Evidence map›Paper›PMID 41186211›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2025

In vitro α-glucosidase inhibition, molecular dynamics and docking study of phenyl carbamoyl methoxy thiosemicarbazone derivatives as potential anti-diabetic agents.

Shirin Valadbeigi, Reza Saghiri, Zahra Kianmehr, Roghieh Mirzazadeh, Shohreh Khatami

Abstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. RSC advances · 2026
    Article
  2. Article
  3. Phytochemical Profiling andFoods (Basel, Switzerland) · 2026
    Article
  4. Phytochemical Characterization ofFood science & nutrition · 2026
    Article
  5. 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

5 authors.

Shirin ValadbeigiDepartment of Biochemistry, NT.C., Islamic Azad University, Tehran, Iran.
Reza SaghiriDepartment of Biochemistry, Pasteur Institute of Iran, Tehran, Iran.
Zahra KianmehrDepartment of Biochemistry, NT.C., Islamic Azad University, Tehran, Iran.
Roghieh MirzazadehDepartment of Biochemistry, Pasteur Institute of Iran, Tehran, Iran.
Shohreh KhatamiDepartment of Biochemistry, Pasteur Institute of Iran, Tehran, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ABSTRRACTAlpha-glucosidase inhibitors have been considered as the most effective agents in preventing hyperglycaemia and alternative targets for the treatment of Diabetes mellitus (DM). This study aimed to synthesise novel phenyl carbamoyl methoxy thiosemicarbazone derivatives and evaluate their potential as α-glucosidase inhibitors through biochemical assays, cytotoxicity screening, molecular docking, and molecular dynamics simulations. The tested derivatives exhibited a range of inhibitory potential, from moderate to strong as compared to acarbose. Derivative 7e revealed the least IC50 value among the tested compounds. 7e in the kinetic assay acted as a competitive inhibitor of the α-glucosidase. The cytotoxic effect 7e was assessed against the A549 and MDA-MB-453 cell lines. MD simulation revealed that

Indexed as

alpha-GlucosidasesGlycoside Hydrolase InhibitorsHypoglycemic AgentsMolecular Docking SimulationMolecular Dynamics SimulationThiosemicarbazonesCell Line, TumorCell ProliferationDose-Response Relationship, DrugHumansMolecular StructureStructure-Activity Relationshipalpha-GlucosidasesGlycoside Hydrolase InhibitorsHypoglycemic AgentsThiosemicarbazonesdocking studymolecular dynamicthiosemicarbazoneα-glucosidase

Identifiers

PMID41186211
PMCPMC12587786

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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.