@article{BouwmanGuldenHeijdenetal.2013,
  author    = {Bouwman, Peter and Gulden, Hanneke van der and Heijden, Ingrid van der and Drost, Rinske and Klijn, Christiaan N. and Prasetyanti, Pramudita and Pieterse, Mark and Wientjens, Ellen and Seibler, Jost and Hogervorst, Frank B. L. and Jonkers, Jos},
  title     = {A High-Throughput Functional Complementation Assay for Classification of BRCA1 Missense Variants},
  series = {Cancer Discovery},
  journal   = {Cancer Discovery},
  number    = {3},
  issn      = {2159-8290},
  doi       = {10.1158/2159-8290.CD-13-0094},
  pages     = {1142 -- 1152},
  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}
}
@article{BreuerRaueKirschbaumetal.2015,
  author    = {Breuer, Lars and Raue, Markus and Kirschbaum, M. and Mang, Thomas and Sch{\"o}ning, Michael Josef and Thoelen, R. and Wagner, Torsten},
  title     = {Light-controllable polymeric material based on temperature-sensitive hydrogels with incorporated graphene oxide},
  series = {Physica status solidi (a)},
  volume    = {212},
  journal   = {Physica status solidi (a)},
  number    = {6},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201431944},
  pages     = {1368 -- 1374},
  year      = {2015},
  abstract  = {Poly(N-isopropylacrylamide) (PNIPAAm) hydrogel films with incorporated graphene oxide (GO) were developed and tested as light-stimulated actuators. GO dispersions were synthesized via Hummers method and characterized toward their optical properties and photothermal energy conversion. The hydrogels were prepared by means of photopolymerization. In addition, the influence of GO within the hydrogel network on the lower critical solution temperature (LCST) was investigated by differential scanning calorimetry (DSC). The optical absorbance and the response to illumination were determined as a function of GO concentration for thin hydrogel films. A proof of principle for the stimulation with light was performed.},
  language  = {en}
}
@article{PilasIkenSelmeretal.2015,
  author    = {Pilas, Johanna and Iken, Heiko and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Development of a multi-parameter sensor chip for the simultaneous detection of organic compounds in biogas processes},
  series = {Physica status solidi (a)},
  volume    = {212},
  journal   = {Physica status solidi (a)},
  number    = {6},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201431894},
  pages     = {1306 -- 1312},
  year      = {2015},
  abstract  = {An enzyme-based multi-parameter biosensor is developed for monitoring the concentration of formate, d-lactate, and l-lactate in biological samples. The sensor is based on the specific dehydrogenation by an oxidized β-nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenase (formate dehydrogenase, d-lactic dehydrogenase, and l-lactic dehydrogenase, respectively) in combination with a diaphorase from Clostridium kluyveri (EC 1.8.1.4). The enzymes are immobilized on a platinum working electrode by cross-linking with glutaraldehyde (GA). The principle of the determination scheme in case of l-lactate is as follows: l-lactic dehydrogenase (l-LDH) converts l-lactate into pyruvate by reaction with NAD+. In the presence of hexacyanoferrate(III), the resulting reduced β-nicotinamide adenine dinucleotide (NADH) is then regenerated enzymatically by diaphorase. The electrochemical detection is based on the current generated by oxidation of hexacyanoferrate(II) at an applied potential of +0.3 V vs. an Ag/AgCl reference electrode. The biosensor will be electrochemically characterized in terms of linear working range and sensitivity. Additionally, the successful practical application of the sensor is demonstrated in an extract from maize silage.},
  language  = {en}
}
@article{SeifarthGossmannGrosseetal.2015,
  author    = {Seifarth, Volker and Goßmann, Matthias and Grosse, J. O. and Becker, C. and Heschel, I. and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l},
  title     = {Development of a Bioreactor to Culture Tissue Engineered Ureters Based on the Application of Tubular OPTIMAIX 3D Scaffolds},
  series = {Urologia Internationalis},
