ArticleFrontiers in bioengineering and biotechnology2022
Biophysical Characterization of the Oligomeric States of Recombinant Immunoglobulins Type-M and Their C1q-Binding Kinetics by Biolayer Interferometry.
Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 0 citations in OpenAlex.
- The fc fragment of IgMs binds C1q to activate the first step of the classical complement pathway, while inhibiting complement-dependent cytotoxicity.The FEBS journal · 2026Article
- Defining the Features of Complement-Active IgM.Journal of molecular biology · 2025Article
- Interaction Studies of Hexameric and Pentameric IgMs with Serum-Derived C1q and Recombinant C1q Mimetics.Life (Basel, Switzerland) · 2024Article
- Protein-Protein Binding Kinetics by Biolayer Interferometry.Advances in experimental medicine and biology · 2024Article
- Investigation of dynamic solution interactions between NET-1 and UNC-5B by multi-wavelength analytical ultracentrifugation.European biophysics journal : EBJ · 2023Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Immunoglobulins type-M (IgMs) are one of the first antibody classes mobilized during immune responses against pathogens and tumor cells. Binding to specific target antigens enables the interaction with the C1 complex which strongly activates the classical complement pathway. This biological function is the basis for the huge therapeutic potential of IgMs. But, due to their high oligomeric complexity,
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