References
- Alape-Giron A, Sanz L, Escolano J, et al. (2008). Snake venomics of the lancehead pitviper Bothrops asper: geographic, individual, and ontogenetic variations. J Proteome Res 7:3556–71
- Braud S, Bon C, Wisner A. (2000). Snake venom proteins acting on hemostasis. Biochimie 82:851–9
- Calvete JJ, Sanz L, Angulo Y, et al. (2009). Venoms, venomics, antivenomics. FEBS Lett 583:1736–43
- Caron EJ, Manock SR, Maudlin J, et al. (2009). Apparent marked reduction in early antivenom reactions compared to historical controls: was it prophylaxis or method of administration? Toxicon 54:779–83
- Cheng AC, Wu HL, Shi GY, Tsai IH. (2012). A novel heparin-dependent inhibitor of activated protein C that potentiates consumptive coagulopathy in Russell’s viper envenomation. J Biol Chem 287:15739–48
- Chijiwa T, Deshimaru M, Nobuhisa I, et al. (2000). Regional evolution of venom-gland phospholipase A2 isoenzymes of Trimeresurus flavoviridis snakes in the southwestern islands of Japan. Biochem J 347:491–9
- Chippaux JP, Williams V, White J. (1991). Snake venom variability: methods of study, results and interpretation. Toxicon 29:1279–303
- Daltry JC, Ponnudurai G, Shin CK, et al. (1996a). Electrophoretic profiles and biological activities: intraspecific variation in the venom of the Malayan pit viper (Calloselasma rhodostoma). Toxicon 34:67–79
- Daltry JC, Wuster W, Thorpe RS. (1996b). Diet and snake venom evolution. Nature 379:537–40
- Harris JB. (1985). Phospholipases in snake venoms and their effects on nerve and muscle. Pharmacol Ther 31:79–102
- Hung DZ, Wu ML, Deng JF, Lin-Shiau SY. (2002a). Russell’s viper snakebite in Taiwan: differences from other Asian countries. Toxicon 40:1291–8
- Hung DZ, Wu ML, Deng JF, et al. (2002b). Multiple thrombotic occlusions of vessels after Russell’s viper envenoming. Pharmacol Toxicol 91:106–10
- Isbister GK, Brown SG, MacDonald E, et al. (2008). Current use of Australian snake antivenoms and frequency of immediate-type hypersensitivity reactions and anaphylaxis. Med J Aust 188:473–6
- Jayanthi GP, Gowda TV. (1988). Geographical variation in India in the composition and lethal potency of Russell’s viper (Vipera russelli) venom. Toxicon 26:257–64
- Joubert FJ, Taljaard N. (1980). Purification, some properties and amino-acid sequences of two phospholipases A (CM-II and CM-III) from Naja naja kaouthia venom. Eur J Biochem 112:493–9
- Kini RM. (1997). Phospholipase A2 a complex multifunctional protein puzzle. In: Kini RM, ed. Venom phospholipase A2 enzymes: structure, function and mechanism. Chichester: John Wiley & Sons, 1–28
- Kini RM. (2006). Anticoagulant proteins from snake venoms: structure, function and mechanism. Biochem J 397:377–87
- Kini RM. (2011). Toxins in thrombosis and haemostasis: potential beyond imagination. J Thromb Haemost 9 Suppl 1:195–208
- Kini RM, Evans HJ. (1989). A model to explain the pharmacological effects of snake venom phospholipases A2. Toxicon 27:613–35
- Laemmli UK. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–5
- Lomonte B, Carmona E. (1992). Individual expression patterns of myotoxin isoforms in the venom of the snake Bothrops asper. Comp Biochem Physiol B 102:325–9
- Markland FS. (1998). Snake venoms and the hemostatic system. Toxicon 36:1749–800
- Menezes MC, Furtado MF, Travaglia-Cardoso SR, et al. (2006). Sex-based individual variation of snake venom proteome among eighteen Bothrops jararaca siblings. Toxicon 47:304–12
- Minton SA, Weinstein SA. (1986). Geographic and ontogenic variation in venom of the western diamondback rattlesnake (Crotalus atrox). Toxicon 24:71–80
