Evidence map›Paper›PMID 30047866›Full record

ArticleeLife2018

Distinct and evolutionary conserved structural features of the human nuclear exosome complex.

Piotr Gerlach, Jan M Schuller, Fabien Bonneau, Jérôme Basquin, Peter Reichelt, Sebastian Falk, Elena Conti

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 12% 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

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

  1. Role of Exosomes in Dermal Wound Healing: A Systematic Review.The Journal of investigative dermatology · 2022
    Pooled it
  2. Article
  3. Review
  4. Article
  5. RiboScreenBiomedicines · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A Biallelic Variant of the RNA Exosome GenemedRxiv : the preprint server for health sciences · 2023
    Article
  17. Article
  18. Article
  19. Review
  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 1 institution in 2 countries.

Piotr Gerlach *Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID 0000-0001-9599-7322
Jan M Schuller *Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID 0000-0002-9121-1764
Fabien BonneauDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID 0000-0001-8787-7662
Jérôme BasquinDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Peter ReicheltDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Sebastian FalkDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID 0000-0001-7848-4621
Elena ContiDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.ORCID 0000-0003-1254-5588
MRC Laboratory of Molecular Biology · GB

Funding

Deutsche Forschungsgemeinschaft GRK1721Deutsche Forschungsgemeinschaft SFB1035Deutsche Forschungsgemeinschaft SFB646European Commission ERC-2016-ADG 740329 EXORICOEuropean Molecular Biology Organization ALTF 1008-2015
6 · The paper itself

Abstract

The nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to date have focused on the yeast system. Here, we reconstituted and studied the properties of a recombinant 14-subunit human nuclear exosome complex. In biochemical assays, the human exosome embeds a longer RNA channel than its yeast counterpart. The 3.8 Å resolution cryo-EM structure of the core complex bound to a single-stranded RNA reveals that the RNA channel path is formed by two distinct features of the hDIS3 exoribonuclease: an open conformation and a domain organization more similar to bacterial RNase II than to yeast Rrp44. The cryo-EM structure of the holo-complex shows how obligate nuclear cofactors position the hMTR4 helicase at the entrance of the core complex, suggesting a striking structural conservation from lower to higher eukaryotes.

Indexed as

Structural Homology, ProteinCell NucleusCrystallography, X-RayExosome Multienzyme Ribonuclease ComplexExosomesHumansProtein BindingProtein ConformationProtein SubunitsRNA HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDIS3 protein, humanDIS3 protein, S cerevisiaeExosome Multienzyme Ribonuclease ComplexMTREX protein, humanProtein SubunitsRNA HelicasesSaccharomyces cerevisiae Proteinsbiochemistrychemical biologycryoEMhDIS3hEXO-14hMTR4humanmolecular biophysicsnuclear exosomeRNA decaystructural biology

Identifiers

PMID30047866
PMCPMC6072439
OpenAlexW2883328413

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.