Evidence map›Paper›PMID 29348201›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution.

Damien B Wilburn, Lisa M Tuttle, Rachel E Klevit, Willie J Swanson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  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. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Egg Coat Proteins Across Metazoan Evolution.Current topics in developmental biology · 2018
    Review
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

4 authors at 1 institution in 1 country.

Damien B WilburnDepartment of Genome Sciences, University of Washington, Seattle, WA 98195; dwilburn@u.washington.edu.ORCID 0000-0002-1255-9982
Lisa M TuttleDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Rachel E KlevitDepartment of Biochemistry, University of Washington, Seattle, WA 98195.ORCID 0000-0002-3476-969X
Willie J SwansonDepartment of Genome Sciences, University of Washington, Seattle, WA 98195.
University of Washington · US

Funding

Detailed functional analysis of gamete recognition protein interactionsR01HD076862 · NICHD · UNIVERSITY OF WASHINGTON · PI SWANSON, WILLIE J · 2014 to 2018
$1.9M
Structural mechanisms and evolution of egg-sperm interactionsF32GM116298 · NIGMS · UNIVERSITY OF WASHINGTON · PI WILBURN, DAMIEN BEAU · 2015 to 2017
$109k
NICHD NIH HHS R01 HD076862NIGMS NIH HHS F32 GM116298
6 · The paper itself

Abstract

Protein evolution is driven by the sum of different physiochemical and genetic processes that usually results in strong purifying selection to maintain biochemical functions. However, proteins that are part of systems under arms race dynamics often evolve at unparalleled rates that can produce atypical biochemical properties. In the marine mollusk abalone, lysin and vitelline envelope receptor for lysin (VERL) are a pair of rapidly coevolving proteins that are essential for species-specific interactions between sperm and egg. Despite extensive biochemical characterization of lysin-including crystal structures of multiple orthologs-it was unclear how sites under positive selection may facilitate recognition of VERL. Using a combination of targeted mutagenesis and multidimensional NMR, we present a high-definition solution structure of sperm lysin from red abalone (

Indexed as

Evolution, MolecularAnimalsBinding SitesGastropodaMagnetic Resonance SpectroscopyMaleModels, MolecularMolecular Dynamics SimulationMucoproteinsMutagenesis, Site-DirectedProtein MultimerizationSpermatozoalysin, gastropodaMucoproteinsfertilizationnuclear magnetic resonancesexual selection

Identifiers

PMID29348201
PMCPMC5819389
OpenAlexW2727157635

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.