Evidence map›Paper›PMID 38976121›Full record

ArticleMolecular diversity2025

Investigation of cholinesterase and α-glucosidase enzyme activities, and molecular docking and dft studies for 1,2-disubstituted cyclopentane derivatives with phenyl and benzyl units.

Tekin Artunç, Yasin Çetinkaya, Parham Taslimi, Abdullah Menzek

Abstract read
In one paragraph

Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Tekin ArtunçDepartment of Chemistry, Faculty of Science, Atatürk University, 25240, Erzurum, Turkey.
Yasin ÇetinkayaDepartment of Chemistry, Faculty of Science, Atatürk University, 25240, Erzurum, Turkey. yasin.cetinkaya@atauni.edu.tr.ORCID http://orcid.org/0000-0001-6617-5055
Parham TaslimiDepartment of Biotechnology, Faculty of Science, Bartin University, 74100, Bartin, Turkey. ptaslimi@bartin.edu.tr.ORCID http://orcid.org/0000-0002-3171-0633
Abdullah MenzekDepartment of Chemistry, Faculty of Science, Atatürk University, 25240, Erzurum, Turkey. abmenzek@ardahan.edu.tr.ORCID http://orcid.org/0000-0001-6177-7532

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Six known products (4-9) were prepared from reaction of adipoyl chloride with 1,2,3-trimethoxybenzene according to the literature. From (2,3,4-trimethoxyphenyl)(2-(2,3,4-trimethoxyphenyl)cyclopent-1-en-1-yl)methanone (4) of them, four new 1,2-disubstituted cyclopentane derivatives (10-13) with phenyl and benzyl units were synthesized by reactions such as hydrazonation, catalytic hydrogenation and bromination. The obtained compounds 4-13 were examined for their in vitro inhibitory activity against acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and α-glucosidase enzymes. All compounds 4-13 showed inhibition at nanomolar level with K

Indexed as

alpha-GlucosidasesCholinesterase InhibitorsCyclopentanesGlycoside Hydrolase InhibitorsMolecular Docking SimulationAcetylcholinesteraseButyrylcholinesteraseDensity Functional TheoryMolecular StructureStructure-Activity RelationshipAcetylcholinesterasealpha-GlucosidasesButyrylcholinesteraseCholinesterase InhibitorsCyclopentanesGlycoside Hydrolase InhibitorsAChEBChEBrominationDensity functional theoryα-Glucosidase

Identifiers

PMID38976121
PMCPMC11909056

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.