Evidence map›Paper›PMID 31034925›Full record

ReviewBiochimica et biophysica acta. Reviews on cancer2019

The small members of the JMJD protein family: Enzymatic jewels or jinxes?

Sangphil Oh, Sook Shin, Ralf Janknecht

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Reviews on cancer, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

42 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. JMJD5: a multifunctional regulator in development, homeostasis, and cancer.Frontiers in cell and developmental biology · 2026
    Review
  5. Article
  6. JMJD8 facilitates hepatic lipid deposition and metabolic dysfunction.American journal of physiology. Endocrinology and metabolism · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Histone demethylases in autophagy and inflammation.Cell communication and signaling : CCS · 2025
    Review
  12. Article
  13. Versatile JMJD proteins: juggling histones and much more.Trends in biochemical sciences · 2024
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Sangphil OhDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA; Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Sook ShinDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA; Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Ralf JanknechtDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA; Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA; Department of Pathology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. Electronic address: ralf-janknecht@ouhsc.edu.
University of Oklahoma Health Sciences Center · US

Funding

Role of the DNPH1 Enzyme in Breast CancerR01CA233613 · NCI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI JANKNECHT, RALF · 2019 to 2023
$1.8M
Regulation of KDM4A by Lysine MethylationR03CA223615 · NCI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI JANKNECHT, RALF · 2018 to 2019
$145k
NCI NIH HHS R01 CA233613NCI NIH HHS R03 CA223615
6 · The paper itself

Abstract

Jumonji C domain-containing (JMJD) proteins are mostly epigenetic regulators that demethylate histones. However, a hitherto neglected subfamily of JMJD proteins, evolutionarily distant and characterized by their relatively small molecular weight, exerts different functions by hydroxylating proteins and RNA. Recently, unsuspected proteolytic and tyrosine kinase activities were also ascribed to some of these small JMJD proteins, further increasing their enzymatic versatility. Here, we discuss the ten human small JMJD proteins (HIF1AN, HSPBAP1, JMJD4, JMJD5, JMJD6, JMJD7, JMJD8, RIOX1, RIOX2, TYW5) and their diverse physiological functions. In particular, we focus on the roles of these small JMJD proteins in cancer and other maladies and how they are modulated in diseased cells by an altered metabolic milieu, including hypoxia, reactive oxygen species and oncometabolites. Because small JMJD proteins are enzymes, they are amenable to inhibition by small molecules and may represent novel targets in the therapy of cancer and other diseases.

Indexed as

Jumonji Domain-Containing Histone DemethylasesAnimalsHumansNeoplasmsJumonji Domain-Containing Histone DemethylasesCancerDemethylationHydroxylationJumonjiOncometabolite

Identifiers

PMID31034925
PMCPMC6525012
OpenAlexW2940451799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.