@article{MoeserLorenzSajfutdinowetal.2018,
  author    = {M{\"o}ser, Christin and Lorenz, Jessica S. and Sajfutdinow, Martin and Smith, David M.},
  title     = {Pinpointed Stimulation of EphA2 Receptors via DNA-Templated Oligovalence},
  series = {International journal of molecular sciences},
  volume    = {19},
  journal   = {International journal of molecular sciences},
  number    = {11},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1422-0067},
  doi       = {10.3390/ijms19113482},
  pages     = {19},
  year      = {2018},
  abstract  = {DNA nanostructures enable the attachment of functional molecules to nearly any unique location on their underlying structure. Due to their single-base-pair structural resolution, several ligands can be spatially arranged and closely controlled according to the geometry of their desired target, resulting in optimized binding and/or signaling interactions. Here, the efficacy of SWL, an ephrin-mimicking peptide that binds specifically to EphrinA2 (EphA2) receptors, increased by presenting up to three of these peptides on small DNA nanostructures in an oligovalent manner. Ephrin signaling pathways play crucial roles in tumor development and progression. Moreover, Eph receptors are potential targets in cancer diagnosis and treatment. Here, the quantitative impact of SWL valency on binding, phosphorylation (key player for activation) and phenotype regulation in EphA2-expressing prostate cancer cells was demonstrated. EphA2 phosphorylation was significantly increased by DNA trimers carrying three SWL peptides compared to monovalent SWL. In comparison to one of EphA2's natural ligands ephrin-A1, which is known to bind promiscuously to multiple receptors, pinpointed targeting of EphA2 by oligovalent DNA-SWL constructs showed enhanced cell retraction. Overall, we show that DNA scaffolds can increase the potency of weak signaling peptides through oligovalent presentation and serve as potential tools for examination of complex signaling pathways.},
  language  = {en}
}
@misc{MoeserLorenzSajfutdinowetal.2018,
  author    = {M{\"o}ser, Christin and Lorenz, Jessica S. and Sajfutdinow, Martin and Smith, David M.},
  title     = {Pinpointed stimulation of EphA2 receptors via DNA-templated oligovalence},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1041},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-46882},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-468828},
  pages     = {21},
  year      = {2018},
  abstract  = {DNA nanostructures enable the attachment of functional molecules to nearly any unique location on their underlying structure. Due to their single-base-pair structural resolution, several ligands can be spatially arranged and closely controlled according to the geometry of their desired target, resulting in optimized binding and/or signaling interactions. Here, the efficacy of SWL, an ephrin-mimicking peptide that binds specifically to EphrinA2 (EphA2) receptors, increased by presenting up to three of these peptides on small DNA nanostructures in an oligovalent manner. Ephrin signaling pathways play crucial roles in tumor development and progression. Moreover, Eph receptors are potential targets in cancer diagnosis and treatment. Here, the quantitative impact of SWL valency on binding, phosphorylation (key player for activation) and phenotype regulation in EphA2-expressing prostate cancer cells was demonstrated. EphA2 phosphorylation was significantly increased by DNA trimers carrying three SWL peptides compared to monovalent SWL. In comparison to one of EphA2's natural ligands ephrin-A1, which is known to bind promiscuously to multiple receptors, pinpointed targeting of EphA2 by oligovalent DNA-SWL constructs showed enhanced cell retraction. Overall, we show that DNA scaffolds can increase the potency of weak signaling peptides through oligovalent presentation and serve as potential tools for examination of complex signaling pathways.},
  language  = {en}
}
@article{OenerQuerebilloDavidetal.2018,
