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Institution

Iğdır University

EducationIğdır, Turkey
About: Iğdır University is a education organization based out in Iğdır, Turkey. It is known for research contribution in the topics: Chemistry & Thin film. The organization has 229 authors who have published 539 publications receiving 4980 citations.


Papers
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Journal ArticleDOI
TL;DR: In the present study, the inhibition effects of rosmarinic acid on tumour-associated carbonic anhydrase IX and XII isoenzymes, AChE, BchE, LPO and GST enzymes were evaluated.
Abstract: Rosmarinic acid (RA) is a natural polyphenol contained in many aromatic plants with promising biological activities. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates. Acetylcholinesterase (AChE, E.C. 3.1.1.7) is intimately associated with the normal neurotransmission by catalysing the hydrolysis of acetylcholine to acetate and choline and acts in combination with butyrylcholinesterase (BChE) to remove acetylcholine from the synaptic cleft. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms, whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and in eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effects of rosmarinic acid on tumour-associated carbonic anhydrase IX and XII isoenzymes, AChE, BChE, LPO and GST enzymes were evaluated. Rosmarinic acid inhibited these enzymes with Kis in the range between micromolar to picomolar. The best inhibitory effect of rosmarinic acid was observed against both AChE and BChE.

168 citations

Journal ArticleDOI
TL;DR: These molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents and demonstrate effective inhibitor compounds with Ki values in the range of 8.34-40.78 μM against GST, and 120.53-892.36 nM against α- Glycosid enzyme.

158 citations

Journal ArticleDOI
TL;DR: In this paper, physicochemical, microbiological and bioactive properties, major sugar and aroma profiles of total 20 artisanal and retail honey samples harvested in Turkey were determined, and it was confirmed that the quality of the analyzed honeys was good, which facilitates its national and international commercialization.

145 citations

Journal ArticleDOI
TL;DR: The inhibition effect of CAPE on human carbonic anhydrase (hCA) isoforms I, II, IX, and XII, AChE, BchE, LPO, and GST was evaluated and CAPE inhibited these enzymes with Kis in the range between micromolar to picomolar.
Abstract: Caffeic acid phenethyl ester (CAPE) is an active component of honeybee propolis extracts. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates including humans as many diverse isoforms. Acetylcholinesterase (AChE) is responsible for acetyl choline (ACh) hydrolysis and plays a fundamental role in nerve impulse transmission by terminating the action of the ACh neurotransmitter at cholinergic synapses and neuromuscular junctions. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effect of CAPE on human carbonic anhydrase (hCA) isoforms I, II, IX, and XII, AChE, BChE, LPO, and GST was evaluated. CAPE inhibited these enzymes with Kis in the range between micromolar to picomolar. The best inhibitory effect was observed against AChE and BChE.

144 citations

Journal ArticleDOI
TL;DR: A series of substituted pyrazole compounds were synthesized and their structure was characterized by IR, NMR, and Mass analysis and emerged as effective inhibitors of the cytosolic carbonic anhydrase I and II isoforms and acetylcholinesterase enzymes with Ki values in the range of 1.23-22.65 ± 5.36 µM.

143 citations


Authors

Showing all 273 results

NameH-indexPapersCitations
Şükrü Beydemir451645944
Mehmet Hakkı Alma261002179
Omer Said Toker261212171
Ibrahim Demirtas241541958
Fikret Türkan21621260
Ramazan Topkaya21571258
Fatih Koç201071250
Ecevit Eyduran20971085
Ahmet Uludag1578791
Bahadir Ceylan1439489
Adem Kocyigit1451548
Muhammed S. Boybay14421113
Turan Aslan1338534
Veli Uygur1350611
Yasemin Akkoyunlu1238460
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202322
202240
2021171
2020105
201973
201848