Evidence map›Paper›PMID 24579949›Full record

ReviewEpigenomics2014

The roles of Jumonji-type oxygenases in human disease.

Catrine Johansson, Anthony Tumber, KaHing Che, Peter Cain, Radosław Nowak, Carina Gileadi, Udo Oppermann

Open access · hybridAbstract readReview
In one paragraph

Review in Epigenomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 1 pooled it
9.1field-weighted citation impact, top 1% 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

103 citing papers in PubMed, 1 synthesis or guideline pooled it, 164 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7.Protein science : a publication of the Protein Society · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Review
  17. Article
  18. JmjC Family of Histone Demethylases Form Nuclear Condensates.International journal of molecular sciences · 2022
    Article
  19. Article
  20. Article

43 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

7 authors at 2 institutions in 1 country.

Catrine JohanssonStructural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Headington, OX3 7DQ, UK.
Anthony Tumber
KaHing Che
Peter Cain
Radosław Nowak
Carina Gileadi
Udo Oppermann
Genomics England · GBUniversity of Oxford · GB

Funding

Versus Arthritis 20522Wellcome Trust 092809
6 · The paper itself

Abstract

The iron- and 2-oxoglutarate-dependent oxygenases constitute a phylogenetically conserved class of enzymes that catalyze hydroxylation reactions in humans by acting on various types of substrates, including metabolic intermediates, amino acid residues in different proteins and various types of nucleic acids. The discovery of jumonji (Jmj), the founding member of a class of Jmj-type chromatin modifying enzymes and transcriptional regulators, has culminated in the discovery of several branches of histone lysine demethylases, with essential functions in regulating the epigenetic landscape of the chromatin environment. This work has now been considerably expanded into other aspects of epigenetic biology and includes the discovery of enzymatic steps required for methyl-cytosine demethylation as well as modification of RNA and ribosomal proteins. This overview aims to summarize the current knowledge on the human Jmj-type enzymes and their involvement in human pathological processes, including development, cancer, inflammation and metabolic diseases.

Indexed as

CytosineDNA MethylationEpigenesis, GeneticHumansInflammationJumonji Domain-Containing Histone DemethylasesMetabolic DiseasesModels, MolecularMultigene FamilyNeoplasmsOxygenasesPhylogenyPolycomb Repressive Complex 2Protein ConformationProtein FoldingCytosineJARID2 protein, humanJumonji Domain-Containing Histone DemethylasesOxygenasesPolycomb Repressive Complex 2

Identifiers

PMID24579949
PMCPMC4233403
OpenAlexW2122234165

What OpenQuestion holds

Textmetadata
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.