Evidence map›Paper›PMID 40192903›Full record

ArticleCell biochemistry and biophysics2025

Some Novel Oxirane-Thiirane Derivatives: Synthesis, Molecular docking and Enzymatic Inhibition for Therapeutic Potential.

Vagif Farzaliyev, Adem Ertürk, Afat Huseynova, Yeliz Demir, Hatice Kızıltaş, Afsun Sujayev, Mir Ali İsakov, Beyim Ibrahimova, İlhami Gülçin

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Article in Cell biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Exploring the Role of Phytoconstituent FromFood science & nutrition · 2025
    Article
  2. 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

9 authors.

Vagif FarzaliyevInstitute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
Adem ErtürkAtaturk University, Faculty of Science, Department of Chemistry, 25240, Erzurum, Türkiye.
Afat HuseynovaBaku State University, Department of Organic Chemistry, 1148, Baku, Azerbaijan.
Yeliz DemirAtaturk University, Faculty of Science, Department of Chemistry, 25240, Erzurum, Türkiye. yelizdemir@ardahan.edu.tr.
Hatice KızıltaşVan Yüzüncü Yıl University, Van Vocational School of Health Services, 65080, Van, Türkiye.
Afsun SujayevInstitute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
Mir Ali İsakovInstitute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
Beyim IbrahimovaInstitute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
İlhami GülçinAtaturk University, Faculty of Science, Department of Chemistry, 25240, Erzurum, Türkiye.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, a series of new oxirane and thiirane (2a-g), were assessed for their influence on various metabolic enzymes, including acetylcholinesterase (AChE) and human carbonic anhydrase isoenzymes (hCA I and hCA II). So, in the first stage, 1-chloro-3-phenothiazylpropanol-2 (2), methyl, methoxy-substituted oxirane, thiirane (2a and 2b), methyl, 1,2-aminopropanethiols (2c-2f), trifluorinated aminethiol derivative (2g), have been synthesized. The structures of synthesized compound were confirmed by IR, NMR analysis. Enzyme inhibition studies demonstrated that all these compounds exhibited potent inhibitory effects on all the target enzymes, surpassing the standard inhibitors, as evidenced by their IC

Indexed as

Carbonic Anhydrase InhibitorsCholinesterase InhibitorsMolecular Docking SimulationAcetylcholinesteraseCarbonic Anhydrase ICarbonic Anhydrase IIHumansAcetylcholinesteraseCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase InhibitorsCholinesterase InhibitorsAcetylcholinesteraseCarbonic anhydraseEnzyme inhibitionOxiraneThiirane

Identifiers

PMID40192903

What OpenQuestion holds

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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.