ReviewInternational journal of molecular sciences2021
Fibrin(ogen) as a Therapeutic Target: Opportunities and Challenges.
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Advanced hydrogel therapeutics for intervertebral disc degeneration: Engineering structural-functional properties in natural and synthetic biomaterials.Bioengineering & translational medicine · 2025Review
- Fibrinogen Oxidation and Thrombosis: Shaping Structure and Function.Antioxidants (Basel, Switzerland) · 2025Review
- Albumin/fibrinogen ratio (AFR): a significant predictor of postoperative delirium in older patients undergoing non-neurosurgical and non-cardiac surgery.BMC geriatrics · 2025Article
- Exploiting the Molecular Properties of Fibrinogen to Control Bleeding Following Vascular Injury.International journal of molecular sciences · 2025Review
- Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025Article
- Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation.Molecular biomedicine · 2024Review
- Dietary Antioxidants and Natural Compounds in Preventing Thrombosis and Cardiovascular Disease.International journal of molecular sciences · 2024Review
- Harmony in Healing: Investigating Platelet-Rich Plasma Activation during Acetylsalicylic Acid Treatment.International journal of molecular sciences · 2024Article
- Fbg αC 389-402 Enhances Factor XIII Cross-Linking in the Fibrinogen αC Region Via Electrostatic and Hydrophobic Interactions.Biochemistry · 2023Article
- Comparative proteomics of human milk casein fraction collected from women of Korean and Han ethnic groups in China.Frontiers in nutrition · 2023Article
- Advances in Fibrin-Based Materials in Wound Repair: A Review.Molecules (Basel, Switzerland) · 2022Review
- Integration of Metabolomics and Proteomics in Exploring the Endothelial Dysfunction Mechanism Induced by Serum Exosomes From Diabetic Retinopathy and Diabetic Nephropathy Patients.Frontiers in endocrinology · 2022Article
- Fibrinogen and Antifibrinolytic Proteins: Interactions and Future Therapeutics.International journal of molecular sciences · 2021Review
- Combination of D-dimer and Albumin in the Prediction of Deep Vein Thrombosis in Patients with Spontaneous Intracerebral Hemorrhage.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/HemostasisArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Fibrinogen is one of the key molecular players in haemostasis. Thrombin-mediated release of fibrinopeptides from fibrinogen converts this soluble protein into a network of fibrin fibres that form a building block for blood clots. Thrombin-activated factor XIII further crosslinks the fibrin fibres and incorporates antifibrinolytic proteins into the network, thus stabilising the clot. The conversion of fibrinogen to fibrin also exposes binding sites for fibrinolytic proteins to limit clot formation and avoid unwanted extension of the fibrin fibres. Altered clot structure and/or incorporation of antifibrinolytic proteins into fibrin networks disturbs the delicate equilibrium between clot formation and lysis, resulting in either unstable clots (predisposing to bleeding events) or persistent clots that are resistant to lysis (increasing risk of thrombosis). In this review, we discuss the factors responsible for alterations in fibrin(ogen) that can modulate clot stability, in turn predisposing to abnormal haemostasis. We also explore the mechanistic pathways that may allow the use of fibrinogen as a potential therapeutic target to treat vascular thrombosis or bleeding disorders. Better understanding of fibrinogen function will help to devise future effective and safe therapies to modulate thrombosis and bleeding risk, while maintaining the fine balance between clot formation and lysis.
Indexed as
Identifiers
What OpenQuestion holds
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.