Evidence map›Paper›PMID 40386629›Full record

Article3 Biotech2025

Multi-pronged approaches to the mechanism-based inactivation of aldose reductase by natural coumarins: molecular insights and experimental validation.

Emadeldin M Kamel, Sarah I Othman, Faris F Aba Alkhayl, Fahad M Alshabrmi, Ahmed A Allam, Noha A Ahmed, Al Mokhtar Lamsabhi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in 3 Biotech, 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. 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

7 authors.

Emadeldin M KamelChemistry Department, Faculty of Science, Beni-Suef University, Beni-Suef, 62514 Egypt.
Sarah I OthmanDepartment of Biology, College of Science, Princess Nourah bint Abdulrahman University, P.O. BOX 84428, 11671 Riyadh, Saudi Arabia.
Faris F Aba AlkhaylDepartment of Medical Laboratories, College of Applied Medical Sciences, Qassim University, 51452 Buraydah, Saudi Arabia.
Fahad M AlshabrmiDepartment of Medical Laboratories, College of Applied Medical Sciences, Qassim University, 51452 Buraydah, Saudi Arabia.
Ahmed A AllamDepartment of Zoology, Faculty of Science, Beni-Suef University, Beni-Suef, 65211 Egypt.
Noha A AhmedDepartment of Zoology, Faculty of Science, Beni-Suef University, Beni-Suef, 65211 Egypt.ORCID 0000-0002-5080-0933
Al Mokhtar LamsabhiDepartamento de Química, Módulo 13, Universidad Autónoma de Madrid, Campus de Excelencia UAM-CSIC Cantoblanco, 28049 Madrid, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we measured the inhibitory potential of six coumarins against aldose reductase using both computational and experimental approaches. Molecular docking, molecular dynamics simulations, and MM/PBSA binding free energy calculations identified auraptene, marmesin, and isopimpinellin as the most promising inhibitors, with binding affinities of ΔG = -34.88, -29.40, and -20.31 kcal/mol, respectively. ADMET analysis indicated favorable pharmacokinetic properties for all three compounds, including high gastrointestinal absorption and bioavailability. In vitro assays confirmed auraptene as the most potent inhibitor with the lowest IC

Indexed as

Aldose reductaseEnzyme kineticsHyperglycemic conditionsIn vitro studyMolecular dynamics simulation

Identifiers

PMID40386629
PMCPMC12081818

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.