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Linked References

1. F. S. Markland, “Snake venoms and the hemostatic system,” Toxicon, vol. 36, no. 12, pp. 1749–1800, 1998. View at Publisher · View at Google Scholar · View at Scopus
2. C. A. Bello, A. L. N. Hermogenes, A. Magalhaes et al., “Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom,” Biochimie, vol. 88, no. 2, pp. 189–200, 2006. View at Publisher · View at Google Scholar · View at Scopus
3. D. Mebs and T. Langeluddeke, “European viper venoms: haemorrhagic and myotoxic activities,” Toxicon, vol. 30, no. 10, pp. 1303–1306, 1992. View at Publisher · View at Google Scholar · View at Scopus
4. A. Leonardi, F. Aragon-Ortiz, F. Gubenšek, and I. Križaj, “Partial primary structure of a fibrinogenase from the venom of the snake Lachesis stenophrys,” Journal of Chromatography A, vol. 852, no. 1, pp. 237–243, 1999. View at Publisher · View at Google Scholar · View at Scopus
5. J. B. Bjarnason and J. W. Fox, “Snake venom metalloendopeptidases: reprolysins,” Methods in Enzymology, vol. 248, pp. 345–368, 1995. View at Publisher · View at Google Scholar · View at Scopus
6. J. W. Fox and S. M. T. Serrano, “Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases,” Toxicon, vol. 45, no. 8, pp. 969–985, 2005. View at Publisher · View at Google Scholar · View at Scopus
7. J. W. Fox and S. M. T. Serrano, “Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity,” FEBS Journal, vol. 275, no. 12, pp. 3016–3030, 2008. View at Publisher · View at Google Scholar · View at Scopus
8. O. H. P. Ramos and H. S. Selistre-De-Araujo, “Snake venom metalloproteases—structure and function of catalytic and disintegrin domains,” Comparative Biochemistry and Physiology C, vol. 142, no. 3-4, pp. 328–346, 2006. View at Publisher · View at Google Scholar · View at Scopus
9. W. J. Wang, C. H. Shih, and T. F. Huang, “Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom,” Biochimie, vol. 87, no. 12, pp. 1065–1077, 2005. View at Publisher · View at Google Scholar · View at Scopus
10. M. T. Assakura, C. A. Silva, R. Mentele, A. C. M. Camargo, and S. M. T. Serrano, “Molecular cloning and expression of structural domains of bothropasin, a P-III metalloproteinase from the venom of Bothrops jararaca,” Toxicon, vol. 41, no. 2, pp. 217–227, 2003. View at Publisher · View at Google Scholar · View at Scopus
11. M. Maruyama, M. Sugiki, E. Yoshida, H. Mihara, and N. Nakajima, “Purification and characterization of two fibrinolytic enzymes from Bothrops jararaca (jararaca) venom,” Toxicon, vol. 30, no. 8, pp. 853–864, 1992. View at Publisher · View at Google Scholar · View at Scopus
12. M. Maruyama, M. Sugiki, K. Anai, and E. Yoshida, “N-terminal amino acid sequences and some characteristics of fibrinolytic/hemorrhagic metalloproteinases purified from Bothrops jararaca venom,” Toxicon, vol. 40, no. 8, pp. 1223–1226, 2002. View at Publisher · View at Google Scholar · View at Scopus
13. M. T. Assakura, A. P. Reichl, M. C. Asperti, and F. R. Mandelbaum, “Isolation of the major proteolytic enzyme from the venom of the snake Bothrops moojeni (Caissaca),” Toxicon, vol. 23, no. 4, pp. 691–706, 1985. View at Scopus
14. S. M. T. Serrano, M. F. C. Matos, F. R. Mandelbaum, and C. A. M. Sampaio, “Basic proteinases from Bothrops moojeni (Caissaca) venom—I. Isolation and activity of two serine proteinases, MSP 1 and MSP 2, on synthetic substrates and on platelet aggregation,” Toxicon, vol. 31, no. 4, pp. 471–481, 1993. View at Publisher · View at Google Scholar · View at Scopus
15. S. M. T. Serrano, C. A. M. Sampaio, and F. R. Mandelbaum, “Basic proteinases from Bothrops moojeni (caissaca) venom—II. Isolation of the metalloproteinase MPB. Comparison of the proteolytic activity on natural substrates by MPB, MSP 1 and MSP 2,” Toxicon, vol. 31, no. 4, pp. 483–492, 1993. View at Publisher · View at Google Scholar · View at Scopus
16. C. P. Bernardes, N. A. Santos-Filho, T. R. Costa et al., “Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom,” Toxicon, vol. 51, no. 4, pp. 574–584, 2008. View at Publisher · View at Google Scholar · View at Scopus
17. M. S. R. Gomes, M. M. Mendes, F. de Oliveira et al., “BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom,” Toxicon, vol. 53, no. 1, pp. 24–32, 2009. View at Publisher · View at Google Scholar · View at Scopus
