ArticleNature2008
Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats.
Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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
64 citing papers in PubMed.
- Molecular interplay between sperm and oocyte: a narrative review.Human reproduction update · 2026Review
- Co-Option and Conflict: The Deep Evolutionary History of ZP-Domain Proteins from ECMs to Species Barriers.International journal of molecular sciences · 2026Review
- PES-8 is required for Cytoskeletal Organization and Contractility in thebioRxiv : the preprint server for biology · 2026Article
- Genetic variation in zona pellucida-3 (ZP3) gene and its association with litter size variation in Kari sheep.Animal biotechnology · 2025Article
- A high-resolution N-glycoproteome landscape of aging mouse ovary.Redox biology · 2025Article
- 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
- Domain Expansion and Functional Diversification in Vertebrate Reproductive Proteins.Molecular biology and evolution · 2022Article
- Comparative Proteomics of theGenes · 2022Article
- Embryological Characteristics of Human Oocytes With Agar-Like Zona Pellucida and Its Clinical Treatment Strategy.Frontiers in endocrinology · 2022Article
- Recurrent Co-Option and Recombination of Cytokine and Three Finger Proteins in Multiple Reproductive Tissues Throughout Salamander Evolution.Frontiers in cell and developmental biology · 2022Article
- The Importance of Gene Duplication and Domain Repeat Expansion for the Function and Evolution of Fertilization Proteins.Frontiers in cell and developmental biology · 2022Review
- Gene Spectrum and Clinical Traits of Nine Patients With Oocyte Maturation Arrest.Frontiers in genetics · 2022Article
- Empty Zona Pellucida Only Case: A Critical Review of the Literature.International journal of environmental research and public health · 2021Review
- Zona Pellucida Genes and Proteins: Essential Players in Mammalian Oogenesis and Fertility.Genes · 2021Review
- Proteomics support the threespine stickleback egg coat as a protective oocyte envelope.Molecular reproduction and development · 2021Article
- Article
- Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.The EMBO journal · 2020Article
- A C. elegans Zona Pellucida domain protein functions via its ZPc domain.PLoS genetics · 2020Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
5 authors.
Funding
Abstract
Species-specific recognition between the egg extracellular matrix (zona pellucida) and sperm is the first, crucial step of mammalian fertilization. Zona pellucida filament components ZP3 and ZP2 act as sperm receptors, and mice lacking either of the corresponding genes produce oocytes without a zona pellucida and are completely infertile. Like their counterparts in the vitelline envelope of non-mammalian eggs and many other secreted eukaryotic proteins, zona pellucida subunits polymerize using a 'zona pellucida (ZP) domain' module, whose conserved amino-terminal part (ZP-N) was suggested to constitute a domain of its own. No atomic structure has been reported for ZP domain proteins, and there is no structural information on any conserved vertebrate protein that is essential for fertilization and directly involved in egg-sperm binding. Here we describe the 2.3 ångström (A) resolution structure of the ZP-N fragment of mouse primary sperm receptor ZP3. The ZP-N fold defines a new immunoglobulin superfamily subtype with a beta-sheet extension characterized by an E' strand and an invariant tyrosine residue implicated in polymerization. The structure strongly supports the presence of ZP-N repeats within the N-terminal region of ZP2 and other vertebrate zona pellucida/vitelline envelope proteins, with implications for overall egg coat architecture, the post-fertilization block to polyspermy and speciation. Moreover, it provides an important framework for understanding human diseases caused by mutations in ZP domain proteins and developing new methods of non-hormonal contraception.
Indexed as
Identifiers
19052627What 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.