Evidence map›Paper›PMID 9192632›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule.

W J Swanson, V D Vacquier

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

35 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Molecular mechanisms and evolution of fertilization proteins.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2021
    Review
  7. 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
  8. Article
  9. Article
  10. Article
  11. Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Egg Coat Proteins Across Metazoan Evolution.Current topics in developmental biology · 2018
    Review
  13. Genomic Signatures of Sexual Conflict.The Journal of heredity · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Detecting coevolution in mammalian sperm-egg fusion proteins.Molecular reproduction and development · 2014
    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

2 authors at 1 institution in 1 country.

W J SwansonMarine Biology Research Division, Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093-0202, USA.
V D Vacquier
Scripps Institution of Oceanography · US

Funding

BIOCHEMISTRY OF SPERM-EGG INTERACTION AND FERTILIZATIONR37HD012986 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VACQUIER, VICTOR D · 1997 to 2006
$3.1M
BIOCHEMISTRY OF SPERM-EGG INTERACTION AND FERTILIZATIONR01HD012986 · NICHD · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI VACQUIER, VICTOR D · 1985 to 1996
–
NICHD NIH HHS HD12986NICHD NIH HHS R37 HD012986
6 · The paper itself

Abstract

Abalone sperm lysin is a 16-kDa acrosomal protein, which nonenzymatically and species selectively creates a hole in the egg vitelline envelope (VE) through which the sperm passes to reach the egg cell membrane. The crystal structures of both monomeric and dimeric lysins have been solved and the sequences of lysins from 20 abalone species have been determined. As a first step in understanding the molecular mechanism by which lysin creates a hole in the VE, its VE receptor was isolated. The VE receptor for lysin (VERL) is an unbranched, rod-like molecule with an approximate relative molecular mass of 2 million; half the mass being carbohydrate. Fluorescence polarization studies showed positive cooperativity in the binding of lysin to VERL (EC50 approximately 9 nM) and were consistent with the species selectivity of lysin in dissolving VEs. Each molecule of VERL bound between 126 and 142 molecules of monomeric lysin (two independent assays), showing that VERL possesses repetitive lysin-binding motifs.

Indexed as

AnimalsEgg ProteinsFemaleLigandsMaleMolluscaMucoproteinsOvumReceptors, Cell SurfaceSpermatozoaSperm-Ovum InteractionsVitelline MembraneEgg ProteinsLigandslysin, gastropodaMucoproteinsReceptors, Cell SurfaceVERL protein, Haliotis

Identifiers

PMID9192632
PMCPMC21225
OpenAlexW1986971453

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.