Evidence map›Paper›PMID 29679324›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Controlling Fibrin Network Morphology, Polymerization, and Degradation Dynamics in Fibrin Gels for Promoting Tissue Repair.

Erin P Sproul, Riley T Hannan, Ashley C Brown

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  7. Biologic principles of minced cartilage implantation: a narrative review.Archives of orthopaedic and trauma surgery · 2023
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  18. Clot Structure and Implications for Bleeding and Thrombosis.Seminars in thrombosis and hemostasis · 2020
    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

3 authors at 3 institutions in 1 country.

Erin P SproulJoint Department of Biomedical Engineering, North Carolina State University and The University of North Carolina at Chapel Hill, Raleigh, NC, USA.
Riley T HannanDepartment of Pathology, University of Virginia, Charlottesville, VA, USA.
Ashley C BrownJoint Department of Biomedical Engineering, North Carolina State University and The University of North Carolina at Chapel Hill, Raleigh, NC, USA. aecarso2@ncsu.edu.
North Carolina State University · USUniversity of North Carolina at Chapel Hill · USUniversity of Virginia · US

Funding

American Heart Association-American Stroke Association 16SDG29870005
6 · The paper itself

Abstract

Fibrin is an integral part of the clotting cascade and is formed by polymerization of the soluble plasma protein fibrinogen. Following stimulation of the coagulation cascade, thrombin activates fibrinogen, which binds to adjacent fibrin(ogen) molecules resulting in the formation of an insoluble fibrin matrix. This fibrin network is the primary protein component in clots and subsequently provides a scaffold for infiltrating cells during tissue repair. Due to its role in hemostasis and tissue repair, fibrin has been used extensively as a tissue sealant. Clinically used fibrin tissue sealants require supraphysiological concentrations of fibrinogen and thrombin to achieve fast polymerization kinetics, which results in extremely dense fibrin networks that are inhibitory to cell infiltration. Therefore, there is much interest in developing fibrin-modifying strategies to achieve rapid polymerization dynamics while maintaining a network structure that promotes cell infiltration. The properties of fibrin-based materials can be finely controlled through techniques that modulate fibrin polymerization dynamics or through the inclusion of fibrin-modifying biomaterials. Here, we describe methods for characterizing fibrin network morphology, polymerization, and degradation (fibrinolysis) dynamics in fibrin constructs for achieving fast polymerization dynamics while promoting cell infiltration.

Indexed as

Biocompatible MaterialsFibrinGelsProtein MultimerizationBiological AssayFibrinolysisHumansMicroscopy, ConfocalPolymerizationTissue EngineeringWound HealingBiocompatible MaterialsFibrinGelsBiomaterialsClot formationFibrinFibrin-based biomaterialsFibrinogenHemostasisTissue engineeringWound healing

Identifiers

PMID29679324
PMCPMC12989979
OpenAlexW2801353301

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.