Inhibitors of Snake Venoms and Development of New Therapeutics

REFERENCES

• J.B. Bjarnason, and J.W. Fox. 1994. Hemorrhagic metalloproteases from snake venoms. Pharmac. Ther. 62 (3):325–372.
   PubMedGoogle Scholar
• J.B. Bjarnason, A. Barrish, G.S. Direnzo, R. Campbell, and J.W. Fox. 1983. Kallikrein-like enzymes from Crotalus atrox venom. J. Biol. Chem. 258 (20):12566–12573.
   PubMedGoogle Scholar
• C.L. Ownby, R.A. Kainer, and A.T. Tu. 1974. Pathogenesis of hemorrhagic induced by rattlesnake venom. Am. J. Pathol. 76 (2):401–408.
   PubMedGoogle Scholar
• A. Rodriguez-Acosta, I. Aguilar, M.E. Giron, and V. Rodriguez-Pulido. 1998. Haemorragic activity of neotropical rattlesnake (Crotalus vegrandis Klauber.; 1941). venom. Nat. Toxins. 6 (1):15–18.
   PubMedGoogle Scholar
• E.A. Dennis. 1994. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem. 269 (18):13057–13060.
   PubMedGoogle Scholar
• RM Kini, and H.J. Evans. 1989. A Model to explain the pharmacological effects of snake venom Phospholipase A2. Toxicon 27 (6):613–635.
   PubMedGoogle Scholar
• E. Valentin, and G. Lambeau. 2000. Increasing molecular diversity of secreted phospholipases a2 and their receptors and binding proteins. Biochim. Biophys. Acta 1488 (1–2):59–70.
   PubMedGoogle Scholar
• E. Valentin, and G. Lambeau. 2000. What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2?. Biochimie. 82 (9–10):815–813.
   PubMedGoogle Scholar
• A.A. Nichol, V. Douglas, and L. Peck. 1933. On the immunity of rattlesnakes to their venom. Copeia 1933 (4):211–213.
   Google Scholar
• V.B. Philpot, and R.G. Smith. 1950. Neutralization of pit viper venom by kingsnake serum. Proc. Soc. Exp. Biol. Med. 74 (3):521–523.
   PubMedGoogle Scholar
• T. Omori-Satoh, S. Sadahiro, A. Ohsaka, and R. Murata. 1972. Purification and characterization of an antihemorrhagic factor in the serum of Trimeresurus flavoviridis a crotalid. Biochim. Biophys. Acta 285 (2):414–426.
   PubMedGoogle Scholar
• M. Ovadia, and E. Kochva. 1977. Neutralization of viperidae and elapidae snake venoms by sera of different animals. Toxicon 15 (6):541–547.
   PubMedGoogle Scholar
• B. PhilpotJr, E. Ezekiel, Y. Laseter, RG Yaeger, and RL Stjernholm. 1978. Neutralization of crotalid venoms by fractions from snake sera. Toxicon 16 (6):603–609.
   PubMedGoogle Scholar
• M. Ovadia. 1978. Isolation and characterization of an anti-hemorrhagic factor from the venom of Vipera palaestinae. Toxicon 16 (6):661–672.
   PubMedGoogle Scholar
• Y. Tomihara, K. Yonaha, M. Nozaki, M. Yamakawa, Y. Kawamura, T. Kamura, and S. Toyama. 1988. Purification of an antihemorrhagic factor from the serum of the nonvenomous snake (Dinodon semicarinatus). Toxicon 26 (4):420–423.
   PubMedGoogle Scholar
• T. Omori-Satoh, Y. Nagaoka, Y. Yamakawa, and D. Mebs. 1994. Inhibition of hemorrhagic activities of various snake venoms by purified antihemorrhagic factor obtained from Japanese habu snake. Toxicon 32 (3):365–368.
   PubMedGoogle Scholar
• C. Phisalix, and G. Bertrand. 1895. Recherches sur l'immunite du herisson contre le venin de vipere. C. R. Soc. Biol. 47 (10):639–641.
   Google Scholar
• J. Vellard. 1945. Resistencia de los “Didelphis” (zarigueya) a los venenos ofidicos (Nota previa). Rev. Brasil. Biol. 5 (3):463–467.
   PubMedGoogle Scholar
• J. Vellard. 1949. Investigaciones sobre inmunidad natural contra los venenos de serpientes I. Pub. Mus. Hist. Nat. Lima Ser A. Zool. 1 (1):72–96.
   Google Scholar
• J.A. KilmonSr.. 1976. High tolerance to snake venom by the virginiana opossum Didelphis virginiana. Toxicon 14 (4):337–340.
   PubMedGoogle Scholar
• R.M. Werner, and J.A. Vick. 1977. Resistance of the opossum (Didelphis virginiana) to envenomation by snakes of the family Crotalidae. Toxicon 15 (1):29–33.
   PubMedGoogle Scholar
• J.C. Pérez, W.C. Haws, and C.H. Hatch. 1978. Resistance of woodrats (Neotoma micropus) to Crotalus atrox venom. Toxicon 16 (2):198–200.
   PubMedGoogle Scholar
• J.C. Pérez, W.C. Haws, V.E. Garcia, and B.M. Jennings3rd. 1978. Resistance of warm-blooded animals to snake venoms. Toxicon 16 (4):375–383.
   PubMedGoogle Scholar
• R.R. Martinez, J.C. Pérez, E.E. Sánchez, and R. Campos. 1999. The antihemorrhagic factor of the Mexican ground squirrel (Spermophilus mexicanus). Toxicon 37 (6):949–954.
   PubMedGoogle Scholar
• G.B. Domont, J. Perales, and H. Moussatche. 1991. Natural anti-snake venom proteins. Toxicon 29 (10):1183–1194.
   PubMedGoogle Scholar
• J.C. Pérez, and E.E. Sánchez. 1999. Natural protease inhibitors to hemorrhagins in snake venoms and their potential use in medicine. Toxicon 37 (5):703–728.
   PubMedGoogle Scholar
• J.O. da Silva, R.S. Fernandes, F.K. Ticli, C.Z. Oliveira, M.V. Mazzi, J.J. Franco, S. Giuliatti, P.S. Pereira, A.M. Soares, and S.V. Sampaio. 2007. Triterpenoid saponins: New metalloprotease snake venom inhibitors isolated from Pentaclethra macroloba. Toxicon 50 (2):283–291.
