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Muhammet Karaman

Researcher at University of North Carolina at Chapel Hill

Publications -  31
Citations -  762

Muhammet Karaman is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Enzyme & Carbonic anhydrase. The author has an hindex of 11, co-authored 28 publications receiving 473 citations. Previous affiliations of Muhammet Karaman include Atatürk University.

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Synthesis, biological evaluation and molecular docking of novel pyrazole derivatives as potent carbonic anhydrase and acetylcholinesterase inhibitors.

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.
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Imidazolinium chloride salts bearing wingtip groups: Synthesis, molecular docking and metabolic enzymes inhibition

TL;DR: A series of symmetrical imidazolinium chloride salts bearing secondary N-alkyl substituents were synthesized in good yield by the reaction of N,N′-dialkylethane-1,2-diamines and HC(OEt)3 in the presence of NH4Cl, characterized by spectroscopic methods.
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The green synthesis and molecular docking of novel N-substituted rhodanines as effective inhibitors for carbonic anhydrase and acetylcholinesterase enzymes.

TL;DR: Novel N-substituted rhodanine derivatives were synthesized by a green synthetic approach over one-pot reaction for inhibition effects of enzymes such as acetylcholinesterase and carbonic anhydrase as a promising approach for pharmacological intervention in a variety of disorders such as epilepsy, Alzheimer's disease and obesity.
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Novel 2-methylimidazolium salts: Synthesis, characterization, molecular docking, and carbonic anhydrase and acetylcholinesterase inhibitory properties.

TL;DR: These obtained novel 2-methylimidazolium salts (1a-e and 2a- e) molecules were effective inhibitors of the carbonic anhydrase I and II isozymes and acetylcholinesterase (AChE) enzymes.