ArticleCommunications biology2024
Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 10 citations in OpenAlex.
- A sequentially activated afterglow probe for AND-gated imaging of alpha-fetoprotein in hepatocellular carcinoma.Bioactive materials · 2027Article
- Machine Learning-Assisted SERS Quantification of Sialylated Alpha-Fetoprotein: From Single-Cell Analysis to Hepatocellular Carcinoma Risk Assessment.Small methods · 2026Article
- Alpha-Fetoprotein Stimulates Cleavage of Membranal MICA/B on Liver Cancer Cell Lead to Escape Immune Surveillance of Natural Killer Cells.Journal of cellular and molecular medicine · 2026Article
- Exploring the Multifunctional Role of Alpha-Fetoprotein in Cancer Progression: Implications for Targeted Therapy in Hepatocellular Carcinoma and Beyond.International journal of molecular sciences · 2025Review
- Sugar symphony: glycosylation in cancer metabolism and stemness.Trends in cell biology · 2025Review
- Properties of the major ZnChemical communications (Cambridge, England) · 2025Article
- HCC-Derived Alpha-Fetoprotein Impairs Bone Regeneration by Impairing Autophagic Flux and Promoting Runx2 Degradation in Osteoblasts.BioFactors (Oxford, England)Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-fetoprotein (AFP), a serum glycoprotein, is expressed during embryonic development and the pathogenesis of liver cancer. It serves as a clinical tumor marker, function as a carcinogen, immune suppressor, and transport vehicle; but the detailed AFP structural information has not yet been reported. In this study, we used single-particle cryo-electron microscopy(cryo-EM) to analyze the structure of the recombinant AFP obtained a 3.31 Å cryo-EM structure and built an atomic model of AFP. We observed and identified certain structural features of AFP, including N-glycosylation at Asn251, four natural fatty acids bound to distinct domains, and the coordination of metal ions by residues His22, His264, His268, and Asp280. Furthermore, we compared the structural similarities and differences between AFP and human serum albumin. The elucidation of AFP's structural characteristics not only contributes to a deeper understanding of its functional mechanisms, but also provides a structural basis for developing AFP-based drug vehicles.
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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.