Evidence map›Paper›PMID 34858949›Full record

ArticleFrontiers in chemistry2021

A Small Ligand That Selectively Binds to the G-quadruplex at the Human Vascular Endothelial Growth Factor Internal Ribosomal Entry Site and Represses the Translation.

Xiao-Xia Hu, Sheng-Quan Wang, Shi-Quan Gan, Lei Liu, Ming-Qing Zhong, Meng-Hao Jia, Fei Jiang, Yan Xu, Chao-Da Xiao, Xiang-Chun Shen

Open access · goldAbstract read
In one paragraph

Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Investigating Potential 5' UTR G-Quadruplexes Within NRF2 mRNA.Current issues in molecular biology · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Secondary structures in RNA synthesis, splicing and translation.Computational and structural biotechnology journal · 2022
    Review
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

10 authors at 2 institutions in 2 countries.

Xiao-Xia HuState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Sheng-Quan WangState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Shi-Quan GanState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Lei LiuState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Ming-Qing ZhongState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Meng-Hao JiaState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Fei JiangState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Yan XuDivision of Chemistry, Department of Medical Sciences, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan.
Chao-Da XiaoState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Xiang-Chun ShenState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, China.
Guiyang Medical University · CNUniversity of Miyazaki · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-quadruplexes are believed to have important biological functions, so many small molecules have been screened or developed for targeting G-quadruplexes. However, it is still a major challenge to find molecules that recognize specific G-quadruplexes. Here, by using a combination of surface plasmon resonance, electrospray ionization mass spectrometry, circular dichroism, Western blot, luciferase assay, and reverse transcriptase stop assay, we observed a small molecule, namely, oxymatrine (OMT) that could selectively bind to the RNA G-quadruplex in 5'-untranslated regions (UTRs) of human vascular endothelial growth factor (hVEGF), but could not bind to other G-quadruplexes. OMT could selectively repress the translation of VEGF in cervical cancer cells. Furthermore, it could recognize VEGF RNA G-quadruplexes in special conformations. The results indicate that OMT may serve as a potentially special tool for studying the VEGF RNA G-quadruplex in cells and as a valuable scaffold for the design of ligands that recognize different G-quadruplexes.

Indexed as

G-quadruplexRNAselective ligandtranslationVEGF

Identifiers

PMID34858949
PMCPMC8630693
OpenAlexW3211975450

What OpenQuestion holds

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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.