Evidence map›Paper›PMID 35520305›Full record

ArticleRSC advances2020

Inhibitory effects of UDP-glucuronosyltransferase (UGT) typical ligands against

Ling Xiao, Dehui Chi, Guiju Sheng, Wenjuan Li, Penghui Lin, Sicheng Liang, Liangliang Zhu, Peipei Dong

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

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

8 authors at 4 institutions in 2 countries.

Ling XiaoSchool of Resources and Environment, Key Laboratory of Aqueous Environment Protection and Pollution Control of Yangtze River, Anqing Normal University Anqing 246133 China.
Dehui ChiDepartment of Food Science and Technology, School of Life Science and Research Center of Aquatic Organism Conservation and Water Ecosystem Restoration, Anqing Normal University No. 1314, North Jixian Road Anqing 246133 China zhuliangliang@aqnu.edu.cn.
Guiju ShengDepartment of Food Science and Technology, School of Life Science and Research Center of Aquatic Organism Conservation and Water Ecosystem Restoration, Anqing Normal University No. 1314, North Jixian Road Anqing 246133 China zhuliangliang@aqnu.edu.cn.
Wenjuan LiDepartment of Food Science and Technology, School of Life Science and Research Center of Aquatic Organism Conservation and Water Ecosystem Restoration, Anqing Normal University No. 1314, North Jixian Road Anqing 246133 China zhuliangliang@aqnu.edu.cn.
Penghui LinCenter for Environmental and Systems Biochemistry, Markey Cancer Center, and Dept. of Toxicology & Cancer Biology, University of Kentucky 789 S. Limestone St Lexington KY 40536 USA.
Sicheng LiangSchool of Pharmacy, The Affiliated Hospital of Southwest Medical University Luzhou 646000 China.
Liangliang ZhuDepartment of Food Science and Technology, School of Life Science and Research Center of Aquatic Organism Conservation and Water Ecosystem Restoration, Anqing Normal University No. 1314, North Jixian Road Anqing 246133 China zhuliangliang@aqnu.edu.cn.ORCID https://orcid.org/0000-0002-3865-9092
Peipei DongCollege of Integrative Medicine, Dalian Medical University No. 9 West Section Lvshun South Road Dalian 116044 China dongpeipei11@163.com.
Anqing Normal University · CNAffiliated Hospital of Southwest Medical University · CNDalian Medical University · CNUniversity of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UDP-glucuronosyltransferases (UGTs) and β-glucuronidase (GUS) catalyze entirely distinct metabolism reactions. UGTs are responsible for the glucuronidation of a variety of drugs, endogenous and environmental chemicals, whereas GUS hydrolyzes glucuronides and liberates the parent substrates. Information on the overlap of ligand selectivity between UGT and GUS is essential for exploring the pharmacological or toxicological effects of the inhibitors of these two metabolic enzymes. This study is conducted to test whether UGTs and GUS share common ligands, by investigating the inhibitory effects towards

Identifiers

PMID35520305
PMCPMC9054634
OpenAlexW3035646270

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.