Evidence map›Paper›PMID 40140437›Full record

ArticleScientific reports2025

Cardaria draba subspecies Shalepensis exerts in vitro and in silico inhibition of α-glucosidase, TRP1, and DLD-1 proliferation.

Ahmet Buğra Ortaakarsu, Özlem Bakır Boğa, Esabi Başaran Kurbanoğlu

Abstract read
In one paragraph

Article in Scientific reports, 2025. 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

3 authors.

Ahmet Buğra OrtaakarsuDepartment of Chemistry, Faculty of Science, Gazi University, Ankara, Turkey. bugra@ortaakarsu.com.
Özlem Bakır BoğaDepartment of Biology, Faculty of Science, Ataturk University, Erzurum, Turkey.
Esabi Başaran KurbanoğluDepartment of Biology, Faculty of Science, Ataturk University, Erzurum, Turkey.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, in vitro enzyme activity assays were performed to investigate the inhibitory effects on α-glucosidase and tyrosinase-related protein 1, while in silico molecular docking, molecular dynamics, and protein dynamics analyses were performed to provide information on molecular mechanisms. According to information obtained from in silico approaches, inhibition properties are responsible for conformational changes in protein structures, occupation of the active site cleft by the dominant compounds in the extract, as well as long-term changes in protein folding due to departure from the usual motion. The IC

Indexed as

alpha-GlucosidasesGlycoside Hydrolase InhibitorsPlant ExtractsCell Line, TumorCell ProliferationHumansMolecular Docking SimulationMolecular Dynamics Simulationalpha-GlucosidasesGlycoside Hydrolase InhibitorsPlant ExtractsCardaria draba L.Colon cancerEnzyme inhibitionMolecular dockingMolecular dynamics

Identifiers

PMID40140437
PMCPMC11947245

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.