Evidence map›Paper›PMID 41244458›Full record

ArticleACS omega2025

Investigating the Structural and Functional Consequences of Pathogenic SNPs on Human VEGFA Dimer: Insights from Molecular Dynamics Study.

Rajib Islam, Md Jahirul Islam, Sadia Jaman, Md Arafat Hossen, Sayeda Samina Ahmed, Syeda Samira Afrose, Md Junaid, Md Shahinozzaman, Mohammad A Halim

Erratum issuedAbstract read
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In one paragraph

Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Rajib IslamDivision of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, 16 Tejkunipara, Tejgaon, Dhaka 1215, Bangladesh.ORCID https://orcid.org/0000-0001-8499-5516
Md Jahirul IslamDivision of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, 16 Tejkunipara, Tejgaon, Dhaka 1215, Bangladesh.
Sadia JamanDivision of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, 16 Tejkunipara, Tejgaon, Dhaka 1215, Bangladesh.
Md Arafat HossenDivision of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, 16 Tejkunipara, Tejgaon, Dhaka 1215, Bangladesh.ORCID https://orcid.org/0009-0001-0313-9011
Sayeda Samina AhmedDivision of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, 16 Tejkunipara, Tejgaon, Dhaka 1215, Bangladesh.
Syeda Samira AfroseGenomic and Proteomic Research Division, ABCD Laboratory, Bangladesh, Chattogram 4226, Bangladesh.
Md JunaidGenomic and Proteomic Research Division, ABCD Laboratory, Bangladesh, Chattogram 4226, Bangladesh.
Md ShahinozzamanDivision of Pharmaceutical Quality Research, Office of Pharmaceutical Quality Research, Center for Drug Evaluation and Research, U.S. Food and Drug Administration, Silver Spring, Maryland 20993, United States.
Mohammad A HalimDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30114, United States.ORCID https://orcid.org/0000-0002-1698-7044

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vascular endothelial growth factor A (VEGFA) is a key regulator of angiogenesis. It forms a homodimer and binds to VEGF receptors to activate signaling pathways important for blood vessel growth and maintenance. In this study, we examined the structural and functional effects of two deleterious mutants, R262Q and C266Y, using integrative computational methods. Molecular dynamics simulations and principal component analysis showed that both mutations disrupted crucial interface interactions, including H-bonds, salt bridges, and disulfide linkages. As a result, the dimer conformation became less stable, which was also supported by binding free energy analysis. In addition, structural superimposition analysis revealed that both mutations changed the receptor-binding shape. This may block normal signaling and affect biological functions. Overall, our findings provide structural insights into how these mutations affect VEGFA dimer and may help guide the development of new therapeutics.

Identifiers

PMID41244458
PMCPMC12613135

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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.