ArticleProceedings of the National Academy of Sciences of the United States of America2004
A duplicated motif controls assembly of zona pellucida domain proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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
67 citing papers in PubMed, 142 citations in OpenAlex.
- Transcriptomic Analysis ofInternational journal of molecular sciences · 2026Article
- Transcriptomic Analysis ofbioRxiv : the preprint server for biology · 2026Article
- A Lipocalin and a Hedgehog-related protein are partners in thebioRxiv : the preprint server for biology · 2026Article
- Spatially resolved gene expression analysis illuminates location-specific functions in the reef-building coral Pocillopora acuta.PloS one · 2026Article
- Crossing the barrier or how regulation of ovastacin controls fertilization and translates into clinical phenotypes.iScience · 2025Review
- SilencingInsects · 2025Article
- Enzymatic isolation of porcine preantral follicles impairs oocyte viability and long-term in vitro growth.The Journal of reproduction and development · 2025Article
- The Pax transcription factor EGL-38 links EGFR signaling to assembly of a cell type-specific apical extracellular matrix in the Caenorhabditis elegans vulva.Developmental biology · 2025Article
- Identification of Six Novel Proteins Containing a ZP Module from Nemertean Species.Biomolecules · 2024Article
- Novel Loss-of-function Variants of ZP3 Associated with Premature Ovarian Insufficiency.Reproductive sciences (Thousand Oaks, Calif.) · 2024Article
- Female fertility and the mammalian egg'sHistology and histopathology · 2024Review
- The Pax transcription factor EGL-38 links EGFR signaling to assembly of a cell-type specific apical extracellular matrix in thebioRxiv : the preprint server for biology · 2024Article
- Article
- Article
- A heterozygousiScience · 2023Article
- Initial detachment of the mouse oocyte from the zona pellucida is mediated by metallopeptidase activity†.Biology of reproduction · 2023Article
- Case report: A novel homozygous variant in ZP3 is associated with human empty follicle syndrome.Frontiers in genetics · 2023Article
- Zona Pellucida like Domain Protein 1 (ZPLD1) Polymerization Is Regulated by Two Distinguished Hydrophobic Motifs.International journal of molecular sciences · 2022Article
- Female fertility and the zona pellucida.eLife · 2022Review
- Zona Pellucida Genes and Proteins: Essential Players in Mammalian Oogenesis and Fertility.Genes · 2021Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer polymerize into filaments and extracellular matrices through zona pellucida (ZP) domains. ZP domain proteins are synthesized as precursors containing C-terminal propeptides that are cleaved at conserved sites. However, the consequences of this processing and the mechanism by which nascent proteins assemble are unclear. By microinjection of mutated DNA constructs into growing oocytes and mammalian cell transfection, we have identified a conserved duplicated motif [EHP (external hydrophobic patch)/IHP (internal hydrophobic patch)] regulating the assembly of mouse ZP proteins. Whereas the transmembrane domain (TMD) of ZP3 can be functionally replaced by an unrelated TMD, mutations in either EHP or IHP do not hinder secretion of full-length ZP3 but completely abolish its assembly. Because mutants truncated before the TMD are not processed, we conclude that the conserved TMD of mammalian ZP proteins does not engage them in specific interactions but is essential for C-terminal processing. Cleavage of ZP precursors results in loss of the EHP, thereby activating secreted polypeptides to assemble by using the IHP within the ZP domain. Taken together, these findings suggest a general mechanism for assembly of ZP domain proteins.
Indexed as
Identifiers
What 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.