@article{VanderVenEhlerVakeeletal.2006,
  author    = {VanderVen, Peter F. M. and Ehler, Elisabeth and Vakeel, Padmanabhan and Eulitz, Stefan and Schenk, J{\"o}rg A. and Milting, Hendrik and Micheel, Burkhard and F{\"u}rst, Dieter Oswald},
  title     = {Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/ VASP},
  doi       = {10.1016/j.yexcr.2006.03.015},
  year      = {2006},
  abstract  = {Filamin c is the predominantly expressed filamin isoform in striated muscles. It is localized in myofibrillar Z- discs, where it binds FATZ and myotilin, and in myotendinous junctions and intercalated discs. Here, we identify Xin, the protein encoded by the human gene 'cardiomyopathy associated 1' (CMYA1) as filamin c binding partner at these specialized structures where the ends of myofibrils are attached to the sarcolemma. Xin directly binds the EVH1 domain proteins Mena and VASP. In the adult heart, Xin and Mena/VASP colocalize with filamin c in intercalated discs. In cultured cardiomyocytes, the proteins also localize in the nonstriated part of myofibrils, where sarcomeres are assembled and an extensive reorganization of the actin cytoskeleton occurs. Unusual intraexonic splicing events result in the existence of three Xin isoforms that associate differentially with its ligands. The identification of the complex filamin c-Xin-Mena/VASP provides a first glance on the role of Xin in the molecular mechanisms involved in developmental and adaptive remodeling of the actin cytoskeleton during cardiac morphogenesis and sarcomere assembly. (c) 2006 Elsevier Inc. All rights reserved},
  language  = {en}
}
@article{Schenk2002,
  author    = {Schenk, J{\"o}rg A.},
  title     = {Two Hybrid cDNA Cloning},
  year      = {2002},
  language  = {en}
}
@article{SchlagOsterzielOezceliketal.2008,
  author    = {Schlag, Peter M. and Osterziel, Karl Joseph and {\"O}zcelik, Cemil and Scherneck, Siegfried and Wenzel, Katrin and Daskalow, Katjana and Herse, Florian and Seitz, Susanne and Zacharias, Ute and Schenk, J{\"o}rg A. and Schulz, Herbert and H{\"u}bner, Norbert and Micheel, Burkhard},
  title     = {The protein phosphatase 1 inhibitor KEPI is down regulated in breast cancer cell lines and tissues and involved in the regulation of the tumour suppressor EGR1 via the MEK-ERK pathway},
  year      = {2008},
  abstract  = {KEPI is a protein kinase C-potentiated inhibitory protein for type 1 Ser/Thr protein phosphatases. We found no or reduced expression of KEPI in breast cancer cell lines, breast tumors and metastases in comparison to normal breast cell lines and tissues, respectively. KEPI protein expression and ubiquitous localization was detected with a newly generated antibody. Ectopic KEPI expression in MCF7 breast cancer cells induced differential expression of 95 genes, including the up-regulation of the tumor suppressors EGR1 (early growth response 1) and PTEN (phosphatase and tensin homolog), which is regulated by EGR1. We further show that the up-regulation of EGR1 in MCF7/KEPI cells is mediated by MEK-ERK signaling. The inhibition of this pathway by the MEK inhibitor UO126 led to a strong decrease in EGR1 expression in MCF7/KEPI cells. These results reveal a novel role for KEPI in the regulation of the tumor suppressor gene EGR1 via activation of the MEK-ERK MAPK pathway.},
  language  = {en}
}
@article{BergholzHeymannSchenketal.1997,
  author    = {Bergholz, Andre and Heymann, Stephan and Schenk, J{\"o}rg A. and Freytag, Johann Christoph},
  title     = {Sequence comparison using a relational database approach},
  isbn      = {0-8186-8114-4},
  year      = {1997},
  language  = {en}
}
@article{SchenkFettkeLenzetal.2012,
  author    = {Schenk, J{\"o}rg A. and Fettke, J{\"o}rg and Lenz, Christine and Albers, Katharina and Mallwitz, Frank and Gajovic-Eichelmann, Nenad and Ehrentreich-F{\"o}rster, Eva and Kusch, Emely and Sellrie, Frank},
  title     = {Secretory leukocyte protease inhibitor (SLPI) might contaminate murine monoclonal antibodies after purification on protein G},
  series = {Journal of biotechnology},
  volume    = {158},
  journal   = {Journal of biotechnology},
  number    = {1-2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2011.12.025},
  pages     = {34 -- 35},
  year      = {2012},
  abstract  = {The large scale production of a monoclonal anti-progesterone antibody in serum free medium followed by affinity chromatography on protein G lead to a contamination of the antibody sample with a protein of about 14 kDa. This protein was identified by mass spectrometry as secretory leukocyte protease inhibitor (SLPI). This SLPI contamination lead to a failure of the fiber-optic based competitive fluorescence assay to detect progesterone in milk. Purification of the monoclonal antibody using protein A columns circumvented this problem.},
