor},
  series = {Physica Status Solidi (a)},
  volume    = {209},
  journal   = {Physica Status Solidi (a)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201100801},
  pages     = {900 -- 904},
  year      = {2012},
  language  = {en}
}
@article{BorgmeierBongaertsMeinhardt2012,
  author    = {Borgmeier, Claudia and Bongaerts, Johannes and Meinhardt, Friedhelm},
  title     = {Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production},
  series = {Journal of biotechnology},
  volume    = {159},
  journal   = {Journal of biotechnology},
  number    = {1-2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2012.02.011},
  pages     = {12 -- 20},
  year      = {2012},
  abstract  = {Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele - known to cause hypersecretion in Bacillus subtilis - resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG - known to interfere with DegU DNA-binding in B. subtilis - did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.},
  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{HenkenOosterhuisOehlschlaegeretal.2012,
  author    = {Henken, F. E. and Oosterhuis, K. and {\"O}hlschl{\"a}ger, Peter and Bosch, L. and Hooijberg, E. and Haanen, J. B. A. G. and Steenbergen, R. D. M.},
  title     = {Preclinical safety evaluation of DNA vaccines encoding modified HPV16 E6 and E7},
  series = {Vaccine},
  volume    = {30},
  journal   = {Vaccine},
  number    = {28},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0264-410X},
  doi       = {10.1016/j.vaccine.2012.04.013},
  pages     = {4259 -- 4266},
  year      = {2012},
  abstract  = {Persistent infection with high-risk human papillomaviruses (hrHPV) can result in the formation of anogenital cancers. As hrHPV proteins E6 and E7 are required for cancer initiation and maintenance, they are ideal targets for immunotherapeutic interventions. Previously, we have described the development of DNA vaccines for the induction of HPV16 E6 and E7 specific T cell immunity. These vaccines consist of 'gene-shuffled' (SH) versions of HPV16 E6 and E7 that were fused to Tetanus Toxin Fragment C domain 1 (TTFC) and were named TTFC-E6SH and TTFC-E7SH. Gene-shuffling was performed to avoid the risk of inducing malignant transformation at the vaccination site. Here, we describe the preclinical safety evaluation of these candidate vaccines by analysis of their transforming capacity in vitro using established murine fibroblasts (NIH 3T3 cells) and primary human foreskin keratinocytes (HFKs). We demonstrate that neither ectopic expression of TTFC-E6SH and TTFC-E7SH alone or in combination enabled NIH 3T3 cells to form colonies in soft agar. In contrast, expression of HPV16 E6WT and E7WT alone or in combination resulted in effective transformation. Similarly, retroviral transduction of HFKs from three independent donors with both TTFC-E6SH and TTFC-E7SH alone or in combination did not show any signs of immortalization. In contrast, the combined expression of E6WT and E7WT induced immortalization in HFKs from all donors. Based on these results we consider it justified to proceed to clinical evaluation of DNA vaccines encoding TTFC-E6SH and TTFC-E7SH in patients with HPV16 associated (pre)malignancies.},
  language  = {en}
}
@article{ImmelGruetzkeSpaeteetal.2012,
  author    = {Immel, Timo and Gr{\"u}tzke, Martin and Sp{\"a}te, Anne-Katrin and Groth, Ulrich and {\"O}hlschl{\"a}ger, Peter and Huhn, Thomas},
  title     = {Synthesis and X-ray structure analysis of a heptacoordinate titanium(IV)-bis-chelate with enhanced in vivo antitumor efficacy},
  series = {Chemical Communications},
  volume    = {48},
  journal   = {Chemical Communications},
  number    = {46},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-548X},
  doi       = {10.1039/C2CC31624B},
  pages     = {5790 -- 5792},