  author    = {{\"O}ner, Ibrahim Halil and Querebillo, Christine Joy and David, Christin and Gernert, Ulrich and Walter, Carsten and Driess, Matthias and Leimk{\"u}hler, Silke and Ly, Khoa Hoang and Weidinger, Inez M.},
  title     = {High electromagnetic field enhancement of TiO2 nanotube electrodes},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {57},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {24},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201802597},
  pages     = {7225 -- 7229},
  year      = {2018},
  abstract  = {We present the fabrication of TiO2 nanotube electrodes with high biocompatibility and extraordinary spectroscopic properties. Intense surface-enhanced resonance Raman signals of the heme unit of the redox enzyme Cytochromeb(5) were observed upon covalent immobilization of the protein matrix on the TiO2 surface, revealing overall preserved structural integrity and redox behavior. The enhancement factor could be rationally controlled by varying the electrode annealing temperature, reaching a record maximum value of over 70 at 475 degrees C. For the first time, such high values are reported for non-directly surface-interacting probes, for which the involvement of charge-transfer processes in signal amplification can be excluded. The origin of the surface enhancement is exclusively attributed to enhanced localized electric fields resulting from the specific optical properties of the nanotubular geometry of the electrode.},
  language  = {en}
}
@article{KielarXinXuetal.2019,
  author    = {Kielar, Charlotte and Xin, Yang and Xu, Xiaodan and Zhu, Siqi and Gorin, Nelli and Grundmeier, Guido and M{\"o}ser, Christin and Smith, David M. and Keller, Adrian},
  title     = {Effect of staple age on DNA origami nanostructure assembly and stability},
  series = {Molecules},
  volume    = {24},
  journal   = {Molecules},
  number    = {14},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1420-3049},
  doi       = {10.3390/molecules24142577},
  pages     = {12},
  year      = {2019},
  abstract  = {DNA origami nanostructures are widely employed in various areas of fundamental and applied research. Due to the tremendous success of the DNA origami technique in the academic field, considerable efforts currently aim at the translation of this technology from a laboratory setting to real-world applications, such as nanoelectronics, drug delivery, and biosensing. While many of these real-world applications rely on an intact DNA origami shape, they often also subject the DNA origami nanostructures to rather harsh and potentially damaging environmental and processing conditions. Furthermore, in the context of DNA origami mass production, the long-term storage of DNA origami nanostructures or their pre-assembled components also becomes an issue of high relevance, especially regarding the possible negative effects on DNA origami structural integrity. Thus, we investigated the effect of staple age on the self-assembly and stability of DNA origami nanostructures using atomic force microscopy. Different harsh processing conditions were simulated by applying different sample preparation protocols. Our results show that staple solutions may be stored at -20 degrees C for several years without impeding DNA origami self-assembly. Depending on DNA origami shape and superstructure, however, staple age may have negative effects on DNA origami stability under harsh treatment conditions. Mass spectrometry analysis of the aged staple mixtures revealed no signs of staple fragmentation. We, therefore, attribute the increased DNA origami sensitivity toward environmental conditions to an accumulation of damaged nucleobases, which undergo weaker base-pairing interactions and thus lead to reduced duplex stability.},
  language  = {en}
}
@article{RenzOttenFaurobertetal.2015,
  author    = {Renz, Marc and Otten, Cecile and Faurobert, Eva and Rudolph, Franziska and Zhu, Yuan and Boulday, Gwenola and Duchene, Johan and Mickoleit, Michaela and Dietrich, Ann-Christin and Ramspacher, Caroline and Steed, Emily and Manet-Dupe, Sandra and Benz, Alexander and Hassel, David and Vermot, Julien and Huisken, Jan and Tournier-Lasserve, Elisabeth and Felbor, Ute and Sure, Ulrich and Albiges-Rizo, Corinne and Abdelilah-Seyfried, Salim},