   PubMedGoogle Scholar
• L.J. Denis, and J. Verweij. 1997. Matrix metalloproteinase inhibitors: Present achievements and future prospects. Investigational New Drugs. 15 (3):175–185.
   PubMedGoogle Scholar
• R. Chirivi, A. Garofalo, M. Crirarmin, L. Bawdes, P. Brown, and R. Giavazzi. 1994. Inhibition of the metastatic spread and grown of B16-BBL6 murine melanoma by a synthetic matrix metalloproteinase inhibitor. Int. J. Cancer. 59 (3):460–464.
   PubMedGoogle Scholar
• S. A. Watson, T.M. Morris, G. Robinson, M.J. Crimmia, P.D. Brown, and J.D. Hardcastle. 1995. Inhibition of organ invasion by the matrix metalloproteinase inhibitor batimastat (BB-94) in two human colon carcinoma metastasis models. Cancer Res. 55 (16):3629–3633.
   PubMedGoogle Scholar
• S.A. Eccles, G.M. Box, W.J. Court, E.A. Boss, W. Thomas, and P.D. Brown. 1996. Control of lymphatic and homologous metastasis of a rat mammary carcinoma by the matrix metalloproteinase inhibitor batimastat (BB-94). Cancer Res. 56 (12):2815–2822.
   PubMedGoogle Scholar
• S. Wojtowicz-Praga, J. Torri, M. Johnson, V. Steen, J. Marshall, E. Ness, R. Dickson, M. Sale, H.S. Rasmussen, T.A. Chiodo, and M.J. Hawkins. 1998. Phase I trial of marimastat, a novel matrix metalloproteinase inhibitor, administered orally to patients with advanced lung cancer. J. Clin. Oncol. 16 (6):2150–2156.
   PubMedGoogle Scholar
• A.F. Chambers, and L.M. Matrisian. 1997. Changing views of the role of matrix metalloproteases in metastasis. J. Natl. Cancer. Inst. 89 (17):1260–1270.
   PubMedGoogle Scholar
• J.B. Bjarnason, and J.W. Fox. 1989. Hemorrhagic toxins from snake venoms. J. Toxicol.-Toxin Reviews 7 (2):121–209.
   Google Scholar
• J.M. Gutiérrez, and B. Lomonte. 1995. Phospholipase A2 myotoxins from Bothrops snake venoms. Toxicon 33 (11):1405–1424.
   PubMedGoogle Scholar
• C.L. Ownby, T.R. Colberg, and G.V. Odell. 1986. Short communications in vivo ability of antimyotoxin a serum plus polyvalent (Crotalidae) antivenom to neutralize prairie rattlesnake (Crotalus viridis viridis) venom. Toxicon 24 (2):197–200.
   PubMedGoogle Scholar
• J.A. Gené, A. Roy, G. Rojas, J.M. Gutierrez, and L. Cerdas. 1989. Comparative study on coagulant, defibrinating, fibrinolytic and fibrinogenolytic activities of Costa Rican crotaline snake venoms and their neutralization by a polyvalent antivenom. Toxicon 27 (8):841–848.
   PubMedGoogle Scholar
• I. Daudu, and R.D.G. Theakston. 1987. Preliminary trial of a new polyspecific antivenom in Nigeria. Ann. Trop. Med. Parasitol. 82 (3):311–313.
   Google Scholar
• S.B. Carroll, B.S. Thalley, R.G.D. Theakston, and G. Laing. 1992. Comparison of the purity and efficacy of affinity purified avian antivenoms with commercial equine crotalids antivenoms. Toxicon 30 (9):1017–1025.
   PubMedGoogle Scholar
• R.D.G. Theakston, H.W. Fan, D.A. Warrell, W.D. Dias Da Silva, S.A. Ward, and H.G. Higashi. 1992. Butantan Institute Antivenom Study Group (BIASG). Use of enzyme immunoassays to compare effect and asses the dosage regimens of three Brazilian Bothrops antivenoms. Am. J. Trop. Med. Hyg. 47 (5):593–604.
   PubMedGoogle Scholar
• M.L. Ferreira, A.M. Moura-Da-Silva, and I. Mota. 1992. Neutralization of different activities of venoms from nine species of Bothrops snakes by Bothrops jararaca antivenom. Toxicon 30 (12):1591–1602.
   PubMedGoogle Scholar
• S. Rawat, G. Laing, D.C. Smith, D. Theakston, and J. Landon. 1994. A new antivenom to treat eastern coral snake (Micrurus fulvius fulvius) envenoming. Toxicon 32 (2):185–190.
   PubMedGoogle Scholar
• G. Borkow, J.M. Gutierrez, and M. Ovadia. 1997. Inhibition of the hemorrhagic activity of Bothrops asper venom by a novel neutralizing mixture. Toxicon 35 (6):865–877.
   PubMedGoogle Scholar
• G. Borkow, J.M. Gutierrez, and M. Ovadia. 1997. Inhibition of toxic activities of Bothrops asper venom and other crotalid snake venoms by a novel neutralizing mixture. Toxicol. Appl. Pharmacol. 147 (2):442–447.
   PubMedGoogle Scholar
• J. Stürzebecher, U. Neumann, and J. Meier. 1991. Inhibition of the protein C activator PROTAC: A serine proteinase from the venom of the southern copperhead snake Agkistrodon contortrix contortrix. Toxicon 29 (2):151–155.
   PubMedGoogle Scholar
• A. Robeva, V. Politi, J.D. Shannon, J.B. Bjarnason, and J.W. Fox. 1991. Synthetic and endogenous inhibitors of snake venom metalloproteases. Biomed. Biochim. Acta 50 (4–6):769–773.
   PubMedGoogle Scholar
• B. Francis, and I.I. Kaiser. 1993. Inhibition of metalloproteases in Bothrops asper venom by endogenous peptides. Toxicon 31 (7):889–899.
   PubMedGoogle Scholar
• W. Bode, C. Fernandez-Catalan, H. Tschesche, F. Grams, H. Nagase, and K. Maskos. 1999. Structural properties of matrix metalloproteinases. Cell. Mol. Life. Sci. 55 (4):639–652.
   PubMedGoogle Scholar
• K. Anai, M. Sugiki, E. Yoshida, and M. Maruyama. 1998. Inhibition of a snake venom hemorrhagic metalloproteinase by human and rat alpha-macroglobulin. Toxicon 36 (8):1127–1139.