  year      = {2012},
  abstract  = {Chelate stabilization of a titanium(IV)-salan alkoxide by ligand exchange with 2,6-pyridinedicarboxylic acid (dipic) resulted in heptacoordinate complex 3 which is not redox-active, stable on silica gel and has increased aqueous stability. 3 is highly toxic in HeLa S3 and Hep G2 and has enhanced antitumor efficacy in a mouse cervical-cancer model.},
  language  = {en}
}
@article{PaulssenKongArciszewskietal.2012,
  author    = {Paulßen, Elisabeth and Kong, Shushu and Arciszewski, Pawel and Wielbalck, Swantje and Abram, Ulrich},
  title     = {Aryl and NHC Compounds of Technetium and Rhenium},
  series = {Journal of the American Chemical Society},
  volume    = {134},
  journal   = {Journal of the American Chemical Society},
  number    = {22},
  publisher = {ACS Publications},
  address   = {Washington, DC},
  issn      = {1520-5126},
  doi       = {10.1021/ja3033718},
  pages     = {9118 -- 9121},
  year      = {2012},
  abstract  = {Air- and water-stable phenyl complexes with nitridotechnetium(V) cores can be prepared by straightforward procedures. [TcNPh2(PPh3)2] is formed by the reaction of [TcNCl2(PPh3)2] with PhLi. The analogous N-heterocyclic carbene (NHC) compound [TcNPh2(HLPh)2], where HLPh is 1,3,4-triphenyl-1,2,4-triazol-5-ylidene, is available from (NBu4)[TcNCl4] and HLPh or its methoxo-protected form. The latter compound allows the comparison of different Tc-C bonds within one compound. Surprisingly, the Tc chemistry with such NHCs does not resemble that of corresponding Re complexes, where CH activation and orthometalation dominate.},
  language  = {en}
}
@article{PaulssenNgyugenKahlckeetal.2012,
  author    = {Paulßen, Elisabeth and Ngyugen, Hung Huy and Kahlcke, Nils and Deflon, Victor M. and Abram, Ulrich},
  title     = {Tricarbonyltechnetium(I) and -rhenium(I) complexes with N′-thiocarbamoylpicolylbenzamidines},
  series = {Polyhedron},
  volume    = {40},
  journal   = {Polyhedron},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0277-5387},
  doi       = {10.1016/j.poly.2012.04.008},
  pages     = {153 -- 158},
  year      = {2012},
  abstract  = {N,N-Dialkylamino(thiocarbonyl)-N′-picolylbenzamidines react with (NEt4)2[M(CO)3X3] (M = Re, X = Br; M = Tc, X = Cl) under formation of neutral [M(CO)3L] complexes in high yields. The monoanionic NNS ligands bind in a facial coordination mode and can readily be modified at the (CS)NR1R2 moiety. The complexes [99Tc(CO)3(LPyMor)] and [Re(CO)3(L)] (L = LPyMor, LPyEt) were characterized by X-ray diffraction. Reactions of [99mTc(CO)3(H2O)3]+ with the N′-thiocarbamoylpicolylbenzamidines give the corresponding 99mTc complexes. The ester group in HLPyCOOEt allows linkage between biomolecules and the metal core.},
  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{ScheerKapelyukhRodeetal.2012,
  author    = {Scheer, Nico and Kapelyukh, Yury and Rode, Anja and Buechel, Sandra and Wolf, C. Roland},
  title     = {Generation and characterization of novel cytochrome P450 Cyp2c gene cluster knockout and CYP2C9 humanized mouse lines},
  series = {Molecular Pharmacology},
  volume    = {82},
  journal   = {Molecular Pharmacology},
  number    = {6},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/mol.112.080036},
  pages     = {1022 -- 1029},
  year      = {2012},
