Evidence map›Paper›PMID 32270045›Full record

ArticleScience advances2020

Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly.

Serafima Guseva, Sigrid Milles, Malene Ringkjøbing Jensen, Nicola Salvi, Jean-Philippe Kleman, Damien Maurin, Rob W H Ruigrok, Martin Blackledge

Abstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
–field-weighted citation impact
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

124 citing papers in PubMed.

  1. Article
  2. Chemical reviews · 2026
    Review
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  6. Article
  7. Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. In Vitro Liquid-Liquid Phase Separation Assay for Viral Proteins.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  20. Article

64 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.

Serafima GusevaInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0001-9706-5035
Sigrid MillesInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0001-9362-9606
Malene Ringkjøbing JensenInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.
Nicola SalviInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0003-1515-6908
Jean-Philippe KlemanInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0001-5648-5295
Damien MaurinInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.
Rob W H RuigrokInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0002-8094-6642
Martin BlackledgeInstitut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.ORCID 0000-0003-0935-721X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many viruses are known to form cellular compartments, also called viral factories. Paramyxoviruses, including measles virus, colocalize their proteomic and genomic material in puncta in infected cells. We demonstrate that purified nucleoproteins (N) and phosphoproteins (P) of measles virus form liquid-like membraneless organelles upon mixing in vitro. We identify weak interactions involving intrinsically disordered domains of N and P that are implicated in this process, one of which is essential for phase separation. Fluorescence allows us to follow the modulation of the dynamics of N and P upon droplet formation, while NMR is used to investigate the thermodynamics of this process. RNA colocalizes to droplets, where it triggers assembly of N protomers into nucleocapsid-like particles that encapsidate the RNA. The rate of encapsidation within droplets is enhanced compared to the dilute phase, revealing one of the roles of liquid-liquid phase separation in measles virus replication.

Indexed as

Virus AssemblyMagnetic Resonance SpectroscopyMeaslesMeasles virusNucleocapsidNucleoproteinsPhosphoproteinsProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsRNA, ViralThermodynamicsViral ProteinsVirus ReplicationNucleoproteinsPhosphoproteinsRecombinant ProteinsRNA, ViralViral Proteins

Identifiers

PMID32270045
PMCPMC7112944

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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.