ArticleRSC advances2018
Immunoactivity of self-assembled antibodies investigated by atomic force microscopy.
Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 11 citations in OpenAlex.
- Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026Article
- Nanoscopic Assessment of Anti-SARS-CoV-2 Spike Neutralizing Antibody Using High-Speed AFM.Nano letters · 2023Article
- Tools shaping drug discovery and development.Biophysics reviews · 2022Review
- Strongyloidiasis Serological Analysis with Three Different Biological Probes and Their Electrochemical Responses in a Screen-Printed Gold Electrode.Sensors (Basel, Switzerland) · 2021Article
- On-Membrane Dynamic Interplay between Anti-GM1 IgG Antibodies and Complement Component C1q.International journal of molecular sciences · 2019Article
- Controlling the Self-Assembly of Biomolecules into Functional Nanomaterials through Internal Interactions and External Stimulations: A Review.Nanomaterials (Basel, Switzerland) · 2019Review
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 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin G (IgG), an antibody, plays a significant role in the immune system, and the functions of IgG molecules have been studied in many research fields such as medicine and engineering. Recently, we found the self-assembly of monoclonal mouse IgG molecules on a mica substrate using atomic force microscopy (AFM); the IgG molecules self-assemble into hexamers and the hexamers form a two-dimensional (2D) crystal. The self-assembly of the IgG molecules is of great interest in terms of the enhancement of the immunoactivity of the antibodies. In this study, we investigated the self-assembly of various IgG molecules on a mica substrate to discuss if the hexamerization of the IgG molecules is a general phenomenon. We also investigated the antigen binding site in the IgG antibody hexamers, and estimated the association rate constant of the self-assembled IgG molecules based on the AFM measurements. The estimated value was lower than that reported in a previous study probably because of the limited mobility of the antigen-binding fragments on the substrate.
Identifiers
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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.