@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} } @article{ArtmannLiSeipeltetal.1999, author = {Artmann, Gerhard and Li, Anlan and Seipelt, H. and M{\"u}ller, C. [u.a.]}, title = {Effects of salicylic acid derivatives on red blood cell membranes. Li, Anlan; Seipelt, H.; M{\"u}ller, C.;Shi, Yong de; Artmann, Gerhard Michael}, series = {Pharmacology and Toxicology. 85 (1999)}, journal = {Pharmacology and Toxicology. 85 (1999)}, isbn = {0902-9938}, pages = {206 -- 211}, year = {1999}, language = {en} } @inproceedings{DigelTemizArtmannNojimaetal.2003, author = {Digel, Ilya and Temiz Artmann, Ayseg{\"u}l and Nojima, H. and Artmann, Gerhard}, title = {Effects of plasma generated ions on bacteria : [poster]}, year = {2003}, abstract = {Summary and Conclusions PCIs were clearly effective in terms of their antibacterial effects with the strains tested. This efficacy increased with the time the bacteries were exposed to PCIs. The bactericidal action has proved to be irreversible. PCIs were significantly less effective in shadowed areas. PCI exposure caused multiple protein damages as observed in SDS PAGE studies. There was no single but multiple molecular mechanism causing the bacterial death.}, subject = {Clusterion}, 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} } @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{StadlerZerlinDigeletal.2008, author = {Stadler, Andreas M. and Zerlin, Kay and Digel, Ilya and B{\"u}ldt, Georg and Zaccai, Guiseppe and Artmann, Gerhard}, title = {Dynamics and interactions of hemoglobin in red blood cells}, series = {Tissue Engineering Part A. 14 (2008), H. 5}, journal = {Tissue Engineering Part A. 14 (2008), H. 5}, isbn = {1937-3341}, pages = {724 -- 724}, year = {2008}, language = {en} } @article{ZerlinDigelStadleretal.2007, author = {Zerlin, Kay and Digel, Ilya and Stadler, Andreas M. and B{\"u}ldt, Georg and Zaccai, Guiseppe and Artmann, Gerhard}, title = {Dynamics and interactions of hemoglobin in human red blood cells and concentrated hemoglobin solutions}, series = {Regenerative medicine. 2 (2007), H. 5}, journal = {Regenerative medicine. 2 (2007), H. 5}, isbn = {1746-0751}, pages = {573 -- 573}, year = {2007}, language = {en} } @article{ArtmannLi1994, author = {Artmann, Gerhard and Li, Anlan}, title = {Dihydroergocryptine maintains erythrocyte fluidity in acidotic and hyperosmolar suspensions modelling hypoxic and ischemic microcirculation. Li, Anlan; Artmann, Gerhard Michael}, series = {Clinical Hemorheology. 15 (1994), H. 2}, journal = {Clinical Hemorheology. 15 (1994), H. 2}, isbn = {0271-5198}, pages = {133 -- 146}, year = {1994}, language = {en} } @article{ArtmannMontanusTeitel1991, author = {Artmann, Gerhard and Montanus, M. and Teitel, P.}, title = {Die photometrische Kapillaraggregation- ein neues Verfahren zur Messung der Erythrozytenaggregation. Montanus, M.; Artmann, Gerhard Michael; Teitel, P.}, series = {Biomedizinische Technik = Biomedical engineering. 36 (1991)}, journal = {Biomedizinische Technik = Biomedical engineering. 36 (1991)}, isbn = {0013-5585}, pages = {213 -- 215}, year = {1991}, language = {de} }