@article{BassamDigelHescheleretal.2013, author = {Bassam, Rasha and Digel, Ilya and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard}, title = {Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences}, series = {BMC Biophysics}, journal = {BMC Biophysics}, publisher = {BioMed Central}, address = {London}, isbn = {2046-1682}, url = {http://nbn-resolving.de/10.1186/2046-1682-6-1}, pages = {1 -- 14}, year = {2013}, language = {en} } @article{BassamHeschelerTemizArtmannetal.2012, author = {Bassam, Rasha and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard and Digel, Ilya}, title = {Effects of spermine NONOate and ATP on the thermal stability of hemoglobin}, series = {BMC Biophysics}, volume = {5}, journal = {BMC Biophysics}, publisher = {BioMed Central}, address = {London}, issn = {2046-1682}, doi = {10.1186/2046-1682-5-16}, pages = {Art. 16}, year = {2012}, abstract = {Background Minor changes in protein structure induced by small organic and inorganic molecules can result in significant metabolic effects. The effects can be even more profound if the molecular players are chemically active and present in the cell in considerable amounts. The aim of our study was to investigate effects of a nitric oxide donor (spermine NONOate), ATP and sodium/potassium environment on the dynamics of thermal unfolding of human hemoglobin (Hb). The effect of these molecules was examined by means of circular dichroism spectrometry (CD) in the temperature range between 25°C and 70°C. The alpha-helical content of buffered hemoglobin samples (0.1 mg/ml) was estimated via ellipticity change measurements at a heating rate of 1°C/min. Results Major results were: 1) spermine NONOate persistently decreased the hemoglobin unfolding temperature T u irrespectively of the Na + /K + environment, 2) ATP instead increased the unfolding temperature by 3°C in both sodium-based and potassium-based buffers and 3) mutual effects of ATP and NO were strongly influenced by particular buffer ionic compositions. Moreover, the presence of potassium facilitated a partial unfolding of alpha-helical structures even at room temperature. Conclusion The obtained data might shed more light on molecular mechanisms and biophysics involved in the regulation of protein activity by small solutes in the cell.}, language = {en} } @article{BayerTemizArtmannDigeletal.2020, author = {Bayer, Robin and Temiz Artmann, Ayseg{\"u}l and Digel, Ilya and Falkenstein, Julia and Artmann, Gerhard and Creutz, Till and Hescheler, J{\"u}rgen}, title = {Mechano-pharmacological testing of L-Type Ca²⁺ channel modulators via human vascular celldrum model}, series = {Cellular Physiology and Biochemistry}, volume = {54}, journal = {Cellular Physiology and Biochemistry}, publisher = {Cell Physiol Biochem Press}, address = {D{\"u}sseldorf}, issn = {1421-9778}, doi = {10.33594/000000225}, pages = {371 -- 383}, year = {2020}, abstract = {Background/Aims: This study aimed to establish a precise and well-defined working model, assessing pharmaceutical effects on vascular smooth muscle cell monolayer in-vitro. It describes various analysis techniques to determine the most suitable to measure the biomechanical impact of vasoactive agents by using CellDrum technology. Methods: The so-called CellDrum technology was applied to analyse the biomechanical properties of confluent human aorta muscle cells (haSMC) in monolayer. The cell generated tensions deviations in the range of a few N/m² are evaluated by the CellDrum technology. This study focuses on the dilative and contractive effects of L-type Ca²⁺ channel agonists and antagonists, respectively. We analyzed the effects of Bay K8644, nifedipine and verapamil. Three different measurement modes were developed and applied to determine the most appropriate analysis technique for the study purpose. These three operation modes are called, particular time mode" (PTM), "long term mode" (LTM) and "real-time mode" (RTM). Results: It was possible to quantify the biomechanical response of haSMCs to the addition of vasoactive agents using CellDrum technology. Due to the supplementation of 100nM Bay K8644, the tension increased approximately 10.6\% from initial tension maximum, whereas, the treatment with nifedipine and verapamil caused a significant decrease in cellular tension: 10nM nifedipine decreased the biomechanical stress around 6,5\% and 50nM verapamil by 2,8\%, compared to the initial tension maximum. Additionally, all tested measurement modes provide similar results while focusing on different analysis parameters. Conclusion: The CellDrum technology allows highly sensitive biomechanical stress measurements of cultured haSMC monolayers. The mechanical stress responses evoked by the application of vasoactive calcium channel modulators were quantified functionally (N/m²). All tested operation modes resulted in equal findings, whereas each mode features operation-related data analysis.