@article{TranMottaghyArltKoerferetal.2017,
  author    = {Tran, Linda and Mottaghy, K. and Arlt-K{\"o}rfer, Sabine and Waluga, Christian and Behbahani, Mehdi},
  title     = {An experimental study of shear-dependent human platelet adhesion and underlying protein-binding mechanisms in a cylindrical Couette system},
  series = {Biomedizinische Technik},
  volume    = {62},
  journal   = {Biomedizinische Technik},
  number    = {4},
  publisher = {De Gruyter},
  address   = {Berlin},
  issn      = {0013-5585},
  doi       = {10.1515/bmt-2015-0034},
  pages     = {383 -- 392},
  year      = {2017},
  language  = {en}
}
@article{MuschallikMolinnusBongaertsetal.2017,
  author    = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten},
  title     = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme},
  series = {Journal of Biotechnology},
  volume    = {258},
  journal   = {Journal of Biotechnology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2017.07.020},
  pages     = {41 -- 50},
  year      = {2017},
  abstract  = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.},
  language  = {en}
}
@article{MoraisGomesSilvaetal.2017,
  author    = {Morais, Paulo V. and Gomes, Vanderley F., Jr. and Silva, Anielle C. A. and Dantas, Noelio O. and Sch{\"o}ning, Michael Josef and Siqueira, Jos{\´e} R., Jr.},
  title     = {Nanofilm of ZnO nanocrystals/carbon nanotubes as biocompatible layer for enzymatic biosensors in capacitive field-effect devices},
  series = {Journal of Materials Science},
  volume    = {52},
  journal   = {Journal of Materials Science},
  number    = {20},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1573-4803},
  doi       = {10.1007/s10853-017-1369-y},
  pages     = {12314 -- 12325},
  year      = {2017},
  abstract  = {The incorporation of nanomaterials that are biocompatible with different types of biological compounds has allowed the development of a new generation of biosensors applied especially in the biomedical field. In particular, the integration of film-based nanomaterials employed in field-effect devices can be interesting to develop biosensors with enhanced properties. In this paper, we studied the fabrication of sensitive nanofilms combining ZnO nanocrystals and carbon nanotubes (CNTs), prepared by means of the layer-by-layer (LbL) technique, in a capacitive electrolyte-insulator-semiconductor (EIS) structure for detecting glucose and urea. The ZnO nanocrystals were incorporated in a polymeric matrix of poly(allylamine) hydrochloride (PAH), and arranged with multi-walled CNTs in a LbL PAH-ZnO/CNTs film architecture onto EIS chips. The electrochemical characterizations were performed by capacitance-voltage and constant capacitance measurements, while the morphology of the films was characterized by atomic force microscopy. The enzymes glucose oxidase and urease were immobilized on film's surface for detection of glucose and urea, respectively. In order to obtain glucose and urea biosensors with optimized amount of sensitive films, we investigated the ideal number of bilayers for each detection system. The glucose biosensor showed better sensitivity and output signal for an LbL PAH-ZnO/CNTs nanofilm with 10 bilayers. On the other hand, the urea biosensor presented enhanced properties even for the first bilayer, exhibiting high sensitivity and output signal. The presence of the LbL PAH-ZnO/CNTs films led to biosensors with better sensitivity and enhanced response signal, demonstrating that the adequate use of nanostructured films is feasible for proof-of-concept biosensors with improved properties that may be employed for biomedical applications.},
  language  = {en}
}
@article{LambersBragard2017,
  author    = {Lambers, Andreas and Bragard, Michael},
  title     = {Kinetische Skulptur - Treffen sich ein E-Techniker und ein K{\"u}nstler ...},
  series = {Elektor : learn, design, share},
  volume    = {48},
  journal   = {Elektor : learn, design, share},
  number    = {9},
  publisher = {Elektor-Verlag},
  address   = {Aachen},
  issn      = {0932-5468},
  pages     = {78 -- 83},
  year      = {2017},
  abstract  = {Die Verbindung der Welten dressierter Elektronen und grenzenloser Kreativit{\"a}t bietet ein großes Potential; zum Beispiel bei modernen Skulpturen, deren Form sich durch Motoren ver{\"a}ndern kann. An der FH Aachen wurde ein solches Projekt verwirklicht: Eine Matrix aus Holzkugeln kann Piktogramme anzeigen, aber auch mathematische Funktionen visualisieren. In diesem Artikel beschreiben wir die clevere Ansteuerung der Motoren.},
  language  = {de}
}
@article{HonarvarfardGamellaPoghossianetal.2017,
  author    = {Honarvarfard, Elham and Gamella, Maria and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Katz, Evgeny},
