Evidence map›Paper›PMID 24733908›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Sea star tenacity mediated by a protein that fragments, then aggregates.

Elise Hennebert, Ruddy Wattiez, Mélanie Demeuldre, Peter Ladurner, Dong Soo Hwang, J Herbert Waite, Patrick Flammang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
12.0field-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

45 citing papers in PubMed, 90 citations in OpenAlex.

  1. Tube feet dynamics drive adaptation in sea star locomotion.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  10. The Involvement of Cell-Type-Specific Glycans inBiomimetics (Basel, Switzerland) · 2022
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  13. Review
  14. Decoding the byssus fabrication by spatiotemporal secretome analysis of scallop foot.Computational and structural biotechnology journal · 2022
    Article
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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

7 authors at 4 institutions in 4 countries.

Elise HennebertLaboratory of Biology of Marine Organisms and Biomimetics, Research Institute for Biosciences, University of Mons, 7000 Mons, Belgium.
Ruddy Wattiez
Mélanie Demeuldre
Peter Ladurner
Dong Soo Hwang
J Herbert Waite
Patrick Flammang
University of Mons · BEPohang University of Science and Technology · KRUniversität Innsbruck · ATUniversity of California, Santa Barbara · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sea stars adhere firmly but temporarily to various substrata as a result of underwater efficient adhesive secretions released by their tube feet. Previous studies showed that this material is mainly made up of proteins, which play a key role in its adhesiveness and cohesiveness. Recently, we solubilized the majority of these proteins and obtained 43 de novo-generated peptide sequences by tandem MS. Here, one of these sequences served to recover the full-length sequence of Sea star footprint protein 1 (Sfp1), by RT-PCR and tube foot transcriptome analysis. Sfp1, a large protein of 3,853 aa, is the second most abundant constituent of the secreted adhesive. By using MS and Western blot analyses, we showed that Sfp1 is translated from a single mRNA and then cleaved into four subunits linked together by disulphide bridges in tube foot adhesive cells. The four subunits display specific protein-, carbohydrate-, and metal-binding domains. Immunohistochemistry and immunocytochemistry located Sfp1 in granules stockpiled by one of the two types of adhesive cells responsible for the secretion of the adhesive material. We also demonstrated that Sfp1 makes up the structural scaffold of the adhesive footprint that remains on the substratum after tube foot detachment. Taken together, the results suggest that Sfp1 is a major structural protein involved in footprint cohesion and possibly in adhesive interactions with the tube foot surface. In recombinant form, it could be used for the design of novel sea star-inspired biomaterials.

Indexed as

AdhesivenessAnimalsAnimal StructuresMolecular Sequence DataProtein BindingProteinsProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsStarfishProteinsProtein SubunitsAsterias rubensechinodermsmarine adhesion

Identifiers

PMID24733908
PMCPMC4035948
OpenAlexW2045318028

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.