ArticleBlood2009
Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations.
Article in Blood, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- The genomic origins and evolutionary path to a key innovation in the world's most venomous snakes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The genomic origins and evolutionary path to a key innovation in the world's most venomous snakes.bioRxiv : the preprint server for biology · 2026Article
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- Potential Application of Recombinant Snake Prothrombin Activator Ecarin in Blood Diagnostics.Biomolecules · 2022Article
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- ptFVa (Arteriosclerosis, thrombosis, and vascular biology · 2021Article
- Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding.Journal of thrombosis and haemostasis : JTH · 2019Review
- Snakebites and microvesicles: Popping bubbles.Research and practice in thrombosis and haemostasis · 2019Article
- Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors.Nature communications · 2017Article
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- A bipartite autoinhibitory region within the B-domain suppresses function in factor V.The Journal of biological chemistry · 2012Article
- A new look at blood coagulation factor V.Current opinion in hematology · 2011Review
- Blood coagulation factors V and VIII: Molecular Mechanisms of Procofactor Activation.Journal of coagulation disorders · 2010Article
- Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom.Toxins · 2010Review
- The molecular basis of factor V and VIII procofactor activation.Journal of thrombosis and haemostasis : JTH · 2009Review
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Venomous snakes produce an array of toxic compounds, including procoagulants to defend themselves and incapacitate prey. The Australian snake Pseudonaja textilis has a venom-derived prothrombin activator homologous to coagulation factors V (FV) and Xa (FXa). Here we show that the FV component (pt-FV) has unique biologic properties that subvert the normal regulatory restraints intended to restrict an unregulated procoagulant response. Unlike human FV, recombinant pt-FV is constitutively active and does not require proteolytic processing to function. Sequence comparisons show that it has shed a large portion of the central B-domain, including residues that stabilize the inactive procofactor state. Remarkably, pt-FV functions in the absence of anionic membranes as it binds snake-FXa with high affinity in solution. Furthermore, despite cleavage in the heavy chain, pt-FV is functionally resistant to activated protein C, an anticoagulant. We speculate this stability is the result of noncovalent interactions and/or a unique disulfide bond in pt-FV linking the heavy and light chains. Taken together, these findings provide a biochemical rationale for the strong procoagulant nature of venom prothrombinase. Furthermore, they illustrate how regulatory mechanisms designed to limit the hemostatic response can be uncoupled to provide a sustained, disseminated procoagulant stimulus for use as a biologic toxin.
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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.