Browsing by Author "Isgor,Y.G."

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Citation - Scopus: 6
The Evaluation of Inhibitory Effects of Selected Plant Extracts on Antioxidant Enzymes
(Parlar Scientific Publications, 2015) Moghaddam,N.S.; Isgor,B.S.; Isgor,Y.G.; Geven,F.; Yildirim,O.; 01. Atılım University
Plants and most of the plant derived compounds have been known because of their potential pharmaceutical effects for a long time. They are playing an important role on the treatment of several diseases from diabetes to various types of cancers. Today most of the clinically effective pharmaceuticals are developed from plant derived ancestors in the history of medicine. In this study different parts of the plants, namely Centaurea virgata (Lam.), Cichorium intybus (L.), Euporbia macroclada (Boiss.), Melilotus officinalis (L.) Pall, and Zygophyllum fabago (L.) were evaluated for their potential medicinal value in terms of biological targets which are participating in antioxidant defense such as catalase (CAT), glutathione-S-transferase (GST), superoxide dismutase (SOD) and glutathione peroxidase (GPx). The results indicate that the highest total phenolic contents of leaf and flower extracts were for E. macroclada. The highest flavonoid contents are detected for the leaves of E. macroclada and Z. fabago. The evaluation of extracts against biological targets reveals that the fruit extract of Z. fabago and the flowers of C. intybus show the inhibition against GST. For CAT, the highest inhibition is observed with E. macroclada leaf extract. Among the extracts analyzed, the only but slight SOD inhibition is determined with flower part of E. macroclada. © by PSP Volume 24 - No 1. 2015.
Citation - Scopus: 4
Kinases and Glutathione Transferases: Selective and Sensitive Targeting
(Higher Education Press Limited Company, 2011) Isgor,Y.G.; Isgor,B.S.; 01. Atılım University
Kinases, representing almost 500 proteins in the human genome, are responsible for catalyzing the phosphorylation reaction of amino acid residues at their targets. As the largest family of kinases, the protein tyrosine kinases (PTKs) have roles in controlling the essential cellular activities, and their deregulation is generally related to pathologic conditions. The recent efforts on identifying their signal transducer or mediator role in cellular signaling revealed the interaction of PTKs with numerous enzymes of different classes, such as Ser/Thr kinases (STKs), glutathione transferases (GSTs), and receptor tyrosine kinases (RTKs). In either regulation or enhancing the signaling, PTKs are determined in close interaction with these enzymes, under specific cellular conditions, such as oxidative stress and inflammation. In this concept, intensive research on thiol metabolizing enzymes recently showed their involvement in the physiologic functions in cellular signaling besides their well known traditional role in antioxidant defense. The shared signaling components between PTK and GST family enzymes will be discussed in depth in this research review to evaluate the results of recent studies important in drug targeting for therapeutic intervention, such as cell viability, migration, differentiation and proliferation. © Higher Education Press and Springer-Verlag Berlin Heidelberg 2011.