@article{WernerGroebelSchuhmacheretal.2009,
  author    = {Werner, Frederik and Groebel, Simone and Schuhmacher, K. and Spelthahn, Heiko and Wagner, Torsten and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Bestimmung der metabolischen Aktivit{\"a}t von Mikroorganismen w{\"a}hrend des Biogasbildungsprozesses},
  series = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  journal   = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  publisher = {TUDpress},
  address   = {Dresden},
  isbn      = {978-3-941298-44-6},
  pages     = {201 -- 204},
  year      = {2009},
  language  = {de}
}
@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{MartinsBlaserFeliksetal.2011,
  author    = {Martins, Berta M. and Blaser, Martin and Feliks, Mikolaj and Ullmann, Matthias G. and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme},
  series = {Journal of the American Chemical Society},
  journal   = {Journal of the American Chemical Society},
  publisher = {ACS Publications},
  address   = {Washington, DC},
  pages     = {1 -- 33},
  year      = {2011},
  language  = {en}
}
@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}
}
@article{WernerGroebelWagneretal.2011,
  author    = {Werner, Frederik and Groebel, Simone and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {{\"U}berwachung der metabolischen Aktivit{\"a}t von Mikroorganismen zur Kontrolle des biologischen Prozesses im Biogasfermenter},
  series = {Biogas 2011 : Energietr{\"a}ger der Zukunft ; 6. Fachtagung, Fachtagung Braunschweig, 08. und 09. Juni 2011 / VDI Energie und Umwelt},
  journal   = {Biogas 2011 : Energietr{\"a}ger der Zukunft ; 6. Fachtagung, Fachtagung Braunschweig, 08. und 09. Juni 2011 / VDI Energie und Umwelt},
  publisher = {VDI-Verl.},
  address   = {D{\"u}sseldorf},
  isbn      = {978-3-18-092121-1},
  pages     = {285 -- 286},
  year      = {2011},
  language  = {de}
}
@article{SchiffelsPinkenburgScheldenetal.2013,
  author    = {Schiffels, Johannes and Pinkenburg, Olaf and Schelden, Maximilian and Aboulnaga, El-Hussiny A. A. and Baumann, Marcus and Selmer, Thorsten},
  title     = {An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from cupriavidus necator in Escherichia coli},
  series = {PLOS one. 2013},
  journal   = {PLOS one. 2013},
  publisher = {Public Library of Science},
  address   = {San Francisco, California},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0068812},
  year      = {2013},
  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{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{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}
}
@techreport{SchoeningSelmerBaumann2012,
  author    = {Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Baumann, Marcus},
  title     = {Schlussbericht zum Projekt "Bio-LAPS" : Optimierung des Betriebs eines Biogasfermenters mit Hilfe eines Feldeffekt-Biosensors auf Basis eines lichtadressierbaren potentiometrischen Sensors (LAPS) : Laufzeit: 01.09.2008 bis 31.01.2012 : F{\"o}rderkennzeichen 07NR264 bzw.22026407},
  publisher = {BMELV},
  address   = {Berlin},
  pages     = {44 S.},
  year      = {2012},
  language  = {de}
}