Evidence map›Paper›PMID 27110811›Full record

ReviewViruses2016

Measles Virus Fusion Protein: Structure, Function and Inhibition.

Philippe Plattet, Lisa Alves, Michael Herren, Hector C Aguilar

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Comprehensive mapping of human CD4Cell reports. Medicine · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Antiviral activity of nitazoxanide againstJournal of virus eradication · 2023
    Article
  19. Article
  20. Review

7 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

4 authors at 3 institutions in 3 countries.

Philippe PlattetDivision of Experimental and Clinical Research, , Vetsuisse Faculty, University of Bern, Bremgartenstrasse 109a, Bern 3001, Switzerland. philippe.plattet@vetsuisse.unibe.ch.
Lisa AlvesClinical Neurology, Department of Veterinary Medicine, University of Cambridge, CB3 0ES, Cambridge, UK. calves.lisa@gmail.com.
Michael HerrenDivision of Experimental and Clinical Research, , Vetsuisse Faculty, University of Bern, Bremgartenstrasse 109a, Bern 3001, Switzerland. michael.herren@vetsuisse.unibe.ch.
Hector C AguilarPaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA 99164, USA. haguilar@vetmed.wsu.edu.
University of Bern · CHUniversity of Cambridge · GBWashington State University · US

Funding

Mechanisms of Nipah virus fusion and entryR01AI109022 · NIAID · WASHINGTON STATE UNIVERSITY · PI AGUILAR-CARRENO, HECTOR · 2014 to 2024
$4.3M
NIAID NIH HHS R01 AI109022NIAID NIH HHS R01AI109022
6 · The paper itself

Abstract

Measles virus (MeV), a highly contagious member of the Paramyxoviridae family, causes measles in humans. The Paramyxoviridae family of negative single-stranded enveloped viruses includes several important human and animal pathogens, with MeV causing approximately 120,000 deaths annually. MeV and canine distemper virus (CDV)-mediated diseases can be prevented by vaccination. However, sub-optimal vaccine delivery continues to foster MeV outbreaks. Post-exposure prophylaxis with antivirals has been proposed as a novel strategy to complement vaccination programs by filling herd immunity gaps. Recent research has shown that membrane fusion induced by the morbillivirus glycoproteins is the first critical step for viral entry and infection, and determines cell pathology and disease outcome. Our molecular understanding of morbillivirus-associated membrane fusion has greatly progressed towards the feasibility to control this process by treating the fusion glycoprotein with inhibitory molecules. Current approaches to develop anti-membrane fusion drugs and our knowledge on drug resistance mechanisms strongly suggest that combined therapies will be a prerequisite. Thus, discovery of additional anti-fusion and/or anti-attachment protein small-molecule compounds may eventually translate into realistic therapeutic options.

Indexed as

Antiviral AgentsBinding SitesDrug DiscoveryHost-Pathogen InteractionsHumansMeaslesMeasles virusModels, MolecularProtein BindingProtein ConformationProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationReceptors, VirusStructure-Activity RelationshipViral Fusion Protein InhibitorsAntiviral AgentsReceptors, VirusViral Fusion Protein InhibitorsViral Fusion Proteinscell entryfusion proteininhibitors and mechanisms of adaptationmeasles virusmembrane fusionneuroinvasionstructural changes

Identifiers

PMID27110811
PMCPMC4848605
OpenAlexW2342152789

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.