ReviewVirology2015
Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.
Review in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
68 citing papers in PubMed, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Protection against lethal canine distemper virus infection by a dual epitope-targeting synthetic antibody.Nature communications · 2026Article
- Proximity labelling of internalizing influenza A viruses reveals a role for neogenin in virus uptake.PLoS pathogens · 2025Article
- Comparative pathology of ducks experimentally inoculated with three different recombinant Newcastle disease viruses.The Journal of veterinary medical science · 2025Article
- Molecular Evolution of theMicroorganisms · 2025Article
- Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies.Nature microbiology · 2024Article
- Unraveling dynamics of paramyxovirus-receptor interactions using nanoparticles displaying hemagglutinin-neuraminidase.PLoS pathogens · 2024Article
- Structural basis for potent neutralization of human respirovirus type 3 by protective single-domain camelid antibodies.Nature communications · 2024Article
- Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein.Nature communications · 2024Article
- Structural Studies of Henipavirus Glycoproteins.Viruses · 2024Review
- The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus.Nature communications · 2024Article
- Suppression of viral RNA polymerase activity is necessary for persistent infection during the transformation of measles virus into SSPE virus.PLoS pathogens · 2023Article
- Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.Journal of virology · 2023Article
- Potently neutralizing human mAbs against the zoonotic pararubulavirus Sosuga virus.JCI insight · 2023Article
- Kinetic analysis of paramyxovirus-sialoglycan receptor interactions reveals virion motility.PLoS pathogens · 2023Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
- Structure and supramolecular organization of the canine distemper virus attachment glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Respiratory Syncytial Virus (RSV) G Protein Enhances the Immune Responses to the RSV F Protein in an Enveloped Virus-Like Particle Vaccine Candidate.Journal of virology · 2023Article
- Influenza A Virus M1 Protein Non-Specifically Deforms Charged Lipid Membranes and Specifically Interacts with the Raft Boundary.Membranes · 2023Article
- Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The Paramyxoviridae include some of the great and ubiquitous disease-causing viruses of humans and animals. In most paramyxoviruses, two viral membrane glycoproteins, fusion protein (F) and receptor binding protein (HN, H or G) mediate a concerted process of recognition of host cell surface molecules followed by fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. The interactions between the F and HN, H or G viral glycoproteins and host molecules are critical in determining host range, virulence and spread of these viruses. Recently, atomic structures, together with biochemical and biophysical studies, have provided major insights into how these two viral glycoproteins successfully interact with host receptors on cellular membranes and initiate the membrane fusion process to gain entry into cells. These studies highlight the conserved core mechanisms of paramyxovirus entry that provide the fundamental basis for rational anti-viral drug design and vaccine development.
Indexed as
Identifiers
What OpenQuestion holds
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.