[1. Anderson SG, Gutierrez JM, Ownby CL. Comparison of the immunogenicity and antigenic composition of ten Central American snake venoms. Toxicon. 1993; 31:1051-9.10.1016/0041-0101(93)90263-I]Open DOISearch in Google Scholar
[2. Harrison RA, Wüster W, Theakston RD. The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody. Toxicon. 2003; 41: 441-9.10.1016/S0041-0101(02)00360-4]Open DOISearch in Google Scholar
[3. Stabeli RG, Magalhaes LM, Selistre-de-Araujo HS, Oliveira EB. Antibodies to a fragment of the Bothrops moojenil-amino acid oxidase cross-react with snake venom components unrelated to the parent protein. Toxicon. 2005; 46: 308-17.10.1016/j.toxicon.2005.04.020]Open DOISearch in Google Scholar
[4. Minton SA, Weinstein SA, Wilde CE 3rd. An enzymelinked immunoassay for detection of North American pit viper venoms. J Toxicol Clin Toxicol. 1984; 22:303-16.10.3109/15563658408992562]Open DOISearch in Google Scholar
[5. Theakston RD. The application of immunoassay techniques, including enzyme-linked immunosorbent assay (ELISA), to snake venom research. Toxicon. 1983; 21:341-52.10.1016/0041-0101(83)90090-9]Open DOISearch in Google Scholar
[6. Barral-Netto M, Schriefer A, Barral A, Almeida AR, Mangabeira A. Serum levels of bothropic venom in patients without anti-venom intervention. Am J Trop Med Hyg. 1991; 45: 751-4.10.4269/ajtmh.1991.45.751]Search in Google Scholar
[7. Gutiérrez JM, Sanz L, Flores-Diaz M, Figueroa L, Madrigal M, Herrera M, et al. Impact of regional variation in Bothrops asper snake venom on the design of antivenoms: integrating antivenomics and neutralization approaches. J Proteome Res. 2010; 9:564-77.10.1021/pr9009518]Open DOISearch in Google Scholar
[8. Hanashiro MA, Da Silva MH, Bier OG. Neutralization of crotoxin and crude venom by rabbit antiserum to crotalus phospholipase A. Immunochemistry. 1978; 15:745-50.10.1016/0161-5890(78)90103-7]Open DOISearch in Google Scholar
[9. Kaiser II, Middlebrook JL, Crumrine MH, Stevenson WW. Cross-reactivity and neutralization by rabbit antisera raised against crotoxin, its subunits and two related toxins. Toxicon. 1986; 24: 669-78.10.1016/0041-0101(86)90030-9]Open DOISearch in Google Scholar
[10. Gowda DC, Jackson CM, Hensley P, Davidson, EA. Factor X-activating glycoprotein of Russell’s viper venom. Polypeptide composition and characterization of the carbohydrate moieties. J Biol Chem. 1994; 269:10644-50.10.1016/S0021-9258(17)34108-X]Search in Google Scholar
[11. Fujikawa K, Legaz ME, Davie EW. Bovine factor X 1 (Stuart factor). Mechanism of activation by protein from Russell’s viper venom. Biochemistry. 1972; 11:4892-99.10.1021/bi00776a003]Open DOISearch in Google Scholar
[12. Di Scipio RG, Hermodson MA, Davie EW. Activation of human factor X (Stuart factor) by a protease from Russell’s viper venom. Biochemistry. 1977; 16:5253-60.10.1021/bi00643a015]Open DOISearch in Google Scholar
[13. Rungsiwongse J, Ratanabanangkoon K. Development of an ELISA to assess the potency of horse therapeutic anti-venom against Thai cobra venom. J Immunol Methods. 1991; 136: 37-43.10.1016/0022-1759(91)90247-D]Search in Google Scholar
[14. LeammLi UK. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227: 680-5.10.1038/227680a0]Search in Google Scholar
[15. Suntravat M, Nuchprayoon I, Perez JC. Comparative study of anticoagulant and procoagulant properties of 28 snake venoms from families Elapidae, Viperidae, and purified Russell’s viper venom-factor X activator (RVV-X). Toxicon 2010; 56: 544-53.10.1016/j.toxicon.2010.05.012]Open DOISearch in Google Scholar
[16. Hu YX, Guo JY, Shen L, Chen Y, Zhang ZC, Zhang YL. Get effective polyclonal antisera in one month. Cell Res. 2002; 12: 157-60.10.1038/sj.cr.7290122]Open DOISearch in Google Scholar
[17. Morita T. Proteases which activate factor X. In: Bailey G ed. Enzymes from Snake Venoms. Fort Collins: Alaken; 1998. p. 179-209.]Search in Google Scholar
[18. Kroon DJ, Baldwin-Ferro A, Lalan P. Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping. Pharm Res. 1992; 9:1386-93.10.1023/A:1015894409623]Open DOISearch in Google Scholar
[19. Jia LG, Shimokawa K, Bjarnason JB, Fox JW. Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins. Toxicon. 1996; 34: 1269-76.10.1016/S0041-0101(96)00108-0]Open DOISearch in Google Scholar
[20. Ramos OH, Selistre-de-Araujo HS. Snake venom metalloproteases-structure and function of catalytic and disintegrin domains. Comp Biochem Physiol C Toxicol Pharmacol. 2006; 142: 328-46.10.1016/j.cbpc.2005.11.00516434235]Search in Google Scholar
[21. Fox JW, Serrano SM. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008; 275: 3016-30.10.1111/j.1742-4658.2008.06466.x18479462]Search in Google Scholar
