Evidence map›Paper›PMID 32927736›Full record

ArticleInternational journal of molecular sciences2020

JMJD6 Regulates Splicing of Its Own Gene Resulting in Alternatively Spliced Isoforms with Different Nuclear Targets.

Nikoleta Raguz, Astrid Heim, Eden Engal, Juste Wesche, Juliane Merl-Pham, Stefanie M Hauck, Steffen Erkelenz, Heiner Schaal, Olivier Bensaude, Alexander Wolf and 2 more

Open access · goldAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Review
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

12 authors at 6 institutions in 3 countries.

Nikoleta RaguzDepartment of Biology II, Ludwig Maximilians University, Munich, Großhaderner Strasse 2, 82152 Planegg-Martinsried, Germany.
Astrid HeimDepartment of Biology II, Ludwig Maximilians University, Munich, Großhaderner Strasse 2, 82152 Planegg-Martinsried, Germany.
Eden EngalDepartment of Biochemistry and Molecular Biology, Institute for Medical Research Israel Canada, Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel.
Juste WescheInstitute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München-German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Juliane Merl-PhamResearch Unit Protein Science, Helmholtz Zentrum München-German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Stefanie M HauckResearch Unit Protein Science, Helmholtz Zentrum München-German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Steffen ErkelenzInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, 50931 Cologne, Germany.
Heiner SchaalInstitute of Virology, Medical Faculty, Heinrich Heine University Duesseldorf, 40225 Duesseldorf, Germany.ORCID 0000-0002-1636-4365
Olivier BensaudeInstitute de Biologie de l'Ecole Normale Supériuere (IBENS), Ecole Normale Supérieure, CNRS, INSERM, PSL Research University, 5005 Paris, France.
Alexander WolfInstitute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München-German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Maayan SaltonDepartment of Biochemistry and Molecular Biology, Institute for Medical Research Israel Canada, Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel.ORCID 0000-0001-8812-5577
Angelika BöttgerDepartment of Biology II, Ludwig Maximilians University, Munich, Großhaderner Strasse 2, 82152 Planegg-Martinsried, Germany.
Helmholtz Zentrum München · DEHebrew University of Jerusalem · ILLudwig-Maximilians-Universität München · DECentre National de la Recherche Scientifique · FRHeinrich Heine University Düsseldorf · DEUniversity of Cologne · DE

Funding

German-Israeli Foundation for Scientific Research and Development I-1436-417.13/2017
6 · The paper itself

Abstract

Jumonji-domain-containing protein 6 (JMJD6) is a Fe(II) and 2-oxogluterate (2OG) dependent oxygenase involved in gene regulation through post-translationally modifying nuclear proteins. It is highly expressed in many cancer types and linked to tumor progression and metastasis. Four alternatively-spliced

Indexed as

RNA SplicingHEK293 CellsHeLa CellsHumansJumonji Domain-Containing Histone DemethylasesNeoplasmsProtein DomainsProtein IsoformsJMJD6 protein, humanJumonji Domain-Containing Histone DemethylasesProtein IsoformshydroxylationpolyS domainsplicing

Identifiers

PMID32927736
PMCPMC7555845
OpenAlexW3084295494

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.