Evidence map›Paper›PMID 38757332›Full record

ArticleCurrent pharmaceutical biotechnology2025

Inhibitory Activity of Quercetin, Rutin, and Hyperoside against Xanthine Oxidase: Kinetics, Fluorescence, and Molecular Docking.

Yali Yu, Yingzhu Xiong, Siman Tong, Yanli Li, Rongcan Cai, Xv Zhang, Feng Gao

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Article in Current pharmaceutical biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Xanthine Oxidase Inhibitory Potential ofInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Dynamic Changes in Jackfruit (Antioxidants (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Article
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

7 authors.

Yali YuCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.
Yingzhu XiongCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.
Siman TongCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.
Yanli LiCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.
Rongcan CaiCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.
Xv ZhangJilin Province Product Quality Supervision and Inspection Institute, Changchun, 130103, Jilin, China.
Feng GaoCollege of Food Science and Engineering, Jilin University, Changchun, 130062, P.R. China.

Funding

Education Department of Jilin Province, China JJKH20190175KJ
6 · The paper itself

Abstract

introductionQuercetin (Qc), rutin (Ru), and hyperoside (Hyp) are three common polyphenols widely distributed in the plant kingdom.

methodsThis study explored the inhibition and mechanisms of Qc, Ru, and Hyp against xanthine oxidase (XOD) by enzyme kinetic analysis, fluorescence analysis, and molecular docking. The inhibitory activities of the three polyphenols on XOD showed the following trend: quercetin > hyperoside > rutin, with IC

resultsThe binding of the three polyphenols to XOD is mainly driven by hydrogen bonding and van der Waals forces, resulting in the formation of an XOD-XA complex with only one affinity binding site. The binding sites of the three RSFQ phenolic compounds are close to those of tryptophan. Molecular docking showed that all three polyphenols enter the active pocket of XOD and maintain the stability of the complex through hydrogen bonding, hydrophobic interaction, and van der Waals forces.

conclusionThe results provide a theoretical basis for quercetin, rutin, and hyperoside to be used as function factors to prevent hyperuricemia.

Indexed as

Enzyme InhibitorsQuercetinRutinXanthine OxidaseFluorescenceKineticsMolecular Docking SimulationEnzyme InhibitorshyperosideQuercetinRutinXanthine Oxidasefluorescence analysishyperosideinhibition kineticsmolecular docking.Quercetinrutinxanthine oxidase

Identifiers

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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.