@article{BassamArtmannHescheleretal.2011,
  author    = {Bassam, Rasha and Artmann, Gerhard and Hescheler, J{\"u}rgen and Graef, T. and Temiz Artmann, Ayseg{\"u}l and Porst, Dariusz and Linder, Peter and Kayser, Peter and Arinkin, Vladimir and Gossmann, Matthias and Digel, Ilya},
  title     = {Alterations in human hemoglobin structure related to red blood cell storage},
  year      = {2011},
  abstract  = {The importance of the availability of stored blood or blood cells, respectively, for urgent transfusion cannot be overestimated. Nowadays, blood storage becomes even more important since blood products are used for epidemiological studies, bio-technical research or banked for transfusion purposes. Thus blood samples must not only be processed, stored, and shipped to preserve their efficacy and safety, but also all parameters of storage must be recorded and reported for Quality Assurance. Therefore, blood banks and clinical research facilities are seeking more accurate, automated means for blood storage and blood processing.},
  subject      = {H{\"a}moglobin},
  language  = {en}
}
@article{PreissLinderWendtetal.2011,
  author    = {Preiß, C. and Linder, Peter and Wendt, K. and Krystek, M. and Digel, Ilya and Gossmann, Matthias and Temiz Artmann, Ayseg{\"u}l and Porst, Dariusz and Kayser, Peter and Bassam, Rasha and Artmann, Gerhard},
  title     = {Engineering technology for plant physiology and plant stress research},
  year      = {2011},
  abstract  = {Plant physiology and plant stress: Plant physiology will be much more important for human mankind because of yield and cultivation limits of crops determined by their resistance to stress. To assess and counteract various stress factors it is necessary to conduct plant research to gain information and results on plant physiology.},
  subject      = {Pflanzenphysiologie},
  language  = {en}
}
@inproceedings{BassamDigelArtmann2009,
  author    = {Bassam, Rasha and Digel, Ilya and Artmann, Gerhard},
  title     = {Effect of nitric oxide on protein thermal stability : [abstract]},
  year      = {2009},
  abstract  = {As a deduction from these results, we can conclude that proteins mainly in vitro, denaturate totally at a temperature between 57°C -62°C, and they also affected by NO and different ions types. In which mainly, NO cause earlier protein denaturation, which means that, NO has a destabilizing effect on proteins, and also different ions will alter the protein denaturation in which, some ions will cause earlier protein denaturation while others not.},
  subject      = {Stickstoffmonoxid},
  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{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}
}
@inproceedings{SchlemmerPorstBassametal.2017,
  author    = {Schlemmer, Katharina and Porst, Dariusz and Bassam, Rasha and Artmann, Gerhard and Digel, Ilya},
  title     = {Effects of nitric oxide (NO) and ATP on red blood cell phenotype and deformability},
  series = {2nd YRA MedTech Symposium 2017 : June 8th - 9th / 2017 / Hochschule Ruhr-West},
  booktitle = {2nd YRA MedTech Symposium 2017 : June 8th - 9th / 2017 / Hochschule Ruhr-West},
  editor    = {Erni, Daniel and Fischerauer, Alice and Himmel, J{\"o}rg and Seeger, Thomas and Thelen, Klaus},
  publisher = {Universit{\"a}t Duisburg-Essen},
  address   = {Duisburg},
  organization    = {MedTech Symposium},
  isbn      = {978-3-9814801-9-1},
  doi       = {10.17185/duepublico/43984},
  pages     = {100 -- 101},
  year      = {2017},
  language  = {en}
}
@phdthesis{BassamAbduljabbar2015,
  author    = {Bassam Abduljabbar, Rasha},
  title     = {Physikalisch-chemische Steuerung der Proteinstabilit{\"a}t in biologischen Systemen},
  year      = {2015},
  language  = {de}
}