ArticleJournal of molecular biology2025
Defining the Features of Complement-Active IgM.
Article in Journal of molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Article
- Effects of Replacing Soybean Meal with Different Proportions of Black Soldier Fly Larvae Meal on Antioxidant Indicators, Immune System, and Gut Health of Xichuan Black-Bone Chickens.Antioxidants (Basel, Switzerland) · 2026Article
- Exploring the structural basis and functional immunodynamics of immunoglobulin M in host defense against fungal pathogens.Frontiers in immunology · 2025Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Immunoglobulin M (IgM) is a class of mammalian antibody that is critical for the early stages of adaptive immunity, and is the most potent Ig-activator of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transitions within IgM upon antigen binding that promote the activation of complement component C1 remain unresolved. Here we examine in vitro complement activation, C1 binding kinetics, and conformational changes within IgM in different antigen-bound states. Binding studies using biolayer interferometry revealed that only in a multivalent complex with a surface-displayed antigen was IgM fully capable of initiating complement activation. Hydrogen/Deuterium exchange with mass spectrometry revealed the predominant structural changes within the Fc domains during transition to the active conformation. Collectively, this work establishes key structural and functional qualities that define the complement-active form of IgM.
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Registered trials
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