Evidence map›Paper›PMID 24056097›Full record

ReviewActa biomaterialia2014

Fibrin-based biomaterials: modulation of macroscopic properties through rational design at the molecular level.

Ashley C Brown, Thomas H Barker

Abstract readReview
In one paragraph

Review in Acta biomaterialia, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 2 pooled it
9.7field-weighted citation impact, top 2% 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

114 citing papers in PubMed, 2 syntheses or guidelines pooled it, 268 citations in OpenAlex.

  1. Pooled it
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  11. Flow diverter surface modifications for aneurysm treatment: A review of the mechanisms and data behind existing technologies.Interventional neuroradiology : journal of peritherapeutic neuroradiology, surgical procedures and related neurosciences · 2026
    Review
  12. Cyclic mechanical stimulation of TDCs improves tendon tissue maturationFrontiers in bioengineering and biotechnology · 2026
    Article
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54 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Ashley C BrownThe School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA; The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA.
Thomas H BarkerThe Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA; The Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. Electronic address: thomas.barker@bme.gatech.edu.
Georgia Institute of Technology · US

Funding

Engineering fibrin polymers for enhanced angiogenesisR01EB011566 · NIBIB · GEORGIA INSTITUTE OF TECHNOLOGY · PI BARKER, THOMAS HARRISON · 2010 to 2013
$1.5M
Fibrinogen-Triggered Matrix Assembly from Designed Peptide-Polymer ConjugatesR21EB013743 · NIBIB · GEORGIA INSTITUTE OF TECHNOLOGY · PI BARKER, THOMAS HARRISON, LYON, LOUIS ANDREW · 2012 to 2013
$384k
NIBIB NIH HHS R01 EB011566NIBIB NIH HHS R21 EB013743
6 · The paper itself

Abstract

Fibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury. Because of these properties and the ease of polymerization of the material, fibrin has been widely utilized as a biomaterial for over a century. Modifying the macroscopic properties of fibrin, such as elasticity and porosity, has been somewhat elusive until recently, yet with a molecular-level rational design approach it can now be somewhat easily modified through alterations of molecular interactions key to the protein's polymerization process. This review outlines the biochemistry of fibrin and discusses methods for modification of molecular interactions and their application to fibrin based biomaterials.

Indexed as

AnimalsBiocompatible MaterialsFibrinHumansPolymerizationProteolysisTissue EngineeringBiocompatible MaterialsFibrinBiomaterial designFibrinFibrin glueTissue engineeringWound repair

Identifiers

PMID24056097
PMCPMC3960324
OpenAlexW2006293762

What OpenQuestion holds

Textmetadata
LicenceTDM
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.