[22. Lu Q, Navdaev A, Clemetson JM, Clemetson KJ. Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis. Toxicon. 2005; 45: 1089-98.10.1016/j.toxicon.2005.02.022]Open DOISearch in Google Scholar
[23. Morita T. Structures and functions of snake venom CLPs (C-type lectin-like proteins) with anticoagulant, procoagulant, and platelet-modulating activities. Toxicon. 2005; 45: 1099-114.10.1016/j.toxicon.2005.02.021]Open DOISearch in Google Scholar
[24. Hsu CC, Wu WB, Huang TF. A snake venom metalloproteinase, kistomin, cleaves platelet glycoprotein VI and impairs platelet functions. J Thromb Haemost. 2008; 6: 1578-85.10.1111/j.1538-7836.2008.03071.x]Search in Google Scholar
[25. Andrews RK, Gardiner EE, Asazuma N, Berlanga O, Tulasne D, Nieswandt B, et al. A novel viper venom metalloproteinase, alborhagin, is an agonist at the platelet collagen receptor GPVI. J Biol Chem. 2001; 276:28092-7.10.1074/jbc.M011352200]Search in Google Scholar
[26. Wijeyewickrema LC, Gardiner EE, Moroi M, Berndt MC, Andrews RK. Snake venom metalloproteinases, crotarhagin and alborhagin, induce ectodomain shedding of the platelet collagen receptor, glycoprotein VI. Thromb Haemost. 2007; 98: 1285-90.10.1160/TH07-06-0402]Search in Google Scholar
[27. Dambisya YM, Lee TL, Gopalakrishnakone P. Action of Calloselasma rhodostoma (Malayan pit viper) venom on human blood coagulation and fibrinolysis using computerized thromboelastography (CTEG). Toxicon. 1994; 32: 1619-26.10.1016/0041-0101(94)90320-4]Open DOISearch in Google Scholar
[28. Yamada D, Sekiya F, Morita T. Prothrombin and factor X activator activities in the venoms of Viperidae snakes. Toxicon. 1997; 35: 1581-9.10.1016/S0041-0101(97)00043-3]Open DOISearch in Google Scholar
[29. Hofmann H, Bon C. Blood coagulation induced by the venom of Bothrops atrox. 2. Identification, purification, and properties of two factor X activators. Biochemistry. 1987; 26: 780-7.10.1021/bi00377a019]Open DOISearch in Google Scholar
[30. Nahas L, Kamiguti AS, Barros MA. Thrombin-like and factor X-activator components of Bothrops snake venoms. Thromb Haemost. 1979;41: 314-28.10.1055/s-0038-1646781]Search in Google Scholar
[31. Komori Y, Nikai T, Sugihara H. Isolation and characterization of factor X activator from the venom of Vipera aspis aspis. Int J Biochem. 1990; 22: 1053-60.10.1016/0020-711X(90)90013-S]Open DOISearch in Google Scholar
[32. Samel M, Siigur J. Medium molecular weight factor X activating enzyme from Vipera berus berus venom. Toxicon. 1995; 33: 41-52.10.1016/0041-0101(94)00143-V]Open DOISearch in Google Scholar
[33. Franssen JH, Janssen-Claessen T, Van Dieijen G. Purification and properties of an activating enzyme of blood clotting factor X from the venom of Cerastes cerastes. Biochim Biophys Acta. 1983; 747: 186-90.10.1016/0167-4838(83)90139-5]Search in Google Scholar
[34. Farid T, Nasser H, Zaki K, el-Asmar MF. Low molecular weight factor X activator from Cerastes vipera (Sahara sand viper) venom. Toxicon. 1993; 31:1007-17.10.1016/0041-0101(93)90260-P]Open DOISearch in Google Scholar
[35. Chung CH, Peng HC, Huang TF. Aggretin, a C-type lectin protein, induces platelet aggregation via integrin alpha(2)beta(1) and GPIb in a phosphatidylinositol 3-kinase independent pathway. Biochem Biophys Res Commun. 2001; 285: 689-95.10.1006/bbrc.2001.522811453648]Search in Google Scholar
[36. Navdaev A, Clemetson JM, Polgar J, Kehrel BE, Glauner M, Magnenat E, et al. Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma (malayan pit viper), stimulates platelets by binding to alpha 2beta 1 integrin and glycoprotein Ib, activating Syk and phospholipase Cgamma 2, but does not involve the glycoprotein VI/Fc receptor gamma chain collagen receptor. J Biol Chem. 2001; 276: 20882-9.10.1074/jbc.M10158520011287424]Search in Google Scholar
[37. Peng M, Lu W, Kirby EP. Alboaggregin-B: a new platelet agonist that binds to platelet membrane glycoprotein Ib. Biochemistry. 1991; 30: 11529-36.10.1021/bi00113a0071747371]Open DOISearch in Google Scholar
[38. Yoshida E, Fujimura Y, Miura S, Sugimoto M, Fukui H, Narita N, et al. Alboaggregin-B and botrocetin, two snake venom proteins with highly homologous amino acid sequences but totally distinct functions on von Willebrand factor binding to platelets. Biochem Biophys Res Commun. 1993; 191: 1386-92.10.1006/bbrc.1993.13718466514]Search in Google Scholar
[39. Usami Y, Suzuki M, Yoshida E, Sakurai Y, Hirano K, Kawasaki T, et al. Primary structure of alboaggregin-B purified from the venom of Trimeresurus albolabris. Biochem Biophys Res Commun. 1996; 219: 727-33. 10.1006/bbrc.1996.03028645249]Search in Google Scholar