@article{MansurovDigelBiisenbaevetal.2012,
  author    = {Mansurov, Z. and Digel, Ilya and Biisenbaev, M. and Savistkaya, I. and Kistaubaeva, A. and Akimbekov, N. and Zhubanova, A.},
  title     = {Bio-composite material on the basis of carbonized rice husk in biomedicine and environmental applications},
  series = {Eurasian Chemico-Technological Journal},
  volume    = {14},
  journal   = {Eurasian Chemico-Technological Journal},
  number    = {2},
  publisher = {Institute of Combustion Problems},
  address   = {Almaty},
  issn      = {2522-4867},
  doi       = {10.18321/ectj105},
  pages     = {115 -- 131},
  year      = {2012},
  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{KurulganDemirciDemirciLinderetal.2012,
  author    = {Kurulgan Demirci, Eylem and Demirci, Taylan and Linder, Peter and Trzewik, J{\"u}rgen and Gierkowski, Jessica Ricarda and Gossmann, Matthias and Kayser, Peter and Porst, Dariusz and Digel, Ilya and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l},
  title     = {rhAPC reduces the endothelial cell permeability via a decrease of contractile tensions induced by endothelial cells},
  series = {Journal of Bioscience and Bioengineering},
  volume    = {113},
  journal   = {Journal of Bioscience and Bioengineering},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1347-4421},
  doi       = {10.1016/j.jbiosc.2012.03.019},
  pages     = {212 -- 219},
  year      = {2012},
  abstract  = {All cells generate contractile tension. This strain is crucial for mechanically controlling the cell shape, function and survival. In this study, the CellDrum technology quantifying cell's (the cellular) mechanical tension on a pico-scale was used to investigate the effect of lipopolysaccharide (LPS) on human aortic endothelial cell (HAoEC) tension. The LPS effect during gram-negative sepsis on endothelial cells is cell contraction causing endothelium permeability increase. The aim was to finding out whether recombinant activated protein C (rhAPC) would reverse the endothelial cell response in an in-vitro sepsis model. In this study, the established in-vitro sepsis model was confirmed by interleukin 6 (IL-6) levels at the proteomic and genomic levels by ELISA, real time-PCR and reactive oxygen species (ROS) activation by florescence staining. The thrombin cellular contraction effect on endothelial cells was used as a positive control when the CellDrum technology was applied. Additionally, the Ras homolog gene family, member A (RhoA) mRNA expression level was checked by real time-PCR to support contractile tension results. According to contractile tension results, the mechanical predominance of actin stress fibers was a reason of the increased endothelial contractile tension leading to enhanced endothelium contractility and thus permeability enhancement. The originality of this data supports firstly the basic measurement principles of the CellDrum technology and secondly that rhAPC has a beneficial effect on sepsis influenced cellular tension. The technology presented here is promising for future high-throughput cellular tension analysis that will help identify pathological contractile tension responses of cells and prove further cell in-vitro models.},
  language  = {en}
}
@article{StadlerGarveyBocahutetal.2012,
  author    = {Stadler, Andreas M. and Garvey, G. J. and Bocahut, A. and Sacquin-Mora, S. and Digel, Ilya and Schneider, G. J. and Natali, F. and Artmann, Gerhard and Zaccai, G.},
  title     = {Thermal fluctuations of haemoglobin from different species : adaptation to temperature via conformational dynamics},
  series = {Journal of the Royal Society Interface},
  volume    = {9},
  journal   = {Journal of the Royal Society Interface},
  number    = {76},
  publisher = {The Royal Society},
  address   = {London},
  issn      = {1742-5689},
  doi       = {10.1098/rsif.2012.0364},
  pages     = {2845 -- 2855},
  year      = {2012},
  abstract  = {Thermodynamic stability, configurational motions and internal forces of haemoglobin (Hb) of three endotherms (platypus, Ornithorhynchus anatinus; domestic chicken, Gallus gallus domesticus and human, Homo sapiens) and an ectotherm (salt water crocodile, Crocodylus porosus) were investigated using circular dichroism, incoherent elastic neutron scattering and coarse-grained Brownian dynamics simulations. The experimental results from Hb solutions revealed a direct correlation between protein resilience, melting temperature and average body temperature of the different species on the 0.1 ns time scale. Molecular forces appeared to be adapted to permit conformational fluctuations with a root mean square displacement close to 1.2 {\AA} at the corresponding average body temperature of the endotherms. Strong forces within crocodile Hb maintain the amplitudes of motion within a narrow limit over the entire temperature range in which the animal lives. In fully hydrated powder samples of human and chicken, Hb mean square displacements and effective force constants on the 1 ns time scale showed no differences over the whole temperature range from 10 to 300 K, in contrast to the solution case. A complementary result of the study, therefore, is that one hydration layer is not sufficient to activate all conformational fluctuations of Hb in the pico- to nanosecond time scale which might be relevant for biological function. Coarse-grained Brownian dynamics simulations permitted to explore residue-specific effects. They indicated that temperature sensing of human and chicken Hb occurs mainly at residues lining internal cavities in the β-subunits.},
  language  = {en}
}