Evidence map›Paper›PMID 32344943›Full record

ArticleNutrients2020

Biological and Computational Studies for Dual Cholinesterases Inhibitory Effect of Zerumbone.

Jayeong Hwang, Kumju Youn, Yeongseon Ji, Seonah Lee, Gyutae Lim, Jinhyuk Lee, Chi-Tang Ho, Sun-Hee Leem, Mira Jun

Open access · goldAbstract read
In one paragraph

Article in Nutrients, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Phenolic Compounds ofBioMed research international · 2025
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  3. Determination of Potential Lead Compound fromInternational journal of molecular sciences · 2024
    Article
  4. Synthesis,Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Article
  5. Exploring the Inhibitory Potential ofTheScientificWorldJournal · 2024
    Article
  6. In silico Study of Antiviral Activity of Polyphenol Compounds fromAdvances and applications in bioinformatics and chemistry : AABC · 2023
    Article
  7. Review
  8. Article
  9. Review
  10. 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

9 authors at 3 institutions in 2 countries.

Jayeong HwangDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.
Kumju YounDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.
Yeongseon JiDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.
Seonah LeeDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.
Gyutae LimKorean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Korea.
Jinhyuk LeeKorean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Korea.
Chi-Tang HoDepartment of Food Science, Rutgers University, New Brunswick, NJ 08901, USA.
Sun-Hee LeemDepartment of Biological Science, Dong-A University, Busan 49315, Korea.
Mira JunDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.
Dong-A University · KRKorea Research Institute of Bioscience and Biotechnology · KRRutgers, The State University of New Jersey · US

Funding

Dong-A University Not applicable
6 · The paper itself

Abstract

Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) mediate the degradation of acetylcholine (ACh), a primary neurotransmitter in the brain. Cholinergic deficiency occurs during the progression of Alzheimer's disease (AD), resulting in widespread cognitive dysfunction and decline. We evaluated the potential effect of a natural cholinesterase inhibitor, zerumbone, using in vitro target enzyme assays, as well as in silico docking and ADMET (absorption, distribution, metabolism, excretion, and toxicity) simulation. Zerumbone showed a predominant cholinesterase inhibitory property with IC

Indexed as

AcetylcholinesteraseBinding SitesButyrylcholinesteraseCholinesterase InhibitorsEnzyme ActivationHumansKineticsMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationMolecular StructureProtein BindingSesquiterpenesStructure-Activity RelationshipAcetylcholinesteraseButyrylcholinesteraseCholinesterase InhibitorsSesquiterpeneszerumboneADMETAlzheimer’s disease (AD)cholinesterasescomputational docking simulationzerumbone

Identifiers

PMID32344943
PMCPMC7281973
OpenAlexW3020719265

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.