@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{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{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{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{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}
}
@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{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{SelmerSommerladeIngendohetal.1994,
  author    = {Selmer, Thorsten and Sommerlade, Hans-J{\"o}rg and Ingendoh, Arnd and Gieselmann, Volkmar},
  title     = {Glycosylation and phosphorylation of arylsulfatase A / Sommerlade, Hans-J{\"o}rg. ; Selmer, Thomas. ; Ingendoh, Arnd ; Gieselmann, Volkmar ; Figura, Kurt von ; Neifer, Klaus ; Schmidt, Bernhard},
  series = {Journal of Biological Chemistry. 269 (1994), H. 33},
  journal   = {Journal of Biological Chemistry. 269 (1994), H. 33},
  isbn      = {1083-351X},
  pages     = {20977 -- 20981},
  year      = {1994},
  language  = {en}
}
@article{SchoeningBiselliSelmeretal.2012,
  author    = {Sch{\"o}ning, Michael Josef and Biselli, Manfred and Selmer, Thorsten and {\"O}hlschl{\"a}ger, Peter and Baumann, Marcus and F{\"o}rster, Arnold and Poghossian, Arshak},
  title     = {Forschung „zwischen" den Disziplinen: das Institut f{\"u}r Nano- und Biotechnologien},
  series = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik},
  volume    = {Publ. online},
  journal   = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik},
  publisher = {Dr. Beyer Internet-Beratung},
  address   = {Ober-Ramstadt},
  pages     = {11 Seiten},
  year      = {2012},
  abstract  = {"Biologie trifft Mikroelektronik", das Motto des Instituts f{\"u}r Nano- und Biotechnologien (INB) an der FH Aachen, unterstreicht die zunehmende Bedeutung interdisziplin{\"a}r gepr{\"a}gter Forschungsaktivit{\"a}ten. Der thematische Zusammenschluss grundst{\"a}ndiger Disziplinen, wie die Physik, Elektrotechnik, Chemie, Biologie sowie die Materialwissenschaften, l{\"a}sst neue Forschungsgebiete entstehen, ein herausragendes Beispiel hierf{\"u}r ist die Nanotechnologie: Hier werden neue Werkstoffe und Materialien entwickelt, einzelne Nanopartikel oder Molek{\"u}le und deren Wechselwirkung untersucht oder Schichtstrukturen im Nanometerbereich aufgebaut, die neue und vorher nicht bekannte Eigenschaften hervorbringen. Vor diesem Hintergrund b{\"u}ndelt das im Jahre 2006 gegr{\"u}ndete INB die an der FH Aachen vorhandenen Kompetenzen von derzeit insgesamt sieben Laboratorien auf den Gebieten der Halbleitertechnik und Nanoelektronik, Nanostrukturen und DNA-Sensorik, der Chemo- und Biosensorik, der Enzymtechnologie, der Mikrobiologie und Pflanzenbiotechnologie, der Zellkulturtechnik, sowie der Roten Biotechnologie synergetisch. In der Nano- und Biotechnologie steckt außergew{\"o}hnliches Potenzial! Nicht zuletzt deshalb stellen sich die Forscher der Herausforderung, in diesem Bereich gemeinsam zu forschen und Schnittstellen zu nutzen, um so bei der Gestaltung neuartiger Ideen und Produkte mitzuwirken, die zuk{\"u}nftig unser allt{\"a}gliches Leben ver{\"a}ndern werden. Im Folgenden werden die verschiedenen Forschungsbereiche kurz zusammenfassend vorgestellt und vorhandene Interaktionen anhand von exemplarisch ausgew{\"a}hlten, aktuellen Forschungsprojekten skizziert.},
  language  = {de}
}
@article{SchiffelsBaumannSelmer2011,
  author    = {Schiffels, Johannes and Baumann, Marcus and Selmer, Thorsten},
  title     = {Facile analysis of short-chain fatty acids as 4-nitrophenyl esters in complex anaerobic fermentation samples by high performance liquid chromatography},
  series = {Journal of Chromatography A. 1218 (2011), H. 34},
  journal   = {Journal of Chromatography A. 1218 (2011), H. 34},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {0021-9673},
  pages     = {5848 -- 5851},
  year      = {2011},
  language  = {en}
}