ArticleNature2016
Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
84 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.
- The Role of Sperm Proteins IZUMO1 and TMEM95 in Mammalian Fertilization: A Systematic Review.International journal of molecular sciences · 2022Pooled it
- Molecular determinants of species-specific gamete adhesion triggering HAP2-mediated membrane fusion.Nature communications · 2026Article
- Rat DCST1 and DCST2 are essential for sperm-egg fusion†.Biology of reproduction · 2026Article
- Comparative sperm proteomics in IVF patients with differential fertilization rates identifies FAM205A as a novel biomarker for male infertility.Asian journal of andrology · 2026Article
- Molecular interplay between sperm and oocyte: a narrative review.Human reproduction update · 2026Review
- Sperm surface protein disulfide isomerase ERp57 is crucial for mammalian fertilization but functions independently of IZUMO1.Cellular & molecular biology letters · 2026Article
- The SPARK complex forms the molecular basis of vertebrate fertilization.bioRxiv : the preprint server for biology · 2026Article
- JUNO-coated beads as a functional assay to capture and characterize fertilization-competent human sperm.Human reproduction open · 2026Article
- Membrane Fusions During Mammalian Fertilization.Advances in experimental medicine and biology · 2026Review
- TheBiomolecules · 2025Review
- Spermatozoa lacking TEX51 display hypofertility and defects in morphology.Communications biology · 2025Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Molecular mechanisms leading to gamete fusion.Fukushima journal of medical science · 2025Review
- CRISPR/Cas9-mediated genome editing reveals seven testis-enriched transmembrane glycoproteins dispensable for male fertility in mice.Andrology · 2025Article
- PRAMEY enhances sperm-egg binding and modulates epigenetic dynamics in bovine embryogenesis.Cell and tissue research · 2025Article
- Allosteric inhibition of the IZUMO1-JUNO fertilization complex by the naturally occurring antisperm antibody OBF13.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A narrative review of sperm selection technology for assisted reproduction techniques.Translational andrology and urology · 2024Review
- SCM-198 ameliorates the quality of postovulatory and maternally aged oocytes by reducing oxidative stress.Journal of ovarian research · 2024Article
- Prediction of Pesticide Interactions with Proteins Involved in Human Reproduction by Using a Virtual Screening Approach: A Case Study of Famoxadone Binding CRBP-III and Izumo.International journal of molecular sciences · 2024Article
- Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fertilization is a fundamental process in sexual reproduction, creating a new individual through the combination of male and female gametes. The IZUMO1 sperm membrane protein and its counterpart oocyte receptor JUNO have been identified as essential factors for sperm-oocyte interaction and fusion. However, the mechanism underlying their specific recognition remains poorly defined. Here, we show the crystal structures of human IZUMO1, JUNO and the IZUMO1-JUNO complex, establishing the structural basis for the IZUMO1-JUNO-mediated sperm-oocyte interaction. IZUMO1 exhibits an elongated rod-shaped structure comprised of a helical bundle IZUMO domain and an immunoglobulin-like domain that are each firmly anchored to an intervening β-hairpin region through conserved disulfide bonds. The central β-hairpin region of IZUMO1 provides the main platform for JUNO binding, while the surface located behind the putative JUNO ligand binding pocket is involved in IZUMO1 binding. Structure-based mutagenesis analysis confirms the biological importance of the IZUMO1-JUNO interaction. This structure provides a major step towards elucidating an essential phase of fertilization and it will contribute to the development of new therapeutic interventions for fertility, such as contraceptive agents.
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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.