  volume    = {2015},
  journal   = {Urologia Internationalis},
  number    = {95},
  publisher = {Karger},
  address   = {Basel},
  issn      = {0042-1138},
  doi       = {10.1159/000368419},
  pages     = {106 -- 113},
  year      = {2015},
  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{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{HandtkeVollandMethlingetal.2014,
  author    = {Handtke, Stefan and Volland, Sonja and Methling, Karen and Albrecht, Dirk and Becher, D{\"o}rte and Nehls, Jenny and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Liesegang, Heiko and Voigt, Birgit and Daniel, Rolf and Hecker, Michael},
  title     = {Cell physiology of the biotechnological relevant bacterium Bacillus pumilus - An omics-based approach},
  series = {Journal of Biotechnology},
  journal   = {Journal of Biotechnology},
  number    = {192(A)},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2014.08.028},
  pages     = {204 -- 214},
  year      = {2014},
  abstract  = {Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43\% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC-MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.},
  language  = {en}
}
@incollection{FrotscherGossmannRaatschenetal.2015,
  author    = {Frotscher, Ralf and Goßmann, Matthias and Raatschen, Hans-J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Staat, Manfred},
  title     = {Simulation of cardiac cell-seeded membranes using the edge-based smoothed FEM},
  series = {Shell and membrane theories in mechanics and biology. (Advanced structured materials ; 45)},
  booktitle = {Shell and membrane theories in mechanics and biology. (Advanced structured materials ; 45)},
  publisher = {Springer},
  address   = {Heidelberg},
  isbn      = {978-3-319-02534-6 ; 978-3-319-02535-3},
  pages     = {187 -- 212},
  year      = {2015},
  abstract  = {We present an electromechanically coupled Finite Element model for cardiac tissue. It bases on the mechanical model for cardiac tissue of Hunter et al. that we couple to the McAllister-Noble-Tsien electrophysiological model of purkinje fibre cells. The corresponding system of ordinary differential equations is implemented on the level of the constitutive equations in a geometrically and physically nonlinear version of the so-called edge-based smoothed FEM for plates. Mechanical material parameters are determined from our own pressure-deflection experimental setup. The main purpose of the model is to further examine the experimental results not only on mechanical but also on electrophysiological level down to ion channel gates. Moreover, we present first drug treatment simulations and validate the model with respect to the experiments.},
  language  = {en}
}
@article{NachtrodtTietschMostaccietal.2014,
  author    = {Nachtrodt, Frederik and Tietsch, Wolfgang and Mostacci, Domiziano and Scherer, Ulrich W.},
  title     = {Set-up and first operation of a plasma oven for treatment of low level radioactive wastes},
  series = {Nuclear technology and radiation protection},
  volume    = {29},
  journal   = {Nuclear technology and radiation protection},
  number    = {Suppl.},
  publisher = {VINČA Institute of Nuclear Sciences},
  address   = {Belgrad},
  issn      = {1451-3994},
  doi       = {10.2298/NTRP140SS47N},
  pages     = {47 -- 51},
  year      = {2014},
  language  = {en}
}
@misc{BesslerMaurerMerkeletal.2009,
  author    = {Bessler, Cornelius and Maurer, Karl-Heinz and Merkel, Marion and Siegert, Petra and Wieland, Susanne},
  title     = {Subtilisin from Bacillus Pumilus and detergent and cleaning agents containing said novel subtilisin [US Patentanmeldung / Internationale Patentanmeldung]},
  publisher = {USPTO; WIPO},
  address   = {Washington; Genf},
  pages     = {1 -- 39},
  year      = {2009},
  language  = {en}
}
@article{PohlSiegertMeschetal.1998,
  author    = {Pohl, Martina and Siegert, Petra and Mesch, K. and Bruhn, H. and Gr{\"o}tzinger, Joachim},
  title     = {Active site mutants of pyruvate decarboxylase from Zymomonas mobilis : a site-directed mutagenesis study of L112, I472, I476, E473 and N482},
