Evidence map›Paper›PMID 35754713›Full record

ArticleiScience2022

Clioquinol as an inhibitor of JmjC-histone demethylase exhibits common and unique histone methylome and transcriptome between clioquinol and hypoxia.

Yunwon Moon, Sehyun Chae, Sujin Yim, Eun Gyeong Yang, Jungwoo Choe, Jiyeon Hyun, Rakwoo Chang, Daehee Hwang, Hyunsung Park

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

Article in iScience, 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
0.1field-weighted citation impact, top 62% 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, 1 citations in OpenAlex.

  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

9 authors at 4 institutions in 1 country.

Yunwon MoonDepartment of Life Science, University of Seoul, Seoul 02504, Republic of Korea.
Sehyun ChaeNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), Daegu 41062, Republic of Korea.
Sujin YimDepartment of Life Science, University of Seoul, Seoul 02504, Republic of Korea.
Eun Gyeong YangBiomedical Research Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Jungwoo ChoeDepartment of Life Science, University of Seoul, Seoul 02504, Republic of Korea.
Jiyeon HyunDepartment of Applied Chemistry, University of Seoul, Seoul 02504, Republic of Korea.
Rakwoo ChangDepartment of Applied Chemistry, University of Seoul, Seoul 02504, Republic of Korea.
Daehee HwangSchool of Biological Sciences, Seoul National University, Seoul 08826, Republic of Korea.
Hyunsung ParkDepartment of Life Science, University of Seoul, Seoul 02504, Republic of Korea.
University of Seoul · KRKorea Brain Research Institute · KRKorea Institute of Science and Technology · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clioquinol (CQ) is a hypoxic mimicker to activate hypoxia-inducible factor-1α (HIF-1α) by inhibiting HIF-1α specific asparaginyl hypoxylase (FIH-1). The structural similarity of the Jumonji C (JmjC) domain between FIH-1 and JmjC domain-containing histone lysine demethylases (JmjC-KDMs) led us to investigate whether CQ could inhibit the catalytic activities of JmjC-KDMs. Herein, we showed that CQ inhibits KDM4A/C, KDM5A/B, and KDM6B and affects H3K4me3, H3K9me3, and H3K27me3 marks, respectively. An integrative analysis of the histone methylome and transcriptome data revealed that CQ-mediated JmjC-KDM inhibition altered the transcription of target genes through differential combinations of KDMs and transcription factors. Notably, functional enrichment of target genes showed that CQ and hypoxia commonly affected the response to hypoxia, VEGF signaling, and glycolysis, whereas CQ uniquely altered apoptosis/autophagy and cytoskeleton/extracellular matrix organization. Our results suggest that CQ can be used as a JmjC-KDM inhibitor, HIF-α activator, and an alternative therapeutic agent in hypoxia-based diseases.

Indexed as

BiochemistryMolecular biologyTranscriptomics

Identifiers

PMID35754713
PMCPMC9218365
OpenAlexW4281770316

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.