Evidence map›Paper›PMID 28704418›Full record

ArticlePloS one2017

The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

J Des Parkin, James D San Antonio, Anton V Persikov, Hayat Dagher, Raymond Dalgleish, Shane T Jensen, Xavier Jeunemaitre, Judy Savige

Abstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Echocardiographic Assessment in Patients with Vascular Ehlers-Danlos Syndrome: Insights from an Unexplored Field.High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2025
    Article
  8. Article
  9. Article
  10. The Effects of Aging on the Intramuscular Connective Tissue.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Regenerative Scar-Free Skin Wound Healing.Tissue engineering. Part B, Reviews · 2019
    Review
  19. Review
  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

8 authors.

J Des ParkinFrom the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.
James D San AntonioOperations, Stryker Global Quality and Operations, Malvern, PA, United States of America.
Anton V PersikovLewis-Sigler Institute for Integrative Genomics, Princeton University, Carl Icahn Lab, Princeton, NJ, United States of America.
Hayat DagherFrom the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.
Raymond DalgleishDepartment of Genetics, University of Leicester, Leicester, United Kingdom.
Shane T JensenWharton Business School, University of Pennsylvania, Philadelphia, PA, United States of America.
Xavier JeunemaitreINSERM U970 Paris Cardiovascular Research Centre, Paris France.
Judy SavigeFrom the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0002-6813-0288

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.

Indexed as

HemostasisAmino Acid SequenceBinding SitesCollagen Type IIIHumansIntegrin alpha2beta1Platelet Membrane GlycoproteinsProtein BindingProtein Interaction MapsProtein Stabilityvon Willebrand FactorCollagen Type IIIIntegrin alpha2beta1Platelet Membrane Glycoproteinsplatelet membrane glycoprotein VIvon Willebrand Factor

Identifiers

PMID28704418
PMCPMC5509119

What OpenQuestion holds

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Registered trials

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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.