   PubMedGoogle Scholar
• N. Heimburger. Biochemistry of Proteinase Inhibitors from human plasma: A Review of Recent Development. Bayer-Symposium V “Proteinase Inhibitors,”, 1974, 14–22.
   Google Scholar
• L.F. Kress, and J. Catanese. 1980. Enzymatic inactivation of human antithrombin III limited proteolysis of the inhibitor by snake venom proteinases in the presence of heparin. Biochim. Biophys. Acta 615 (1):178–86.
   PubMedGoogle Scholar
• H. Noguchi. In Natural immunity of certain animals from snake venom. Washington, DC: Carnegie InstitutION; 1909: 1–268.
   Google Scholar
• C.H. Kellaway. 1931. The immunity of Australian snakes to their own venoms. Med. J. Aus. 2:35–52.
   Google Scholar
• P.L. Swanson. 1946. Effects of snake venoms on snakes. Copeia 1946 (4):242–249.
   Google Scholar
• V.B. PhilpotJr., and H. F. Deutsch. 1956. Inhibition and activation of venom proteases. Biochim. Biophys. Acta 21 (3):524–530.
   PubMedGoogle Scholar
• L. Nahas, A.S. Kamiguti, E. Sousa, M.C.C. Silva, M.A.A. Ribeiro de Barros, and P. Morena. 1983. The inactivating effect of Bothrops jararaca and Walerophis merremii snake plasma on the coagulant activity of various snake venoms. Toxicon 21 (2):239–246.
   PubMedGoogle Scholar
• M.M. Tanizaki, H. Kawasaki, K. Suzuki, and F.R. Mandelbaum. 1991. Purification of a proteinase inhibitor from the plasma of Bothrops jararaca (jararaca). Toxicon 29 (6):673–681.
   PubMedGoogle Scholar
• G. Borkow, J.M. Gutierrez, and M. Ovadia. 1995. Isolation, characterization and mode of neutralization of a potent antihemorrhagic factor from the serum of the snake Bothrops asper. Biochim. Biophys. Acta 1245 (2):232–238.
   PubMedGoogle Scholar
• Y. Yamakawa, and T. Omori-Satoh. 1992. Primary structure of the antihemorrhagic factor in serum of the Japanese habu: A snake venom metalloproteinase inhibitor with a double-headed cystatin domain. J. Biochem. 112 (5):583–589.
   PubMedGoogle Scholar
• K.F. Huang, L.P. Chow, and S.H. Chiou. 1999. Isolation and characterization of a novel proteinase inhibitor from the snake serum of Taiwan habu (Trimeresurus mucrosquamatus). Biochem. Biophys. Res. Commun. 263 (3):610–616.
   PubMedGoogle Scholar
• K.F. Huang, S.H. Chiou, TP Ko, and A.H.J. Wang. 2002. Determinants of the Inhibition of a Taiwan Habu venom metalloproteinase by its endogenous inhibitors revealed by x-ray crystallography and synthetic inhibitor analogues. Eur. J. Biochem. 269 (12):3047–3056.
   PubMedGoogle Scholar
• N. Ohkura, H. Okuhara, S. Inoue, K. Ikeda, and K. Hayashi. 1997. Purification and characterization of three distinct types of phospholipase A2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon blomhoffii siniticus. Biochem. J. 325 (Pt 2):527–531.
   PubMedGoogle Scholar
• D. Bonnett, and S.I. Guttman. 1971. Inhibition of moccasin (Agkistrodon piscivorus) venom proteolytic activity by the serum of the Florida king snake (Lampropeltis getulus floridana). Toxicon 9 (4):417–425.
   PubMedGoogle Scholar
• G. Borkow, J.M. Gutierrez, and M. A Ovadia. 1994. potent antihemorrhagin in the serum of the non-venomous water snake Natrix tessellata: Isolation, characterization and mechanism of neutralization. Biochim. Biophys. Acta 1201 (3):482–490.
   PubMedGoogle Scholar
• K. Okumura, S. Inoue, K. Ikeda, and K. Hayashi. 2002. Identification of beta-type phospholipase A(2) inhibitor in a nonvenomous snake, Elaphe quadrivirgata. Arch. Biochem. Biophys. 408 (1):124–130.
   PubMedGoogle Scholar
• R. Pérez-Hernandez, P. Soriano, and D. Lew. Marsupiales de Venezuela. Caracas: Departamento de Asuntos Públicos de Lagoven S.A. filial de Petróleos de Venezuela S.A. 1994.
   Google Scholar
• D.J. Schmidly. In Accounts of Wild Animals. Texas mammals east of the Balcoes fault zone. College Station, TX: Texas A & M Press, 1983, 34–38.
   Google Scholar
• R.M. Werner, and R.E. Faith. 1978. Decrease in the lethal effect of snake venom by serum of the opossum, Didelphis marsupialis. Lab. Anim. Sci. 28 (6):710–713.
   PubMedGoogle Scholar
• J.M. Menchaca, and J.C. Pérez. 1981. The purification and characterization of an antihemorrhagic factor in opossum (Didelphis virginiana) serum. Toxicon 19 (5):623–632.
   PubMedGoogle Scholar
• M.R. McKeller, and J.C. Pérez. 2002. The effects of Western Diamondback Rattlesnake (Crotalus atrox) venom on the production of antihemorrhagins and/or antibodies in the Virginia opossum (Didelphis virginiana). Toxicon 40 (4):427–439.
   PubMedGoogle Scholar
• S.F. Tarng, S.Y. Huang, and J.C. Pérez. 1986. Isolation of antihemorrhagic factors in opossum (Didelphis virginiana) serum using a monoclonal antibody immunoadsorbent. Toxicon 24 (6):567–573.
   PubMedGoogle Scholar
• J.G. Soto, J.C. Perez, and S.A. Minton. 1988. Proteolytic, hemorrhagic and hemolytic activities of snake venoms. Toxicon 26 (9):875–882.
   PubMedGoogle Scholar
• P.A. Melo, and G. Suarez-Kurtz. 1988. Release of sarcoplasmic enzyimes from skeletal muscle by Bothrops jararacussu venom: Antagonism by heparin and by the serum of South American marsupialis. Toxicon 26 (1):87–95.
