@article{HuckSchiffelsHerreraetal.2013,
  author    = {Huck, Christina and Schiffels, Johannes and Herrera, Cony N. and Schelden, Maximilian and Selmer, Thorsten and Poghossian, Arshak and Baumann, Marcus and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Metabolic responses of Escherichia coli upon glucose pulses captured by a capacitive field-effect sensor},
  series = {Physica Status Solidi (A)},
  volume    = {210},
  journal   = {Physica Status Solidi (A)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201200900},
  pages     = {926 -- 931},
  year      = {2013},
  abstract  = {Living cells are complex biological systems transforming metabolites taken up from the surrounding medium. Monitoring the responses of such cells to certain substrate concentrations is a challenging task and offers possibilities to gain insight into the vitality of a community influenced by the growth environment. Cell-based sensors represent a promising platform for monitoring the metabolic activity and thus, the "welfare" of relevant organisms. In the present study, metabolic responses of the model bacterium Escherichia coli in suspension, layered onto a capacitive field-effect structure, were examined to pulses of glucose in the concentration range between 0.05 and 2 mM. It was found that acidification of the surrounding medium takes place immediately after glucose addition and follows Michaelis-Menten kinetic behavior as a function of the glucose concentration. In future, the presented setup can, therefore, be used to study substrate specificities on the enzymatic level and may as well be used to perform investigations of more complex metabolic responses. Conclusions and perspectives highlighting this system are discussed.},
  language  = {en}
}
@article{SelmerPinkenburg2008,
  author    = {Selmer, Thorsten and Pinkenburg, Olaf},
  title     = {Method of cloning at least one nucleic acid molecule of interest using type IIS restriction endonucleases, and corresponding cloning vectors, kits and system using type IIS restriction endonucleases / Selmer, Thorsten ; Pinkenburg, Olaf},
  year      = {2008},
  language  = {en}
}
@book{Selmer1996,
  author    = {Selmer, Thorsten},
  title     = {Nachweis einer neuartigen posttranslationalen Modifikation in Sulfatasen und ihr Fehlen in Enzymen aus Patienten mit multipler Sulfatase-Defizienz},
  publisher = {Cuvillier},
  address   = {G{\"o}ttingen},
  pages     = {XIII, 143, IX S. : graph. Darst.},
  year      = {1996},
  language  = {de}
}
@article{SelmerPierikHeider2005,
  author    = {Selmer, Thorsten and Pierik, Antonio J. and Heider, Johann},
  title     = {New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria},
  series = {Biological Chemistry. 386 (2005), H. 10},
  journal   = {Biological Chemistry. 386 (2005), H. 10},
  isbn      = {1431-6730},
  pages     = {981 -- 988},
  year      = {2005},
  language  = {en}
}
@article{SelmerJennemannBaueretal.1999,
  author    = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut},
  title     = {Novel glycoinositolphosphosphingolipids, basidiolipids, from Agaricus / Jennemann, Richard ; Bauer, Bernhard, L. ; Bertalanffy, Helmut ; Geyer, Rudolf ; Gschwind, Ruth, M. ; Selmer, Thorsten ; Wiegandt, Herbert},
  series = {European Journal of Biochemistry. 259 (1999), H. 1-2},
  journal   = {European Journal of Biochemistry. 259 (1999), H. 1-2},
  isbn      = {0014-2956},
  pages     = {331 -- 338},
  year      = {1999},
  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{PilasYaziciSelmeretal.2017,
  author    = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate},
  series = {Electrochimica Acta},
  volume    = {251},
  journal   = {Electrochimica Acta},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2017.07.119},
  pages     = {256 -- 262},
  year      = {2017},
  abstract  = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.},
  language  = {en}
}
@article{PilasMarianoKeusgenetal.2015,
  author    = {Pilas, Johanna and Mariano, K. and Keusgen, M. and Selmer, Thorsten and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes},
  series = {Procedia Engineering},
  volume    = {120},
  journal   = {Procedia Engineering},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1877-7058},
  doi       = {10.1016/j.proeng.2015.08.702},
  pages     = {532 -- 535},
  year      = {2015},
  language  = {en}
}
@article{SelmerBuckel1999,
  author    = {Selmer, Thorsten and Buckel, Wolfgang},
  title     = {Oxygen Exchange between Acetate and the Catalytic Glutamate Residue in Glutaconate CoA-transferase from Acidaminococcus fermentans. IMPLICATIONS FOR THE MECHANISM OF CoA-ESTER HYDROLYSIS},
  series = {Journal of Biological Chemistry. 274 (1999), H. 30},
  journal   = {Journal of Biological Chemistry. 274 (1999), H. 30},
  isbn      = {1083-351X},
  pages     = {20772 -- 20778},
  year      = {1999},
  language  = {en}
}
@article{SelmerAndrei2001,
  author    = {Selmer, Thorsten and Andrei, Paula I.},
  title     = {p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol},
  series = {European Journal of Biochemistry. 268 (2001), H. 5},
  journal   = {European Journal of Biochemistry. 268 (2001), H. 5},
  isbn      = {0014-2956},
  pages     = {1363 -- 1372},
  year      = {2001},
  language  = {en}
}