  series = {European journal of biochemistry},
  volume    = {Vol. 257},
  journal   = {European journal of biochemistry},
  number    = {Iss. 3},
  issn      = {1432-1033 (E-Journal); 1742-4658 (E-Journal); 0014-2956 (Print); 1742-464X (Print)},
  pages     = {538 -- 546},
  year      = {1998},
  language  = {en}
}
@article{IdingSiegertMeschetal.1998,
  author    = {Iding, Hans and Siegert, Petra and Mesch, K. and Pohl, Martina},
  title     = {Application of α-keto acid decarboxylases in biotransformations},
  series = {Biochimica et biophysica acta (BBA) - Protein structure and molecular enzymology},
  volume    = {Vol. 1385},
  journal   = {Biochimica et biophysica acta (BBA) - Protein structure and molecular enzymology},
  number    = {Iss. 2},
  issn      = {1879-2588 (E-Journal); 0167-4838 (Print)},
  pages     = {307 -- 322},
  year      = {1998},
  language  = {en}
}
@article{IdingDuennwaldGreineretal.2000,
  author    = {Iding, Hans and D{\"u}nnwald, Thomas and Greiner, Lasse and Liese, Andreas and M{\"u}ller, Michael and Siegert, Petra and Gr{\"o}tzinger, Joachim and Demir, Ayhan S. and Pohl, Martina},
  title     = {Benzoylformate Decarboxylase from Pseudomonas putida as Stable Catalyst for the Synthesis of Chiral 2-Hydroxy Ketones},
  series = {Chemistry - a European journal},
  volume    = {Vol. 6},
  journal   = {Chemistry - a European journal},
  number    = {Iss. 8},
  issn      = {1521-3765 (E-Journal); 0947-6539 (Print)},
  pages     = {1483 -- 1495},
  year      = {2000},
  language  = {en}
}
@inproceedings{SiegertIdingBaumannetal.2000,
  author    = {Siegert, Petra and Iding, Hans and Baumann, Martin and McLeish, Michael J. and Kenyon, George L. and Pohl, Martina},
  title     = {Broadening of the substrate spectra of two ThDP-dependent decarboxylases using site-directed-mutagenesis},
  series = {Proceedings of the 4th International Congress on Biochemical Engineering : 17 and 18 February 2000, Stuttgart},
  booktitle = {Proceedings of the 4th International Congress on Biochemical Engineering : 17 and 18 February 2000, Stuttgart},
  organization    = {International Congress on Biochemical Engineering <4, 2000, Stuttgart>},
  isbn      = {3-8167-5570-4},
  pages     = {38 -- 42},
  year      = {2000},
  language  = {en}
}
@article{DuennwaldDemirSiegertetal.2000,
  author    = {D{\"u}nnwald, Thomas and Demir, Ayhan S. and Siegert, Petra and Pohl, Martina and M{\"u}ller, Michael},
  title     = {Enantioselective Synthesis of (S)-2-Hydroxypropanone Derivatives by Benzoylformate Decarboxylase Catalyzed C-C Bond Formation},
  series = {European journal of organic chemistry},
  volume    = {Vol. 2000},
  journal   = {European journal of organic chemistry},
  number    = {Iss. 11},
  issn      = {0365-5490 (E-Journal); 1099-0690 (E-Journal); 0075-4617 (Print); 0170-2041 (Print); 0947-3440 (Print); 1434-193X (Print); 1434-243X (Print)},
  pages     = {2161 -- 2170},
  year      = {2000},
  language  = {en}
}
@article{DuennwaldDemirSiegertetal.2001,
  author    = {D{\"u}nnwald, Thomas and Demir, Ayhan S. and Siegert, Petra and Pohl, Martina and M{\"u}ller, Michael},
  title     = {ChemInform Abstract: Enantioselective synthesis of (S)-2-Hydroxypropanone derivatives by Benzoylformate Decarboxylase Catalyzed C—C Bond Formation},
  series = {Cheminform},
  volume    = {Vol. 32},
  journal   = {Cheminform},
  number    = {Iss. 4},
  issn      = {1522-2667 (E-Journal); 0931-7597 (Print)},
  pages     = {Publ. online},
  year      = {2001},
  language  = {en}
}
@article{DuenkelmannKolterJungNitscheetal.2002,
  author    = {D{\"u}nkelmann, Pascal and Kolter-Jung, Doris and Nitsche, Adam and Demir, Ayhan S. and Siegert, Petra and Lingen, Bettina and Baumann, Martin and Pohl, Martina and M{\"u}ller, Michael},
  title     = {Development of a donor-acceptor concept for enzymatic cross-coupling reactions of adehydes : the first asymmetric cross-benzoin condensation},
  series = {Journal of the American Chemical Society},
  volume    = {Vol. 124},
  journal   = {Journal of the American Chemical Society},
  issn      = {1520-5126 (E-Journal); 0002-7863 (Print)},
