Evidence map›Paper›PMID 31312965›Full record

ArticleJournal of computer-aided molecular design2019

Rational Design, synthesis and biological evaluation of novel triazole derivatives as potent and selective PRMT5 inhibitors with antitumor activity.

Kongkai Zhu, Jingwei Shao, Hongrui Tao, Xue Yan, Cheng Luo, Hua Zhang, Wenhu Duan

Abstract read
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In one paragraph

Article in Journal of computer-aided molecular design, 2019. 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
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.

  1. Article
  2. Review
  3. Acquired resistance to PRMT5 inhibition induces concomitant collateral sensitivity to paclitaxel.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

7 authors.

Kongkai ZhuSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China. hkhhh.k@163.com.
Jingwei ShaoDepartment of Medicinal Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai, 201203, People's Republic of China.
Hongrui TaoSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China.
Xue YanSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China.
Cheng LuoDrug Discovery and Design Center, CAS Key Laboratory of Receptor Research, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, People's Republic of China.
Hua ZhangSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China. bio_zhangh@ujn.edu.cn.
Wenhu DuanDepartment of Medicinal Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai, 201203, People's Republic of China. whduan@simm.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 5 (PRMT5) is responsible for the mono-methylation and symmetric dimethylation of arginine, and its expression level and methyl transferring activity have been demonstrated to have a close relationship with tumorigenesis, development and poor clinical outcomes of human cancers. Two PRMT5 small molecule inhibitors (GSK3326595 and JNJ-64619178) have been put forward into clinical trials. Here, we describe the design, synthesis and biological evaluation of a series of novel, potent and selective PRMT5 inhibitors with antiproliferative activity against Z-138 mantle cell lymphoma cell line. Among them, compound C_4 exhibited the highest potency with enzymatic and cellular level IC

Indexed as

Cell Line, TumorCell ProliferationEnzyme InhibitorsHumansMethylationMolecular Docking SimulationNeoplasmsProtein-Arginine N-MethyltransferasesProtein BindingPyrimidinesPyrrolesQuinolinesStructure-Activity RelationshipTriazolesEnzyme InhibitorsGSK-3326595JNJ-64619178PRMT5 protein, humanProtein-Arginine N-MethyltransferasesPyrimidinesPyrrolesQuinolinesTriazolesAnti-proliferativeCellular target validationDesign and synthesisPRMT5 inhibitor

Identifiers

What OpenQuestion holds

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Registered trials

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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.