  title     = {An enzyme-based reversible Controlled NOT (CNOT) logic gate operating on a semiconductor transducer},
  series = {Applied Materials Today},
  volume    = {9},
  journal   = {Applied Materials Today},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {2352-9407},
  doi       = {10.1016/j.apmt.2017.08.003},
  pages     = {266 -- 270},
  year      = {2017},
  abstract  = {An enzyme-based biocatalytic system mimicking operation of a logically reversible Controlled NOT (CNOT) gate has been interfaced with semiconductor electronic transducers. Electrolyte-insulator-semiconductor (EIS) structures have been used to transduce chemical changes produced by the enzyme system to an electronically readable capacitive output signal using field-effect features of the EIS device. Two enzymes, urease and esterase, were immobilized on the insulating interface of EIS structure producing local pH changes performing XOR logic operation controlled by various combinations of the input signals represented by urea and ethyl butyrate. Another EIS transducer was functionalized with esterase only, thus performing Identity (ID) logic operation for the ethyl butyrate input. Both semiconductor devices assembled in parallel operated as a logically reversible CNOT gate. The present system, despite its simplicity, demonstrated for the first time logically reversible function of the enzyme system transduced electronically with the semiconductor devices. The biomolecular realization of a CNOT gate interfaced with semiconductors is promising for integration into complex biomolecular networks and future biosensor/biomedical applications.},
  language  = {en}
}
@article{RoehlenPilasSchoeningetal.2017,
  author    = {R{\"o}hlen, Desiree and Pilas, Johanna and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid},
  series = {Applied Biochemistry and Biotechnology},
  volume    = {183},
  journal   = {Applied Biochemistry and Biotechnology},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1559-0291},
  doi       = {10.1007/s12010-017-2578-1},
  pages     = {566 -- 581},
  year      = {2017},
  abstract  = {Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM-1 (L-malate biosensor) and 0.4 μA mM-1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0-10.0 mM with a sensitivity of 0.09 μA mM-1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.},
  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{AlbannaLuekeSjapicetal.2017,
  author    = {Albanna, Walid and Lueke, Jan Niklas and Sjapic, Volha and Kotliar, Konstantin and Hescheler, J{\"u}rgen and Clusmann, Hans and Sjapic, Sergej and Alpdogan, Serdan and Schneider, Toni and Schubert, Gerrit Alexander and Neumaier, Felix},
  title     = {Electroretinographic Assessment of Inner Retinal Signaling in the Isolated and Superfused Murine Retina},
  series = {Current Eye Research},
  journal   = {Current Eye Research},
  number    = {Article in press},
  publisher = {Taylor \& Francis},
  address   = {London},
  issn      = {1460-2202},
  doi       = {10.1080/02713683.2017.1339807},
  pages     = {1 -- 9},
  year      = {2017},
  language  = {en}
}
@article{SeifarthGrosseGrossmannetal.2017,
  author    = {Seifarth, Volker and Grosse, Joachim O. and Grossmann, Matthias and Janke, Heinz Peter and Arndt, Patrick and Koch, Sabine and Epple, Matthias and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l},
  title     = {Mechanical induction of bi-directional orientation of primary porcine bladder smooth muscle cells in tubular fibrin-poly(vinylidene fluoride) scaffolds for ureteral and urethral repair using cyclic and focal balloon catheter stimulation},
  series = {Journal of Biomaterials Applications},
  volume    = {32},
  journal   = {Journal of Biomaterials Applications},
  number    = {3},
  publisher = {Sage},
  address   = {London},
  issn      = {1530-8022},
  doi       = {10.1177/0885328217723178},
  pages     = {321 -- 330},
  year      = {2017},
  language  = {en}
}
@article{BalzerStreitHeinze2017,
  author    = {Balzer, Hermann and Streit, Daniel and Heinze, Marcel},
  title     = {Implikationen der Digitalisierung f{\"u}r den Finanzbereich der Unternehmung und das Rollenbild des CFO},
  series = {Betriebswirtschaftliche Implikationen der digitalen Transformation. ZfbF - Schmalenbachs Zeitschrift f{\"u}r betriebswirtschaftliche Forschung, Sonderheft 72},
  journal   = {Betriebswirtschaftliche Implikationen der digitalen Transformation. ZfbF - Schmalenbachs Zeitschrift f{\"u}r betriebswirtschaftliche Forschung, Sonderheft 72},
  number    = {72},
  editor    = {Krause, Stefan},
  publisher = {Springer},
  address   = {Berlin},
  doi       = {10.1007/978-3-658-18751-4_14},
  pages     = {267 -- 283},
  year      = {2017},
  language  = {de}
}