ArticleiScience2023
Screening and characterization of inhibitory vNAR targeting nanodisc-assembled influenza M2 proteins.
Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 14 citations in OpenAlex.
- Camelid VHHs as a Versatile Platform for Combating Viral Infections.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Conformation and Membrane Topology of the N-Terminal Ectodomain of Influenza A M2 Protein.Membranes · 2025Article
- Unique antibodies across the animal kingdom (birds, camelids, and sharks): therapeutic potential against human respiratory viral infections.Frontiers in immunology · 2025Review
- VNAR: shark single-domain antibodies for the new era of medical biotechnology.Frontiers in immunology · 2025Review
- The application of nanodiscs in membrane protein drug discovery & development and drug delivery.Frontiers in chemistry · 2024Review
- Methods for Engineering Binders to Multi-Pass Membrane Proteins.Bioengineering (Basel, Switzerland) · 2023Review
- Shark IgNAR: The Next Broad Application Antibody in Clinical Diagnoses and Tumor Therapies?Marine drugs · 2023Review
Corrections and comments
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Authors and funding
27 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus poses a constant challenge to human health. The highly conserved influenza matrix-2 (M2) protein is an attractive target for the development of a universal antibody-based drug. However, screening using antigens with subphysiological conformation in a nonmembrane environment significantly reduces the generation of efficient antibodies. Here, M2(1-46) was incorporated into nanodiscs (M2-nanodiscs) with M2 in a membrane-embedded tetrameric conformation, closely resembling its natural physiological state in the influenza viral envelope. M2-nanodisc generation, an antigen, was followed by
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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 Socratic graph.