ArticleScientific reports2017
Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026Review
- Native N-glycome profiling of single cells and ng-level blood isolates using label-free capillary electrophoresis-mass spectrometry.Nature communications · 2024Article
- Structural basis for Fc receptor recognition of immunoglobulin M.Nature structural & molecular biology · 2023Article
- Plasmodium falciparum has evolved multiple mechanisms to hijack human immunoglobulin M.Nature communications · 2023Article
- An Unexpected Role for Cell Density Rather than IgM in Cell-Surface Display of the Fc Receptor for IgM on Human Lymphocytes.ImmunoHorizons · 2022Article
- Sialylation as an Important Regulator of Antibody Function.Frontiers in immunology · 2022Review
- Differences between Human and Mouse IgM Fc Receptor (FcµR).International journal of molecular sciences · 2021Article
- Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes.Communications biology · 2021Article
- Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021Article
- Identification of Amino Acid Residues in Human IgM Fc Receptor (FcµR) Critical for IgM Binding.Frontiers in immunology · 2020Article
- Mapping of the binding site for FcμR in human IgM-Fc.Biochimica et biophysica acta. Proteins and proteomics · 2020Article
- Genetic Diversity ofAnimals : an open access journal from MDPI · 2019Article
- Secreted IgM: New tricks for an old molecule.Journal of leukocyte biology · 2019Review
- A generalized quantitative antibody homeostasis model: maintenance of global antibody equilibrium by effector functions.Clinical & translational immunology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
IgM is the first antibody to be produced in immune responses and plays an important role in the neutralization of bacteria and viruses. Human IgM is heavily glycosylated, featuring five N-linked glycan sites on the μ chain and one on the J-chain. Glycosylation of IgG is known to modulate the effector functions of Fcγ receptors. In contrast, little is known about the effect of glycosylation on IgM binding to the human Fcμ receptor (hFCMR). In this study, we identify the Cμ4 domain of IgM as the target of hFCMR, and show that binding and internalization of IgM by hFCMR is glycan-independent. We generated a homology-based structure for hFCMR and used molecular dynamic simulations to show how this interaction with IgM may occur. Finally, we reveal an inhibitory function for IgM in the proliferation of T cells.
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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.