ArticleBiophysical journal2012
Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen.
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 56 papers, 1 of them a synthesis that pooled it.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Effects of Post-Translational Modifications of Fibrinogen on Clot Formation, Clot Structure, and Fibrinolysis: A Systematic Review.Arteriosclerosis, thrombosis, and vascular biology · 2020Pooled it
- Reduced protein carbonylation on hormone therapy is associated with improved fibrinolysis in postmenopausal women: the impact of PAI-1 and TAFI activity.Journal of thrombosis and thrombolysis · 2024Trial
- Fibrin formation and lysis in hyperglycaemia - molecular and cellular drivers.Current opinion in hematology · 2026Review
- Structure-functionality relationship of collagen-fibrin interpenetrating hydrogels for engineered tumor-stroma models.Acta biomaterialia · 2026Article
- Protein carbonylation as a modulator of fibrin clot properties in thyroid disorders: impact of therapy.Journal of thrombosis and thrombolysis · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Investigating PolySTAT's role in clot contraction and fibrin network mechanics.Biomaterials science · 2025Article
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Acetaldehyde exposure alters fibrin polymerization, fibrinolysis, and fibrin network structureResearch and practice in thrombosis and haemostasis · 2025Article
- Fibrinogen Oxidation and Thrombosis: Shaping Structure and Function.Antioxidants (Basel, Switzerland) · 2025Review
- Fibrinogen post-translational modifications are biochemical determinants of fibrin clot properties and interactions.The FEBS journal · 2025Review
- Fibrinogen Structural Changes and Their Potential Role in Endometriosis-Related Thrombosis.Antioxidants (Basel, Switzerland) · 2024Article
- Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation.Molecular biomedicine · 2024Review
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Trauma-induced dysfibrinogenemia: the von Clauss assay does not accurately measure fibrinogen levels after injury.Blood vessels, thrombosis & hemostasis · 2024Article
- Cysteine and methionine oxidation in thrombotic disorders.Current opinion in chemical biology · 2023Review
- Acoustic droplet vaporization for on-demand modulation of microporosity in smart hydrogels.Acta biomaterialia · 2023Article
- Re-mining serum proteomics data reveals extensive post-translational modifications upon Zika and dengue infection.Molecular omics · 2023Article
- Plasma-Derived Fibrin Hydrogels Containing Graphene Oxide for Infections Treatment.ACS materials letters · 2023Article
- Natural Polyphenols May Normalize Hypochlorous Acid-Evoked Hemostatic Abnormalities in Human Blood.Antioxidants (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Using a combination of structural and mechanical characterization, we examine the effect of fibrinogen oxidation on the formation of fibrin clots. We find that treatment with hypochlorous acid preferentially oxidizes specific methionine residues on the α, β, and γ chains of fibrinogen. Oxidation is associated with the formation of a dense network of thin fibers after activation by thrombin. Additionally, both the linear and nonlinear mechanical properties of oxidized fibrin gels are found to be altered with oxidation. Finally, the structural modifications induced by oxidation are associated with delayed fibrin lysis via plasminogen and tissue plasminogen activator. Based on these results, we speculate that methionine oxidation of specific residues may be related to hindered lateral aggregation of protofibrils in fibrin gels.
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