Evidence map›Paper›PMID 40511643›Full record

ArticleCurrent pharmaceutical design2026

An

Khalid Alshaghdali, Munazzah Tasleem, Talal Alharazi, Tolgahan Acar, Gamal Mohamed Elawad Ahmed, Emad Abboh, Kamal Yassin, Amre Nasr, Mohd Saeed, Dharmendra Kumar Yadav and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Current pharmaceutical design, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Khalid AlshaghdaliDepartment of Medical Laboratory Sciences, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.
Munazzah TasleemCenter for Global Health and Research, Saveetha Medical College and Hospital, Chennai, 602105, India.
Talal AlharaziDepartment of Medical Laboratory Sciences, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.
Tolgahan AcarDepartment of Physical Therapy, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.
Gamal Mohamed Elawad AhmedDepartment of Medical Laboratory Sciences, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.
Emad AbbohCollege of Medicine, University of Hail, Hail, Saudi Arabia.
Kamal YassinDepartment of Biochemistry, Umea University, Umea, Sweden.
Amre NasrDepartment of Basic Medical Sciences, College of Medicine, King Saud bin Abdulaziz University for Health Sciences, King Abdulaziz Medical City, Riyadh, Saudi Arabia.
Mohd SaeedDepartment of Biology, College of Sciences, University of Hail, Hail, Saudi Arabia.
Dharmendra Kumar YadavCollege of Pharmacy, Gachon University of Medicine and Science, Hambakmoeiro, Yeonsugu, Incheon City, 21924, South Korea.
Amir SaeedDepartment of Medical Laboratory Sciences, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.

Funding

Scientific Research Deanship at University of Ha'il - Saudi Arabia RG-21 160
6 · The paper itself

Abstract

introductionAldose reductase-2 (ALR2) is a key enzyme in the polyol pathway whose overexpression is implicated in several diabetic complications, including neuropathy, nephropathy, retinopathy, and atherosclerotic plaque formation. Under hyperglycemic conditions, the intracellular accumulation of sorbitol and the depletion of NADPH lead to osmotic imbalance and oxidative stress, driven by the formation of reactive oxygen species and advanced glycation end products. Although various ALR2 inhibitors have been developed, their clinical application has been hampered by nonselective inhibition of both ALR2 and the homologous enzyme ALR1.

methodsIn this study, we employed a comprehensive

resultsThese bonds exhibited the ligand stability. Further, the MD simulation analysis, followed by postsimulation analysis, verified the dynamic stability of these four natural compounds and compared them with the native ligand of the target protein. These natural compounds exhibit particularly stable binding within the ALR2 selectivity pocket, demonstrating an inhibitory effect over ALR1 when compared with the reference inhibitor, Epalrestat.

conclusionThese promising

Indexed as

Aldehyde ReductaseBiological ProductsDiabetes ComplicationsEnzyme InhibitorsComputer SimulationHumansMolecular Docking SimulationMolecular Dynamics SimulationAldehyde ReductaseBiological ProductsEnzyme InhibitorsAldose reductase-2diabetes.molecular dockingmolecular dynamics simulationscoring functionsselectivity binding pocket

Identifiers

PMID40511643

What OpenQuestion 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 OpenQuestion graph.