ReviewMolecular biomedicine2024
Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation.
Review in Molecular biomedicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- Crosstalk between lactylation and other post-translational modifications in health and diseases.Molecular biomedicine · 2026Review
- Histone and non-histone protein acetylation in a tail regeneration model (Ambystoma mexicanum).Biology open · 2026Article
- 3D Fibrin/Gelatin Hydrogel System Enhances the Therapeutic Potency of DPSC-Derived Extracellular Vesicles Compared to 2D Culture in Accelerating Diabetic Wound Healing via Angiogenesis and Immune Modulation.Journal of functional biomaterials · 2026Article
- Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen.Protein science : a publication of the Protein Society · 2026Article
- Feminizing and masculinizing gender-affirming hormone therapy affects fibrin clot characteristics in opposite directions.Research and practice in thrombosis and haemostasis · 2026Article
- Natural Polymers in Tissue Engineering and Regeneration: Material-Cell Mechanotransduction, Biofabrication Strategies, and Clinical Translation.Biomedicines · 2026Review
- Fibrinogen and Fibrin as Growth Factor Regulators: Pathological Implications, and Translational Opportunities.Biomolecules · 2026Review
- Protein carbonylation as a modulator of fibrin clot properties in thyroid disorders: impact of therapy.Journal of thrombosis and thrombolysis · 2026Article
- Purification, characterization, and anticoagulant mechanism of an anticoagulant protein from marineFrontiers in microbiology · 2026Article
- Dysfibrinogenemia and elevated anti-cyclic citrullinated peptide antibodies: a rare and intriguing case.Archives of medical science : AMS · 2026Article
- Fibrinogen in extracellular matrix remodeling: functional switching, source heterogeneity, and biomaterial translation.Frontiers in cell and developmental biology · 2026Review
- Glycosylation Profiles in Cardiovascular Diseases: A Bibliometric Analysis.Health data science · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Predictive Value of the FDAPR Index for Ischemic Stroke in Patients with Coronary Heart Disease: A Machine Learning Study Based on a Multilayer Perceptron.International journal of general medicine · 2026Article
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Exploring the Antimicrobial and Antiviral Properties of Cryptic Peptides from Human Fibrinogen.International journal of molecular sciences · 2025Article
- Reactive Nitrogen Species and Fibrinogen: Exploring the Effects of Nitration on Blood Clots.Antioxidants (Basel, Switzerland) · 2025Review
- Exploring Plasma Proteome Thermal Stability in Peripheral Arterial Disease: Biophysical Findings Under Cilostazol Therapy.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Homocysteinylation of Fibrinogen: A Post-Translational Link to Thrombosis.International journal of molecular sciences · 2025Review
- Fibrinogen Oxidation and Thrombosis: Shaping Structure and Function.Antioxidants (Basel, Switzerland) · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Fibrinogen, a blood plasma protein with a key role in hemostasis and thrombosis, is highly susceptible to post-translational modifications (PTMs), that significantly influence clot formation, structure, and stability. These PTMs, which include acetylation, amidation, carbamylation, citrullination, dichlorination, glycation, glycosylation, guanidinylation, hydroxylation, homocysteinylation, malonylation, methylation, nitration, oxidation, phosphorylation and sulphation, can alter fibrinogen biochemical properties and affect its functional behavior in coagulation and fibrinolysis. Oxidation and nitration are notably associated with oxidative stress, impacting fibrin fiber formation and promoting the development of more compact and resistant fibrin networks. Glycosylation and glycation contribute to altered fibrinogen structural properties, often resulting in changes in fibrin clot density and susceptibility to lysis, particularly in metabolic disorders like diabetes. Acetylation and phosphorylation, influenced by medications such as aspirin, modulate clot architecture by affecting fiber thickness and clot permeability. Citrullination and homocysteinylation, although less studied, are linked to autoimmune conditions and cardiovascular diseases, respectively, affecting fibrin formation and stability. Understanding these modifications provides insights into the pathophysiology of thrombotic disorders and highlights potential therapeutic targets. This review comprehensively examines the current literature on fibrinogen PTMs, their specific sites, biochemical pathways, and their consequences on fibrin clot architecture, clot formation and clot lysis.
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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 Socratic graph.