  abstract  = {Compared with rodents and many other animal species, the human cytochrome P450 (P450) Cyp2c gene cluster varies significantly in the multiplicity of functional genes and in the substrate specificity of its enzymes. As a consequence, the use of wild-type animal models to predict the role of human CYP2C enzymes in drug metabolism and drug-drug interactions is limited. Within the human CYP2C cluster CYP2C9 is of particular importance, because it is one of the most abundant P450 enzymes in human liver, and it is involved in the metabolism of a wide variety of important drugs and environmental chemicals. To investigate the in vivo functions of cytochrome P450 Cyp2c genes and to establish a model for studying the functions of CYP2C9 in vivo, we have generated a mouse model with a deletion of the murine Cyp2c gene cluster and a corresponding humanized model expressing CYP2C9 specifically in the liver. Despite the high number of functional genes in the mouse Cyp2c cluster and the reported roles of some of these proteins in different biological processes, mice deleted for Cyp2c genes were viable and fertile but showed certain phenotypic alterations in the liver. The expression of CYP2C9 in the liver also resulted in viable animals active in the metabolism and disposition of a number of CYP2C9 substrates. These mouse lines provide a powerful tool for studying the role of Cyp2c genes and of CYP2C9 in particular in drug disposition and as a factor in drug-drug interaction.},
  language  = {en}
}
@article{LempiaeinenCouttetBolognanietal.2012,
  author    = {Lempi{\"a}inen, Harri and Couttet, Philippe and Bolognani, Federico and M{\"u}ller, Arne and Dubost, Val{\´e}rie and Luisier, Rapha{\"e}lle and Rio-Espinola, Alberto del and Vitry, Veronique and Unterberger, Elif B. and Thomson, John P. and Treindl, Fridolin and Metzger, Ute and Wrzodek, Clemens and Hahne, Florian and Zollinger, Tulipan and Brasa, Sarah and Kalteis, Magdalena and Marcellin, Magali and Giudicelli, Fanny and Braeuning, Albert and Morawiec, Laurent and Zamurovic, Natasa and L{\"a}ngle, Ulrich and Scheer, Nico and Sch{\"u}beler, Dirk and Goodman, Jay and Chibout, Salah-Dine and Marlowe, Jennifer and Theil, Dietlinde and Heard, David J. and Grenet, Olivier and Zell, Andreas and Templin, Markus F. and Meehan, Richard R. and Wolf, Roland C. and Elcombe, Clifford R. and Schwarz, Michael and Moulin, Pierre and Terranova, R{\´e}mi and Moggs, Jonathan G.},
  title     = {Identification of Dlk1-Dio3 imprinted gene cluster non-coding RNAs as novel candidate biomarkers for liver tumor promotion},
  series = {Toxicological Sciences},
  volume    = {131},
  journal   = {Toxicological Sciences},
  number    = {2},
  publisher = {Oxford University Press},
  address   = {Oxford},
  issn      = {1094-2025},
  doi       = {10.1093/toxsci/kfs303},
  pages     = {375 -- 386},
  year      = {2012},
  abstract  = {The molecular events during nongenotoxic carcinogenesis and their temporal order are poorly understood but thought to include long-lasting perturbations of gene expression. Here, we have investigated the temporal sequence of molecular and pathological perturbations at early stages of phenobarbital (PB) mediated liver tumor promotion in vivo. Molecular profiling (mRNA, microRNA [miRNA], DNA methylation, and proteins) of mouse liver during 13 weeks of PB treatment revealed progressive increases in hepatic expression of long noncoding RNAs and miRNAs originating from the Dlk1-Dio3 imprinted gene cluster, a locus that has recently been associated with stem cell pluripotency in mice and various neoplasms in humans. PB induction of the Dlk1-Dio3 cluster noncoding RNA (ncRNA) Meg3 was localized to glutamine synthetase-positive hypertrophic perivenous hepatocytes, sug- gesting a role for β-catenin signaling in the dysregulation of Dlk1-Dio3 ncRNAs. The carcinogenic relevance of Dlk1-Dio3 locus ncRNA induction was further supported by in vivo genetic dependence on constitutive androstane receptor and β-catenin pathways. Our data identify Dlk1-Dio3 ncRNAs as novel candidate early biomarkers for mouse liver tumor promotion and provide new opportunities for assessing the carcinogenic potential of novel compounds.},
  language  = {en}
}
@article{ScheerKapelyukhMcEwanetal.2012,
