Evidence map›Paper›PMID 24530984›Full record

ReviewCurrent opinion in virology2014

Activation of paramyxovirus membrane fusion and virus entry.

Theodore S Jardetzky, Robert A Lamb

Abstract readReview
In one paragraph

Review in Current opinion in virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing 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

102 citing papers in PubMed.

  1. Article
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  11. Syncytial therapeutics: Receptor-specific and direct-to-cytosol biologic drug delivery mediated by measles fusion complex.Journal of controlled release : official journal of the Controlled Release Society · 2025
    Article
  12. Article
  13. Review
  14. Article
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  16. bioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Review

42 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

2 authors.

Theodore S JardetzkyDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, United States. Electronic address: tjardetz@stanford.edu.
Robert A LambDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500, United States; Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, United States. Electronic address: ralamb@northwestern.edu.

Funding

STRUCTURAL STUDIES OF PARAMYXOVIRUS FUSION PROTEINSR01GM061050 · NIGMS · STANFORD UNIVERSITY · PI JARDETZKY, THEODORE S · 2000 to 2015
$3.1M
STRUCTURE &EXPRESSION OF THE PARAMYXOVIRUS SV5 GENOMER01AI023173 · NIAID · NORTHWESTERN UNIVERSITY · PI LAMB, ROBERT A · 1986 to 2010
$3.1M
Howard Hughes Medical InstituteNIAID NIH HHS AI-23173NIAID NIH HHS R01 AI023173NIGMS NIH HHS GM-61050NIGMS NIH HHS R01 GM061050
6 · The paper itself

Abstract

The paramyxoviruses represent a diverse virus family responsible for a wide range of human and animal diseases. In contrast to other viruses, such as HIV and influenza virus, which use a single glycoprotein to mediate host receptor binding and virus entry, the paramyxoviruses require two distinct proteins. One of these is an attachment glycoprotein that binds receptor, while the second is a fusion glycoprotein, which undergoes conformational changes that drive virus-cell membrane fusion and virus entry. The details of how receptor binding by one protein activates the second to undergo conformational changes have been poorly understood until recently. Over the past couple of years, structural and functional data have accumulated on representative members of this family, including parainfluenza virus 5, Newcastle disease virus, measles virus, Nipah virus and others, which suggest a mechanistic convergence of activation models. Here we review the data indicating that paramyxovirus attachment glycoproteins shield activating residues within their N-terminal stalk domains, which are then exposed upon receptor binding, leading to the activation of the fusion protein by a 'provocateur' mechanism.

Indexed as

Virus InternalizationAnimalsHumansMembrane FusionParamyxoviridaeParamyxoviridae InfectionsReceptors, VirusViral Fusion ProteinsReceptors, VirusViral Fusion Proteins

Identifiers

PMID24530984
PMCPMC4028362

What OpenQuestion holds

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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.