Evidence map›Paper›PMID 27282391›Full record

ArticleeLife2016

Architecture and RNA binding of the human negative elongation factor.

Seychelle M Vos, David Pöllmann, Livia Caizzi, Katharina B Hofmann, Pascaline Rombaut, Tomasz Zimniak, Franz Herzog, Patrick Cramer

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 91 citations in OpenAlex.

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  12. Mechanism of mammalian transcriptional repression by noncoding RNA.Nature structural & molecular biology · 2025
    Article
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  17. Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
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  19. Article
  20. Review

2 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Seychelle M VosDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
David PöllmannDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Livia CaizziDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Katharina B HofmannDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Pascaline RombautGene Center Munich, Ludwig-Maximilians-Universität München, Munich, Germany.
Tomasz ZimniakGene Center Munich, Ludwig-Maximilians-Universität München, Munich, Germany.
Franz HerzogGene Center Munich, Ludwig-Maximilians-Universität München, Munich, Germany.
Patrick CramerDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0001-5454-7755
Max Planck Institute for Biophysical Chemistry · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription regulation in metazoans often involves promoter-proximal pausing of RNA polymerase (Pol) II, which requires the 4-subunit negative elongation factor (NELF). Here we discern the functional architecture of human NELF through X-ray crystallography, protein crosslinking, biochemical assays, and RNA crosslinking in cells. We identify a NELF core subcomplex formed by conserved regions in subunits NELF-A and NELF-C, and resolve its crystal structure. The NELF-AC subcomplex binds single-stranded nucleic acids in vitro, and NELF-C associates with RNA in vivo. A positively charged face of NELF-AC is involved in RNA binding, whereas the opposite face of the NELF-AC subcomplex binds NELF-B. NELF-B is predicted to form a HEAT repeat fold, also binds RNA in vivo, and anchors the subunit NELF-E, which is confirmed to bind RNA in vivo. These results reveal the three-dimensional architecture and three RNA-binding faces of NELF.

Indexed as

Crystallography, X-RayGene Expression RegulationHumansModels, MolecularProtein BindingProtein ConformationRNATranscription FactorsTranscription, GeneticNSMF protein, humanRNATranscription Factorsbiochemistrybiophysicsgene regulationgene transcriptionhumanpromoter-proximal pausingRNA polymerase IIstructural biology

Identifiers

PMID27282391
PMCPMC4940160
OpenAlexW2411559641

What OpenQuestion holds

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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.