Evidence map›Paper›PMID 24840575›Full record

ArticleInternational journal of molecular sciences2014

Biological evaluation and 3D-QSAR studies of curcumin analogues as aldehyde dehydrogenase 1 inhibitors.

Hui Wang, Zhiyun Du, Changyuan Zhang, Zhikai Tang, Yan He, Qiuyan Zhang, Jun Zhao, Xi Zheng

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 2 institutions in 2 countries.

Hui WangSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. wanghuibetty1988@126.com.
Zhiyun DuSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. zhiyundu@gdut.edu.cn.
Changyuan ZhangSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. changyuanzhang@126.com.
Zhikai TangSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. tzkcarlos@163.com.
Yan HeSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. hxg_129@126.com.
Qiuyan ZhangSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. fumaihuanxue@126.com.
Jun ZhaoSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. junzhao60@hotmail.com.
Xi ZhengSchool of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China. zhengxi08@hotmail.com.
Guangdong University of Technology · CNRutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde dehydrogenase 1 (ALDH1) is reported as a biomarker for identifying some cancer stem cells, and down-regulation or inhibition of the enzyme can be effective in anti-drug resistance and a potent therapeutic for some tumours. In this paper, the inhibitory activity, mechanism mode, molecular docking and 3D-QSAR (three-dimensional quantitative structure activity relationship) of curcumin analogues (CAs) against ALDH1 were studied. Results demonstrated that curcumin and CAs possessed potent inhibitory activity against ALDH1, and the CAs compound with ortho di-hydroxyl groups showed the most potent inhibitory activity. This study indicates that CAs may represent a new class of ALDH1 inhibitor.

Indexed as

Quantitative Structure-Activity RelationshipAldehyde Dehydrogenase 1 FamilyBinding SitesCatalytic DomainCurcuminEnzyme InhibitorsHumansIsoenzymesKineticsMolecular Docking SimulationRetinal DehydrogenaseAldehyde Dehydrogenase 1 FamilyALDH1A1 protein, humanCurcuminEnzyme InhibitorsIsoenzymesRetinal Dehydrogenase

Identifiers

PMID24840575
PMCPMC4057759
OpenAlexW2096355252

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.