- Mukherjee AK, Ghosal SK, Maity CR. (2000). Some biochemical properties of Russell’s viper (Daboia russelli) venom from Eastern India: correlation with clinico-pathological manifestation in Russell’s viper bite. Toxicon 38:163–75
- Nakashima K, Nobuhisa I, Deshimaru M, et al. (1995). Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes. Proc Natl Acad Sci USA 92:5605–9
- Ogawa T, Nakashima K, Nobuhisa I, et al. (1996). Accelerated evolution of snake venom phospholipase A2 isozymes for acquisition of diverse physiological functions. Toxicon 34:1229–36
- Phillips RE, Theakston RD, Warrell DA, et al. (1988). Paralysis, rhabdomyolysis and haemolysis caused by bites of Russell’s viper (Vipera russelli pulchella) in Sri Lanka: failure of Indian (Haffkine) antivenom. Q J Med 68:691–715
- Pla D, Gutierrez JM, Calvete JJ. (2012). Second generation snake antivenomics: comparing immunoaffinity and immunodepletion protocols. Toxicon 60:688–99
- Prasad BN, Kemparaju K, Bhatt KG, Gowda TV. (1996). A platelet aggregation inhibitor phospholipase A2 from Russell’s viper (Vipera russelli) venom: isolation and characterization. Toxicon 34:1173–85
- Prasad NB, Uma B, Bhatt SK, Gowda VT. (1999). Comparative characterisation of Russell’s viper (Daboia/Vipera russelli) venoms from different regions of the Indian peninsula. Biochim Biophys Acta 1428:121–36
- Rodrigues VM, Soares AM, Mancin AC, et al. (1998). Geographic variations in the composition of myotoxins from Bothrops neuwiedi snake venoms: biochemical characterization and biological activity. Comp Biochem Physiol A Mol Integr Physiol 121:215–22
- Saad E, Curtolo BL, Biscola N, et al. (2012). Intraspecific variation of biological activities in venoms from wild and captive Bothrops jararaca. J Toxicol Environ Health A 75:1081–90
- Saravu K, Somavarapu V, Shastry AB, Kumar R. (2012). Clinical profile, species-specific severity grading, and outcome determinants of snake envenomation: an Indian tertiary care hospital-based prospective study. Indian J Crit Care Med 16:187–92
- Shashidharamurthy R, Jagadeesha DK, Girish KS, Kemparaju K. (2002). Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution. Mol Cell Biochem 229:93–101
- Shashidharamurthy R, Kemparaju K. (2007). Region-specific neutralization of Indian cobra (Naja naja) venom by polyclonal antibody raised against the eastern regional venom: a comparative study of the venoms from three different geographical distributions. Int Immunopharmacol 7:61–9
- Simpson ID, Norris RL. (2007). Snakes of medical importance in India: is the concept of the “Big 4” still relevant and useful? Wilderness. Environ Med 18:2–9
- Stone SF, Isbister GK, Shahmy S, et al. (2013). Immune response to snake envenoming and treatment with antivenom; complement activation, cytokine production and mast cell degranulation. PLoS Negl Trop Dis 7:e2326
- Than T, Hutton RA, Myint L, et al. (1988). Haemostatic disturbances in patients bitten by Russell’s viper (Vipera russelli siamensis) in Burma. Br J Haematol 69:513–20
- Tsai IH, Tsai HY, Wang YM, et al. (2007). Venom phospholipases of Russell’s vipers from Myanmar and eastern India – cloning, characterization and phylogeographic analysis. Biochim Biophys Acta 1774:1020–8
- Warrell DA. (1989). Snake venoms in science and clinical medicine. 1. Russell’s viper: biology, venom and treatment of bites. Trans R Soc Trop Med Hyg 83:732–40
- White J. (2005). Snake venoms and coagulopathy. Toxicon 45:951–67
- Williams V, White J. (1992). Variation in the composition of the venom from a single specimen of Pseudonaja textilis (common brown snake) over one year. Toxicon 30:202–6
- Zupunski V, Kordis D, Gubensek F. (2003). Adaptive evolution in the snake venom Kunitz/BPTI protein family. FEBS Lett 547:131–6