Evidence map›Paper›PMID 32341466›Full record

ArticleActa pharmacologica Sinica2020

An in vitro Förster resonance energy transfer-based high-throughput screening assay identifies inhibitors of SUMOylation E2 Ubc9.

Yu-Zhe Wang, Xiao Liu, George Way, Vipul Madarha, Qing-Tong Zhou, De-Hua Yang, Jia-Yu Liao, Ming-Wei Wang

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

Article in Acta pharmacologica Sinica, 2020. 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
0.3field-weighted citation impact, top 47% 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. Review
  2. Structural insights into the interaction of three Y-shaped ligands with PI3Kα.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Nanobodies and chemical cross-links advance the structural and functional analysis of PI3Kα.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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 4 institutions in 2 countries.

Yu-Zhe WangThe National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai, 201203, China.
Xiao LiuSchool of Pharmacy, Shanghai Medical College, Fudan University, Shanghai, 200032, China.
George WayDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, Riverside, CA, 92521, USA.
Vipul MadarhaDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, Riverside, CA, 92521, USA.
Qing-Tong ZhouiHuman Institute, ShanghaiTech University, Shanghai, 201210, China.
De-Hua YangThe National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai, 201203, China. dhyang@simm.ac.cn.
Jia-Yu LiaoDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, Riverside, CA, 92521, USA. jliao@engr.ucr.edu.
Ming-Wei WangThe National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai, 201203, China. mwwang@simm.ac.cn.
University of California, Riverside · USNational Center for Drug Screening · CNShanghai Medical College of Fudan University · CNShanghaiTech University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation is one of the posttranslational modifications that mediate cellular activities such as transcription, DNA repair, and signal transduction and is involved in the cell cycle. However, only a limited number of small molecule inhibitors have been identified to study its role in cellular processes. Here, we report a Förster resonance energy transfer (FRET) high-throughput screening assay based on the interaction between E2 Ubc9 and E3 PIAS1. Of the 3200 compounds screened, 34 (1.1%) showed higher than 50% inhibition and 4 displayed dose-response inhibitory effects. By combining this method with a label-free surface plasmon resonance (SPR) assay, false positives were excluded leading to discovering WNN0605-F008 and WNN1062-D002 that bound to Ubc9 with K

Indexed as

AnimalsEnzyme InhibitorsFluorescence Resonance Energy TransferGTPase-Activating ProteinsHEK293 CellsHigh-Throughput Screening AssaysHumansMCF-7 CellsMolecular Docking SimulationProtein BindingProtein Inhibitors of Activated STATProtein MultimerizationSf9 CellsSmall Molecule LibrariesSmall Ubiquitin-Related Modifier ProteinsSpodopteraEnzyme InhibitorsGTPase-Activating ProteinsPIAS1 protein, humanProtein Inhibitors of Activated STATRANGAP1 protein, humanSmall Molecule LibrariesSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Förster resonance energy transferhigh-throughput screeningPIAS1SUMOylation inhibitorsurface plasmon resonanceUbc9WNN0605-F008

Identifiers

PMID32341466
PMCPMC7656853
OpenAlexW3020373167

What OpenQuestion holds

Textmetadata
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.