Evidence map›Paper›PMID 28360925›Full record

ReviewFrontiers in genetics2017

Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions.

Janice Kwok, Marie O'Shea, David A Hume, Andreas Lengeling

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. High-throughputbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. The Azalea Hypothesis of Alzheimer Disease: A Functional Iron Deficiency Promotes Neurodegeneration.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. JMJD family proteins in cancer and inflammation.Signal transduction and targeted therapy · 2022
    Review
  17. Widespread hydroxylation of unstructured lysine-rich protein domains by JMJD6.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

4 authors at 2 institutions in 1 country.

Janice KwokThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh Edinburgh, UK.
Marie O'SheaThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh Edinburgh, UK.
David A HumeThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh Edinburgh, UK.
Andreas LengelingThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh Edinburgh, UK.
University of Edinburgh · GBRoslin Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysyl hydroxylation and arginyl demethylation are post-translational events that are important for many cellular processes. The jumonji domain containing protein 6 (JMJD6) has been reported to catalyze both lysyl hydroxylation and arginyl demethylation on diverse protein substrates. It also interacts directly with RNA. This review summarizes knowledge of JMJD6 functions that have emerged in the last 15 years and considers how a single Jumonji C (JmjC) domain-containing enzyme can target so many different substrates. New links and synergies between the three main proposed functions of Jmjd6 in histone demethylation, promoter proximal pause release of polymerase II and RNA splicing are discussed. The physiological context of the described molecular functions is considered and recently described novel roles for JMJD6 in cancer and immune biology are reviewed. The increased knowledge of JMJD6 functions has wider implications for our general understanding of the JmjC protein family of which JMJD6 is a member.

Indexed as

chromatindemethylationhydroxylationJmjC domainpausingPSRsplicingtranscription

Identifiers

PMID28360925
PMCPMC5352680
OpenAlexW2593832951

What OpenQuestion holds

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LicenceCC BY
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.