  pages     = {12084 -- 12085},
  year      = {2002},
  language  = {en}
}
@incollection{SiegertPohlKneenetal.2004,
  author    = {Siegert, Petra and Pohl, Martina and Kneen, Malea M. and Pogozheva, Irina D. and Kenyon, George L. and McLeish, Michael J.},
  title     = {Exploring the substrate specificity of benzoylformate decarboxylase, pyruvate decarboxylase, and benzaldehyde lyase},
  series = {Thiamine : catalytic mechanisms in normal and disease states / ed. by Frank Jordan ...},
  booktitle = {Thiamine : catalytic mechanisms in normal and disease states / ed. by Frank Jordan ...},
  publisher = {Dekker},
  address   = {New York, NY},
  isbn      = {0-8247-4062-9},
  pages     = {275 -- 290},
  year      = {2004},
  language  = {en}
}
@article{SiegertMcLeishBaumannetal.2005,
  author    = {Siegert, Petra and McLeish, Michael J. and Baumann, Martin and Iding, Hans and Kneen, Malea M. and Kenyon, George L. and Pohl, Martina},
  title     = {Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida},
  series = {Protein engineering, design, and selection : peds},
  volume    = {Vol. 18},
  journal   = {Protein engineering, design, and selection : peds},
  number    = {Iss. 7},
  issn      = {1460-213X (E-Journal); 1741-0134 (E-Journal); 0269-2139 (Print); 1741-0126 (Print)},
  pages     = {345 -- 357},
  year      = {2005},
  language  = {en}
}
@incollection{WendorffEggertPohletal.2007,
  author    = {Wendorff, Marion and Eggert, Thorsten and Pohl, Martina and Dresen, Carola and M{\"u}ller, Michael and Jaeger, Karl-Erich and Sprenger, Georg A. and Sch{\"u}rmann, Melanie and Sch{\"u}rmann, Martin and Johnen, Sandra and Sprenger, Gerda and Sahm, Hermann and Inoue, Tomoyuki and Sch{\"o}rken, Ulrich and Breittaupt, Holger and Fr{\"o}lich, Bettina and Heim, Petra and Iding, Hans and Juchem, Bettina and Siegert, Petra and Kula, Maria-Regina and Weckbecker, Andrea and Hummel, Werner and Fessner, Wolf-Dieter and Elling, Lothar and Wolberg, Michael and Bode, Silke and Feldmann, Ralf and Geilenkirchen, Petra and Schubert, Thomas and Walter, Lydia and D{\"u}nnwald, Thomas and Demir, Ayhan S. and Kolter-Jung, Doris and Nitsche, Adam and D{\"u}nkelmann, Pascal and Cosp, Annabel and Lingen, Bettina},
  title     = {Catalytic asymmetric synthesis : section 2.2},
  series = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...},
  booktitle = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  isbn      = {978-3-527-31473-7},
  pages     = {298 -- 413},
  year      = {2007},
  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{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{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{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{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{WhiteheadOehlschlaegerAlmajhdietal.2014,
  author    = {Whitehead, Mark and {\"O}hlschl{\"a}ger, Peter and Almajhdi, Fahad N. and Alloza, Leonor and Marz{\´a}bal, Pablo and Meyers, Ann E. and Hitzeroth, Inga I. and Rybicki, Edward P.},
  title     = {Human papillomavirus (HPV) type 16 E7 protein bodies cause tumour regression in mice},
  series = {BMC cancer},
  journal   = {BMC cancer},
  number    = {14:367},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2407},
  doi       = {10.1186/1471-2407-14-367},
  pages     = {1 -- 15},
  year      = {2014},
  language  = {en}
}
@inproceedings{BrandiniBaumann1997,
  author    = {Brandini, Frederico P. and Baumann, Marcus},
  title     = {The potential role of melted 'brown ice' as sources of chelators and ammonia to the surface waters of the Weddell Sea, Antarctica},
  series = {Proceedings of the NIPR Symposium on Polar Biology : 10},
  booktitle = {Proceedings of the NIPR Symposium on Polar Biology : 10},
  address   = {Tokyo},
  organization    = {National Institute of Polar Research},
  issn      = {0914-563X},
  pages     = {1 -- 13},
  year      = {1997},
  language  = {en}
}
@article{TuegBaumann1995,
  author    = {T{\"u}g, Helmut and Baumann, Marcus},
