ArticleNature communications2023
The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function.
Article in Nature communications, 2023. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Ellagic Acid Mitigates Lead (Pb)-Induced Toxicity inAntioxidants (Basel, Switzerland) · 2026Article
- Novel function of Teleost skin: Antigen excretion across the epidermis mediated by secretory IgMFundamental research · 2026Article
- Article
- Chimeric Immunoglobulin and human Immunoglobulin M structures provide insights on joining-chain independent assembly and function.bioRxiv : the preprint server for biology · 2025Article
- Unusual traits shape the architecture of the Ig ancestor molecule.Communications biology · 2025Article
- Evolution of the Immunoglobulin Isotypes-Variations of Biophysical Properties among Animal Classes.Biomolecules · 2023Article
Corrections and comments
- Update of
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Polymeric (p) immunoglobulins (Igs) serve broad functions during vertebrate immune responses. Typically, pIgs contain between two and six Ig monomers, each with two antigen binding fragments and one fragment crystallization (Fc). In addition, many pIgs assemble with a joining-chain (JC); however, the number of monomers and potential to include JC vary with species and heavy chain class. Here, we report the cryo-electron microscopy structure of IgM from a teleost (t) species, which does not encode JC. The structure reveals four tIgM Fcs linked through eight C-terminal tailpieces (Tps), which adopt a single β-sandwich-like domain (Tp assembly) located between two Fcs. Specifically, two of eight heavy chains fold uniquely, resulting in a structure distinct from mammalian IgM, which typically contains five IgM monomers, one JC and a centrally-located Tp assembly. Together with mutational analysis, structural data indicate that pIgs have evolved a range of assembly mechanisms and structures, each likely to support unique antibody effector functions.
Indexed as
Identifiers
What OpenQuestion holds
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.