ArticleThe Journal of biological chemistry2012
A bipartite autoinhibitory region within the B-domain suppresses function in factor V.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed.
- [From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2026Review
- Basic regions of factor V and tissue factor pathway inhibitor mediate heavy chain and acidic region interactions on factor V revealed by tethered chemical cleavage.Journal of thrombosis and haemostasis : JTH · 2025Article
- Article
- Structural architecture of the acidic region of the B domain of coagulation factor V.Journal of thrombosis and haemostasis : JTH · 2024Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- Factor V variants in bleeding and thrombosis.Research and practice in thrombosis and haemostasis · 2024Article
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- A hydrophobic patch (PLVIVG; 1481-1486) in the B-domain of factor V-short is crucial for its synergistic TFPIα-cofactor activity with protein S and for the formation of the FXa-inhibitory complex comprising FV-short, TFPIα, and protein S.Journal of thrombosis and haemostasis : JTH · 2022Article
- Factor V east Texas variant causes bleeding in a three-generation family.Journal of thrombosis and haemostasis : JTH · 2022Article
- Major bleeding during oral anticoagulant therapy associated with factor V activation by factor Xa.Journal of thrombosis and haemostasis : JTH · 2022Article
- A Novel Phenotype of the Factor 5 Gene Mutation (Homozygote Met1736Val and Heterozygote Asp68His) Is Associated With Moderate Factor V Deficiency.Frontiers in medicine · 2022Article
- ptFVa (Arteriosclerosis, thrombosis, and vascular biology · 2021Article
- F5-Atlanta: A novel mutation in F5 associated with enhanced East Texas splicing and FV-short production.Journal of thrombosis and haemostasis : JTH · 2021Article
- F5-Atlanta: Factor V-short strikes again.Journal of thrombosis and haemostasis : JTH · 2021Article
- Structure-function of anticoagulant TIX-5, the inhibitor of factor Xa-mediated FV activation.Journal of thrombosis and haemostasis : JTH · 2021Article
- Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding.Journal of thrombosis and haemostasis : JTH · 2019Review
- Occlusion of anion-binding exosite 2 in meizothrombin explains its impaired ability to activate factor V.The Journal of biological chemistry · 2019Article
- Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors.Research and practice in thrombosis and haemostasis · 2018Article
- TFPIα interacts with FVa and FXa to inhibit prothrombinase during the initiation of coagulation.Blood advances · 2017Article
- Factor V has an anticoagulant cofactor activity that targets the early phase of coagulation.The Journal of biological chemistry · 2017Article
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.
Funding
Abstract
Activation of blood coagulation factor V (FV) is a key reaction of hemostasis. FV circulates in plasma as an inactive procofactor, and proteolytic removal of a large central B-domain converts it to an active cofactor (FVa) for factor Xa (FXa). Here we show that two short evolutionary conserved segments of the B-domain, together termed the procofactor regulatory region, serve an essential autoinhibitory function. This newly identified motif consists of a basic (963-1008) and an acidic (1493-1537) region and defines the minimal sequence requirements to maintain FV as a procofactor. Our data suggest that dismantling this autoinhibitory region via deletion or proteolysis is the driving force to unveil a high affinity binding site(s) for FXa. These findings document an unexpected sequence-specific role for the B-domain by negatively regulating FV function and preventing activity of the procofactor. These new mechanistic insights point to new ways in which the FV procofactor to cofactor transition could be modulated to alter hemostasis.
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.