   PubMedGoogle Scholar
• J. Perales, R. Munoz, S. Graterol, O. Oviedo, and H. Moussatche. 1989. New findings on the purification and characterization of an anti-bothropic factor from Didelphis marsupialis (opossum) serum. Braz. J. Med. Biol. Res. 22 (1):25–28.
   PubMedGoogle Scholar
• J. Perales, R. Munoz, and H. Moussatche. 1986. Isolation and partial characterization of a protein fraction from the opossum (Didelphis marsupialis) serum with protecting property against the Bothrops jararaca snake venom. An. Acad. Brasil. Cienc. 58 (1):155–162.
   PubMedGoogle Scholar
• J. Perales, C.Z. Amorin, S.L.G. Rocha, G.B. Domont, and H. Mousatche. 1992. Neutralization of the oedematogenic activity of Bothrops jararaca venom on the mouse paw by an antibothropic fraction isolated from opossum (Didelphis marsupialis) serum. Agents Actions 37 (3–4):250–259.
   PubMedGoogle Scholar
• A.G.C. Neves-Ferreira, J. Perales, M. Ovadia, H. Moussatche, and G.B. Domont. 1997. Inhibitory properties of the antibothropic complex from the South American opossum (Didelphis marsupialis) serum. Toxicon 35 (6):849–863.
   PubMedGoogle Scholar
• J.J. Catanese, and L.F. Kress. 1992. Isolation from opossum serum of a metalloproteinase inhibitor homologous to human α1B-glycoprotein. Biochemistry 31 (2):410–418.
   PubMedGoogle Scholar
• J.J. Catanese, and L.F. Kress. 1993. Opossum serum α1proteinase inhibitor: Purification, linear sequence and resistance to inactivation by rattlesnake venom metalloproteases. Biochemistry 32 (2):509–515.
   PubMedGoogle Scholar
• F. Pifano, I. Aguilar, M.E. Girón, N. Gamboa, and A. Rodriguez-Acosta. 1993. Natural resistance of opossum (Didelphis marsupialis) to the mapanare (Bothrops lanceolatus) snake venom. Rom. Arch. Microbiol. Immunol. 52 (2):131–136.
   PubMedGoogle Scholar
• A. Rodriguez-Acosta, I. Aguilar, and M.E. Giron. 1995. Antivenom activity of opossum (Didelphys marsupialis) serum fractions against uracoan rattlesnake (Crotalus vegrandis Klauber, 1941) venom. Rom. Arch. Microbiol. Immunol. 54 (4):325–330.
   PubMedGoogle Scholar
• J. Perales, H. Moussatche, S. Marangoni, B. Oliveira, and G.B. Domont. 1994. Isolation and partial characterization of an anti-bothropic complex from the serum of South American Didelphidae. Toxicon 32 (10):1237–1249.
   PubMedGoogle Scholar
• M.F. Lovo Farah, M. One, J.C. Novello, M.H. Toyama, J. Perales, H. Moussatche, G.B. Domont, B. Oliveira, and S. Marangoni. 1996. Isolation of protein factors from opossum (Didelphis albiventris) serum which protect against Bothrops jararaca venom. Toxicon 34 (9):1067–1071.
   PubMedGoogle Scholar
• A.G.C. Neves-Ferreira, N. Cardinale, S.L.G. Rocha, J. Perales, and G.B. Domont. 2000. Isolation and characterization of DM40 and DM43, two snake venom metalloproteinase inhibitors from Didelphis marsupialis serum. Biochim. Biophys. Acta 1474 (3):309–320.
   PubMedGoogle Scholar
• A.G. Neves-Ferreira, J. Perales, J.W. Fox, J.D. Shannon, D.L. Makino, R.C. Garratt, and G.B. Domont. 2002. Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum. J. Biol. Chem. 277 (15):13129–13137.
   PubMedGoogle Scholar
• A. Rodriguez-Acosta, I. Aguilar, and M.E. Giron. 1995. Antivenom activity of opossum (Didelphis marsupialis) serum fraction. Toxicon 33 (1):95–98.
   PubMedGoogle Scholar
• G. Lambeau, M. Lazdunzki, and J. Barhanin. 1991. Properties of Receptors for Neurotoxic Phospholipases A2 in Different Tissues. Neurochem. Res. 16 (6):651–658.
   PubMedGoogle Scholar
• R.D. Dunn, and K.W. Broady. 2001. Snake Inhibitors of Phospholipase A2 Enzymes. Biochim. Biophys. Acta 1533 (1):29–37.
   PubMedGoogle Scholar
• G. Faure. 2000. Natural inhibitors of toxic phospholipases A2. Biochimie. 82 (9–10):833–840.
   PubMedGoogle Scholar
• M.E. Pineda, M.E. Girón, A. Estrella, E.E. Sánchez, I. Aguilar, I. Fernandez, A.M. Vargas, H. Scannone, and A. Rodríguez-Acosta. 2008. Inhibition of the hemorrhagic and proteolytic activities of Lansberg's hognose pit viper (Porthidium lansbergii hutmanni) venom by opossum (Didelphis marsupialis) serum: Isolation of Didelphis marsupialis 0.15 DM fraction by DEAE-cellulose chromatography. Immunopharmacol. Immunotoxicol. In Press.
   PubMedGoogle Scholar
• S.L. Rocha, B. Lomonte, A.G. Neves-Ferreira, M.R. Trugilho, I. Junqueira-de-Azevedo, P.L. Ho, G.B. Domont, J.M. Gutierrez, and J. Perales. 2002. Functional analysis of DM64.; an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum. Eur. J. Biochem. 269 (24):6052–6062.
   PubMedGoogle Scholar
• A. Menez. 1998. Functional architectures of animal toxins: A clue to drug design?. Toxicon 36 (11):1557–1572.
   PubMedGoogle Scholar
• C. de Wit, and B.R. Westrom. 1985. Identification and characterization of trypsin, chymotrypsin and elastase inhibitors in the hedgehog, Erinaceus europaeus, and their immunological relationships to those of other mammals (rat, pig, and human). Comp. Biochem. Physiol. A. 82 (4):791–796.
   PubMedGoogle Scholar
• C.A. de Wit, and B.R. Westrom. 1987. Venom resistance in the hedgehog, Erinaceus europaeus: Purification and identification of nacroglobulin inhibitors as plasma antihemorrhagic factors. Toxicon 25 (3):315–323.
