Evidence map›Paper›PMID 30733343›Full record

ReviewBiochemical Society transactions2019

Twenty years of Mediator complex structural studies.

Alexis Verger, Didier Monté, Vincent Villeret

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
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  9. Central Med23 deficiency leads to malformation of dentate gyrus and ADHD-like behaviors in mice.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2025
    Article
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  20. Assembly of RNA polymerase II transcription initiation complexes.Current opinion in structural biology · 2022
    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

3 authors at 1 institution in 1 country.

Alexis VergerUMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France alexis.verger@univ-lille.fr.ORCID 0000-0002-0299-2344
Didier MontéUMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France.
Vincent VilleretUMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mediator is a large multiprotein complex conserved in all eukaryotes that plays an essential role in transcriptional regulation. Mediator comprises 25 subunits in yeast and 30 subunits in humans that form three main modules and a separable four-subunit kinase module. For nearly 20 years, because of its size and complexity, Mediator has posed a formidable challenge to structural biologists. The first two-dimensional electron microscopy (EM) projection map of Mediator leading to the canonical view of its division in three topological modules named Head, Middle and Tail, was published in 1999. Within the last few years, optimization of Mediator purification combined with technical and methodological advances in cryo-electron microscopy (cryo-EM) have revealed unprecedented details of Mediator subunit organization, interactions with RNA polymerase II and parts of its core structure at high resolution. To celebrate the twentieth anniversary of the first Mediator EM reconstruction, we look back on the structural studies of Mediator complex from a historical perspective and discuss them in the light of our current understanding of its role in transcriptional regulation.

Indexed as

Cryoelectron MicroscopyHumansMediator ComplexProtein ConformationSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsMediator ComplexSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsCryo-EMMediator complexstructural biologytranscription

Identifiers

PMID30733343
PMCPMC6393861
OpenAlexW2914476117

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.