  title     = {Reply to the comments by R.L. McKenzie and P.V. Johnston on our paper "Problems of UV-B radiation measurements in biological research: Critical Remarks on current techniques and suggestions for improvements"},
  series = {Geophysical research letters},
  volume    = {Vol. 22},
  journal   = {Geophysical research letters},
  number    = {Iss. 9},
  issn      = {1944-8007 (E-Journal); 0094-8276 (Print)},
  pages     = {1159 -- 1160},
  year      = {1995},
  language  = {en}
}
@incollection{MedlinBarkerBaumannetal.1994,
  author    = {Medlin, L. K. and Barker, G. L. A. and Baumann, Marcus and Hayes, P. K.},
  title     = {Molecular biology and systematics},
  series = {The Haptophyte Algae (Special volume / Systematics Association : 51)},
  booktitle = {The Haptophyte Algae (Special volume / Systematics Association : 51)},
  publisher = {Clarendon Press},
  address   = {Oxford},
  isbn      = {0-19-857772-9},
  pages     = {393 -- 411},
  year      = {1994},
  language  = {en}
}
@article{MedlinLangeBaumann1994,
  author    = {Medlin, L. K. and Lange, M. and Baumann, Marcus},
  title     = {Genetic differentiation among three colony-forming species of Phaeocystis : further evidence for the phylogeny of the Prymnesiophyta},
  series = {Phycologia},
  volume    = {Vol. 33},
  journal   = {Phycologia},
  number    = {Iss. 3},
  issn      = {0031-8884},
  pages     = {199 -- 212},
  year      = {1994},
  language  = {en}
}
@article{TuegBaumann1994,
  author    = {T{\"u}g, Helmut and Baumann, Marcus},
  title     = {Problems of UV-B radiation measurements in biological research : critical remarks on current techniques and suggestions for improvements},
  series = {Geophysical research letters},
  volume    = {Vol. 21},
  journal   = {Geophysical research letters},
  number    = {Iss. 8},
  issn      = {1944-8007 (E-Journal); 0094-8276 (Print)},
  pages     = {689 -- 692},
  year      = {1994},
  language  = {en}
}
@article{AletseeBaumann1991,
  author    = {Aletsee, Ludwig and Baumann, Marcus},
  title     = {A laboratory incubator equipped with facilities to automatically simulate natural irradiance},
  series = {Boletim do Instituto Oceanogr{\´a}fico / Universidade de S{\~a}o Paulo},
  volume    = {Vol. 39},
  journal   = {Boletim do Instituto Oceanogr{\´a}fico / Universidade de S{\~a}o Paulo},
  number    = {No. 2},
  issn      = {1982-436X; 0080-6331},
  pages     = {155 -- 159},
  year      = {1991},
  language  = {en}
}
@inproceedings{Baumann1989,
  author    = {Baumann, Marcus},
  title     = {Primary production and phytoplankton growth in the marginal ice zone of the Fram Strait and the interpretation of the field data with autecological experiments (Abstract)},
  series = {Oceanography and biology of Arctic seas : selected papers from the ICES Symposium on Marine Sciences of the Arctic and Subarctic Regions, held in Santander, 28 - 30 September 1987. (Rapports et proc{\`e}s-verbaux des r{\´e}unions / Conseil International pour l'Exploration de la Mer ; 188)},
  booktitle = {Oceanography and biology of Arctic seas : selected papers from the ICES Symposium on Marine Sciences of the Arctic and Subarctic Regions, held in Santander, 28 - 30 September 1987. (Rapports et proc{\`e}s-verbaux des r{\´e}unions / Conseil International pour l'Exploration de la Mer ; 188)},
  editor    = {Hempel, G.},
  publisher = {International Council for the Exploration of the Sea},
  address   = {Copenhagen},
  organization    = {Symposium on Marine Sciences of the Arctic and Subarctic Regions <1987, Santander>},
  pages     = {128},
  year      = {1989},
  language  = {en}
}
@article{JahnkeBaumann1987,
  author    = {Jahnke, J. and Baumann, Marcus},
  title     = {Differentiation between Phaeocystis pouchetii (Har.) Lagerheim and Phaeocystis globosa Scherffel},
  series = {Hydrobiological bulletin},
  volume    = {Vol. 21},
  journal   = {Hydrobiological bulletin},
  number    = {Iss. 2},
  issn      = {0165-1404 (Print); 1573-5125 (E-Journal)},
  pages     = {141 -- 147},
  year      = {1987},
  language  = {en}
}
@article{SmithBaumannWilsonetal.1987,
  author    = {Smith, Walker O. and Baumann, Marcus and Wilson, David L. and Aletsee, Ludwig},
