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Author

Cüneyt Türkeş

Other affiliations: Atatürk University
Bio: Cüneyt Türkeş is an academic researcher from Erzincan University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 21, co-authored 38 publications receiving 965 citations. Previous affiliations of Cüneyt Türkeş include Atatürk University.

Papers published on a yearly basis

Papers
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Journal ArticleDOI
TL;DR: The novel synthesized compounds (MZ1-MZ11) have a higher enzyme inhibitory potential than ACR, TAC, and AZA, respectively and may have the potential to be used as alternative medicines after further research in the treatment of many diseases such as diabetes, Alzheimer's disease, heart failure, ulcer, and epilepsy.

103 citations

Journal ArticleDOI
TL;DR: ADME prediction study of the designed N-substituted phthalazine sulfonamides showed that they are not only with carbonic anhydrase and acetylcholinesterase inhibitory activities but also with appropriate pharmacokinetic, physicochemical parameters and drug-likeness properties.

99 citations

Journal ArticleDOI
TL;DR: Among these drugs, cinnarizine was found to be the most potent AR inhibitor (Ki: 2.07 ± 0.72 μM), and may be useful in the treatment and/or prevention of diabetic complications.
Abstract: Aldose reductase (AR) belongs to NADPH-dependent oxidoreductases and converts glucose to sorbitol in the polyol pathway. AR inhibition is essential to prevent diabetic complications. Here, AR was purified from sheep kidney using simple methods and determined the interactions between some calcium channel blockers and the enzyme. It was found that calcium channel blockers (cinnarizine, nilvadipine, amlodipine besylate, nifedipine, isradipine, and nitrendipine) exhibit potential inhibitor properties for sheep kidney AR with IC50 values in the range of 5.87–8.77 μM and Ki constants in the range of 2.07 ± 0.72–5.62 ± 1.53 μM. The calcium channel blockers showed different inhibition mechanisms. It was determined that all studied compounds showed competitive inhibition effect except for isradipine and nitrendipine. They showed non-competitive inhibition. Among these drugs, cinnarizine was found to be the most potent AR inhibitor (Ki: 2.07 ± 0.72 μM). They may be useful in the treatment and/or prevention of diabetic complications.

68 citations

Journal ArticleDOI
TL;DR: In this article, a 2.6-disubstituted imidazo[2,1-b][1,3,4]thiadiazole derivatives (9a-k, 10a, and 11a) and 2.5,6-trisubstitized imidazole derivatives(12a-20a) were investigated for the inhibition of human carbonic anhydrase (hCA, EC 4.2.1) I and II isoforms and also of acetylcholinesterase (AChE

65 citations

Journal ArticleDOI
TL;DR: The paraoxonase-I (PON1) enzyme was purified from human serum by using different and simple chromatographic techniques and inhibition effects of some chemotherapeutic drugs on the PON1 were investigated.
Abstract: Background Metabolic processes in living organisms are closely related to the catalytic activity of enzymes. Changes in enzyme activity cause various diseases e.g., neurological, cancer, metabolic and cardiovascular. Most of the current therapeutic drugs available in clinical utilization function as enzyme inhibitors. Objective The main goal of the current study to contribute to this growing drug design area (such as medication discovery and development) by investigating protein-drug interactions. Methods The paraoxonase-I (PON1) enzyme was purified from human serum by using different and simple chromatographic techniques. Additionally, it was investigated inhibition effects of some chemotherapeutic drugs on the PON1. Results The purification results for PON1 depicted a 3880.83 EU/mg proteins specific activity and the molecular weight was calculated as 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These drugs found to strongly inhibit PON1, with IC50 values ranging from 0.222±0.002 to 688.300±0.897 µM. Ki constants for vincristine sulfate, epirubicin hydrochloride, and doxorubicin hydrochloride were determined to be 0.235±0.032 µM, 221.400±29.270 µM, and 913.300±201.000 µM, respectively. Conclusion These drugs showed in competitive inhibition. Also, the molecular docking poses of these agents inside the catalytic sites of 1V04 and 3SRE were analysis.

63 citations


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01 Jan 2007
TL;DR: The terms "antioxidant", "oxidative stress" and "oxoidative damage" are widely used but rarely defined as discussed by the authors, and a brief review attempts to define them and to examine the ways in which oxidative stress and oxidative damage can affect cell behaviour both in vivo and in cell culture, using cancer as an example.
Abstract: The terms 'antioxidant', 'oxidative stress' and 'oxidative damage' are widely used but rarely defined. This brief review attempts to define them and to examine the ways in which oxidative stress and oxidative damage can affect cell behaviour both in vivo and in cell culture, using cancer as an example.

1,309 citations

Journal ArticleDOI
TL;DR: The results obtained from the current studies clearly show that novel bromophenol derivatives 20-24 have considerable antioxidant, antiradical, and AChE inhibition effects.

182 citations

Journal ArticleDOI
TL;DR: Results show that hCA I, II, and AChE were effectively inhibited by the novel sulfamoylcarbamates 17-21 and sulfamide derivatives 22-26, which were docked within the active sites of the corresponding enzymes revealing the reasons of the effective inhibitory activity.

131 citations

Journal ArticleDOI
TL;DR: Induced fit docking process performed on the compounds inhibiting hCA I, hCA II, AChE, and BChE receptors will be useful for design of more potent and selective inhibitors against the enzymes.

117 citations

Journal ArticleDOI
TL;DR: Results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.
Abstract: Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate () respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a Ki of 29.2 nM against hCA I, and 24.2 nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, Ki parameter of taxifolin was determined to be 16.7 nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.

114 citations