  author    = {Scheer, Nico and Kapelyukh, Yury and McEwan, Jillian and Beuger, Vincent and Stanley, Lesley A. and Rode, Anja and Wolf, C. Roland},
  title     = {Modeling Human Cytochrome P450 2D6 Metabolism and Drug-drug Interaction by a Novel Panel of Knockout and Humanized Mouse Lines},
  series = {Molecular Pharmacology},
  volume    = {81},
  journal   = {Molecular Pharmacology},
  number    = {1},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/mol.111.075192},
  pages     = {63 -- 72},
  year      = {2012},
  abstract  = {The highly polymorphic human cytochrome P450 2D6 enzyme is involved in the metabolism of up to 25\% of all marketed drugs and accounts for significant individual differences in response to CYP2D6 substrates. Because of the differences in the multiplicity and substrate specificity of CYP2D family members among species, it is difficult to predict pathways of human CYP2D6-dependent drug metabolism on the basis of animal studies. To create animal models that reflect the human situation more closely and that allow an in vivo assessment of the consequences of differential CYP2D6 drug metabolism, we have developed a novel straightforward approach to delete the entire murine Cyp2d gene cluster and replace it with allelic variants of human CYP2D6. By using this approach, we have generated mouse lines expressing the two frequent human protein isoforms CYP2D6.1 and CYP2D6.2 and an as yet undescribed variant of this enzyme, as well as a Cyp2d cluster knockout mouse. We demonstrate that the various transgenic mouse lines cover a wide spectrum of different human CYP2D6 metabolizer phenotypes. The novel humanization strategy described here provides a robust approach for the expression of different CYP2D6 allelic variants in transgenic mice and thus can help to evaluate potential CYP2D6-dependent interindividual differences in drug response in the context of personalized medicine.},
  language  = {en}
}
@article{SchiffelsPinkenburgScheldenetal.2013,
  author    = {Schiffels, Johannes and Pinkenburg, Olaf and Schelden, Maximilian and Aboulnaga, El-Hussiny A. A. and Baumann, Marcus and Selmer, Thorsten},
  title     = {An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from cupriavidus necator in Escherichia coli},
  series = {PLOS one. 2013},
  journal   = {PLOS one. 2013},
  publisher = {Public Library of Science},
  address   = {San Francisco, California},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0068812},
  year      = {2013},
  language  = {en}
}
@article{AbulnagaPinkenburgSchiffelsetal.2013,
  author    = {Abulnaga, El-Hussiny and Pinkenburg, Olaf and Schiffels, Johannes and E-Refai, Ahmed and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli},
  series = {Journal of bacteriology},
  volume    = {195},
  journal   = {Journal of bacteriology},
  number    = {16},
  issn      = {1098-5530 [E-Journal]},
  pages     = {3704 -- 3713},
  year      = {2013},
  language  = {en}
}
@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{WilmingBegemannKuhneetal.2013,
  author    = {Wilming, Anja and Begemann, Jens and Kuhne, Stefan and Regestein, Lars and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and B{\"u}chs, Jochen},
  title     = {Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations},
  series = {Biochemical engineering journal},
  volume    = {Vol. 73},
  journal   = {Biochemical engineering journal},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-295X (E-Journal); 1369-703X (Print)},
  pages     = {29 -- 37},
  year      = {2013},
  language  = {en}
}
@article{VoigtSchroeterJuergenetal.2013,
  author    = {Voigt, Birgit and Schroeter, Rebecca and J{\"u}rgen, Britta and Albrecht, Dirk and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Schweder, Thomas and Hecker, Michael},
  title     = {The response of Bacillus licheniformis to heat and ethanol stress and the role of the SigB regulon},
