Evidence map›Paper›PMID 31586050›Full record

ArticleNature communications2019

Atomic-level insight into mRNA processing bodies by combining solid and solution-state NMR spectroscopy.

Reinier Damman, Stefan Schütz, Yanzhang Luo, Markus Weingarth, Remco Sprangers, Marc Baldus

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Crucial role of the cGAS N terminus in mediating flowable and functional cGAS-DNA condensate formation via DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
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  7. Journal of biomolecular NMR · 2023
    Article
  8. Article
  9. A call to order: Examining structured domains in biomolecular condensates.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  10. Review
  11. Article
  12. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    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

6 authors at 2 institutions in 2 countries.

Reinier DammanNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-6311-9250
Stefan SchützDepartment of Biophysics I, University of Regensburg, 93053, Regensburg, Germany.
Yanzhang LuoNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-9149-2423
Markus WeingarthNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0003-0831-8673
Remco SprangersDepartment of Biophysics I, University of Regensburg, 93053, Regensburg, Germany. remco.sprangers@ur.de.ORCID http://orcid.org/0000-0001-7323-6047
Marc BaldusNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands. m.baldus@uu.nl.ORCID http://orcid.org/0000-0001-7068-5613
Utrecht University · NLUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation is increasingly recognized as a process involved in cellular organization. Thus far, a detailed structural characterization of this intrinsically heterogeneous process has been challenging. Here we combine solid- and solution-state NMR spectroscopy to obtain atomic-level insights into the assembly and maturation of cytoplasmic processing bodies that contain mRNA as well as enzymes involved in mRNA degradation. In detail, we have studied the enhancer of decapping 3 (Edc3) protein that is a central hub for processing body formation in yeast. Our results reveal that Edc3 domains exhibit diverse levels of structural organization and dynamics after liquid-liquid phase separation. In addition, we find that interactions between the different Edc3 domains and between Edc3 and RNA in solution are largely preserved in the condensed protein state, allowing processing bodies to rapidly form and dissociate upon small alterations in the cellular environment.

Indexed as

RNA StabilityHydrophobic and Hydrophilic InteractionsNuclear Magnetic Resonance, BiomolecularProtein DomainsRNA, FungalRNA, MessengerSchizosaccharomyces pombe ProteinsStatic ElectricityEdc3 protein, S pombeRNA, FungalRNA, MessengerSchizosaccharomyces pombe Proteins

Identifiers

PMID31586050
PMCPMC6778109
OpenAlexW2978653885

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.