Evidence map›Paper›PMID 37527664›Full record

ArticleJournal of medicinal chemistry2023

5-Substituted Pyridine-2,4-dicarboxylate Derivatives Have Potential for Selective Inhibition of Human Jumonji-C Domain-Containing Protein 5.

Lennart Brewitz, Yu Nakashima, Sonia K Piasecka, Eidarus Salah, Sally C Fletcher, Anthony Tumber, Thomas P Corner, Tristan J Kennedy, Giorgia Fiorini, Armin Thalhammer and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Structure-guided optimisation ofChemical science · 2023
    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

13 authors at 2 institutions in 2 countries.

Lennart BrewitzChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.ORCID 0000-0002-9465-777X
Yu NakashimaChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Sonia K PiaseckaInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, B15 2TT Birmingham, U.K.
Eidarus SalahChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Sally C FletcherInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, B15 2TT Birmingham, U.K.
Anthony TumberChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Thomas P CornerChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Tristan J KennedyInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, B15 2TT Birmingham, U.K.
Giorgia FioriniChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Armin ThalhammerChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Kirsten E ChristensenChemical Crystallography, Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.
Mathew L ColemanInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, B15 2TT Birmingham, U.K.
Christopher J SchofieldChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, U.K.ORCID 0000-0002-0290-6565
Mansfield University · USUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J003018/1Biotechnology and Biological Sciences Research Council BB/R000344/1Cancer Research UK 16466Cancer Research UK 24552Cancer Research UK 28285Cancer Research UK C33483/A2567Cancer Research UK C8717/A18245Cancer Research UK TICCPP-2022/100001Wellcome TrustWellcome Trust 106244/Z/14/Z
6 · The paper itself

Abstract

Jumonji-C domain-containing protein 5 (JMJD5) is a 2-oxoglutarate (2OG)-dependent oxygenase that plays important roles in development, circadian rhythm, and cancer through unclear mechanisms. JMJD5 has been reported to have activity as a histone protease, as an

Indexed as

HistonesNeoplasmsCircadian RhythmHumansJumonji Domain-Containing Histone DemethylasesOxygenasesPyridinesHistonesJumonji Domain-Containing Histone DemethylasesOxygenasesPyridines

Identifiers

PMID37527664
PMCPMC10424186
OpenAlexW4385443358

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.