  title     = {Regulation of beta 1 Integrin-Klf2-Mediated angiogenesis by CCM proteins},
  series = {Developmental cell},
  volume    = {32},
  journal   = {Developmental cell},
  number    = {2},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1534-5807},
  doi       = {10.1016/j.devcel.2014.12.016},
  pages     = {181 -- 190},
  year      = {2015},
  abstract  = {Mechanotransduction pathways are activated in response to biophysical stimuli during the development or homeostasis of organs and tissues. In zebrafish, the blood-flow-sensitive transcription factor Klf2a promotes VEGF-dependent angiogenesis. However, the means by which the Klf2a mechanotransduction pathway is regulated to prevent continuous angiogenesis remain unknown. Here we report that the upregulation of klf2 mRNA causes enhanced egfl7 expression and angiogenesis signaling, which underlies cardiovascular defects associated with the loss of cerebral cavernous malformation (CCM) proteins in the zebrafish embryo. Using CCM-protein-depleted human umbilical vein endothelial cells, we show that the misexpression of KLF2 mRNA requires the extracellular matrix-binding receptor beta 1 integrin and occurs in the absence of blood flow. Downregulation of beta 1 integrin rescues ccm mutant cardiovascular malformations in zebrafish. Our work reveals a beta 1 integrin-Klf2-Egfl7-signaling pathway that is tightly regulated by CCM proteins. This regulation prevents angiogenic overgrowth and ensures the quiescence of endothelial cells.},
  language  = {en}
}
@misc{HinzLoefflerDeekenetal.2021,
  author    = {Hinz, Carsten and L{\"o}ffler, Robert and Deeken, Johannes and Hansen, Barbara and Huhn, Nicola and Klitsch, Constantin and Kost, Andr{\´e} and Penning, Isabelle and Richter, Christin and Sch{\"a}fer, David and Schulz, Oliver and Simon, Veronika and Tuncel, Teresa},
  title     = {\#Politik Wirtschaft - Nordrhein-Westfalen. Band 7/8},
  publisher = {Buchner},
  address   = {Bamberg},
  isbn      = {978-3-661-70077-9},
  pages     = {400},
  year      = {2021},
  abstract  = {Seit dem Schuljahr 2020/21 gilt in Nordrhein-Westfalen ein neuer Kernlehrplan f{\"u}r die Realschule, Gesamtschule und Sekundarschule. Daf{\"u}r haben wir gemeinsam mit Fachkr{\"a}ften aus dem Bundesland die \#-Schulbuchreihen entwickelt. Mit \#Politik Wirtschaft - Nordrhein-Westfalen bieten wir Ihnen innovative und aktuelle Produkte f{\"u}r einen modernen Politik- und Wirtschaftsunterricht. Neben dem neuen Lehrplan sind die Vorgaben des Medienkompetenzrahmens und die besonderen Herausforderungen heterogener Lerngruppen ber{\"u}cksichtigt. Wir bieten Ihnen einen problemorientierten und sch{\"u}lernahen Unterricht. Die Rubrik "Gemeinsam aktiv" erm{\"o}glicht ein selbstgesteuertes Lernen. Die Sch{\"u}lerinnen und Sch{\"u}ler erarbeiten sich projektartig gr{\"o}ßere Einheiten eines Kapitels. Sie k{\"o}nnen Ihren Unterricht einfach und schnell besonders vielf{\"a}ltig und spannend gestalten. Durch Fallbeispiele werden die Sch{\"u}lerinnen und Sch{\"u}ler direkt angesprochen. Eine kreative Vielfalt aus Bild-, Grafik- und Textmaterial, aktivierende Aufgaben, Methoden-und Grundwissenseiten und ein Kompetenzcheck zum Abschluss der Großkapitel vervollst{\"a}ndigen das Angebot. Zu jeder Unterrichtseinheit wird passgenau zum Schulbuch unterschiedliches Differenzierungsmaterial (Texte in einfacher Sprache, Vorstrukturierung von Aufgaben u.v.m.) erstellt. Dieses steht Ihnen in unserem digitalen Lehrermaterial click \& teach zur Verf{\"u}gung und kann von Ihnen nach individuellen Bed{\"u}rfnissen f{\"u}r einzelne digitale Schulb{\"u}cher click \& study freigeschaltet werden.},
  language  = {de}
}
@book{DeekenHinzKlitschetal.2022,
  author    = {Deeken, Johannes and Hinz, Carsten and Klitsch, Constantin and L{\"o}ffler, Robert and Penning, Isabelle and Richter, Christin and Sch{\"a}fer, David},
  title     = {\#Wirtschaft - Nordrhein-Westfalen},