18. P. K. Akao, C. C. C. Tonoli, M. S. Navarro et al., “Structural studies of BmooMPα-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom,” Toxicon, vol. 55, no. 2-3, pp. 361–368, 2010. View at Publisher · View at Google Scholar · View at Scopus
19. V. M. Rodrigues, A. M. Soares, R. Guerra-Sá, V. Rodrigues, M. R. M. Fontes, and J. R. Giglio, “Structural and functional characterization of neuwiedase, a nonhemorrhagic fibrin(ogen)olytic metalloprotease from Bothrops neuwiedi snake venom,” Archives of Biochemistry and Biophysics, vol. 381, no. 2, pp. 213–224, 2000. View at Publisher · View at Google Scholar · View at Scopus
20. C. Baldo, I. Tanjoni, I. R. León et al., “BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP,” Toxicon, vol. 51, no. 1, pp. 54–65, 2008. View at Publisher · View at Google Scholar · View at Scopus
21. D. S. Lopes, C. Baldo, C. de Freitas Oliveira et al., “Characterization of inflammatory reaction induced by neuwiedase, a P-I metalloproteinase isolated from Bothrops neuwiedi venom,” Toxicon, vol. 54, no. 1, pp. 42–49, 2009. View at Publisher · View at Google Scholar · View at Scopus
22. A. Magalhães, H. P. B. Magalhães, M. Richardson et al., “Purification and properties of a coagulant thrombin-like enzyme from the venom of Bothrops leucurus,” Comparative Biochemistry and Physiology A, vol. 146, no. 4, pp. 565–575, 2007. View at Publisher · View at Google Scholar · View at Scopus
23. E. F. Sanchez, L. M. Gabriel, S. Gontijo et al., “Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom,” Archives of Biochemistry and Biophysics, vol. 468, no. 2, pp. 193–204, 2007. View at Publisher · View at Google Scholar · View at Scopus
24. S. Marcussi, C. P. Bernardes, N. A. Santos-Filho et al., “Molecular and functional characterization of a new non-hemorrhagic metalloprotease from Bothrops jararacussu snake venom with antiplatelet activity,” Peptides, vol. 28, no. 12, pp. 2328–2339, 2007. View at Publisher · View at Google Scholar · View at Scopus
25. M. V. Mazzi, S. Marcussi, G. B. Carlos et al., “A new hemorrhagic metalloprotease from Bothrops jararacussu snake venom: isolation and biochemical characterization,” Toxicon, vol. 44, no. 2, pp. 215–223, 2004. View at Publisher · View at Google Scholar · View at Scopus
26. M. V. Mazzi, A. J. Magro, S. F. Amui et al., “Molecular characterization and phylogenetic analysis of BjussuMP-I: a RGD-P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake venom,” Journal of Molecular Graphics and Modelling, vol. 26, no. 1, pp. 69–85, 2007. View at Publisher · View at Google Scholar · View at Scopus
27. J. Gutiérrez, M. Romero, C. Díaz, G. Borkow, and M. Ovadia, “Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo),” Toxicon, vol. 33, no. 1, pp. 19–29, 1995. View at Publisher · View at Google Scholar · View at Scopus
28. A. Franceschi, A. Rucavado, N. Mora, and J. M. Gutiérrez, “Purification and characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper,” Toxicon, vol. 38, no. 1, pp. 63–77, 2000. View at Publisher · View at Google Scholar · View at Scopus
29. Y. A. Senis, P. Y. Kim, G. L. J. Fuller et al., “Isolation and characterization of cotiaractivase, a novel low molecular weight prothrombin activator from the venom of Bothrops cotiara,” Biochimica et Biophysica Acta, vol. 1764, no. 5, pp. 863–871, 2006. View at Publisher · View at Google Scholar · View at Scopus
30. N. A. Santos-Filho, L. B. Silveira, C. Z. Oliveira et al., “A new acidic myotoxic, anti-platelet and prostaglandin I2 inductor phospholipase A₂ isolated from Bothrops moojeni snake venom,” Toxicon, vol. 52, no. 8, pp. 908–917, 2008. View at Publisher · View at Google Scholar · View at Scopus
31. R. F. Itzhaki and D. M. Gill, “A micro-biuret method for estimating proteins,” Analytical Biochemistry, vol. 9, no. 4, pp. 401–410, 1964. View at Scopus
32. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
33. A. Henschen, “Analysis of cysteine residues, disulfide bridges, and sulfydryl groups in proteins,” in Advanced Methods in Protein Microsequence Analysis, B. Wittmann-Liebold, J. Salnikow, and V. A. Erdmann, Eds., pp. 244–255, Springer, Berlin, Germany, 1986.
