Evidence map›Paper›PMID 27824121›Full record

ArticleScientific reports2016

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology.

Christopher R So, Kenan P Fears, Dagmar H Leary, Jenifer M Scancella, Zheng Wang, Jinny L Liu, Beatriz Orihuela, Dan Rittschof, Christopher M Spillmann, Kathryn J Wahl

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. TheProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

10 authors at 2 institutions in 1 country.

Christopher R SoChemistry Division, Code 6176, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Kenan P FearsChemistry Division, Code 6176, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Dagmar H LearyCenter for Biomolecular Science and Engineering, Code 6900, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Jenifer M ScancellaChemistry Division, Code 6176, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Zheng WangCenter for Biomolecular Science and Engineering, Code 6900, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Jinny L LiuCenter for Biomolecular Science and Engineering, Code 6900, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Beatriz OrihuelaNicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, 135 Duke Marine Lab Rd, Beaufort, NC, USA.
Dan RittschofNicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, 135 Duke Marine Lab Rd, Beaufort, NC, USA.
Christopher M SpillmannCenter for Biomolecular Science and Engineering, Code 6900, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
Kathryn J WahlChemistry Division, Code 6176, US Naval Research Laboratory, 4555 Overlook Ave, SW, Washington, DC, USA.
United States Naval Research Laboratory · USMarine Conservation Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Barnacles adhere by producing a mixture of cement proteins (CPs) that organize into a permanently bonded layer displayed as nanoscale fibers. These cement proteins share no homology with any other marine adhesives, and a common sequence-basis that defines how nanostructures function as adhesives remains undiscovered. Here we demonstrate that a significant unidentified portion of acorn barnacle cement is comprised of low complexity proteins; they are organized into repetitive sequence blocks and found to maintain homology to silk motifs. Proteomic analysis of aggregate bands from PAGE gels reveal an abundance of Gly/Ala/Ser/Thr repeats exemplified by a prominent, previously unidentified, 43 kDa protein in the solubilized adhesive. Low complexity regions found throughout the cement proteome, as well as multiple lysyl oxidases and peroxidases, establish homology with silk-associated materials such as fibroin, silk gum sericin, and pyriform spidroins from spider silk. Distinct primary structures defined by homologous domains shed light on how barnacles use low complexity in nanofibers to enable adhesion, and serves as a starting point for unraveling the molecular architecture of a robust and unique class of adhesive nanostructures.

Indexed as

AnimalsArthropod ProteinsCellulasesFibroinsMolecular WeightOxidoreductasesProteomicsSequence Analysis, RNASequence Homology, Amino AcidThoracicaArthropod ProteinsCellulasesFibroinsOxidoreductases

Identifiers

PMID27824121
PMCPMC5099703
OpenAlexW2557098556

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.