  series = {Proteomics},
  volume    = {Vol. 13},
  journal   = {Proteomics},
  number    = {Iss. 14},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1615-9861 (E-Journal); 1615-9853 (Print)},
  pages     = {2140 -- 2146},
  year      = {2013},
  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}
}
@article{WiegandDietrichHerteletal.2013,
  author    = {Wiegand, Sandra and Dietrich, Sascha and Hertel, Robert and Bongaerts, Johannes and Evers, Stefan and Volland, Sonja and Daniel, Rolf and Liesegang, Heiko},
  title     = {RNA-Seq of Bacillus licheniformis: active regulatory RNA features expressed within a productive fermentation},
  series = {BMC genomics},
  volume    = {Vol. 14},
  journal   = {BMC genomics},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2164},
  pages     = {667},
  year      = {2013},
  language  = {en}
}
@article{DuttaHartkopfFroederWitteetal.2013,
  author    = {Dutta, Suryendu and Hartkopf-Fr{\"o}der, Christoph and Witte, Karin and Brocke, Rainer and Mann, Ulrich},
  title     = {Molecular characterization of fossil palynomorphs by transmission micro-FTIR spectroscopy: implications for hydrocarbon source evaluation},
  series = {International journal of coal geology},
  volume    = {Vol. 115},
  journal   = {International journal of coal geology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1872-7840 (E-Journal); 0166-5162 (Print)},
  pages     = {13 -- 23},
  year      = {2013},
  language  = {en}
}
@inproceedings{TakenagaHerreraWerneretal.2013,
  author    = {Takenaga, Shoko and Herrera, Cony F. and Werner, Frederik and Biselli, Manfred and Schnitzler, Thomas and Sch{\"o}ning, Michael Josef and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten},
  title     = {Detection of the metabolic activity of cells by differential measurements based on a single light-addressable potentiometric sensor chip},
  series = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  booktitle = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  organization    = {Dresdner Sensor-Symposium <11, 2013>},
  isbn      = {978-3-9813484-5-3},
  pages     = {63 -- 67},
  year      = {2013},
  language  = {en}
}
@article{MartinezJakobTuetal.2013,
  author    = {Martinez, Ronny and Jakob, Felix and Tu, Ran and Siegert, Petra and Maurer, Karl-Heinz and Schwaneberg, Ulrich},
  title     = {Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution},
  series = {Biotechnology and bioengineering},
  volume    = {Vol. 110},
  journal   = {Biotechnology and bioengineering},
  number    = {Iss. 3},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1097-0290 (E-Journal); 0006-3592 (Print); 0368-1467 (Print)},
  pages     = {711 -- 720},
  year      = {2013},
  language  = {en}
}
@article{JakobMartinezMandaweetal.2013,
  author    = {Jakob, Felix and Martinez, Ronny and Mandawe, John and Hellmuth, Hendrik and Siegert, Petra and Maurer, Karl-Heinz and Schwaneberg, Ulrich},
  title     = {Surface charge engineering of a Bacillus gibsonii subtilisin protease},
  series = {Applied microbiology and biotechnology},
  volume    = {Vol. 97},
  journal   = {Applied microbiology and biotechnology},
  number    = {Iss. 15},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {6793 -- 6802},
  year      = {2013},
  language  = {en}
}
@article{ScheerSnaithWolfetal.2013,
  author    = {Scheer, Nico and Snaith, Mike and Wolf, C. Roland and Seibler, Jost},
  title     = {Generation and utility of genetically humanized mouse models},
  series = {Drug Discovery Today},
  volume    = {Vol 18},
  journal   = {Drug Discovery Today},
  number    = {23-24},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1359-6446},
  doi       = {10.1016/j.drudis.2013.07.007},
  pages     = {1200 -- 1211},
  year      = {2013},
  language  = {en}
}