Evidence map›Paper›PMID 21044602›Full record

ArticleBiophysical journal2010

Evidence that αC region is origin of low modulus, high extensibility, and strain stiffening in fibrin fibers.

John R Houser, Nathan E Hudson, Lifang Ping, E Timothy O'Brien, Richard Superfine, Susan T Lord, Michael R Falvo

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 75 citations in OpenAlex.

  1. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
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  5. Rupture mechanics of blood clot fibrin fibers: A coarse-grained model study.Journal of the mechanics and physics of solids · 2025
    Article
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  10. Review
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  19. Fibrinogen and fibrin: An illustrated review.Research and practice in thrombosis and haemostasis · 2019
    Review
  20. 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

7 authors at 1 institution in 1 country.

John R HouserDepartment of Physics and Astronomy, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Nathan E Hudson
Lifang Ping
E Timothy O'Brien
Richard Superfine
Susan T Lord
Michael R Falvo
University of North Carolina at Chapel Hill · US

Funding

INTERACTIVE GRAPHICS FOR MOLECULAR STUDIES &MICROSCOPYP41EB002025 · NIBIB · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUPERFINE, RICHARD · 2003 to 2019
$16.9M
MUTAGENIC STUDIES OF FIBRINOGEN ALPHA CHAIN FUNCTIONR01HL031048 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LORD, SUSAN T · 1987 to 2010
$3.5M
A GENETIC APPROACH TO THE FIBRINOGEN-FIBRIN CONVERSIONR23HL031048 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI LORD, SUSAN T · 1985 to 1986
–
NHLBI NIH HHS HL31048NHLBI NIH HHS R01 HL031048NIBIB NIH HHS P41 EB002025NIBIB NIH HHS P41-EB002025
6 · The paper itself

Abstract

Fibrin fibers form the structural scaffold of blood clots and perform the mechanical task of stemming blood flow. Several decades of investigation of fibrin fiber networks using macroscopic techniques have revealed remarkable mechanical properties. More recently, the microscopic origins of fibrin's mechanics have been probed through direct measurements on single fibrin fibers and individual fibrinogen molecules. Using a nanomanipulation system, we investigated the mechanical properties of individual fibrin fibers. The fibers were stretched with the atomic force microscope, and stress-versus-strain data was collected for fibers formed with and without ligation by the activated transglutaminase factor XIII (FXIIIa). We observed that ligation with FXIIIa nearly doubled the stiffness of the fibers. The stress-versus-strain behavior indicates that fibrin fibers exhibit properties similar to other elastomeric biopolymers. We propose a mechanical model that fits our observed force extension data, is consistent with the results of the ligation data, and suggests that the large observed extensibility in fibrin fibers is mediated by the natively unfolded regions of the molecule. Although some models attribute fibrin's force-versus-extension behavior to unfolding of structured regions within the monomer, our analysis argues that these models are inconsistent with the measured extensibility and elastic modulus.

Indexed as

Models, MolecularBiomechanical PhenomenaBiophysical PhenomenaBlood CoagulationElastic ModulusElastomersFactor XIIIaFibrinHumansIn Vitro TechniquesMicroscopy, Atomic ForceModels, BiologicalProtein Structure, TertiaryRecombinant ProteinsStress, MechanicalTensile StrengthElastomersFactor XIIIaFibrinRecombinant Proteins

Identifiers

PMID21044602
PMCPMC2965937
OpenAlexW2150290852

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.