Evidence map›Paper›PMID 25054138›Full record

ArticleBioMed research international2014

Investigation of estrogen receptor (ESR1) for breast cancer from traditional Chinese medicine.

Tzu-Chieh Hung, Wen-Yuan Lee, Kuen-Bao Chen, Yueh-Chiu Chan, Calvin Yu-Chian Chen

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact, top 91% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Oxidation-derived metabolites sustain the antioxidant network of quercetin.Journal of computer-aided molecular design · 2026
    Article
  2. Article
  3. Detection ofFrontiers in oncology · 2020
    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

5 authors at 3 institutions in 1 country.

Tzu-Chieh HungDepartment of Biomedical Informatics, Asia University, Taichung 41354, Taiwan.
Wen-Yuan LeeDepartment of Biomedical Informatics, Asia University, Taichung 41354, Taiwan ; School of Medicine, College of Medicine, China Medical University, Taichung 40402, Taiwan ; Department of Neurosurgery, China Medical University Hospital, No. 2 Yude Road, North District, Taichung 40447, Taiwan.
Kuen-Bao ChenDepartment of Biomedical Informatics, Asia University, Taichung 41354, Taiwan ; School of Medicine, College of Medicine, China Medical University, Taichung 40402, Taiwan ; Department of Anesthesiology, China Medical University Hospital, Taichung 40447, Taiwan.
Yueh-Chiu ChanSchool of Medicine, College of Medicine, China Medical University, Taichung 40402, Taiwan.
Calvin Yu-Chian ChenDepartment of Biomedical Informatics, Asia University, Taichung 41354, Taiwan ; School of Medicine, College of Medicine, China Medical University, Taichung 40402, Taiwan ; Research Center for Chinese Medicine & Acupuncture, China Medical University, Taichung 40402, Taiwan ; Human Genetic Center, Department of Medical Research, China Medical University Hospital, Taichung 40447, Taiwan.
Asia University · TWChina Medical University · TWChina Medical University Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, an important topic of breast cancer had been published in 2013. In this report, estrogen receptor (ESR1) had defined the relation of hormone-cause breast cancer. The screening of traditional Chinese medicine (TCM) database has found the molecular compounds by simulating molecular docking and molecular dynamics to regulate ESR1. S-Allylmercaptocysteine and 5-hydroxy-L-tryptophan are selected according to the highest docking score than that of other TCM compounds and Raloxifene (control). The simulation from molecular dynamics is helpful in analyzing and detecting the protein-ligand interactions. After a comparing the control and the Apo form, then based on the docking poses, hydrophobic interactions, hydrogen bond and structure variations, this research postulates that S-allylmercaptocysteine may be more appropriate than other compounds for protein-ligand interaction.

Indexed as

Medicine, Chinese Traditional5-HydroxytryptophanBinding SitesBreast NeoplasmsComputational BiologyComputer SimulationCrystallography, X-RayCysteineDatabases, FactualDrug DesignEstrogen Receptor alphaFemaleHumansLigandsMolecular Docking SimulationProtein Binding5-HydroxytryptophanCysteineESR1 protein, humanEstrogen Receptor alphaLigandsProteinsS-allylmercaptocysteine

Identifiers

PMID25054138
PMCPMC4098895
OpenAlexW2039064665

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.