  number    = {7/8},
  editor    = {Kirchner, Vera},
  publisher = {Buchner},
  address   = {Bamberg},
  isbn      = {978-3-661-82252-5},
  pages     = {192},
  year      = {2022},
  language  = {de}
}
@book{MientusKlempinNowaketal.2023,
  author    = {Mientus, Lukas and Klempin, Christiane and Nowak, Anna and Wyss, Corinne and Aufschnaiter, Claudia von and Faix, Ann-Christin and te Poel, Kathrin and Wahbe, Nadia and Pieper, Martin and H{\"o}ller, Katharina and Kallenbach, Lea and F{\"o}rster, Magdalena and Redecker, Anke and Dick, Mirjam and Holle, J{\"o}rg and Schneider, Edina and Rehfeldt, Daniel and Brauns, Sarah and Abels, Simone and Ferencik-Lehmkuhl, Daria and Fr{\"a}nkel, Silvia and Frohn, Julia and Liebsch, Ann-Catherine and Pech, Detlef and Schreier, Pascal and Jessen, Moiken and Großmann, Uta and Skintey, Lesya and Voerkel, Paul and Vaz Ferreira, Mergenfel A. and Zimmermann, Jan-Simon and Buddeberg, Magdalena and Henke, Vanessa and Hornberg, Sabine and V{\"o}lschow, Yvette and Warrelmann, Julia-Nadine and Malek, Jennifer and Tinnefeld, Anja and Schmidt, Peggy and Bauer, Tobias and J{\"a}nisch, Christopher and Spitzer, Lisa and Franken, Nadine and Degeling, Maria and Preisfeld, Angelika and Meier, Jana and K{\"u}th, Simon and Scholl, Daniel and Vogelsang, Christoph and Watson, Christina and Weißbach, Anna and Kulgemeyer, Christoph and Oetken, Mandy and Gorski, Sebastian and Kubsch, Marcus and Sorge, Stefan and Wulff, Peter and Fellenz, Carolin D. and Schnell, Susanne and Larisch, Cathleen and Kaiser, Franz and Knott, Christina and Reimer, Stefanie and Stegm{\"u}ller, Nathalie and Boukray{\^a}a Trabelsi, Kathrin and Schißlbauer, Franziska and Lemberger, Lukas and Barth, Ulrike and Wiehl, Angelika and Rogge, Tim and B{\"o}hnke, Anja and Dietz, Dennis and Großmann, Leroy and Wienmeister, Annett and Zoppke, Till and Jiang, Lisa and Gr{\"u}nbauer, Stephanie and Ostersehlt, D{\"o}rte and Peukert, Sophia and Sch{\"a}fer, Christoph and L{\"o}big, Anna and Br{\"o}ll, Leena and Brandt, Birgit and Breuer, Meike and Dausend, Henriette and Krelle, Michael and Andersen, Gesine and Falke, Sascha and Kindermann-G{\"u}zel, Kristin and K{\"o}rner, Katrina and Lottermoser, Lisa-Marie and P{\"u}gner, Kati and Sonnenburg, Nadine and Akarsu, Selim and Rechl, Friederike and Gadinger, Laureen and Heinze, Lena and Wittmann, Eveline and Franke, Manuela and Lachmund, Anne-Marie and B{\"o}ttger, Julia and Hannover, Bettina and Behrendt, Renata and Conty, Valentina and Grundmann, Stephanie and Ghassemi, Novid and Opitz, Ben and Br{\"a}mer, Martin and Gasparjan, David and Sambanis, Michaela and K{\"o}ster, Hilde and L{\"u}cke, Martin and Nordmeier, Volkhard and Schaal, Sonja and Haberbosch, Maximilian and Meissner, Maren and Schaal, Steffen and Br{\"u}chner, Melanie and Riehle, Tamara and Leopold, Bengta Marie and Gerlach, Susanne and Rau-Patschke, Sarah and Skorsetz, Nina and Weber, Nadine and Damk{\"o}hler, Jens and Elsholz, Markus and Trefzger, Thomas and Lewek, Tobias and Borowski, Andreas},
  title     = {Reflexion in der Lehrkr{\"a}ftebildung},
  series = {Potsdamer Beitr{\"a}ge f{\"u}r Lehrkr{\"a}ftebildung und Bildungsforschung},
  journal   = {Potsdamer Beitr{\"a}ge f{\"u}r Lehrkr{\"a}ftebildung und Bildungsforschung},
  number    = {4},
  editor    = {Mientus, Lukas and Klempin, Christiane and Nowak, Anna},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  isbn      = {978-3-86956-566-8},
  issn      = {2626-3556},
  doi       = {10.25932/publishup-59171},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-591717},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {452},
  year      = {2023},