   PubMedGoogle Scholar
• C. de Wit, and B.R. Westrom. 1987. Purification and characterization of alpha-2, alpha-2-beta and beta macroglobulin inhibitors in the hedgehog, Erinaceus europaeus: Beta-macroglobulin identified as the plasma antihemorrhagic factor. Toxicon 25 (11):1209–1219.
   PubMedGoogle Scholar
• A. Calmette. Les venins, les animaux venimeux et la sérothérapie antivenimeuse. Paris: Masson, 1907.
   Google Scholar
• Y. Tomihara, K. Yonaha, M. Nozaki, M. Yamakawa, T. Kamura, and S. Toyama. 1987. Purification of three antihemorrhagic factors from the serum of a mongoose (Herpestes edwardsii). Toxicon 25 (6):685–689.
   PubMedGoogle Scholar
• J.C. Pérez, S. Pichyangkul, and V.E. Garcia. 1979. The resistance of three species of warm-blooded animals to western diamondback rattlesnake (Crotalus atrox) venom. Toxicon 17 (6):601–607.
   PubMedGoogle Scholar
• S. Pichyangkul, and J.C. Pérez. 1981. Purification and characterization of naturally occurring antihemorragic factor in the serum of the hispid cotton rat (Sigmodon hispidus). Toxicon 19 (2):205–215.
   PubMedGoogle Scholar
• V.E. Garcia, and J.C. Pérez. 1984. The purification and characterization of an antihemorrhagic factor in woodrat (Neotoma micropus) serum. Toxicon 22 (1):129–138.
   PubMedGoogle Scholar
• C. de Wit. 1982. Resistance of the Prairie vole (Microtus ochrogaster) and the woodrat (Neotoma floridana) in Kansas to venom of the Osage copperhead (Agkistrodon contortrix phaeogaster). Toxicon 20 (4):709–714.
   PubMedGoogle Scholar
• T. Omori-Satoh, Y. Nagaoka, and D. Mebs. 1994. Muscle extract of hedgehog Erinaceus europaeus inhibits hemorrhagic activity of snake venoms. Toxicon 32 (10):1279–1281.
   PubMedGoogle Scholar
• T. Omori-Satoh, M. Takahashi, Y. Nagaoka, and D. Mebs. 1998. Comparison of antihemorrhagic activities in skeletal muscle extracts from various animals against Bothrops jararaca snake venom. Toxicon 32 (2):421–423.
   Google Scholar
• N.S. Poran, R.G. Coss, and E. Benjamini. 1987. Resistance of California ground squirrels (Spermophilus beecheyi) to the venom of the northern pacific rattlesnake (Crotalus viridis oreganus): A study of adaptive variation. Toxicon 7:767–777.
   Google Scholar
• J.E. Biardi, R.G. Coss, and D.G. Smith. 2000. California ground squirrel (Spermophilus beecheyi) blood sera inhibit crotalid venom proteolytic activity. Toxicon 38 (5):713–721.
   PubMedGoogle Scholar
• J.E. Biardi, D.C. Chien, and R.G. Coss. 2006. California ground squirrel (Spermophilus beecheyi) defenses against rattlesnake venom digestive and hemostatic toxins. J. Chem. Ecol. 32 (1):137–154.
   PubMedGoogle Scholar
• J.A. Galán, E.E. Sánchez, A. Rodríguez-Acosta, and J.C. Pérez. 2004. Neutralization of venoms from two Southern Pacific rattlesnakes (Crotalus helleri) with commercial antivenoms and endothermic animal sera. Toxicon 43 (7):791–799.
   PubMedGoogle Scholar
• W.B. Mors, M.C. do Nascimento, J.P. Parente, M.H. da Silva, P.A. Melo, and G. Suarez-Kurtz. 1989. Neutralization of lethal and myotoxic activities of South American rattlesnake venom by extracts and constituents of the plant Eclipta prostrata (Asteraceae). Toxicon 27 (9):1003–1009.
   PubMedGoogle Scholar
• P. Melo, M.C. do Nascimento, W.B. Mors, and G. Suarez-Kurtz. 1994. Inhibition of the myotoxic and hemorrhagic activities of crotalid venoms by Eclipta prostrata (Asteraceae) extracts and constituents. Toxicon 32 (5):595–603.
   PubMedGoogle Scholar
• B.M. Ruppelt, E.F. Pereira, L.C. Gonçalves, and N.A. Pereira. 1991. Pharmacological screening of plants recommended by folk medicine as anti-snake venom—I. Analgesic and anti-inflammatory activities. Mem. Inst. Oswaldo Cruz. 86 (Suppl 2):203–205.
   PubMedGoogle Scholar
• M.O. Uguru, J.C. Aguiyi, and A.A. Gesa. 1997. Mechanism of action of the aqueous seed extract of Mucuna pruriens on the guinea pig ileum. Phytother. Res. 11 (4):328–329.
   Google Scholar
• N.A. Pereira, B.M. Pereira, M.C. do Nascimento, J.P. Parente, and W.B. Mors. 1994. Pharmacological screening of plants recommended by folk medicine as snake venom antidotes; IV. Protection against Jararaca venom by isolated constituents. Planta. Med. 60 (2):99–100.
   Google Scholar
• J.O. da Silva, J.S. Coppede, V.C. Fernandes, C.D. Santana, F.K. Ticli, M.V. Mazzi, J.R. Giglio, P.S. Pereira, A.M. Soares, and S.V. Sampaio. 2005. Antihemorrhagic, antinucleolytic and other antiophidian properties of the aqueous extract from Pentaclethra macroloba. J. Ethnopharmacol. 100 (1–2):145–152.
   PubMedGoogle Scholar
• W.L. Cavalcante, T.O. Campos, M. Dal Pai-Silva, P.S. Pereira, C.Z. Oliveira, A.M. Soares, and M. Gallacci. 2007. Neutralization of snake venom phospholipase A2 toxins by aqueous extract of Casearia sylvestris (Flacourtiaceae) in mouse neuromuscular preparation. J Ethnopharmacol. 112 (3):490–497.
   PubMedGoogle Scholar
• A. Gomes, A. Saha, I. Chatterjee, and A.K. Chakravarty. 2007. Viper and cobra venom neutralization by beta-sitosterol and stigmasterol isolated from the root extract of Pluchea indica Less. (Asteraceae). Phytomedicine 14 (9):637–643.
