Evidence map›Paper›PMID 25288750›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein.

Robert Cox, Adrian Pickar, Shihong Qiu, Jun Tsao, Cynthia Rodenburg, Terje Dokland, Andrew Elson, Biao He, Ming Luo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  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

9 authors.

Robert CoxDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294;
Adrian PickarDepartment of Infectious Diseases, College of Veterinary Medicine, The University of Georgia, Athens, GA 30602; and.
Shihong QiuDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294;
Jun TsaoDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294;
Cynthia RodenburgDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294;
Terje DoklandDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294;
Andrew ElsonDepartment of Infectious Diseases, College of Veterinary Medicine, The University of Georgia, Athens, GA 30602; and.
Biao HeDepartment of Infectious Diseases, College of Veterinary Medicine, The University of Georgia, Athens, GA 30602; and.
Ming LuoDepartment of Chemistry, Georgia State University, Atlanta, GA 30302 mluo@gsu.edu.

Funding

Mechanism of Paramyxovirus ReplicationR01AI106307 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HE, BIAO, LUO, MING · 2013 to 2016
$2.3M
NIAID NIH HHS R01 AI106307
6 · The paper itself

Abstract

Mumps virus (MuV) is a highly contagious pathogen, and despite extensive vaccination campaigns, outbreaks continue to occur worldwide. The virus has a negative-sense, single-stranded RNA genome that is encapsidated by the nucleocapsid protein (N) to form the nucleocapsid (NC). NC serves as the template for both transcription and replication. In this paper we solved an 18-Å-resolution structure of the authentic MuV NC using cryo-electron microscopy. We also observed the effects of phosphoprotein (P) binding on the MuV NC structure. The N-terminal domain of P (PNTD) has been shown to bind NC and appeared to induce uncoiling of the helical NC. Additionally, we solved a 25-Å-resolution structure of the authentic MuV NC bound with the C-terminal domain of P (PCTD). The location of the encapsidated viral genomic RNA was defined by modeling crystal structures of homologous negative strand RNA virus Ns in NC. Both the N-terminal and C-terminal domains of MuV P bind NC to participate in access to the genomic RNA by the viral RNA-dependent-RNA polymerase. These results provide critical insights on the structure-function of the MuV NC and the structural alterations that occur through its interactions with P.

Indexed as

AnimalsCell LineCricetinaeCryoelectron MicroscopyGenome, ViralMolecular ConformationMumps virusNucleocapsidPhosphoproteinsPlasmidsProtein BindingProtein Structure, TertiaryRNA-Dependent RNA PolymeraseRNA, ViralVirionPhosphoproteinsRNA-Dependent RNA PolymeraseRNA, Viralmononegaviraleparamyxovirusreplication

Identifiers

PMID25288750
PMCPMC4210330

What OpenQuestion holds

Textmetadata
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.