ArticleCell2017
Structural Basis of Egg Coat-Sperm Recognition at Fertilization.
Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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.
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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
46 citing papers in PubMed, 109 citations in OpenAlex.
- Spatiotemporal translation of sperm acrosome associated proteins during early capacitation modulates sperm fertilizing ability.Journal of advanced research · 2026Article
- Zona pellucida-inspired smart viral vectors: a biomimetic platform for multi-modal immune evasion and triple-stimuli responsive gene delivery.Frontiers in bioengineering and biotechnology · 2026Article
- A scalable equivariant graph network framework for precise protein function prediction.Genome biology · 2025Article
- Crossing the barrier or how regulation of ovastacin controls fertilization and translates into clinical phenotypes.iScience · 2025Review
- Structural basis of ZP2-targeted female nonhormonal contraception.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- CIROZ is dispensable in ancestral vertebrates but essential for left-right patterning in humans.American journal of human genetics · 2025Article
- Identification of Six Novel Proteins Containing a ZP Module from Nemertean Species.Biomolecules · 2024Article
- Involvement of Metalloproteases in the Fertilization of the AscidianBiomolecules · 2024Article
- Mapping the proteome landscape of Indian Zebu (Sahiwal) spermatozoa using high-resolution mass spectrometry andAnimal biotechnology · 2024Article
- The conserved genetic program of male germ cells uncovers ancient regulators of human spermatogenesis.eLife · 2024Article
- Female fertility and the mammalian egg'sHistology and histopathology · 2024Review
- ZP2: the precision regulator of egg coat architecture during fertilization.Science China. Life sciences · 2024Article
- Article
- Article
- Divergent molecular signatures in fish Bouncer proteins define cross-fertilization boundaries.Nature communications · 2023Article
- Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins.Nature communications · 2022Article
- Mechanisms of Sperm-Egg Interactions: What Ascidian Fertilization Research Has Taught Us.Cells · 2022Review
- Domain Expansion and Functional Diversification in Vertebrate Reproductive Proteins.Molecular biology and evolution · 2022Article
- Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH.Nature structural & molecular biology · 2022Article
- Identification of Sperm-Binding Sites in the N-Terminal Domain of Bovine Egg Coat Glycoprotein ZP4.International journal of molecular sciences · 2022Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.
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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.