ArticleJournal of virology2012
Reversible inhibition of fusion activity of a paramyxovirus fusion protein by an engineered disulfide bond in the membrane-proximal external region.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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.
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Who cites it
10 citing papers in PubMed.
- Review
- Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide.The Journal of membrane biology · 2022Review
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Transmembrane Domain Dissociation Is Required for Hendra Virus F Protein Fusogenic Activity.Journal of virology · 2019Article
- Flexibility of the Head-Stalk Linker Domain of Paramyxovirus HN Glycoprotein Is Essential for Triggering Virus Fusion.Journal of virology · 2016Article
- Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.Journal of virology · 2015Article
- A Cysteine Zipper Stabilizes a Pre-Fusion F Glycoprotein Vaccine for Respiratory Syncytial Virus.PloS one · 2015Article
- Unity in diversity: shared mechanism of entry among paramyxoviruses.Progress in molecular biology and translational science · 2015Review
- Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Cysteines were introduced into the membrane-proximal external region (MPER) of the paramyxovirus F protein. A disulfide bond formed, and the mutant protein was expressed at the cell surface but was fusion inactive. Reduction of the disulfide bond restored fusion activity. The data indicate that in addition to dissociation of the three-helix bundle stalk domain of prefusion F, the MPER region also needs to separate for F to be able to refold and cause fusion.
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Registered trials
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.