@article{KirchnerReisertPuetzetal.2012,
  author    = {Kirchner, Patrick and Reisert, Steffen and P{\"u}tz, Patrick and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Characterisation of polymeric materials as passivation layer for calorimetric H2O2 gas sensors},
  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.201100773},
  pages     = {859 -- 863},
  year      = {2012},
  abstract  = {Calorimetric gas sensors for monitoring the H₂O₂ concentration at elevated temperatures in industrial sterilisation processes have been presented in previous works. These sensors are built up in form of a differential set-up of a catalytically active and passive temperature-sensitive structure. Although, various types of catalytically active dispersions have been studied, the passivation layer has to be established and therefore, chemically as well as physically characterised. In the present work, fluorinated ethylene propylene (FEP), perfluoralkoxy (PFA) and epoxy-based SU-8 photoresist as temperature-stable polymeric materials have been investigated for sensor passivation in terms of their chemical inertness against H₂O₂, their hygroscopic properties as well as their morphology. The polymeric materials were deposited via spin-coating on the temperature-sensitive structure, wherein spin-coated FEP and PFA show slight agglomerates. However, they possess a low absorption of humidity due to their hydrophobic surface, whereas the SU-8 layer has a closed surface but shows a slightly higher absorption of water. All of them were inert against gaseous H₂O₂ during the characterisation in H₂O₂ atmosphere that demonstrates their suitability as passivation layer for calorimetric H₂O₂ gas sensors.},
  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}
}
@inproceedings{BohrnMuchaWerneretal.2012,
  author    = {Bohrn, Ulrich and Mucha, Andreas and Werner, Frederik and St{\"u}tz, Evamaria and B{\"a}cker, Matthias and Krumbe, Christoph and Schienle, Meinrad and Fleischer, Maximilian and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Detection of toxic chromium species in water using cellbased sensor systems},
  isbn      = {978-3-9813484-2-2},
  doi       = {10.5162/IMCS2012/P2.1.14},
  pages     = {1364 -- 1367},
  year      = {2012},
  language  = {en}
}
@inproceedings{BohrnStuetzFleischeretal.2012,
  author    = {Bohrn, Ulrich and St{\"u}tz, Evamaria and Fleischer, Maximilian and Sch{\"o}ning, Michael Josef and Wagner, Patrick},
  title     = {Living cell-based gas sensor system for the detection of acetone in air},
  isbn      = {978-3-9813484-2-2},
  doi       = {10.5162/IMCS2012/3.2.3},
  pages     = {269 -- 272},
  year      = {2012},
  language  = {en}
}
@inproceedings{TakenagaWernerSawadaetal.2012,
  author    = {Takenaga, Shoko and Werner, Frederik and Sawada, Kazuaki and Sch{\"o}ning, Michael Josef},
  title     = {Comparison of label-free ACh image sensors based on CCD and LAPS},
  isbn      = {978-3-9813484-2-2},
  doi       = {10.5162/IMCS2012/4.2.6},
  pages     = {356 -- 359},
  year      = {2012},
  language  = {en}
}
@article{SchoeningBaecker2012,
  author    = {Sch{\"o}ning, Michael Josef and B{\"a}cker, Matthias},
  title     = {Chip-basierte Sensoren f{\"u}r die Biotechnik},
  volume    = {13},
  number    = {2},
  publisher = {BIOCOM},
  address   = {Berlin},
  issn      = {1611-0854},
  year      = {2012},
  language  = {de}
}
@article{SpelthahnSchubertSchoening2012,
  author    = {Spelthahn, Heiko and Schubert, J{\"u}rgen and Sch{\"o}ning, Michael Josef},
  title     = {D{\"u}nnschichtsensoren f{\"u}r die Schwermetallanalytik : Mikroelektroden auf Chalkogenidglasbasis},
  series = {GIT Labor-Fachzeitschrift},
  journal   = {GIT Labor-Fachzeitschrift},
  number    = {4},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  pages     = {285 -- 287},
  year      = {2012},
  abstract  = {Die Detektion von Schadstoffen repr{\"a}sentiert in der Umweltanalytik eine wichtige Aufgabenstellung. Gerade die Abwasser- bzw. Brauchwasseranalytik sowie die Prozesskontrolle haben einen hohen Stellenwert. Siliziumbasierte D{\"u}nnschichtsensoren bieten eine kosteng{\"u}nstige M{\"o}glichkeit, „online"-Messungen bzw. Vor-Ort-Messungen zeitnah durchzuf{\"u}hren. In dieser Arbeit wird ein potentiometrisches Sensorarray auf der Basis von Chalkogenidgl{\"a}sern zur Detektion von Schwermetallen in w{\"a}ssrigen Medien vorgestellt.},
  language  = {de}
}
@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{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}
}