Evidence map›Paper›PMID 23062346›Full record

ArticleBiophysical journal2012

A modular fibrinogen model that captures the stress-strain behavior of fibrin fibers.

Rodney D Averett, Bryant Menn, Eric H Lee, Christine C Helms, Thomas Barker, Martin Guthold

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
  2. Rupture mechanics of blood clot fibrin fibers: A coarse-grained model study.Journal of the mechanics and physics of solids · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
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  13. Article
  14. Article
  15. Article
  16. Fibrin mechanical properties and their structural origins.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Review
  17. Biophysical Mechanisms Mediating Fibrin Fiber Lysis.BioMed research international · 2017
    Review
  18. Fibrin Formation, Structure and Properties.Sub-cellular biochemistry · 2017
    Review
  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

6 authors at 3 institutions in 1 country.

Rodney D AverettWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University School of Medicine, Atlanta, GA, USA.
Bryant Menn
Eric H Lee
Christine C Helms
Thomas Barker
Martin Guthold
Georgia Institute of Technology · USWake Forest University · USUniversity of Illinois Urbana-Champaign · US

Funding

Effects of Diabetes on the Multiscale Mechanical Behavior of Clot StructuresK01HL115486 · NHLBI · UNIVERSITY OF GEORGIA · PI AVERETT, RODNEY D · 2012 to 2016
$697k
NHLBI NIH HHS K01 HL115486
6 · The paper itself

Abstract

We tested what to our knowledge is a new computational model for fibrin fiber mechanical behavior. The model is composed of three distinct elements: the folded fibrinogen core as seen in the crystal structure, the unstructured α-C connector, and the partially folded α-C domain. Previous studies have highlighted the importance of all three regions and how they may contribute to fibrin fiber stress-strain behavior. Yet no molecular model has been computationally tested that takes into account the individual contributions of all these regions. Constant velocity, steered molecular dynamics studies at 0.025 Å/ps were conducted on the folded fibrinogen core and the α-C domain to determine their force-displacement behavior. A wormlike chain model with a persistence length of 0.8 nm (Kuhn length = 1.6 nm) was used to model the mechanical behavior of the unfolded α-C connector. The three components were combined to calculate the total stress-strain response, which was then compared to experimental data. The results show that the three-component model successfully captures the experimentally determined stress-strain behavior of fibrin fibers. The model evinces the key contribution of the α-C domains to fibrin fiber stress-strain behavior. However, conversion of the α-helical coiled coils to β-strands, and partial unfolding of the protein, may also contribute.

Indexed as

Molecular Dynamics SimulationStress, MechanicalAnimalsBiomechanical PhenomenaBlood CoagulationCattleElasticityFibrinFibrinogenProtein FoldingProtein Structure, TertiaryFibrinFibrinogen

Identifiers

PMID23062346
PMCPMC3471473
OpenAlexW2072721575

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.