ArticleThe Journal of biological chemistry2013
Assembly of subtype 1 influenza neuraminidase is driven by both the transmembrane and head domains.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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
38 citing papers in PubMed, 59 citations in OpenAlex.
- ELISA-based quantification of neuraminidase in commercial influenza vaccines using virus-derived reference antigens.Microbiology spectrum · 2026Article
- INAAC: An affinity chromatography strategy enabling characterization and quantification of influenza neuraminidase antigens in vaccines.The Journal of biological chemistry · 2026Article
- Influenza Neuraminidase Virus-Like Particle-Based Nanocarriers as a New Platform for the Delivery of Small-Peptide Antigens.Molecular biotechnology · 2026Article
- Article
- Broad neuraminidase antibodies confer protection against seasonal and avian influenza viruses.Nature communications · 2025Article
- Ultrapotent SARS coronavirus-neutralizing single-domain antibodies that clamp the spike at its base.Nature communications · 2025Article
- Fluorescence-barcoded cell lines stably expressing membrane-anchored influenza neuraminidases.Vaccine · 2025Article
- Recombinant expression and functional characterization of influenza A virus neuraminidase in a mammalian cell system.Frontiers in microbiology · 2025Article
- Boosting neuraminidase immunity in the presence of hemagglutinin with the next generation of influenza vaccines.NPJ vaccines · 2024Article
- Modulation of human-to-swine influenza a virus adaptation by the neuraminidase low-affinity calcium-binding pocket.Communications biology · 2024Article
- Capsid virus-like particle display improves recombinant influenza neuraminidase antigen stability and immunogenicity in mice.iScience · 2024Article
- Development of Digital Droplet PCR Targeting the Influenza H3N2 Oseltamivir-Resistant E119V Mutation and Its Performance through the Use of Reverse Genetics Mutants.Current issues in molecular biology · 2023Article
- Antigenic comparison of the neuraminidases from recent influenza A vaccine viruses and 2019-2020 circulating strains.NPJ vaccines · 2022Article
- Structure-based design of stabilized recombinant influenza neuraminidase tetramers.Nature communications · 2022Article
- Pre-existing antibodies directed against a tetramerizing domain enhance the immune response against artificially stabilized soluble tetrameric influenza neuraminidase.NPJ vaccines · 2022Article
- Influenza A Virus Neuraminidase Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Design of the Recombinant Influenza Neuraminidase Antigen Is Crucial for Its Biochemical Properties and Protective Efficacy.Journal of virology · 2021Article
- Influenza A viruses balance ER stress with host protein synthesis shutoff.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuraminidase (NA) is one of the two major influenza surface antigens and the main influenza drug target. Although NA has been well characterized and thought to function as a tetramer, the role of the transmembrane domain (TMD) in promoting proper NA assembly has not been systematically studied. Here, we demonstrate that in the absence of the TMD, NA is synthesized and transported in a predominantly inactive state. Substantial activity was rescued by progressive truncations of the stalk domain, suggesting the TMD contributes to NA maturation by tethering the stalk to the membrane. To analyze how the TMD supports NA assembly, the TMD was examined by itself. The NA TMD formed a homotetramer and efficiently trafficked to the plasma membrane, indicating the TMD and enzymatic head domain drive assembly together through matching oligomeric states. In support of this, an unrelated strong oligomeric TMD rescued almost full NA activity, whereas the weak oligomeric mutant of this TMD restored only half of wild type activity. These data illustrate that a large soluble domain can force assembly with a poorly compatible TMD; however, optimal assembly requires coordinated oligomerization between the TMD and the soluble domain.
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.