}, language = {en} } @article{BogoyavlenskiyBerezinOgnevaetal.1999, author = {Bogoyavlenskiy, A. P. and Berezin, V. E. and Ogneva, A. V. and Tolmacheva, V. P. and Digel, Ilya and Khudyakova, S. S.}, title = {Immunostimulating activity of a saponin-containing extract of Saponaria officinalis}, series = {Voprosy virusologii}, volume = {44}, journal = {Voprosy virusologii}, number = {5}, issn = {0507-4088}, pages = {229 -- 232}, year = {1999}, language = {en} } @article{BogoyavlenskiyDigelBerezin1997, author = {Bogoyavlenskiy, A. P. and Digel, Ilya and Berezin, V. E.}, title = {Assessment of dot-blot ELISA sensitivity on membrane sorbent using various peroxidase substrates}, year = {1997}, abstract = {The sensitivity of the peroxidase reaction in dot-blot ELISA significantly depends on the substrate. The highest sensitivity is observed using benzidine and diamine- phenol combinations as the substrates due to the reaction of the coupled oxidation (NADI)}, subject = {Enzyme-linked immunosorbent assay}, language = {en} } @article{DachwaldMikuckiTulaczyketal.2014, author = {Dachwald, Bernd and Mikucki, Jill and Tulaczyk, Slawek and Digel, Ilya and Espe, Clemens and Feldmann, Marco and Francke, Gero and Kowalski, Julia and Xu, Changsheng}, title = {IceMole : A maneuverable probe for clean in situ analysis and sampling of subsurface ice and subglacial aquatic ecosystems}, series = {Annals of Glaciology}, volume = {55}, journal = {Annals of Glaciology}, number = {65}, publisher = {Cambridge University Press}, address = {Cambridge}, issn = {1727-5644}, doi = {10.3189/2014AoG65A004}, pages = {14 -- 22}, year = {2014}, abstract = {There is significant interest in sampling subglacial environments for geobiological studies, but they are difficult to access. Existing ice-drilling technologies make it cumbersome to maintain microbiologically clean access for sample acquisition and environmental stewardship of potentially fragile subglacial aquatic ecosystems. The IceMole is a maneuverable subsurface ice probe for clean in situ analysis and sampling of glacial ice and subglacial materials. The design is based on the novel concept of combining melting and mechanical propulsion. It can change melting direction by differential heating of the melting head and optional side-wall heaters. The first two prototypes were successfully tested between 2010 and 2012 on glaciers in Switzerland and Iceland. They demonstrated downward, horizontal and upward melting, as well as curve driving and dirt layer penetration. A more advanced probe is currently under development as part of the Enceladus Explorer (EnEx) project. It offers systems for obstacle avoidance, target detection, and navigation in ice. For the EnEx-IceMole, we will pay particular attention to clean protocols for the sampling of subglacial materials for biogeochemical analysis. We plan to use this probe for clean access into a unique subglacial aquatic environment at Blood Falls, Antarctica, with return of a subglacial brine sample.}, language = {en} } @article{DemirciTrzewikLinderetal.2004, author = {Demirci, T. and Trzewik, J. and Linder, Peter and Digel, Ilya and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l}, title = {Mechanical Stimulation of 3T3 Fibroblasts Activates Genes: ITGB5 and p53 Responses as Quantified on the mRNA Level}, series = {Biomedizinische Technik . 49 (2004), H. Erg.-Bd. 2}, journal = {Biomedizinische Technik . 49 (2004), H. Erg.-Bd. 2}, isbn = {0932-4666}, pages = {1030 -- 1031}, year = {2004}, language = {en} } @article{DemirciKurulganDemirciTrzewiketal.2009, author = {Demirci, Taylan and Kurulgan Demirci, Eylem and Trzewik, J{\"u}rgen and Linder, Peter and Digel, Ilya and Artmann, Gerhard and Sakizli, Meral and Temiz Artmann, Ayseg{\"u}l}, title = {Gene expression profile analysis of 3T3/NIH fibroblasts after one hour mechanical stress}, series = {IUBMB Life. 61 (2009), H. 3}, journal = {IUBMB Life. 61 (2009), H. 3}, publisher = {Wiley-VCH}, address = {Weinheim}, isbn = {1521-6543}, pages = {311 -- 312}, year = {2009}, language = {en} } @article{Digel2011, author = {Digel, Ilya}, title = {Primary thermosensory events in cells}, series = {Transient receptor potential channels / Md. Shahidul Islam, ed.}, journal = {Transient receptor potential channels / Md. Shahidul Islam, ed.}, publisher = {Springer}, address = {Dordrecht [u.a.]}, isbn = {978-94-007-0264-6}, pages = {451 -- 468}, year = {2011}, language = {en} } @article{Digel2008, author = {Digel, Ilya}, title = {Controlling microbial adhesion : a surface engineering approach}, series = {Bioengineering in Cell and Tissue Research / Artmann, Gerhard M. ; Chien, Shu (Eds.)}, journal = {Bioengineering in Cell and Tissue Research / Artmann, Gerhard M. ; Chien, Shu (Eds.)}, publisher = {Springer}, address = {Berlin [u.a.]}, isbn = {978-3-540-75408-4}, pages = {601 -- 625}, year = {2008}, language = {en} }