@article{AboulnagaZouSelmeretal.2018,
  author    = {Aboulnaga, E. A. and Zou, H. and Selmer, Thorsten and Xian, M.},
  title     = {Development of a plasmid-based, tunable, tolC-derived expression system for application in Cupriavidus necator H16},
  series = {Journal of Biotechnology},
  volume    = {274},
  journal   = {Journal of Biotechnology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2018.03.007},
  pages     = {15 -- 27},
  year      = {2018},
  abstract  = {Cupriavidus necator H16 gains increasing attention in microbial research and biotechnological application due to its diverse metabolic features. Here we present a tightly controlled gene expression system for C. necator including the pBBR1-vector that contains hybrid promoters originating from C. necator native tolC-promoter in combination with a synthetic tetO-operator. The expression of the reporter gene from these plasmids relies on the addition of the exogenous inducer doxycycline (dc). The novel expression system offers a combination of advantageous features as; (i) high and dose-dependent recombinant protein production, (ii) tight control with a high dynamic range (On/Off ratio), which makes it applicable for harmful pathways or for toxic protein production, (iii) comparable cheap inducer (doxycycline, dc), (iv) effective at low inducer concentration, that makes it useful for large scale application, (v) rapid, diffusion controlled induction, and (vi) the inducer does not interfere within the cell metabolism. As applications of the expression system in C. necator H16, the growth ability on glycerol was enhanced by constitutively expressing the E. coli glpk gene-encoding for glycerol kinase. Likewise, we used the system to overcome the expression toxicity of mevalonate pathway in C. necator H16. With this system, the mevalonate-genes were successfully introduced in the host and the recombinant strains could produce about 200 mg/l mevalonate.},
  language  = {en}
}
@article{AboulnagaPinkenburgSchiffelsetal.2013,
  author    = {Aboulnaga, E. H. and Pinkenburg, O. and Schiffels, Johannes and El-Refai, A. and Buckel, W. and Selmer, Thorsten},
  title     = {Butyrate production in Escherichia coli: Exploitation of an oxygen tolerant bifurcating butyryl-CoA dehydrogenase/electron transferring flavoprotein complex from Clostridium difficile},
  series = {Journal of bacteriology. June 14, 2013},
  journal   = {Journal of bacteriology. June 14, 2013},
  issn      = {1098-5530 (E-Journal) ; 0021-9193 (Print)},
  pages     = {Epub ahead of print},
  year      = {2013},
  language  = {de}
}
@article{AbulnagaPinkenburgSchiffelsetal.2013,
  author    = {Abulnaga, El-Hussiny and Pinkenburg, Olaf and Schiffels, Johannes and E-Refai, Ahmed and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli},
  series = {Journal of bacteriology},
  volume    = {195},
  journal   = {Journal of bacteriology},
  number    = {16},
  issn      = {1098-5530 [E-Journal]},
  pages     = {3704 -- 3713},
  year      = {2013},
  language  = {en}
}
@article{BalakrishnanAndreiSelmerSelmeretal.2010,
  author    = {Balakrishnan, Karthikeyan and Andrei-Selmer, Luminita-Cornelia and Selmer, Thorsten and Bacher, Michael and Dodel, Richard},
  title     = {Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β},
  series = {Journal of Alzheimer's Disease},
  volume    = {20},
  journal   = {Journal of Alzheimer's Disease},
  number    = {1},
  isbn      = {1387-2877},
  pages     = {135 -- 143},
  year      = {2010},
  language  = {en}
}
@article{DantismRoehlenSelmeretal.2019,
  author    = {Dantism, Shahriar and R{\"o}hlen, Desiree and Selmer, Thorsten and Wagner, Torsten and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Quantitative differential monitoring of the metabolic activity of Corynebacterium glutamicum cultures utilizing a light-addressable potentiometric sensor system},
  series = {Biosensors and Bioelectronics},
  volume    = {139},
  journal   = {Biosensors and Bioelectronics},
  publisher = {Elsevier},
  address   = {Amsterdam},
  doi       = {10.1016/j.bios.2019.111332},