   PubMedGoogle Scholar
• S. Ushanandini, S. Nagaraju, K. Harish Kumar, M. Vedavathi, D.K. Machiah, K. Kemparaju, B.S. Vishwanath, T.V. Gowda, and K.S. Girish. 2006. The anti-snake venom properties of Tamarindus indica (leguminosae) seed extract. Phytother. Res. 20 (10):851–858.
   PubMedGoogle Scholar
• D.K. Machiah, K.S. Girish, and T.V. Gowda. 2006. A glycoprotein from a folk medicinal plant Withania somnifera inhibits hyaluronidase activity of snake venoms. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 143 (2):158–161.
   PubMedGoogle Scholar
• KS Girish, and K. Kemparaju. 2006. Inhibition of Naja naja venom hyaluronidase: role in the management of poisonous bite. Life Sci. 78 (13):1433–1440.
   PubMedGoogle Scholar
• F.K. Ticli, L.I. Hage, R.S. Cambraia, P.S. Pereira, A.J. Magro, M.R. Fontes, R.G. Stábeli, J.R. Giglio, S.C. França, A.M. Soares, and S.V. Sampaio. 2005. Rosmarinic acid, a new snake venom phospholipase A2 inhibitor from Cordia verbenacea (Boraginaceae): antiserum action potentiation and molecular interaction. Toxicon 46 (3):318–27.
   PubMedGoogle Scholar
• S. Daduang, N. Sattayasai, J. Sattayasai, P. Tophrom, A. Thammathaworn, A. Chaveerach, and M. Konkchaiyaphum. 2005. Screening of plants containing Naja naja siamensis cobra venom inhibitory activity using modified ELISA technique. Anal. Biochem. 41 (2):316–325.
   Google Scholar
• P. Pithayanukul, P. Ruenraroengsak, R. Bavovada, N. Pakmanee, R. Suttisri, and S. Saen-oon. 2005. Inhibition of Naja kaouthia venom activities by plant polyphenols. J. Ethnopharmacol. 97 (3):527–533.
   PubMedGoogle Scholar
• V. Núñez, R. Otero, J. Barona, M. Saldarriaga, R.G. Osorio, R. Fonnegra, S.L. Jiménez, A. Díaz, and J.C. Quintana. 2004. Neutralization of the edema-forming: Defibrinating and coagulant effects of Bothrops asper venom by extracts of plants used by healers in Colombia. Braz. J. Med. Biol. Res. 37 (7):969–977.
   PubMedGoogle Scholar
• L.C. Yang, F. Wang, and M. Liu. 1998. A study of an endothelin antagonist from a Chinese anti-snake venom medicinal herb. J. Cardiovasc. Pharmacol. 31 (Suppl 1):S249–S250.
   Google Scholar
• I.U. Asuzu, and A.L. Harvey. 2003. The antisnake venom activities of Parkia biglobosa (Mimosaceae) stem bark extract. Toxicon 42 (7):763–768.
   PubMedGoogle Scholar
• R. Guerranti, J.C. Aguiyi, E. Errico, R. Pagani, and E. Marinello. 2001. Effects of Mucuna pruriens extract on activation of prothrombin by Echis carinatus venom. J. Ethnopharmacol. 75 (2–3):175–180.
   PubMedGoogle Scholar
• P.J. Houghton, and IM Osibogun. 1993. Flowering plants used against snakebite. J. Ethnopharmacol. 39 (1):1–29.
   PubMedGoogle Scholar
• M.S. Abubakar, M.I. Sule, U.U. Pateh, E.M. Abdurahman, A.K. Haruna, and B.M. Jahun. 2000. In vitro snake venom detoxifying action of the leaf extract of Guiera senegalensis. J. Ethnopharmacol. 69 (3):253–257.
   PubMedGoogle Scholar
• C. Lans, T. Harper, K. Georges, and E. Bridgewater. 2001. Medicinal and ethnoveterinary remedies of hunters in Trinidad. BMC. Complement Altern. Med. 1 (10): 14726882-1-10.
   PubMedGoogle Scholar
• R. Ejzemberg, M.H. da Silva, L. Pinto, and W.B. Mors. 1999. Action of chlorogenic acid on the complement system. An. Acad. Bras. Cienc. 71 (2):273–277.
   PubMedGoogle Scholar
• W. Martz. 1992. Plants with a reputation against snakebite. Toxicon 30 (10):1131–1142.
   PubMedGoogle Scholar
• R. Reyes-Chilpa, F. Gómez-Garibay, L. Quijano, G. Magos-Guerrero, and T. Ríos. 1994. Preliminary results on the protective effect of (-)-edunol, a pterocarpan from Brongniartia podalyrioides (Leguminosae):Against Bothrops atrox venom in mice. J. Ethnopharmacol. 42 (3):199–203.
   PubMedGoogle Scholar
• Z.E. Selvanayagam, S.G. Gnanavendhan, K. Balakrishna, R.B. Rao, J. Sivaraman, K. Subramanian, and R. Puri. 1996. Ehretianone, a novel quinonoid xanthene from Ehretia buxifolia with antisnake venom activity. J. Nat. Prod. 59 (7):664–667.
   PubMedGoogle Scholar
• L.A. Ferreira, O.B. Henriques, A.A. Andreoni, G.R. Vital, M.M. Campos, G.G. Habermehl, and V.L. de Moraes. 1999. Antivenom and biological effects of ar-turmerone isolated from Curcuma longa (Zingiberaceae). Toxicon 30 (10):1211–1218.
   Google Scholar
• M Batina, F. de, A.C. Cintra, E.L. Veronese, M.A. Lavrador, J.R. Giglio, P.S. Pereira, D.A. Dias, S.C. Franca, and S.V. Sampaio. 2000. Inhibition of the lethal and myotoxic activities of Crotalus durissus terrificus venom by Tabernaemontana catharinensis: Identification of one of the active components. Planta. Med. 66 (5):424–428.
   PubMedGoogle Scholar
• J.H.Y. Vilegas, F.M. Lançasa, W. Vilegas, and G.L. Pozettib. Further triterpenes, steroids and furocoumarins from Brazilian medicinal plants of Dorstenia genus (Moraceae). J. Braz. Chem. Soc.1997 66 (5):529–535.
   Google Scholar
• D. Hazlett. 1986. Ethnobotanical observations from Cabecar and Guaymí settlements in Central America. Econ. Bot. 40 (4):339–352.
