ArticleBlood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis2010
Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance.
Article in Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 24 citations in OpenAlex.
- Soluble tissue factor generated by necroptosis-triggered shedding is responsible for thrombosis.Cell research · 2025Article
- Article
- Coagulation factor VIIa binds to herpes simplex virus 1-encoded glycoprotein C forming a factor X-enhanced tenase complex oriented on membranes.Journal of thrombosis and haemostasis : JTH · 2020Article
- Tissue Factor Prothrombotic Activity Is Regulated by Integrin-arf6 Trafficking.Arteriosclerosis, thrombosis, and vascular biology · 2017Article
- Synergies of phosphatidylserine and protein disulfide isomerase in tissue factor activation.Thrombosis and haemostasis · 2014Review
- Analysis of tissue factor expression in various cell model systems: cryptic vs. active.Journal of thrombosis and haemostasis : JTH · 2013Article
- Regulation of tissue factor coagulant activity on cell surfaces.Journal of thrombosis and haemostasis : JTH · 2012Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Kinetic analysis of the tissue factor (TF)-factor VIIa (FVIIa) binding interaction is helpful in investigating the structure-function relationships of TF-FVIIa. However, a wide variation exists among the reported binding affinities of FVIIa to TF, particularly when comparing KD values obtained from functional activity assays versus ligand binding studies. Surface plasmon resonance (SPR) technique was used frequently to investigate binding kinetics of FVIIa to TF in a lipid-free environment. In the present study we used TF embedded in a phospholipid bilayer for determining binding kinectis using SPR. The data revealed that FVIIa had a much higher binding affinity (>100-fold) for TF embedded in the phospholiid bilayer than TF in a lipid-free environment, approaching the KD values that were noted in the enzymatic activity assays. The present data suggest that SPR binding studies using TF embedded in phospholipids is more appropriate for investigating how FVIIa (or FVIIa mutants/derivatives) may interact with TF in physiological settings.
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Registered trials
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