References
- Bos MHA, Boltz M, St. Pierre L, et al. (2009). Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations. Blood 2114:686–92
- Bos MHA, Camire RM. (2010). Procoagulant adaptation of a blood coagulation prothrombinase-like complex in Australian Elapid venom. Toxins 2:1554–67
- Bos MHA, Camire, RM. (2012). A bipartite autoinhibitory region within the B-domain suppresses function in factor V. J Biol Chem 287:26342--51
- Camire RM. (2002). Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J Biol Chem 277:37863–70
- Camire RM, Bos MHA. (2009). The molecular basis of factor V and VIII procofactor activation. J Thromb Haemost 7:1951–61
- Duckers C, Simioni P, Spiezia L, et al. (2008). Low plasma levels of tissue factor pathway inhibitor in patients with congenital factor V deficiency. Blood 112:3615–23
- Higgins DL, Mann KG. (1983). The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J Biochem 258:6503–8
- Krishnaswamy S. (1990). Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation. J Biol Chem 265:3708–18
- Krishnaswamy S, Jones KC, Mann KG. (1988). Prothrombinase complex assembly. Kinetic mechanism of enzyme assembly on phospholipid vesicles. J Biol Chem 263:3823–34
- Kumar S, Stayrook S, Huntington JA, et al. (2011). High resolution X-ray structure of snake venom factor V: evolution of a hemostatic cofactor to a toxin poised to inflict maximal damage to mammalian blood coagulation. Blood (ASH 2011 Meeting Abstracts) 118:375
- Lechtenberg BC, Murray-Rust TA, Johnson DJ, et al. (2013). Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis. Blood, doi: 10.1182/blood-2013-06-511733
- Lee CJ, Wu S, Pedersen LG. (2011). A proposed ternary complex model of prothrombinase with prothrombin: protein-protein docking and molecular dynamics simulations. J Thromb Haemost 9:2123–6
- Mann KG. (1976). Prothrombin. Methods Enzymol 45:123–56
- Mann KG, Hockin MF, Begin KJ, Kalafatis M. (1997). Activated protein C cleavage of factor Va leads to dissociation of the A2 domain. J Biol Chem 272:20678–83
- Mann KG, Nesheim ME, Church WR, et al. (1990). Surface dependent reactions of the vitamin K-dependent enzyme complexes. Blood 76:1–16
- Masci PP, Whitaker AN, de Jersey J. (1988). Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis. Biochem Int 17:825–35
- Minh Le TN, Reza MA, Swarup S, Kini RM. (2005). Gene duplication of coagulation factor V and origin of venom prothrombin activator in Pseudonaja textilis snake. Thromb Haemost 93:420–9
- Morrissey JH. (1981). Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 117:307–10
- Rao VS, Kini RM. (2002). Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex. Thromb Haemost 88:611–19
- Rao VS, Swarup S, Kini RM. (2003). The nonenzymatic subunit of pseutarin C, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom, shows structural similarity to mammalian coagulation factor V. Blood 102:1347–54
- Rao VS, Swarup S, Kini RM. (2004). The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa. Thromb Haemost 92:509–21
- Segers K, Dahlbäck B, Rosing J, Nicolaes GA. (2008). Identification of surface epitopes of human coagulation factor Va that are important for interaction with activated protein C and heparin. J Biol Chem 283:22573–81
- Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J. (1986). Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake). J Biol Chem 261:13258–67
- Sutherland S, Tibballs J. (2001). Australian animal toxins: the creatures, their toxins and care of the poisoned patient. Melbourne, Australia: Oxford University Press
- Verhoef D, Camire RM, Reitsma PH, Bos MHA. (2013). Functional characterization of a structural element unique to venom factor V from the Australian common brown snake Pseudonaja textilis. J Thromb Haemost (ISTH 2013 Meeting Abstracts) 11(S2):AS 36.3