  abstract  = {Reflexion ist eine Schl{\"u}sselkategorie f{\"u}r die professionelle Entwicklung von Lehrkr{\"a}ften, welche als Ausbildungsziel in den Bildungsstandards f{\"u}r die Lehrkr{\"a}ftebildung verankert ist. Eine Verstetigung universit{\"a}r gepr{\"a}gter Forschung und Modellierung in der praxisnahen Anwendung im schulischen Kontext bietet Potentiale nachhaltiger Professionalisierung. Die St{\"a}rkung reflexionsbezogener Kompetenzen durch Empirie und Anwendung scheint eine phasen{\"u}bergreifende Herausforderung der Lehrkr{\"a}ftebildung zu sein, die es zu bew{\"a}ltigen gilt. Ziele des Tagungsbandes Reflexion in der Lehrkr{\"a}ftebildung sind eine theoretische Sch{\"a}rfung des Konzeptes „Reflexive Professionalisierung" und der Austausch {\"u}ber Fragen der Einbettung wirksamer reflexionsbezogener Lerngelegenheiten in die Lehrkr{\"a}ftebildung. Forschende und Lehrende der‚ drei Phasen (Studium, Referendariat sowie Fort- und Weiterbildung) der Lehrkr{\"a}ftebildung stellen Lehrkonzepte und Forschungsprojekte zum Thema Reflexion in der Lehrkr{\"a}ftebildung vor und diskutieren diese. Gemeinsam mit Teilnehmenden aller Phasen und von verschiedenen Standorten der Lehrkr{\"a}ftebildung werden zuk{\"u}nftige Herausforderungen identifiziert und L{\"o}sungsans{\"a}tze herausgearbeitet.},
  language  = {de}
}
@book{KirchnerDeekenHinzetal.2022,
  author    = {Kirchner, Vera and Deeken, Johannes and Hinz, Carsten and Klitsch, Constantin and L{\"o}ffler, Robert and Penning, Isabelle and Richter, Christin and Sch{\"a}fer, David},
  title     = {Differenzierungsheft},
  series = {\#Wirtschaft Band 7/8 - Nordrhein-Westfalen},
  journal   = {\#Wirtschaft Band 7/8 - Nordrhein-Westfalen},
  publisher = {Buchner},
  address   = {Bamberg},
  isbn      = {978-3-66182-249-5},
  pages     = {56},
  year      = {2022},
  language  = {de}
}
@misc{BeneckeDeekenHammeretal.2020,
  author    = {Benecke, Karin and Deeken, Johannes and Hammer, Carolin and Hinz, Carsten and L{\"o}ffler, Robert and Penning, Isabelle and Richter, Christin and Sch{\"a}fer, David and Scherer, Hubertus},
  title     = {\#Wirtschaft - Niedersachsen},
  editor    = {Kirchner, Vera},
  publisher = {Buchner},
  address   = {Bamberg},
  isbn      = {978-3-661-82241-9},
  pages     = {320},
  year      = {2020},
  language  = {de}
}
@article{KruseAltattanLauxetal.2022,
  author    = {Kruse, Marlen and Altattan, Basma and Laux, Eva-Maria and Grasse, Nico and Heinig, Lars and M{\"o}ser, Christin and Smith, David M. and H{\"o}lzel, Ralph},
  title     = {Characterization of binding interactions of SARS-CoV-2 spike protein and DNA-peptide nanostructures},
  series = {Scientific reports},
  volume    = {12},
  journal   = {Scientific reports},
  number    = {1},
  publisher = {Macmillan Publishers Limited, part of Springer Nature},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/s41598-022-16914-9},
  pages     = {12},
  year      = {2022},
  abstract  = {Binding interactions of the spike proteins of the severe acute respiratory syndrome corona virus 2 (SARS-CoV-2) to a peptide fragment derived from the human angiotensin converting enzyme 2 (hACE2) receptor are investigated. The peptide is employed as capture moiety in enzyme linked immunosorbent assays (ELISA) and quantitative binding interaction measurements that are based on fluorescence proximity sensing (switchSENSE). In both techniques, the peptide is presented on an oligovalent DNA nanostructure, in order to assess the impact of mono- versus trivalent binding modes. As the analyte, the spike protein and several of its subunits are tested as well as inactivated SARS-CoV-2 and pseudo viruses. While binding of the peptide to the full-length spike protein can be observed, the subunits RBD and S1 do not exhibit binding in the employed concentrations. Variations of the amino acid sequence of the recombinant full-length spike proteins furthermore influence binding behavior. The peptide was coupled to DNA nanostructures that form a geometric complement to the trimeric structure of the spike protein binding sites. An increase in binding strength for trimeric peptide presentation compared to single peptide presentation could be generally observed in ELISA and was quantified in switchSENSE measurements. Binding to inactivated wild type viruses could be shown as well as qualitatively different binding behavior of the Alpha and Beta variants compared to the wild type virus strain in pseudo virus models.},
  language  = {en}
}