34. M. Richardson, A. M. C. Pimenta, M. P. Bemquerer et al., “Comparison of the partial proteomes of the venoms of Brazilian spiders of the genus Phoneutria,” Comparative Biochemistry and Physiology C, vol. 142, no. 3-4, pp. 173–187, 2006. View at Publisher · View at Google Scholar · View at Scopus
35. W. Edgar and C. R. M. Prentice, “The proteolytic action of ancrod on human fibrinogen and its polypeptide chains,” Thrombosis Research, vol. 2, no. 1, pp. 85–95, 1973. View at Scopus
36. H. Kondo, S. Kondo, H. Ikezawa, R. Murata, and A. Ohsaka, “Studies on the quantitative method for determination of hemorrhagic activity of habu snake venom,” Japanese Journal of Medical Science & Biology, vol. 13, pp. 43–51, 1960.
37. R. D. G. Theakston and H. A. Reid, “Development of simple standard assay procedures for the characterization of snake venoms,” Bulletin of the World Health Organization, vol. 61, no. 6, pp. 949–956, 1983. View at Scopus
38. J. A. Gene, A. Roy, G. Rojas, J. M. Gutierrez, and L. Cerdas, “Comparative study on coagulant, defibrinating, fibrinolytic and fibrinogenolytic activities of Costa Rican crotaline snal venoms and their neutralization by a polyvalent antivenom,” Toxicon, vol. 27, no. 8, pp. 841–848, 1989. View at Scopus
39. A. Leonardi, F. Gubenseek, and I. Frizaj, “Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes,” Toxicon, vol. 40, no. 1, pp. 55–62, 2002. View at Publisher · View at Google Scholar · View at Scopus
40. B. Rates, K. K. F. Ferraz, M. H. Borges, M. Richardson, M. E. De Lima, and A. M. C. Pimenta, “Tityus serrulatus venom peptidomics: assessing venom peptide diversity,” Toxicon, vol. 52, no. 5, pp. 611–618, 2008. View at Publisher · View at Google Scholar · View at Scopus
41. J. M. Gutiérrez and A. Rucavado, “Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage,” Biochimie, vol. 82, no. 9-10, pp. 841–850, 2000. View at Publisher · View at Google Scholar · View at Scopus
42. G. L. Zaganelli, M. G. M. Zaganelli, A. Magalhães, C. R. Diniz, and M. E. De Lima, “Purification and characterization of a fibrinogen-clotting enzyme from the venom of jararacucu (Bothrops jararacussu),” Toxicon, vol. 34, no. 7, pp. 807–819, 1996. View at Publisher · View at Google Scholar · View at Scopus
43. A. Lobo de Araújo, J. L. Donato, and C. Bon, “Purification and characterization of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes,” Toxicon, vol. 40, no. 1, pp. 55–92, 1998.
44. M. B. Smolka, S. Marangoni, B. Oliveira, and J. C. Novello, “Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus,” Toxicon, vol. 36, no. 7, pp. 1059–1063, 1998. View at Publisher · View at Google Scholar · View at Scopus
45. H. C. Castro, D. L. S. Dutra, and A. L. Oliveira-Carvalho, “Bothroalternin, a trombin inhibitor from the venom of Bothrops alternatus,” Toxicon, vol. 29, article 1279, 1998.
46. F. Oliveira, V. M. Rodrigues, M. H. Borges et al., “Purification and partial characterization of a new proteolytic enzyme from the venom of Bothrops moojeni (Caissaca),” Biochemistry and Molecular Biology International, vol. 47, no. 6, pp. 1069–1077, 1999. View at Scopus
47. A. M. Soares, S. H. Andrião-Escarso, Y. Angulo et al., “Structural and functional characterization of myotoxin I, a Lys49 phospholipase A₂ homologue from Bothrops moojeni (Caissaca) snake venom,” Archives of Biochemistry and Biophysics, vol. 373, no. 1, pp. 7–15, 2000. View at Publisher · View at Google Scholar · View at Scopus
48. S. L. Loayza, M. Trikha, F. S. Markland, P. Riquelme, and J. Kuo, “Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrir snake venom, and comparison of their EDTA sensitivities,” Journal of Chromatography B, vol. 662, no. 2, pp. 227–243, 1994. View at Publisher · View at Google Scholar · View at Scopus
49. E. F. Sanchez, C. T. Souza, C. A. Bello, M. Richardson, E. B. Oliveira, and A. Magalhaes, “Resolution of isoforms of mutalysin II, the metalloproteinase from bushmaster snake venom,” Toxicon, vol. 41, no. 8, pp. 1021–1031, 2003. View at Publisher · View at Google Scholar · View at Scopus
