Evidence map›Paper›PMID 25105277›Full record

ReviewViruses2014

Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.

Farah El Najjar, Anthony P Schmitt, Rebecca Ellis Dutch

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 2 pooled it
4.9field-weighted citation impact, top 5% 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

77 citing papers in PubMed, 2 syntheses or guidelines pooled it, 109 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
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  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. The CRM1-dependent NESVeterinary research · 2025
    Article
  13. Nonlytic Egress and Transmission in the Virus World.Annual review of biochemistry · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

17 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

3 authors at 2 institutions in 1 country.

Farah El NajjarDepartment of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536, USA. farah.najjar@uky.edu.
Anthony P SchmittDepartment of Veterinary and Biomedical Sciences, The Pennsylvania State University, University Park, PA 16802, USA. aps13@psu.edu.
Rebecca Ellis DutchDepartment of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536, USA. rdutc2@uky.edu.
University of Kentucky · USPennsylvania State University · US

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI PAUMI, CHRISTIAN M · 2004 to 2011
$16.5M
SV5 and Hendra virus F protein promoted membrane fusionR01AI051517 · NIAID · UNIVERSITY OF KENTUCKY · PI DUTCH, REBECCA E. · 2002 to 2019
$4.4M
Hendra virus trafficking and assemblyR21AI108260 · NIAID · UNIVERSITY OF KENTUCKY · PI DUTCH, REBECCA E., SCHMITT, ANTHONY P · 2014 to 2015
$418k
NCRR NIH HHS #2P20 RR020171NCRR NIH HHS P20 RR020171NIAID NIH HHS R01 AI051517NIAID NIH HHS R21 AI108260NIAID NIH HHS R21AI108260
6 · The paper itself

Abstract

Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of the viral matrix protein, the ribonucleoprotein complex and the surface glycoproteins at the plasma membrane of infected cells and subsequent viral budding. Two major glycoproteins expressed on the viral envelope, the attachment protein and the fusion protein, promote attachment of the virus to host cells and subsequent virus-cell membrane fusion. Incorporation of the surface glycoproteins into infectious progeny particles requires coordinated interplay between the three viral structural components, driven primarily by the matrix protein. In this review, we discuss recent progress in understanding the contributions of the matrix protein and glycoproteins in driving paramyxovirus assembly and budding while focusing on the viral protein interactions underlying this process and the intracellular trafficking pathways for targeting viral components to assembly sites. Differences in the mechanisms of particle production among the different family members will be highlighted throughout.

Indexed as

Virus AssemblyVirus ReleaseAnimalsGlycoproteinsHumansParamyxovirinaeViral Envelope ProteinsViral Matrix ProteinsGlycoproteinsViral Envelope ProteinsViral Matrix Proteins

Identifiers

PMID25105277
PMCPMC4147685
OpenAlexW2079120949

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.