Evidence map›Paper›PMID 20161127›Full record

ArticleFuture virology2009

Glycoprotein interactions in paramyxovirus fusion.

Ronald M Iorio, Vanessa R Melanson, Paul J Mahon

Open access · greenAbstract read
In one paragraph

Article in Future virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

60 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Exploring Therapeutic Targets From Spreading Patterns Against Respiratory Syncytial Virus.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Pseudotyped Virus for Henipavirus.Advances in experimental medicine and biology · 2023
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Respiratory syncytial virus entry and how to block it.Nature reviews. Microbiology · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Paramyxovirus Glycoproteins and the Membrane Fusion Process.Current clinical microbiology reports · 2016
    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

3 authors at 1 institution in 1 country.

Ronald M IorioProgram in Immunology & Virology, University of Massachusetts Medical School, Worcester, MA 01655, USA and Department of Molecular Genetics & Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA, Tel.: +1 508 856 5257, , ronald.iorio@umassmed.edu.
Vanessa R Melanson
Paul J Mahon
United States Army Medical Research Institute of Infectious Diseases · US

Funding

Technologies for Human Cellular ImmunologyU19AI057319 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GREENOUGH, THOMAS C · 2003 to 2013
$34.4M
Glycoprotein interactions in paramyxovirus fusionR01AI049268 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IORIO, RONALD M · 2001 to 2011
$3.6M
Glycoprotein interactions in paramyxovirus fusionR56AI049268 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IORIO, RONALD M · 2006 to 2006
$402k
NIAID NIH HHS R01 AI049268NIAID NIH HHS R56 AI049268NIAID NIH HHS U19 AI057319
6 · The paper itself

Abstract

The Paramyxoviridae are enveloped, negative-stranded RNA viruses, some of which recognize sialic acid-containing receptors, while others recognize specific proteinaceous receptors. The major cytopathic effect of paramyxovirus infection is membrane fusion-induced syncytium formation. Paramyxoviruses are unusual in that the receptor-binding and fusion-promoting activities reside on two different spike structures, the attachment and fusion glycoproteins, respectively. For most paramyxoviruses, this distribution of functions requires a mechanism by which the two processes can be linked for the promotion of fusion. This is accomplished by a virus-specific interaction between the two proteins. An increasing body of evidence supports the notion that members of this family of viruses utilize this glycoprotein interaction in different ways in order to mediate the regulation of the fusion protein activation, depending on the type of receptor utilized by the virus.

Identifiers

PMID20161127
PMCPMC2743013
OpenAlexW2043760732

What OpenQuestion holds

Textmetadata
LicenceTDM
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.