ArticleBlood2026
Tissue transglutaminase drives fibrin β-chain cross-linking: a novel fibrin modification observed in patients with trauma.
Article in Blood, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Article
- Human Transglutaminases: Updated Insights into Activation Mechanisms, Allosteric Regulation and Disease.International journal of molecular sciences · 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
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
abstractCovalent cross-linking of fibrin by the plasma transglutaminase coagulation factor XIII (FXIII) is a key determinant of blood clot stability and function. FXIII-catalyzed formation of ε-N-(γ-glutamyl)-lysyl cross-links is restricted to the fibrin γ-chain and α-chain and follows thrombin-driven fibrin polymerization. Fibrinogen is also cross-linked by tissue transglutaminase (TG2) in a reaction favoring intramolecular and intermolecular α-γ cross-linking. Emerging evidence indicates that fibrinogen is a relevant substrate of TG2 in conditions of acute tissue damage. Remarkably, beyond detection of prototypical FXIII-directed cross-links (ie, α-α, γ-γ), we identified entirely novel covalent cross-links involving the fibrinogen β-chain (ie, β-α, via FGB-Q82). Addition of TG2 to in vitro clotting reactions and analysis of fibrin(ogen) in reducing conditions revealed loss of β-chain polypeptide paired with formation of high-molecular weight β-chain species. Mass spectrometry-based cross-linking proteomic analysis of in vitro clots recapitulated the precise TG2-directed β-chain cross-links observed in clots made using plasma from patients following traumatic injury. The results indicate in vitro and ex vivo cross-linking of the fibrin β-chain and highlight a novel example of TG2 emerging as a relevant plasma transglutaminase.
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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.