Evidence map›Paper›PMID 33191913›Full record

ArticleeLife2020

Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex.

Sandra K Schuller, Jan M Schuller, J Rajan Prabu, Marc Baumgärtner, Fabien Bonneau, Jérôme Basquin, Elena Conti

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021
    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

7 authors at 2 institutions in 2 countries.

Sandra K Schuller *Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID https://orcid.org/0000-0002-1800-8014
Jan M Schuller *Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID https://orcid.org/0000-0002-9121-1764
J Rajan PrabuDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID https://orcid.org/0000-0002-7726-9310
Marc BaumgärtnerDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Fabien BonneauDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID http://orcid.org/0000-0001-8787-7662
Jérôme BasquinDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Elena ContiDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID https://orcid.org/0000-0003-1254-5588
Max Planck Society · DELoewe Center for Synthetic Microbiology · DE

Funding

Deutsche Forschungsgemeinschaft 201302640Deutsche Forschungsgemeinschaft 369799452European Commission EXORICOGerman Research Foundation DFGGerman Research Foundation GRK1721German Research Foundation SFB/TRR 237
6 · The paper itself

Abstract

The yeast THO complex is recruited to active genes and interacts with the RNA-dependent ATPase Sub2 to facilitate the formation of mature export-competent messenger ribonucleoprotein particles and to prevent the co-transcriptional formation of RNA:DNA-hybrid-containing structures. How THO-containing complexes function at the mechanistic level is unclear. Here, we elucidated a 3.4 Å resolution structure of

Indexed as

Adenosine TriphosphatasesCryoelectron MicroscopyNucleic AcidsProtein ConformationRibonucleoproteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine Triphosphatasesmessenger ribonucleoproteinNucleic AcidsRibonucleoproteinsRNA-dependent ATPaseSaccharomyces cerevisiae ProteinsTHO2 protein, S cerevisiaeTranscription FactorsCryoEMhelicasemolecular biophysicsR-loopsRNARNA exportS. cerevisiaestructural biologytranscription

Identifiers

PMID33191913
PMCPMC7744097
OpenAlexW3101069359

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.