Evidence map›Paper›PMID 35528018›Full record

ArticleFrontiers in endocrinology2022

Inhibition of Human Sulfotransferases by Phthalate Monoesters.

Hui Huang, Bei-Di Lan, Yu-Jing Zhang, Xiao-Juan Fan, Min-Cui Hu, Guo-Qiang Qin, Fei-Ge Wang, Yue Wu, Tao Zheng, Jun-Hui Liu

Abstract read
In one paragraph

Article in Frontiers in endocrinology, 2022. 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
–field-weighted citation impact
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.

  1. Review
  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

10 authors.

Hui HuangDepartment of Cardiology, General Hospital of Ningxia Medical University, Yinchuan, China.
Bei-Di LanDepartment of CardioMetabolic Center, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Yu-Jing ZhangDepartment of Cardiology, General Hospital of Ningxia Medical University, Yinchuan, China.
Xiao-Juan FanDepartment of CardioMetabolic Center, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Min-Cui HuTianjin Life Science Research Center, Department of Microbiology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China.
Guo-Qiang QinHuman Resources Department, The First Affiliated Hospital of Jinzhou Medical University, Jinzhou, China.
Fei-Ge WangHuman Resources Department, The First Affiliated Hospital of Jinzhou Medical University, Jinzhou, China.
Yue WuDepartment of CardioMetabolic Center, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Tao ZhengDepartment of CardioMetabolic Center, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Jun-Hui LiuDepartment of CardioMetabolic Center, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Objective: This study aimed to investigate the inhibition of human important phase II metabolic enzyme sulfotransferases (SULTs) by phthalate monoesters, which are important metabolites of phthalate esters (PAEs). Method: Recombinant SULT-catalyzed metabolism of p-nitrophenol (PNP) was employed as the probe reactions of SULTs to investigate the inhibition of 8 kinds of phthalate monoesters towards SULT isoforms. An Result: Multiple phthalate monoesters have been demonstrated to exert strong inhibition potential towards SULT1A1, SULT1B1, and SULT1E1, and no significant inhibition of phthalate monoesters towards SULT1A3 was found. The activity of SULT1A1 was strongly inhibited by mono-hexyl phthalate (MHP), mono-octyl phthalate (MOP), mono-benzyl phthalate (MBZP), and mono-ethylhexyl phthalate (MEHP). Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1. MHP, MOP, and MEHP significantly inhibited the activity of SULT1E1. MOP was chosen as the representative phthalate monoester to determine the inhibition kinetic parameters ( Conclusions: All these information will be beneficial for understanding the risk of phthalate monoester exposure from a new perspective.

Indexed as

EstersSulfotransferasesHumansPhthalic AcidsProtein IsoformsEstersphthalic acidPhthalic AcidsProtein IsoformsSulfotransferasesenzyme inhibitionin silico dockingin vitro–in vivo extrapolationphthalate esters (PAEs)sulfotransferases (SULTs)

Identifiers

PMID35528018
PMCPMC9072656

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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.