ArticlePloS one2015
Physical determinants of fibrinolysis in single fibrin fibers.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
- Thrombin-dependent nanoscale architecture and fibrinolytic remodeling of hydrated fibrin clots revealed by expansion microscopy.Journal of thrombosis and haemostasis : JTH · 2026Article
- Platelet-derived biomaterials in osteoporosis: mechanisms, evidence and translational prospects.Journal of biological engineering · 2026Review
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025Article
- A mathematical model of plasmin-mediated fibrinolysis of single fibrin fibers.PLoS computational biology · 2024Article
- Are all fibrinogen concentrates the same? The effects of two fibrinogen therapies in an afibrinogenemic patient and in a fibrinogen deficient plasma model. A clinical and laboratory case report.Frontiers in medicine · 2024Article
- Fibrinogen and fibrin: synthesis, structure, and function in health and disease.Journal of thrombosis and haemostasis : JTH · 2023Review
- A simplified mesoscale 3D model for characterizing fibrinolysis under flow conditions.Scientific reports · 2023Article
- Molecular engineering of cyclic azobenzene-peptide hybrid ligands for the purification of human blood Factor VIII via photo-affinity chromatography.Advanced functional materials · 2023Article
- Article
- Structural control of fibrin bioactivity by mechanical deformation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Engineered Molecular Therapeutics Targeting Fibrin and the Coagulation System: a Biophysical Perspective.Biophysical reviews · 2022Review
- Microscale structural changes of individual fibrin fibers during fibrinolysis.Acta biomaterialia · 2022Article
- The Utility and Potential of Mathematical Models in Predicting Fibrinolytic Outcomes.Current opinion in biomedical engineering · 2021Article
- Synthetic hydrogels as blood clot mimicking wound healing materials.Progress in biomedical engineering (Bristol, England) · 2021Article
- Inherent fibrin fiber tension propels mechanisms of network clearance during fibrinolysis.Acta biomaterialia · 2020Article
- Detection of Citrullinated Fibrin in Plasma Clots of Rheumatoid Arthritis Patients and Its Relation to Altered Structural Clot Properties, Disease-Related Inflammation and Prothrombotic Tendency.Frontiers in immunology · 2020Article
- Fibrinogen alpha amyloidosis: insights from proteomics.Expert review of proteomics · 2019Review
- The biophysics and mechanics of blood from a materials perspective.Nature reviews. Materials · 2019Article
- Fibrinogen and fibrin: An illustrated review.Research and practice in thrombosis and haemostasis · 2019Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Fibrin fibers form the structural backbone of blood clots; fibrinolysis is the process in which plasmin digests fibrin fibers, effectively regulating the size and duration of a clot. To understand blood clot dissolution, the influence of clot structure and fiber properties must be separated from the effects of enzyme kinetics and perfusion rates into clots. Using an inverted optical microscope and fluorescently-labeled fibers suspended between micropatterned ridges, we have directly measured the lysis of individual fibrin fibers. We found that during lysis 64 ± 6% of fibers were transected at one point, but 29 ± 3% of fibers increase in length rather than dissolving or being transected. Thrombin and plasmin dose-response experiments showed that the elongation behavior was independent of plasmin concentration, but was instead dependent on the concentration of thrombin used during fiber polymerization, which correlated inversely with fiber diameter. Thinner fibers were more likely to lyse, while fibers greater than 200 ± 30 nm in diameter were more likely to elongate. Because lysis rates were greatly reduced in elongated fibers, we hypothesize that plasmin activity depends on fiber strain. Using polymer physics- and continuum mechanics-based mathematical models, we show that fibers polymerize in a strained state and that thicker fibers lose their prestrain more rapidly than thinner fibers during lysis, which may explain why thick fibers elongate and thin fibers lyse. These results highlight how subtle differences in the diameter and prestrain of fibers could lead to dramatically different lytic susceptibilities.
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Registered trials
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.