Evidence map›Paper›PMID 31889992›Full record

ArticleChinese medicine2019

Inhibition of human carboxylesterases by ginsenosides: structure-activity relationships and inhibitory mechanism.

Zhao-Hui Sun, Jing Chen, Yun-Qing Song, Tong-Yi Dou, Li-Wei Zou, Da-Cheng Hao, Hai-Bin Liu, Guang-Bo Ge, Ling Yang

Open access · goldAbstract read
In one paragraph

Article in Chinese medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. An in vitro evaluation of common botanical extracts on carboxylesterase 1 catalytic activity.Drug metabolism and disposition: the biological fate of chemicals · 2025
    Article
  3. Kinetic conversion of BIOGF1K enriched in compound K fromCurrent research in pharmacology and drug discovery · 2023
    Article
  4. Article
  5. 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 1 country.

Zhao-Hui Sun1Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203 China.
Jing Chen2School of Life Science and Medicine, Dalian University of Technology, Panjin, 124221 China.
Yun-Qing Song1Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203 China.
Tong-Yi Dou2School of Life Science and Medicine, Dalian University of Technology, Panjin, 124221 China.
Li-Wei Zou1Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203 China.
Da-Cheng Hao3School of Environment and Chemical Engineering, Dalian Jiaotong University, Dalian, 116028 China.
Hai-Bin LiuNational Engineering Research Center for Gelatin-based Traditional Chinese Medicine, Dong-E-E-Jiao Co. Ltd., Liaocheng, 252201 China.
Guang-Bo Ge1Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203 China.
Ling Yang1Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203 China.
Shanghai University of Traditional Chinese Medicine · CNDalian University · CNDalian Jiaotong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHuman carboxylesterases (hCES) are key serine hydrolases responsible for the hydrolysis of a wide range of endogenous and xenobiotic esters. Although it has been reported that some ginsenosides can modulate the activities of various enzymes, the inhibitory effects of ginsenosides on hCES have not been well-investigated.

methodsIn this study, more than 20 ginsenosides were collected and their inhibitory effects on hCES1A and hCES2A were assayed using the highly specific fluorescent probe substrates for each isoenzyme. Molecular docking simulations were also performed to investigate the interactions between ginsenosides and hCES.

resultsAmong all tested ginsenosides, Dammarenediol II (DM) and 20S-

conclusionThe structure-inhibition relationships of ginsenosides as hCES inhibitors was investigated for the first time. Our results revealed that DM and DMG were potent inhibitors against both hCES1A and hCES2A, while PPD and PPT were selective and strong inhibitors against hCES2A.

Indexed as

GinsenosidesHuman carboxylesterases (hCES)Inhibitory mechanismSelectivityStructure–inhibition relationships

Identifiers

PMID31889992
PMCPMC6915887
OpenAlexW2995939597

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.