  title     = {Phytoplankton biomass and productivity in the marginal ice zone of the Fram Strait during summer 1984},
  series = {Journal of geophysical research},
  volume    = {Vol. 92},
  journal   = {Journal of geophysical research},
  number    = {Iss. C7},
  issn      = {2156-2202 (E-Journal); 2169-9291 (E-Journal); 0148-0227 (Print); 2169-9275 (Print)},
  pages     = {6777 -- 6786},
  year      = {1987},
  language  = {en}
}
@article{KueppersSteffenHellmuthetal.2014,
  author    = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang},
  title     = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer},
  series = {Microbial cell factories},
  volume    = {13},
  journal   = {Microbial cell factories},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1475-2859 (E-Journal)},
  doi       = {10.1186/1475-2859-13-46},
  pages     = {Article No. 46},
  year      = {2014},
  language  = {en}
}
@article{TakenagaBiselliSchnitzleretal.2014,
  author    = {Takenaga, Shoko and Biselli, Manfred and Schnitzler, Thomas and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten and Sch{\"o}ning, Michael Josef},
  title     = {Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis-Menten-like kinetics for cell culturing},
  series = {Physica status solidi A : Applications and materials science},
  volume    = {211},
  journal   = {Physica status solidi A : Applications and materials science},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)},
  doi       = {10.1002/pssa.201330464},
  pages     = {1410 -- 1415},
  year      = {2014},
  abstract  = {The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17-200 mM) follows a Michaelis-Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.},
  language  = {en}
}
@article{GuoMiyamotoWagneretal.2014,
  author    = {Guo, Yuanyuan and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {Theoretical study and simulation of light-addressable potentiometric sensors},
  series = {Physica status solidi (A) : applications and materials},
  volume    = {211},
  journal   = {Physica status solidi (A) : applications and materials},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201330354},
  pages     = {1467 -- 1472},
  year      = {2014},
  abstract  = {The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.},
  language  = {en}
}
@article{HeineHerrmannSelmeretal.2014,
  author    = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.},
  title     = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily},
  series = {Proteins},
  volume    = {82},
  journal   = {Proteins},
  number    = {9},
  publisher = {Wiley-Liss},
  address   = {New York},
  issn      = {1097-0134 (E-Journal); 0887-3585 (Print)},
  doi       = {10.1002/prot.24557},
  pages     = {2041 -- 2053},
  year      = {2014},
  abstract  = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.},
  language  = {en}
}
@article{SchroeterHoffmannVoigtetal.2014,
  author    = {Schroeter, Rebecca and Hoffmann, Tamara and Voigt, Birgit and Meyer, Hanna and Bleisteiner, Monika and Muntel, Jan and J{\"u}rgen, Britta and Albrecht, Dirk and Becher, D{\"o}rte and Lalk, Michael and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Putzer, Harald and Hecker, Michael and Schweder, Thomas and Bremer, Erhard},
  title     = {Stress responses of the industrial workhorse Bacillus licheniformis to osmotic challenges},
  series = {PLoS ONE},
  volume    = {8},
  journal   = {PLoS ONE},
  number    = {11},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0080956},
  pages     = {e80956},
  year      = {2014},
