Evidence map›Paper›PMID 33565603›Full record

ArticleBiotechnology and bioengineering2021

Development of cell-based high throughput luminescence assay for drug discovery in inhibiting OCT4/DNA-PKcs and OCT4-MK2 interactions.

Ismail S Mohiuddin, Sung-Jen Wei, In-Hyoung Yang, Gloria M Martinez, Shengping Yang, Eun J Cho, Kevin N Dalby, Min H Kang

Open access · greenAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2021. 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
0.3field-weighted citation impact, top 45% 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, 5 citations in OpenAlex.

  1. DNA-PKcs as an upstream mediator of OCT4-induced MYC activation in small cell lung cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    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 3 institutions in 1 country.

Ismail S MohiuddinCancer Center, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.
Sung-Jen WeiCancer Center, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.
In-Hyoung YangCancer Center, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.
Gloria M MartinezCancer Center, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.
Shengping YangDepartment of Biostatistics, Pennington Biomedical Research Center, Baton Rouge, Louisiana, USA.
Eun J ChoDivision of Chemical Biology and Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, USA.
Kevin N DalbyDivision of Chemical Biology and Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, USA.
Min H KangCancer Center, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.ORCID 0000-0003-3603-7035
Texas Tech University · USAustin College · USPennington Biomedical Research Center · US

Funding

MYC activation in tumor progression of neuroblastomaR01CA232591 · NCI · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI KANG, MIN HEE · 2019 to 2023
$1.9M
Pharmacokinetics and pharmacogenomics for 13-cis retinoic acid in neuroblastomaR01CA168699 · NCI · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI KANG, MIN HEE · 2013 to 2016
$844k
NCI NIH HHS R01 CA168699NCI NIH HHS R01CA168699NCI NIH HHS R01 CA232591
6 · The paper itself

Abstract

Amplification-independent c-MYC overexpression is suggested in multiple cancers. Targeting c-MYC activity has therapeutic potential, but efforts thus far have been mostly unsuccessful. To find a druggable target to modulate c-MYC activity in cancer, we identified two kinases, MAPKAPK2 (MK2) and the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), which phosphorylate the Ser111 and the Ser93 residues of OCT4, respectively, to transcriptionally activate c-MYC. Using these observations, we present here a novel cell-based luminescence assay to identify compounds that inhibit the interaction between these kinases and OCT4. After screening approximately 80,000 compounds, we identified 56 compounds ("hits") that inhibited the luminescence reaction between DNA-PKcs and OCT4, and 65 hits inhibiting the MK2-OCT4 interaction. Using custom antibodies specific for pOCT4

Indexed as

Cell Line, TumorCytological TechniquesDNA-Activated Protein KinaseDrug DiscoveryHEK293 CellsHigh-Throughput Screening AssaysHumansIntracellular Signaling Peptides and ProteinsLuminescent MeasurementsMAP-Kinase-Activated Kinase 2Octamer Transcription Factor-3Protein BindingProtein Kinase InhibitorsProtein Serine-Threonine KinasesDNA-Activated Protein KinaseIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Octamer Transcription Factor-3Protein Kinase InhibitorsProtein Serine-Threonine Kinasesc-MYCDNA-PKcsdrug discoverykinase modulationMK2protein-protein interaction

Identifiers

PMID33565603
PMCPMC8597627
OpenAlexW3128670515

What OpenQuestion holds

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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.