Evidence map›Paper›PMID 29915238›Full record

ArticleNature chemical biology2018

The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.

Suzana Markolovic, Qinqin Zhuang, Sarah E Wilkins, Charlotte D Eaton, Martine I Abboud, Maximiliano J Katz, Helen E McNeil, Robert K Leśniak, Charlotte Hall, Weston B Struwe and 13 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7.Protein science : a publication of the Protein Society · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. JMJD8 Functions as a Novel AKT1 Lysine Demethylase.International journal of molecular sciences · 2022
    Article
  12. Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Developmentally regulated GTPases: structure, function and roles in disease.Cellular and molecular life sciences : CMLS · 2021
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

23 authors at 5 institutions in 3 countries.

Suzana MarkolovicChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Qinqin ZhuangInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Sarah E WilkinsChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Charlotte D EatonInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Martine I AbboudChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0003-2141-5988
Maximiliano J KatzInstituto Leloir, Buenos Aires, Argentina.
Helen E McNeilInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Robert K LeśniakChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Charlotte HallInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Weston B StruweChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Rebecca KonietznyTarget Discovery Institute, University of Oxford, Oxford, UK.
Simon DavisTarget Discovery Institute, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7840-2411
Ming YangTarget Discovery Institute, University of Oxford, Oxford, UK.
Wei GeChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-9907-512X
Justin L P BeneschChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-1507-3742
Benedikt M KesslerTarget Discovery Institute, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-8160-2446
Peter J RatcliffeTarget Discovery Institute, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-7980-7151
Matthew E CockmanTarget Discovery Institute, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3310-4821
Roman FischerTarget Discovery Institute, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-9715-5951
Pablo WappnerInstituto Leloir, Buenos Aires, Argentina.
Rasheduzzaman ChowdhuryChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK. rashed.chowdhury@stanford.edu.
Mathew L ColemanInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK. m.coleman@bham.ac.uk.
Christopher J SchofieldChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK. christopher.schofield@chem.ox.ac.uk.
University of Oxford · GBUniversity of Birmingham · GBThe Francis Crick Institute · GBFundación Instituto Leloir · ARCancer Research UK Clinical Trials Unit · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D011523/1Biotechnology and Biological Sciences Research Council BB/L009846/1British Heart Foundation RG/11/1/28684Cancer Research UK 24552Medical Research Council MR/N021053/1Wellcome Trust
6 · The paper itself

Abstract

Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involving both N- and C-terminal regions and disulfide bond formation. A proteomic approach identifies two related members of the translation factor (TRAFAC) family of GTPases, developmentally regulated GTP-binding proteins 1 and 2 (DRG1/2), as activity-dependent JMJD7 interactors. Mass spectrometric analyses demonstrate that JMJD7 catalyzes Fe(II)- and 2OG-dependent hydroxylation of a highly conserved lysine residue in DRG1/2; amino-acid analyses reveal that JMJD7 catalyzes (3S)-lysyl hydroxylation. The functional assignment of JMJD7 will enable future studies to define the role of DRG hydroxylation in cell growth and disease.

Indexed as

BiocatalysisGTP PhosphohydrolasesHumansHydroxylationJumonji Domain-Containing Histone DemethylasesModels, MolecularGTP PhosphohydrolasesJumonji Domain-Containing Histone Demethylases

Identifiers

PMID29915238
PMCPMC6027965
OpenAlexW2808604828

What OpenQuestion holds

Textmetadata
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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.