  abstract  = {The Gram-positive endospore-forming bacterium Bacillus licheniformis can be found widely in nature and it is exploited in industrial processes for the manufacturing of antibiotics, specialty chemicals, and enzymes. Both in its varied natural habitats and in industrial settings, B. licheniformis cells will be exposed to increases in the external osmolarity, conditions that trigger water efflux, impair turgor, cause the cessation of growth, and negatively affect the productivity of cell factories in biotechnological processes. We have taken here both systems-wide and targeted physiological approaches to unravel the core of the osmostress responses of B. licheniformis. Cells were suddenly subjected to an osmotic upshift of considerable magnitude (with 1 M NaCl), and their transcriptional profile was then recorded in a time-resolved fashion on a genome-wide scale. A bioinformatics cluster analysis was used to group the osmotically up-regulated genes into categories that are functionally associated with the synthesis and import of osmostress-relieving compounds (compatible solutes), the SigB-controlled general stress response, and genes whose functional annotation suggests that salt stress triggers secondary oxidative stress responses in B. licheniformis. The data set focusing on the transcriptional profile of B. licheniformis was enriched by proteomics aimed at identifying those proteins that were accumulated by the cells through increased biosynthesis in response to osmotic stress. Furthermore, these global approaches were augmented by a set of experiments that addressed the synthesis of the compatible solutes proline and glycine betaine and assessed the growth-enhancing effects of various osmoprotectants. Combined, our data provide a blueprint of the cellular adjustment processes of B. licheniformis to both sudden and sustained osmotic stress.},
  language  = {en}
}
@article{WangDruckenmuellerElbersetal.2014,
  author    = {Wang, Ren-Qi and Druckenm{\"u}ller, Katharina and Elbers, Gereon and Guenther, Klaus and Crou{\´e}, Jean-Philippe},
  title     = {Analysis of aquatic-phase natural organic matter by optimized LDI-MS method},
  series = {Journal of mass spectrometry},
  volume    = {49},
  journal   = {Journal of mass spectrometry},
  number    = {2},
  publisher = {Wiley},
  address   = {Bognor Regis},
  issn      = {1096-9888},
  doi       = {10.1002/jms.3321},
  pages     = {154 -- 160},
  year      = {2014},
  abstract  = {The composition and physiochemical properties of aquatic-phase natural organic matter (NOM) are most important problems for both environmental studies and water industry. Laser desorption/ionization (LDI) mass spectrometry facilitated successful examinations of NOM, as humic and fulvic acids in NOM are readily ionized by the nitrogen laser. In this study, hydrophobic NOMs (HPO NOMs) from river, reservoir and waste water were characterized by this technique. The effect of analytical variables like concentration, solvent composition and laser energy was investigated. The exact masses of small molecular NOM moieties in the range of 200-1200 m/z were determined in reflectron mode. In addition, spectra of post-source-decay experiments in this range showed that some compounds from different natural NOMs had the same fragmental ions. In the large mass range of 1200-15 000 Da, macromolecules and their aggregates were found in HPO NOMs from natural waters. Highly humic HPO exhibited mass peaks larger than 8000 Da. On the other hand, the waste water and reservoir water mainly had relatively smaller molecules of about 2000 Da. The LDI-MS measurements indicated that highly humic river waters were able to form large aggregates and membrane foulants, while the HPO NOMs from waste water and reservoir water were unlikely to form large aggregates. Copyright © 2014 John Wiley \& Sons, Ltd.},
  language  = {en}
}
@article{HandtkeSchroeterJuergenetal.2014,
  author    = {Handtke, Stefan and Schroeter, Rebecca and J{\"u}rgen, Britta and Methling, Karen and Schl{\"u}ter, Rabea and Albrecht, Dirk and Hijum, Sacha A. F. T. van and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Schweder, Thomas and Hecker, Michael and Voigt, Birgit},
  title     = {Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress},
  series = {PLOS one},
  volume    = {9},
  journal   = {PLOS one},
  number    = {1},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0085625},
  pages     = {e85625},
  year      = {2014},
  abstract  = {Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.},
  language  = {en}
}
@misc{BerndtHoeckerKuropkaetal.1991,
  author    = {Berndt, Heinz and H{\"o}cker, Hartwig and Kuropka, Rolf and Kinkel, Joachim},
