ArticleThe Journal of biological chemistry2020
A mutation in the kringle domain of human factor XII that causes autoinflammation, disturbs zymogen quiescence, and accelerates activation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 24 citations in OpenAlex.
- Crystal structure of coagulation factor XII N-terminal domains 1-5.Acta crystallographica. Section D, Structural biology · 2025Article
- A brief comparison of human factor XII-AlaResearch and practice in thrombosis and haemostasis · 2025Article
- Factor XII Structure-Function Relationships.Seminars in thrombosis and hemostasis · 2024Review
- A single-domain antibody targeting factor XII inhibits both thrombosis and inflammation.Nature communications · 2024Article
- Tale of two systems: the intertwining duality of fibrinolysis and lipoprotein metabolism.Journal of thrombosis and haemostasis : JTH · 2023Review
- Genetic Variants Leading to Urticaria and Angioedema and Associated Biomarkers.The journal of allergy and clinical immunology. In practice · 2023Article
- Mechanisms involved in hereditary angioedema with normal C1-inhibitor activity.Frontiers in physiology · 2023Review
- Model for surface-dependent factor XII activation: the roles of factor XII heavy chain domains.Blood advances · 2022Article
- Identification of the factor XII contact activation site enables sensitive coagulation diagnostics.Nature communications · 2021Article
- Illustrated State-of-the-Art Capsules of the ISTH 2020 Congress.Research and practice in thrombosis and haemostasis · 2021Review
- A Pathophysiological Perspective on the SARS-CoV-2 Coagulopathy.HemaSphere · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coagulation factor XII (FXII) drives production of the inflammatory peptide bradykinin. Pathological mutations in the
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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.