  pages     = {Artikel 111332},
  year      = {2019},
  language  = {en}
}
@article{DemmerChowdhurySelmeretal.2017,
  author    = {Demmer, Julius K. and Chowdhury, Nilanjan Pal and Selmer, Thorsten and Ermler, Ulrich and Buckel, Wolfgang},
  title     = {The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile},
  series = {Nature Communications},
  volume    = {8},
  journal   = {Nature Communications},
  number    = {1},
  issn      = {2041-1723},
  doi       = {10.1038/s41467-017-01746-3},
  pages     = {1 -- 10},
  year      = {2017},
  language  = {en}
}
@inproceedings{GroebelWernerJoerresetal.2011,
  author    = {Groebel, Simone and Werner, Frederik and J{\"o}rres, Niklas and Jansen, F. and Kasper, Katharina and Schiffels, Johannes and Sprenger, B. and Baumann, Marcus and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Entwicklung einer Sensor-{\"U}berwachung f{\"u}r Biogasanlagen auf Basis von Prozessdaten einer Parallelanlage},
  series = {10. Dresdner Sensor-Symposium : Dresden, 5. - 7. Dezember 2011 ; miniaturisierte analytische Verfahren, Hochtemperatur-Sensoren, Sensoren f{\"u}r Bioprozess- und Verfahrenstechnik, Sensoren f{\"u}r die Medizin, Chemische Verfahrenstechnik, Lebensmittelanalytik, innovative Sensorl{\"o}sungen, Sensoren f{\"u}r die Wasserqualit{\"a}t, Selbst{\"u}berwachung / Gerald Gerlach ... (Hg.)},
  booktitle = {10. Dresdner Sensor-Symposium : Dresden, 5. - 7. Dezember 2011 ; miniaturisierte analytische Verfahren, Hochtemperatur-Sensoren, Sensoren f{\"u}r Bioprozess- und Verfahrenstechnik, Sensoren f{\"u}r die Medizin, Chemische Verfahrenstechnik, Lebensmittelanalytik, innovative Sensorl{\"o}sungen, Sensoren f{\"u}r die Wasserqualit{\"a}t, Selbst{\"u}berwachung / Gerald Gerlach ... (Hg.)},
  publisher = {TUDpress},
  address   = {Dresden},
  isbn      = {978-3-942710-53-4},
  doi       = {10.5162/10dss2011/4.3},
  pages     = {81 -- 84},
  year      = {2011},
  abstract  = {Beim Ausbau nachhaltiger, regenerativer Energieversorgung hat die Umwandlung von organischer Biomasse in Biogas ein großes Potential. Der zugrundeliegende, komplexe biologische Prozess wird noch immer unzureichend verstanden und bedarf systematischer Untersuchungen der Prozessparameter, um einen hohen Ertrag bei guter Gasqualit{\"a}t zu erm{\"o}glichen. Die Fragestellungen zur Entschl{\"u}sselung des Prozesses sind sowohl verfahrenstechnischer als auch mikrobiologischer Natur. Aus mikrobiologischer Sicht ist die Kenntnis der tats{\"a}chlich beteiligten prozesstragenden Mikroorganismen von erheblicher Bedeutung, aus verfahrenstechnischer Sicht die Kenntnis der physikalischen und chemischen Faktoren, welche die mikrobiologischen Prozesse und kontrollieren. Im Zusammenspiel aller dieser Parameter wird die Biogasbildung bef{\"o}rdert oder behindert, bis zum Abbruch des Prozesses. Eine m{\"o}gliche Kontrollmethode ist die Messung der metabolischen Aktivit{\"a}t prozesstragender Organismen. Diese soll, beruhend auf fundierten Prozessdaten, gewonnen durch eine Parallelanlage, mit einem lichtadressierbaren potentiometrischen Sensor-System (LAPS) realisiert werden. Dieser Sensor ist in der Lage, pH-Wert-{\"a}nderungen zu detektieren, die durch den Stoffwechsel der auf dem Chip immobilisierten Organismen hervorgerufen werden, um eine Online-{\"U}berwachung von Biogasanlagen zu erm{\"o}glichen.},
  language  = {de}
}
@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{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}
}
@inproceedings{KasparGroebelKuperjansetal.2013,
  author    = {Kaspar, K. and Groebel, Simone and Kuperjans, Isabel and Dielmann, Klaus-Peter and Selmer, Thorsten},
  title     = {Charakterisierung der Bioz{\"o}nose von Biogasfermentern in Abh{\"a}ngigkeit verschiedener Substrate},
  series = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  booktitle = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  publisher = {Profair Consult+Project},
  address   = {Hildesheim},
  issn      = {978-3-9813776-3-7},
  pages     = {69 -- 74},
  year      = {2013},
  language  = {de}
}