Evidence map›Paper›PMID 23335731›Full record

ReviewMolecular human reproduction2013

The molecular basis of gamete recognition in mice and humans.

Matteo A Avella, Bo Xiong, Jurrien Dean

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular human reproduction, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
13.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.

  1. Pooled it
  2. Sexual selection and pseudogenization in primate fertilization.Evolution; international journal of organic evolution · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Biomolecules · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. The conserved fertility factor SPACA4/Bouncer has divergent modes of action in vertebrate fertilization.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Matteo A AvellaLaboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA. matteo.avella@nih.gov
Bo Xiong
Jurrien Dean
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Molecular Biology of the OocyteZIADK015603 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI DEAN, JURRIEN · 2009 to 2025
$43.2M
Intramural NIH HHS
6 · The paper itself

Abstract

Successful fertilization heralds the onset of development and requires both gamete recognition and a definitive block to polyspermy. Sperm initially bind and penetrate the extracellular zona pellucida (ZP) that surrounds ovulated eggs, but are unable to bind the zona surrounding preimplantation embryos. The ZP of humans is composed of four (ZP1-4) and that of mouse three (ZP1-3) glycoproteins. Models for gamete recognition developed in mice had proposed that sperm bind to ZP3 glycans. However, phenotypes observed in genetically engineered mice are not consistent with this widely accepted model. More recently, taking advantage of the observation that human sperm do not bind to mouse eggs, human ZP2 was defined as the zona ligand in transgenic mouse models using gain-of-function assays. The sperm-binding site is an N-terminal domain of ZP2 that is cleaved by ovastacin, a metalloendoprotease released from egg cortical granules following fertilization. Proteolysis of this docking site provides a definitive block to polyspermy as sperm bind to uncleaved, but not cleaved ZP2 even after fertilization and cortical granule exocytosis. While progress has been made in defining the ZP ligand, less headway has been made in identifying the cognate sperm receptor. Although a number of sperm receptor candidates have been documented to interact with specific proteins in the ZP in vitro, continued fertility after genetic ablation of the cognate gene indicates that none are essential for gamete recognition. These on-going investigations inform reproductive medicine and suggest new therapies to improve fertility and/or provide contraception, thus expanding reproductive choices for human couples.

Indexed as

AnimalsEgg ProteinsFemaleGene Expression Regulation, DevelopmentalHumansMaleMembrane GlycoproteinsMetalloproteasesMiceMice, TransgenicProtein Structure, TertiaryProteolysisReceptors, Cell SurfaceSpermatozoaSperm-Ovum InteractionsZona PellucidaASTL protein, humanEgg ProteinsMembrane GlycoproteinsMetalloproteasesReceptors, Cell SurfaceZona Pellucida GlycoproteinsZP1 protein, humanZp1 protein, mouseZP2 protein, humanZp2 protein, mouseZP3 protein, humanZp3 protein, mouse

Identifiers

PMID23335731
PMCPMC3632220
OpenAlexW2158795116

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.