Evidence map›Paper›PMID 24349617›Full record

ArticleAmerican journal of translational research2013

Histone lysine demethylase (KDM) subfamily 4: structures, functions and therapeutic potential.

Roselyne M Labbé, Andreana Holowatyj, Zeng-Quan Yang

Abstract read
In one paragraph

Article in American journal of translational research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing 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

99 citing papers in PubMed.

  1. Article
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  11. Article
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  13. Review
  14. Discovery and structural studies of histone demethylases.Frontiers in epigenetics and epigenomics · 2025
    Review
  15. Article
  16. Review
  17. KDM4 Regulates the Glycolysis of Hemocytes in the Immune Priming ofInternational journal of molecular sciences · 2024
    Article
  18. H3K9me3 Levels Affect the Proliferation of Bovine Spermatogonial Stem Cells.International journal of molecular sciences · 2024
    Article
  19. Review
  20. Article

39 more citing papers are in PubMed but not listed here.

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

3 authors.

Roselyne M LabbéKarmanos Cancer Institute, Department of Oncology, Wayne State University Detroit, MI 48201, USA.
Andreana HolowatyjKarmanos Cancer Institute, Department of Oncology, Wayne State University Detroit, MI 48201, USA.
Zeng-Quan YangKarmanos Cancer Institute, Department of Oncology, Wayne State University Detroit, MI 48201, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KDM4 histone demethylases catalyze the removal of methyl marks from histone lysine residues to epigenetically regulate chromatin structure and gene expression. KDM4 expression is tightly regulated to insure proper function in diverse biological processes, such as cellular differentiation. Mounting evidence has shown that disrupting KDM4 expression is implicated in the establishment and progression of multiple diseases including cancer. In particular, genomic regions encoding the KDM4A, B and C genes are often amplified, disrupting normal cellular proliferation. Furthermore, KDM4 demethylases are promising druggable targets. In this review, we highlight the latest advances in characterizing the structures and regulatory mechanisms of KDM4 proteins, as well as our current understanding of their alterations and roles in tumorigenesis. We also review the reported KDM4 inhibitors and discuss their potential as therapeutic agents.

Indexed as

cancerHistone lysine demethylaseJmjC domainKDM4

Identifiers

PMID24349617
PMCPMC3853420

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.