Evidence map›Paper›PMID 19794156›Full record

ArticleBiology of reproduction2010

Zonadhesin D3-polypeptides vary among species but are similar in Equus species capable of interbreeding.

Steve Tardif, Heidi A Brady, Kelly R Breazeale, Ming Bi, Leslie D Thompson, Jason E Bruemmer, Laura B Bailey, Daniel M Hardy

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biology of reproduction, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Comparative Study on the Sperm Proteomes of Horses and Donkeys.Animals : an open access journal from MDPI · 2024
    Article
  2. Article
  3. Article
  4. Review
  5. Sperm function tests in clinical practice.Turkish journal of urology · 2017
    Review
  6. Article
  7. Review
  8. 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

8 authors at 3 institutions in 1 country.

Steve TardifDepartment of Cell Biology & Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA.
Heidi A Brady
Kelly R Breazeale
Ming Bi
Leslie D Thompson
Jason E Bruemmer
Laura B Bailey
Daniel M Hardy
Texas Tech University · USColorado State University · USTexas Tech University Health Sciences Center · US

Funding

FUNCTIONS OF PROTEIN DOMAINS IN GAMETE INTERACTIONSR29HD035166 · NICHD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI HARDY, DANIEL M · 1998 to 2002
$320k
NICHD NIH HHS HD-35166
6 · The paper itself

Abstract

Zonadhesin is a rapidly evolving protein in the sperm acrosome that confers species specificity to sperm-zona pellucida adhesion. Though structural variation in zonadhesin likely contributes to its species-specific function, the protein has not previously been characterized in organisms capable of interbreeding. Here we compared properties of zonadhesin in several animals, including the horse (Equus caballus), donkey (E. asinus), and Grevy's zebra (E. grevyi) to determine if variation in zonadhesin correlates with ability of gametes to cross-fertilize. Zonadhesin localized to the apical acrosomes of spermatozoa from all three Equus species, similar to its localization in other animals. Likewise, in horse and donkey testis, zonadhesin was detected only in germ cells, first in the acrosomal granule of round spermatids and then in the developing acrosomes of elongating spermatids. Among non-Equus species, D3-domain polypeptides of mature, processed zonadhesin varied markedly in size and detergent solubility. However, zonadhesin D3-domain polypeptides in horse, donkey, and zebra spermatozoa exhibited identical electrophoretic mobility and detergent solubility. Equus zonadhesin D3-polypeptides (p110/p80 doublet) were most similar in size to porcine and bovine zonadhesin D3-polypeptides (p105). Sequence comparisons revealed that the horse zonadhesin precursor's domain content and arrangement are similar to those of zonadhesin from other large animals. Partial sequences of horse and donkey zonadhesin were much more similar to each other (>99% identity) than they were to orthologous sequences of human, pig, rabbit, and mouse zonadhesin (52%-72% identity). We conclude that conservation of zonadhesin D3-polypeptide properties correlates with ability of Equus species to interbreed.

Indexed as

AcrosomeAmino Acid SequenceAnimalsBreedingEquidaeFemaleFertilizationHorsesHumansMaleMembrane ProteinsMolecular Sequence DataSolubilitySpecies SpecificitySpermatozoaMembrane Proteinszonadhesin

Identifiers

PMID19794156
PMCPMC2809229
OpenAlexW2145534942

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.