   Google Scholar
• J.F. Morton. 1990. Mucilaginous plants and their uses in medicine. J. Ethnopharmacol. 29 (3):245–266.
   PubMedGoogle Scholar
• F.G. Coe, and G.J. Anderson. 1996. Screening of medicinal plants used by the Garífuna of Eastern Nicaragua for bioactive compounds. J. Ethnopharmacol. 53 (1):29–50.
   PubMedGoogle Scholar
• J.J. Moreno. 1993. Effect of aristolochic acid on arachidonic acid cascade and in vivo models of inflammation. Immunopharmacology 26 (1):1–9.
   PubMedGoogle Scholar
• M.J. Hutt, and P.J. Houghton. 1998. A survey from the literature of plants used to treat scorpion stings. Review article. J. Ethnopharmacol. 60 (2):97–110.
   PubMedGoogle Scholar
• W. Wong. 1976. Some folk medicinal plants from Trinidad. Econ. Bot. 30 (2):103–142.
   Google Scholar
• O. Castro, J.M. Gutierrez, M. Barrios, I. Castro, M. Romero, and E. Umana. 1999. Neutralization of the hemorrhagic effect induced by Bothrops asper (Serpentes: Viperidae) venom with tropical plant extracts. Rev. Biol. Trop. 47 (3):605–616.
   PubMedGoogle Scholar
• P.A. Melo, and C.L. Ownby. 1999. Ability of wedelolactone, heparin and para-bromophenacyl bromide to antagonize the myotoxic effects of two crotaline venoms and their PLA2 myotoxins. Toxicon 37 (1):199–215.
   PubMedGoogle Scholar
• G. Bourdy, S.J. DeWalt, L.R. Chávez de Michel, A. Roca, E. Deharo, V. Muñoz, L. Balderrama, C. Quenevo, and A. Gimenez. 2000. Medicinal plants uses of the Tacana, an Amazonian Bolivian ethnic group. J. Ethnopharmacol. 70 (2):87–109.
   PubMedGoogle Scholar
• W. Setzer, T. Green, K. Whitake, D. Moriarity, C. Yancey, R. Lawton, and R. Bates. 1995. A cytotoxic diacetylene from Dendropanax arboreus. Planta. Med. 61 (5):470–471.
   PubMedGoogle Scholar
• M.W. Bernart, J. Cardellina, M. Balaschak, M. Alexander, R. Shoemaker, and M. Boyd. 1996. Cytotoxic falcarinol oxylipins from Dendropanax arboreus. J. Nat. Prod. 59 (8):748–753.
   PubMedGoogle Scholar
• R. Otero, V. Núñez, S.L. Jiménez, R. Fonnegra, R.G. Osorio, M.E. García, and A. Díaz. 2000a. Snakebites and ethnobotany in the northwest region of Colombia. Part II: Neutralization of lethal and enzymatic effects of Bothrops atrox venom. J. Ethnopharmacol. 71 (3):505–511.
   PubMedGoogle Scholar
• I. Indrayanto, B. Setiawan, and N. Cholies. 1994. Differential diosgenin accumulation in Costus speciosus and its tissue cultures. Planta. Med. 60 (5):483–484.
   PubMedGoogle Scholar
• K. Inoue, M. Shibuya, K. Yamamoto, and Y. Ebizuka. 1996. Molecular cloning and bacterial expression of a cDNA encoding furostanol glycoside 26-O-beta-glucosidase of Costus speciosus.. FEBS. Lett. 389 (3):273–277.
   PubMedGoogle Scholar
• R.W. Snow, R. Bronzan, T. Roques, C. Nyamawi, S. Murphy, and K. Marsh. 1994. The prevalence and morbidity of snake bite and treatment-seeking behavior among a rural Kenyan population. Ann. Trop. Med. Parasitol. 88 (6):665–671.
   PubMedGoogle Scholar
• JO Kokwaro. Nairobi. Medicinal Plants of East Africa. East Africa Education Publishers, 1994
   Google Scholar
• J.C. Aguiyi, A.C. Igweh, U.G. Egesie, and R. Leoncini. 1999. Studies of possible protection against snake venom using Mucuna pruriens protein immunization. Fitoterapia 70 (1):21–24.
   Google Scholar
• R. Guerranti, J.C. Aguiyi, R. Leoncini, R. Pagani, G. Cinci, and E. Marinello. 1999. Characterization of the factor responsible for the antisnake activity of Mucuna pruriens seeds. J. Prev. Med. Hyg. 1 (40):25–28.
   Google Scholar
• R. Guerranti, J.C. Aguiyi, S. Neri, R. Leoncini, R. Pagani, and E. Marinello. 2002. Proteins from Mucuna pruriens and enzymes from Echis carinatus venom. J. Ethnopharmacol. 277 (19):17072–17078.
   Google Scholar
• A. Rodriguez-Acosta, W. Uzcategui, R. Azuaje, I. Aguilar, and M.E. Girón. 2000. Clinical and Epidemiological Analysis of Bothrops Snake accidents in Venezuela. Rev. Cub. Med. Trop. 52 (2):90–94.
   PubMedGoogle Scholar
• R. Otero, V. Núñez, J. Barona, R. Fonnegra, S.L. Jiménez, R.G. Osorio, M. Saldarriaga, and A. Díaz. Snakebites and ethnobotany in the northwest region of Colombia. Part III: Neutralization of the haemorrhagic effect of Bothrops atrox venom. J. Ethnopharmacol. 2000b 73 (1–2):233–241.
   Google Scholar
• L. Joly, S. Guerra, R. Séptimo, P. Solís, M. Correa, M. Gupta, S. Levy, and F Sandberg. 1987. Ethnobotanical inventory of medicinal plants used by the Guaymi Indians in Western Panama. Part I. J. Ethnopharmacol. 20 (2):145–171.
   PubMedGoogle Scholar
• L. de Almeida, A.C.O. Cintra, E.L.G. Veronese, A. Nomizo, J.J. Franco, E.C. Arantes, J.R. Giglio, and S. V. Sampaio. 2004. Anticrotalic and antitumoral activities of gel filtration fractions of aqueous extract from Tabernaemontana catharinensis (Apocynaceae). Comp. Biochem. Physiol. Part C. 137 (1):19–27.