  title     = {Silane coated inorganic materials for chromatography : United States Patent},
  publisher = {[The United States Patent and Trademark Office]},
  address   = {[Alexandria, VA u.a.]},
  pages     = {9 S. : graph. Darst.},
  year      = {1991},
  language  = {en}
}
@inproceedings{KroggelBerndt1984,
  author    = {Kroggel, Matthias and Berndt, Heinz},
  title     = {The 0-hydroxiphenyloxicarbonyl-group a new base labile amine protecting group},
  series = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  booktitle = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  editor    = {Ragnarsson, Ulf},
  publisher = {Almquist \& Wiksell},
  address   = {Stockholm},
  isbn      = {91-22-00715-6},
  pages     = {81 -- 83},
  year      = {1984},
  language  = {en}
}
@inproceedings{SchnabelBerndt1973,
  author    = {Schnabel, Eberhard and Berndt, Heinz},
  title     = {Zur selektive Abspaltbarkeit der t-Butyloxycarbonylgruppe},
  series = {Peptides 1971 : proceedings of the Eleventh European Peptide Symposium, Vienna, Austria, April 1971},
  booktitle = {Peptides 1971 : proceedings of the Eleventh European Peptide Symposium, Vienna, Austria, April 1971},
  editor    = {Nesvadba, H.},
  publisher = {North-Holland Publ. [u.a.]},
  address   = {Amsterdam [u.a.]},
  isbn      = {0-7204-4120-X},
  pages     = {69 -- 70},
  year      = {1973},
  language  = {en}
}
@inproceedings{BerndtTurck1984,
  author    = {Berndt, Heinz and Turck, Christoph W.},
  title     = {Syntheses of defined peptide derivatives by aminolysis of 3-[Nα-benzyloxycarbonyl peptidyloxy] -2-hydroxy-N-methyl-benzamides at elevated temperatures II. Synthesis of the peptide derivatives Z-Ala-X-Gly-N(Et)2, X=Phe, Leu, Val, Ser (But), Glu (OBut)},
  series = {Chemistry of peptides and proteins : proceedings of the Fourth USSR-FRG Symposium, T{\"u}bingen, Federal Republic of Germany, June 8 - 12, 1982 / ed. Wolfgang Voelter ... - Vol. 2},
  booktitle = {Chemistry of peptides and proteins : proceedings of the Fourth USSR-FRG Symposium, T{\"u}bingen, Federal Republic of Germany, June 8 - 12, 1982 / ed. Wolfgang Voelter ... - Vol. 2},
  editor    = {Voelter, Wolfgang},
  publisher = {de Gruyter},
  address   = {Berlin [u.a.]},
  isbn      = {3-11009-580-7},
  pages     = {97 -- 103},
  year      = {1984},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Synthesis of hapten-polypeptide conjugates as antigen models for the N-terminal region of the α-2-chain of rabbit skin collagen},
  series = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  volume    = {1978},
  journal   = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  number    = {3},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-5463},
  doi       = {10.1039/P19780000260},
  pages     = {260 -- 263},
  year      = {1978},
  abstract  = {Synthesis of derivatives of the peptide sequence L-pyroglutamyl-L-phenylalanyl-L-aspartyl-glycyl-L-lysyl-glycyl-glycyl-glycine as the antigenic determinant representing the N-terminal non-helical region of the α-2-chain of rabbit skin collagen, and conjugation to two different polypeptide carriers, are described.},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Studies on sulfur-containing peptides : tert-butyloxycarbonylsulfenyl and benzyloxycarbonylsulfenyl derivatives as protecting groups for cysteine},
  series = {The journal of organic chemistry},
  volume    = {43},
  journal   = {The journal of organic chemistry},
  number    = {25},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0022-3263},
  doi       = {10.1021/jo00419a046},
  pages     = {4893 -- 4895},
  year      = {1978},
  language  = {en}
}
@article{MatoniBerndt1980,
  author    = {Matoni, Georg and Berndt, Heinz},
  title     = {Thermal synthesis of the optical pure pentapeptide derivative Z-(L)-Ala-(L)-Phe-Gly-(L)-Phe-Gly-OMe},
  series = {Tetrahedron letters},
  volume    = {21},
  journal   = {Tetrahedron letters},
  number    = {1},
  issn      = {0040-4039},
  doi       = {10.1016/S0040-4039(00)93618-9},
  pages     = {37 -- 40},
  year      = {1980},
  language  = {en}
}