Evidence map›Paper›PMID 31147442›Full record

ArticleThe Journal of biological chemistry2019

Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6.

Md Saiful Islam, Michael A McDonough, Rasheduzzaman Chowdhury, Joseph Gault, Amjad Khan, Elisabete Pires, Christopher J Schofield

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. High-throughputbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. An HSF1-JMJD6-HSP feedback circuit promotes cell adaptation to proteotoxic stress.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. JMJD8 Functions as a Novel AKT1 Lysine Demethylase.International journal of molecular sciences · 2022
    Article
  16. Article
  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

7 authors at 2 institutions in 2 countries.

Md Saiful IslamDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.ORCID 0000-0001-9842-0676
Michael A McDonoughDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.ORCID 0000-0003-4664-6942
Rasheduzzaman ChowdhuryDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Joseph GaultDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Amjad KhanDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Elisabete PiresDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Christopher J SchofieldDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom christopher.schofield@chem.ox.ac.uk.ORCID 0000-0002-0290-6565
University of Oxford · GBMansfield University · US

Funding

Cancer Research UK 18245Wellcome Trust
6 · The paper itself

Abstract

JmjC domain-containing protein 6 (JMJD6) is a 2-oxoglutarate (2OG)-dependent oxygenase linked to various cellular processes, including splicing regulation, histone modification, transcriptional pause release, hypoxia sensing, and cancer. JMJD6 is reported to catalyze hydroxylation of lysine residue(s) of histones, the tumor-suppressor protein p53, and splicing regulatory proteins, including u2 small nuclear ribonucleoprotein auxiliary factor 65-kDa subunit (U2AF65). JMJD6 is also reported to catalyze

Indexed as

CatalysisCrystallography, X-RayEstrogen Receptor alphaHumansHydroxylationJumonji Domain-Containing Histone DemethylasesKineticsLysineProtein ConformationSubstrate SpecificityESR1 protein, humanEstrogen Receptor alphaJMJD6 protein, humanJumonji Domain-Containing Histone DemethylasesLysine2-oxoglutarate and iron dependent dioxygenaseC-5 hydroxylysinedioxygenaseenzyme catalysisenzyme structurehydroxylasehydroxylysine (Hyl)hypoxiaJmjC domain-containing protein 6JMJD6metalloenzymeRNA splicingsubstrate specificityX-ray crystallography

Identifiers

PMID31147442
PMCPMC6663879
OpenAlexW2947776821

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.