@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}
}
@misc{MaurerO'ConnellSiegertetal.2012,
  author    = {Maurer, Karl-Heinz and O'Connell, Timothy and Siegert, Petra and Weber, Thomas and Tondera, Susanne and Hellmuth, Hendrik},
  title     = {Fl{\"u}ssige Tensidzubereitung enthaltend Lipase und Phosphonat [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 22},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierenden Komponente, die eine Phenylalkyldicarbons{\"a}ure umfasst) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 15},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (durch den Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine mehrfach substituierte Benzolcarbons{\"a}ure umfasst, die an mindestens zwei Kohlenstoffatomen des Benzolrestes eine Carboxylgruppe aufweist) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 16},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Phthaloylglutamins{\"a}ure und/oder eine Phthaloylasparagins{\"a}ure umfasst) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 16},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Aminophthals{\"a}ure umfasst) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 16},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Oligoamino-biphenyl-oligocarbons{\"a}ure umfasst) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 16},
  year      = {2012},
  language  = {de}
}
@misc{SiegertMerkelHellmuthetal.2012,
  author    = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz},
  title     = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die ein Monosaccharidglycerat umfasst) [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 17},
  year      = {2012},
  language  = {de}
}
@misc{SiegertSchwanebergMartinezMoyaetal.2012,
  author    = {Siegert, Petra and Schwaneberg, Ulrich and Martinez Moya, Ronny and Merkel, Marion and Spitz, Astrid and Wieland, Susanne and Hellmuth, Hendrik and Maurer, Karl-Heinz},
  title     = {Leistungsverbesserte Proteasevariante [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 29},
  year      = {2012},
  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}
}