  language  = {en}
}
@article{LuebbeSchenkNaundorfetal.1999,
  author    = {L{\"u}bbe, L. and Schenk, J{\"o}rg A. and Naundorf, H. and Karsten, U. and Wunderlich, V.},
  title     = {Reverse transformation of human mammary carcinoma cells},
  year      = {1999},
  language  = {en}
}
@article{StechMerkSchenketal.2012,
  author    = {Stech, Marlitt and Merk, Helmut and Schenk, J{\"o}rg A. and St{\"o}cklein, Walter F. M. and W{\"u}stenhagen, Doreen Anja and Micheel, Burkhard and Duschl, Claus and Bier, Frank Fabian and Kubick, Stefan},
  title     = {Production of functional antibody fragments in a vesicle-based eukaryotic cell-free translation system},
  series = {Journal of biotechnology},
  volume    = {164},
  journal   = {Journal of biotechnology},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2012.08.020},
  pages     = {220 -- 231},
  year      = {2012},
  abstract  = {Cell-free protein synthesis is of increasing interest for the rapid and high-throughput synthesis of many proteins, in particular also antibody fragments. In this study, we present a novel strategy for the production of single chain antibody fragments (scFv) in a eukaryotic in vitro translation system. This strategy comprises the cell-free expression, isolation and label-free interaction analysis of a model antibody fragment synthesized in two differently prepared insect cell lysates. These lysates contain translocationally active microsomal structures derived from the endoplasmic reticulum (ER), allowing for posttranslational modifications of cell-free synthesized proteins. Both types of these insect cell lysates enable the synthesis and translocation of scFv into ER-derived vesicles. However, only the one that has a specifically adapted redox potential yields functional active antibody fragments. We have developed a new methodology for the isolation of functional target proteins based on the translocation of cell-free produced scFv into microsomal structures and subsequent collection of protein-enriched vesicles. Antibody fragments that have been released from these vesicles are shown to be well suited for label-free binding studies. Altogether, these results show the potential of insect cell lysates for the production, purification and selection of antibody fragments in an easy-to-handle and time-saving manner.},
  language  = {en}
}
@article{RohdeSchenkHeymannetal.1998,
  author    = {Rohde, M. and Schenk, J{\"o}rg A. and Heymann, Stephan and Behrsing, Olaf and Scharte, Gudrun and Kempter, Gerhard and Woller, Jochen and H{\"o}hne, Wolfgang and Warsinke, Axel and Micheel, Burkhard},
  title     = {Production and characterization of monoclonal antibodeis against urea derivatives},
  year      = {1998},
  language  = {en}
}
@article{GrothReszkaSchenk1996,
  author    = {Groth, Detlef and Reszka, R. and Schenk, J{\"o}rg A.},
  title     = {Polyethylene glycol-mediated transformation of escherichia coli is increased by room temperature incubation},
  year      = {1996},
  language  = {en}
}
@article{PecherSpahnSchirrmannetal.2001,
  author    = {Pecher, Gabriele and Spahn, Gunter and Schirrmann, Thomas and Kulbe, Hagen and Ziegner, Maja and Schenk, J{\"o}rg A. and Sandig, Volker},
  title     = {Mucin gene (MUC1) transfer into human dendritic cells by cationic liposomes and recombinant adenovirus},
  issn      = {0250-7005},
  year      = {2001},
  abstract  = {BACKGROUND: Dendritic cells (DC) as antigen presenting cells play an important role in immunotherapy of cancer. Mucin, encoded by the gene MUC1, is a human tumor antigen expressed in breast, pancreatic and ovarian cancers. Therefore, MUC1-transfected DC would be an attractive tool in constructing cancer vaccines. MATERIALS AND METHODS: Using two different cationic liposome preparations and, for comparison, a recombinant adenovirus expressing mucin, we tested the efficiency of mucin gene transfer into DC by flow cytometry. We investigated if these transfected DC were able to specifically stimulate autologous peripheral blood lymphocytes (PBL) from healthy donors. RESULTS: Flow cytometry revealed that 5-20\% of DC transfected with liposomes Lipofectin and 20-40\% of DC transduced with adenovirus expressed the relevant mucin epitopes. The expression of mucin on DC was similar to the expression of mucin found on carcinoma cells. After antigen uptake, DC specifically stimulated autologous PBL. CONCLUSION: We have shown that cationic liposomal gene transfer into human DC was feasible. We could obtain antigen specific stimulation of PBL at a similar rate as with adenoviral MUC1-transduced DC.},
  language  = {en}
}