   PubMedGoogle Scholar
• Y.C. Hung, V. Sava, M.Y. Hong, and G.S. Huang. 2004. Inhibitory effects on phopholipase A2 and antivenin activity of melanin extracted from Thea sinensis Linn. Life Sci. 74 (16):2037–2047.
   PubMedGoogle Scholar
• C. Yoosook, Y. Panpisutchai, S. Chaichana, T. Santisuk, and V. Reutrakul. 1999. Evaluation of anti-HSV-2 activities of Barleria lupulina and Clinacanthus nutans. J. Ethnopharmacol. 67 (2):179–187.
   PubMedGoogle Scholar
• T. Kanchanapoom, R. Kasai, and K. Yamasaki. 2001. Iridoid glucosides from Barleria lupulina. Phytochemistry 58 (2):337–341.
   PubMedGoogle Scholar
• P. Pithayanukul, S. Laovachirasuwan, R. Bavovada, N. Pakmanee, and R. Suttisri. 2004. Anti-venom potential of butanolic extract of Eclipta prostrata against Malayan pit viper venom. J Ethnopharmacol. 90 (2–3):347–352.
   PubMedGoogle Scholar
• E. Haslam. Polyphenols-vegetable tannins. In: J.D. Phillipson, D.C. Ayres, and J. Baster (Eds.), Plant polyphenols: vegetable tannins revisited. Cambridge: Cambridge University Press, 1989, 1–81.
   Google Scholar
• M.I. Alam, and A. Gomes. 2003. Snake venom neutralization by Indian medicinal plants (Vitex negundo and Emblica officinalis) root extracts. J. Ethnopharmacol. 86 (1):75–80.
   PubMedGoogle Scholar
• K.S. Girish, H.P. Mohanakumari, S. Nagaraju, B.S. Vishwanath, and K. Kemparaju. 2004. Hyaluronidase and protease activities from Indian snake venoms: neutralization by Mimosa pudica root extract. Fitoterapia 75 (3–4):378–380.
   PubMedGoogle Scholar
• K. Kemparaju, and K.S. Girish. 2006. Snake venom hyaluronidase: A therapeutic target. Cell Biochem. Funct. 24 (1):7–12.
   PubMedGoogle Scholar
• P.B. Jurgilas, A.G.C. Neves. Ferreira, G.B. Domont, H. Moussatché, and J. Perales. 1999. Detection of an antibothropic fraction in opossum (Didelphis marsupialis) milk that neutralizes Bothrops jararaca venom. Toxicon 37 (1):167–172.
   PubMedGoogle Scholar
• A.G.C. Neves-Ferreira, R.H. Valente, P.G. Sa, S.L.G. Rocha, H. Moussatché, G.B. Domont, and J. Perales. 1999. New methodology for the obtainment of antibothropic factors from the South American opossum (Didelphis marsupialis) and jararaca snake (Bothrops jararaca). Toxicon 37 (10):1417–1429.
   PubMedGoogle Scholar
• L.M. Salgueiro, A. Rodríguez-Acosta, P. Rivas-Vetencourt, M. Zerpa, G. Carrillo, I. Aguilar, M.E. Girón, C.E. Acevedo, and K. Gendzekhadze. 2001. Inhibition of crotalidae venom hemorrhagic activities by Didelphis marsupialis liver spheroids culture supernatants. J. Nat. Toxins 10 (2):91–97.
   PubMedGoogle Scholar
• P.O. Seglen. Methods in Enzymology. Preparation of Isolated Rat Liver Cells, D.M. Prescot Ed. 1976, 29–83.
   Google Scholar
• J. Landry, D. Bernier, C. Oullet, R. Goyette, and N. Marceau. 1985. Spheroidal aggregate culture of rat liver cells: Histotypic reorganization; biomatrix deposition; and maintenance of functional activities. J. Cell. Biol. 101 (3):914–923.
   PubMedGoogle Scholar
• A.P. Li, S.M. Colburn, and D.J. Beck. 1992. A simplified method for the culturing of primary adult rat and human hepatocytes as multicellular spheroids. In Vitro. Cell. Dev. Biol. 28A (9–10):673–677.
   PubMedGoogle Scholar
• J.Z. Tong, P. De Lagausie, V. Furlan, T. Cresteil, O. Bernard, and F. Alvarez. 1992. Long-term culture of adult rat hepatocyte spheroids. Exp. Cell Res. 200 (2):326–332.
   PubMedGoogle Scholar
• E.E. Sánchez, C. García, J.C. Pérez, and S.J. De la Zerda. 1998. The detection of hemorrhagic proteins in snake venoms using monoclonal antibodies against virginiana opossum (Didelphis virginiana) serum. Toxicon 36 (10):1451–1459.
   PubMedGoogle Scholar
• J.L. Glenn, R.C. Straight, M.C. Wolfe, and D.L. Hardy. 1983. Geographical variation in Crotalus scutulatus scutulatus (Mojave rattlesnake) venom properties. Toxicon 21 (1):119–130.
   PubMedGoogle Scholar
• E.E. Sánchez, J.A. Galán, R.L. Powell, S.R. Reyes, J.G. Soto, W.K. Russell, D.H. Russell, and J.C. Pérez. 2005. Disintegrin, hemorrhagic, and proteolytic activities of Mohave rattlesnake, Crotalus scutulatus scutulatus venoms lacking Mojave toxin. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 141 (2):124–132.
   PubMedGoogle Scholar
• A.M. Salazar, A. Rodriguez-Acosta, M.E. Girón, I. Aguilar, and B. Guerrero. 2007. A comparative analysis of the clotting and fibrinolytic activities of the snake venom (Bothrops atrox) from different geographical areas in Venezuela. Thromb Res. 120 (1):95–104.
   PubMedGoogle Scholar
• I. Aguilar, B. Guerrero, A.M. Salazar, M.E. Girón, J.C. Pérez, E.E. Sánchez, and A. Rodríguez-Acosta. 2007. Individual venom variability in the South American rattlesnake Crotalus durissus cumanensis. Toxicon 50 (2):214–224.
   PubMedGoogle Scholar
• M.E. Girón, A.M. Salazar, I. Aguilar, J.C. Pérez, E.E. Sánchez, C.L. Arocha-Piñango, A. Rodríguez-Acosta, and B. Guerrero. 2008. Hemorrhagic, coagulant and fibrino(geno)lytic activities of crude venom and fractions from mapanare (Bothrops colombiensis) snakes. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 147 (1):113–121.
   PubMedGoogle Scholar