ArticleNature communications2024
A single-domain antibody targeting factor XII inhibits both thrombosis and inflammation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
What it found
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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
18 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Factor XII-A New Therapeutic Target? A Systematic Review.International journal of molecular sciences · 2026Pooled it
- Engineering bioactive citrate-based hydrogels for wound repair: From structure-function design to microenvironmental regulation.Bioactive materials · 2027Review
- Deep learning-guided high-throughput screening and molecular dynamics simulations facilitate the discovery of potential FXIIa inhibitors.Journal of molecular modeling · 2026Article
- Potential Role of Contact Pathway Factors in Catheter-Related Thrombosis: Emerging Evidence and Therapeutic Strategies.Biomolecules · 2026Review
- Nanobodies targeting SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2026Review
- Chemical proteomics reveals sinomenine's anti-inflammatory mechanism through serum protein covalent modification.Chinese medicine · 2026Article
- A Snail Galactosed Glycosaminoglycan Inhibits Thrombosis without Affecting Hemostasis via Disrupting FIXa-FVIIIa Complex Generation.ACS central science · 2026Article
- Developing Safer Anticoagulant Candidates: Structure-Activity Relationship Studies of 5-Amino-Triazole-Based FXIIa Inhibitors.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2026Article
- Factor XII in Thrombosis and Thromboinflammation: From Molecular Biology to Clinical Translation.International journal of molecular sciences · 2026Review
- Bannakunin: a dual-target Kunitz inhibitor bridging anticoagulation (FXa/XIIa) and anti-platelet (α2β1/P2Y12) pathways.Cellular & molecular biology letters · 2026Article
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Tinkering with Blood: Optimizing the Coagulation System for Therapeutic Purposes.Bioengineering (Basel, Switzerland) · 2025Review
- Sonodynamic and Bioorthogonal Sonocatalytic Thrombotic Therapy Based on AIE Cationic Tetranuclear Ir(III) Complex Nanoplatform Guided by NIR-Chemiluminescence Imaging.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Targeting hemostatic enzymes: from mechanistic insights to therapeutic frontiers.Current opinion in hematology · 2025Review
- Unveiling the role of coagulation-related genes in acute myeloid leukemia prognosis and immune microenvironment through machine learning.European journal of medical research · 2025Article
- Factor XII-driven coagulation traps bacterial infections.The Journal of experimental medicine · 2025Article
- Coagulation Factor XII Is an Antibacterial Protein That Acts Against Bacterial Infection via Its Heavy Chain.International journal of molecular sciences · 2025Article
- Advancements in research on the thrombo-inflammation mechanisms mediated by factor XII in ischemic stroke.Journal of thrombosis and thrombolysis · 2025Review
Corrections and comments
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Authors and funding
17 authors.
Funding
Abstract
Factor XII (FXII) is the zymogen of the plasma protease FXIIa that activates the intrinsic coagulation pathway and the kallikrein kinin-system. The role of FXII in inflammation has been obscure. Here, we report a single-domain antibody (nanobody, Nb) fused to the Fc region of a human immunoglobulin (Nb-Fc) that recognizes FXII in a conformation-dependent manner and interferes with FXIIa formation. Nb-Fc treatment inhibited arterial thrombosis in male mice without affecting hemostasis. In a mouse model of extracorporeal membrane oxygenation (ECMO), FXII inhibition or knockout reduced thrombus deposition on oxygenator membranes and systemic microvascular thrombi. ECMO increased circulating levels of D-dimer, alkaline phosphatase, creatinine and TNF-α and triggered microvascular neutrophil adherence, platelet aggregation and their interaction, which were substantially attenuated by FXII blockade. Both Nb-Fc treatment and FXII knockout markedly ameliorated immune complex-induced local vasculitis and anti-neutrophil cytoplasmic antibody-induced systemic vasculitis, consistent with selectively suppressed neutrophil migration. In human blood microfluidic analysis, Nb-Fc treatment prevented collagen-induced fibrin deposition and neutrophil adhesion/activation. Thus, FXII is an important mediator of inflammatory responses in vasculitis and ECMO, and Nb-Fc provides a promising approach to alleviate thrombo-inflammatory disorders.
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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.