ArticleCommunications biology2022
Structural analysis of human CEACAM1 oligomerization.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Physics-Informed Artificial Intelligence Design of Picomolar Nanobodies Enables Deep Tumor Penetration and High-Contrast Imaging.Research (Washington, D.C.) · 2026Article
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- CEACAM1 in vascular homeostasis and inflammation.European journal of clinical investigation · 2024Review
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The human (h) CEACAM1 GFCC' face serves as a binding site for homophilic and heterophilic interactions with various microbial and host ligands. hCEACAM1 has also been observed to form oligomers and micro-clusters on the cell surface which are thought to regulate hCEACAM1-mediated signaling. However, the structural basis for hCEACAM1 higher-order oligomerization is currently unknown. To understand this, we report a hCEACAM1 IgV oligomer crystal structure which shows how GFCC' face-mediated homodimerization enables highly flexible ABED face interactions to arise. Structural modeling and nuclear magnetic resonance (NMR) studies predict that such oligomerization is not impeded by the presence of carbohydrate side-chain modifications. In addition, using UV spectroscopy and NMR studies, we show that oligomerization is further facilitated by the presence of a conserved metal ion (Zn
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Registered trials
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