Evidence map›Paper›PMID 19057509›Full record

ArticleThe EMBO journal2009

Identification, structure, and functional requirement of the Mediator submodule Med7N/31.

Tobias Koschubs, Martin Seizl, Laurent Larivière, Fabian Kurth, Sonja Baumli, Dietmar E Martin, Patrick Cramer

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Upregulation of MED7 was associated with progression in hepatocellular carcinoma.Cancer biomarkers : section A of Disease markers · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Twenty years of Mediator complex structural studies.Biochemical Society transactions · 2019
    Review
  11. The complex structure and function of Mediator.The Journal of biological chemistry · 2018
    Review
  12. Mediator subunit MED31 is required for radial patterning ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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 3 institutions in 1 country.

Tobias KoschubsGene Center and Center for Integrated Protein Science Munich (CIPSM), Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität (LMU) München, Munich, Germany.
Martin Seizl
Laurent Larivière
Fabian Kurth
Sonja Baumli
Dietmar E Martin
Patrick Cramer
Ludwig-Maximilians-Universität München · DECenter for Integrated Protein Science Munich · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mediator is a modular multiprotein complex required for regulated transcription by RNA polymerase (Pol) II. Here, we show that the middle module of the Mediator core contains a submodule of unique structure and function that comprises the N-terminal part of subunit Med7 (Med7N) and the highly conserved subunit Med31 (Soh1). The Med7N/31 submodule shows a conserved novel fold, with two proline-rich stretches in Med7N wrapping around the right-handed four-helix bundle of Med31. In vitro, Med7N/31 is required for activated transcription and can act in trans when added exogenously. In vivo, Med7N/31 has a predominantly positive function on the expression of a specific subset of genes, including genes involved in methionine metabolism and iron transport. Comparative phenotyping and transcriptome profiling identify specific and overlapping functions of different Mediator submodules.

Indexed as

Protein Structure, QuaternaryAmino Acid SequenceCrystallography, X-RayDrosophila ProteinsGenetic Complementation TestMediator ComplexModels, MolecularMolecular Sequence DataSaccharomyces cerevisiaeSequence AlignmentTrans-ActivatorsTranscription FactorsTranscription, GeneticDrosophila ProteinsMed31 protein, DrosophilaMediator ComplexTrans-ActivatorsTranscription Factors

Identifiers

PMID19057509
PMCPMC2633081
OpenAlexW1978627780

What OpenQuestion holds

Textmetadata
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.