Evidence map›Paper›PMID 40268723›Full record

ArticleChemistry & biodiversity2025

Thymidine Phosphorylase Inhibitory Potential and Molecular Docking Studies of Secondary Metabolites Isolated From Fernandoa adenophylla (Wall. ex G. Don) Steenis.

Abdur Rauf, Majid Khan, Umer Rashid, Anees Saeed, Zafar Ali Shah, Zubair Ahmad, Abdulhakeem S Alamri, Walaa F Alsanie, Imtiaz Khan, Humaira Hussain and 2 more

Abstract read
In one paragraph

Article in Chemistry & biodiversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

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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

12 authors.

Abdur RaufDepartment of Chemistry, University of Swabi, Swabi, Khyber Pakhtunkhwa, Pakistan.
Majid KhanCollege of Chemistry, Fuzhou University, Fuzhou, China.
Umer RashidDepartment of Chemistry, COMSATS University Islamabad, Abbottabad Campus, Abbottabad, Pakistan.
Anees SaeedDepartment of Chemistry, COMSATS University Islamabad, Abbottabad Campus, Abbottabad, Pakistan.
Zafar Ali ShahDepartment of Agricultural Chemistry and Biochemistry, The University of Agriculture, Peshawar, Pakistan.
Zubair AhmadDepartment of Chemistry, University of Swabi, Swabi, Khyber Pakhtunkhwa, Pakistan.ORCID https://orcid.org/0000-0001-9645-6042
Abdulhakeem S AlamriDepartment of Clinical Laboratory Sciences, The Faculty of Applied Medical Sciences, Taif University, Taif, Saudi Arabia.
Walaa F AlsanieDepartment of Clinical Laboratory Sciences, The Faculty of Applied Medical Sciences, Taif University, Taif, Saudi Arabia.
Imtiaz KhanDepartment of Entomology, The University of Agriculture, University of Peshawar, Peshawar, Pakistan.
Humaira HussainDepartment of Biochemistry, Abbottabad University of Science & Technology, Abbottabad, Pakistan.
Majid AlhomraniDepartment of Clinical Laboratory Sciences, The Faculty of Applied Medical Sciences, Taif University, Taif, Saudi Arabia.
Marcello IritiDepartment of Biomedical, Surgical and Dental Sciences, University of Milan, Milan, Italy.ORCID https://orcid.org/0000-0002-5063-1236

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study investigates the potential of Fernandoa adenophylla, a South American plant, as a reservoir of compounds with thymidine phosphorylase (TP) inhibitory activity. Through a comprehensive approach combining in vitro assays and molecular docking analysis, we isolated and characterized bioactive compounds from F. adenophylla, including lapachol, alpha-lapachone, Peshawaraquinone, dehydro-α-lapachone, and indanone derivative (Methyl-1,2-dihydroxy-2-(3-methylbut-2-en-1-yl)-3-oxo-2,3-dihydro-1H-indene-1carboxylate). Our results reveal substantial TP inhibition by these compounds, with Lapachol (1) and Indanone derivative (5) demonstrating notable potency, exhibiting IC

Indexed as

Enzyme InhibitorsMolecular Docking SimulationThymidine PhosphorylaseDose-Response Relationship, DrugEscherichia coliHumansMolecular StructureStructure-Activity RelationshipEnzyme InhibitorsThymidine PhosphorylaseFernandoa adenophyllainhibitionin silico studythymidine phosphorylase

Identifiers

PMID40268723
PMCPMC12435400

What OpenQuestion holds

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LicenceCC BY
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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.