50. R. N. Ferreira, B. Rates, M. Richardson et al., “Complete amino-acid sequence, crystallization and preliminary X-ray diffraction studies of leucurolysin-a, a nonhaemorrhagic metalloproteinase from Bothrops leucurus snake venom,” Acta Crystallographica Section F, vol. 65, no. 8, pp. 798–801, 2009. View at Publisher · View at Google Scholar · View at Scopus
51. O. H. Jeon and D. S. Kim, “Molecular cloning and functional characterization of a snake venom metalloprotease,” European Journal of Biochemistry, vol. 263, no. 2, pp. 526–533, 1999. View at Publisher · View at Google Scholar · View at Scopus
52. E. F. Sanchez, C. R. Diniz, and M. Richardson, “The complete amino acid sequence of the haemorrhagic factor LHFII, a metalloproteinase isolated from the venom of the Bushmaster snake (Lachesis muta muta),” FEBS Letters, vol. 282, no. 1, pp. 178–182, 1991. View at Publisher · View at Google Scholar · View at Scopus
53. T. Matsui, Y. Fujimura, and K. Titani, “Snake venom proteases affecting hemostasis and thrombosis,” Biochimica et Biophysica Acta, vol. 1477, no. 1-2, pp. 146–156, 2000. View at Publisher · View at Google Scholar · View at Scopus
54. J. B. Bjarnason and J. W. Fox, “Hemorrhagic metalloproteinases from snake venoms,” Pharmacology and Therapeutics, vol. 62, no. 3, pp. 325–372, 1994. View at Publisher · View at Google Scholar · View at Scopus
55. S. Herrick, O. Blanc-Brude, A. Gray, and G. Laurent, “Fibrinogen,” The International Journal of Biochemistry & Cell Biology, vol. 31, no. 7, pp. 741–746, 1999. View at Publisher · View at Google Scholar · View at Scopus
56. W. Stocker, F. Grams, U. Baumann et al., “The metzincins—topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases,” Protein Science, vol. 4, no. 5, pp. 823–840, 1995. View at Scopus
57. Z. Z. Sapru, A. T. Tu, and G. S. Bailey, “Purification and characterization of a fibrinogenase from the venom of western diamondback rattlesnakes (Crotalus atrox),” Biochimica et Biophysica Acta, vol. 747, no. 3, pp. 225–231, 1983. View at Publisher · View at Google Scholar · View at Scopus
58. T. F. Huang, J. H. Chang, and C. Ouyang, “Characterization of hemorrhagic principles from Trimeresurus gramineus snake venom,” Toxicon, vol. 22, no. 1, pp. 45–52, 1984. View at Scopus
59. E. N. Baramova, J. D. Shannon, J. B. Bjarnason, S. L. Gonias, and J. W. Fox, “Interaction of hemorrhagic metalloproteinases with human α2-macroglobulin,” Biochemistry, vol. 29, no. 4, pp. 1069–1074, 1990. View at Scopus
60. L. F. M. Izidoro, V. M. Rodrigues, R. S. Rodrigues et al., “Neutralization of some hematological and hemostatic alterations induced by neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi pauloensis snake venom, by the aqueous extract from Casearia mariquitensis (Flacourtiaceae),” Biochimie, vol. 85, no. 7, pp. 669–675, 2003. View at Publisher · View at Google Scholar · View at Scopus
61. W. Stocker, F. X. Gomis-Ruth, W. Bode, and R. Zwilling, “Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases,” European Journal of Biochemistry, vol. 214, no. 1, pp. 215–231, 1993. View at Scopus
62. W. Bode, F. Grams, P. Reinemer et al., “The metzincin-superfamily of zinc-peptidases,” Advances in Experimental Medicine and Biology, vol. 389, pp. 1–11, 1996. View at Scopus
63. A. L. Guan, A. D. Retzios, G. N. Henderson, and F. S. Markland, “Purification and characterization of a fibrinolytic enzyme from venom of the southern copperhead snake (Agkistrodon contortrix contortrix),” Archives of Biochemistry and Biophysics, vol. 289, no. 2, pp. 197–207, 1991. View at Scopus
64. A. D. Retzios and F. S. Markland, “A direct-acting fibrinolytic enzyme from the venom of Agkistrodon contortrix contortrix: effects on various components of the human blood coagulation and fibrinolysis systems,” Thrombosis Research, vol. 52, no. 6, pp. 541–552, 1988. View at Scopus
65. C. F. Toombs, “Alfimeprase: pharmacology of a novel fibrinolytic metalloproteinase for thrombolysis,” Haemostasis, vol. 31, no. 3–6, pp. 141–147, 2001. View at Scopus
66. C. F. Toombs, “New directions in thrombolytic therapy,” Current Opinion in Pharmacology, vol. 1, no. 2, pp. 164–168, 2001. View at Publisher · View at Google Scholar · View at Scopus
67. V. J. Marder and S. Sherry, “Thrombolytic therapy: current status,” The New England Journal of Medicine, vol. 318, no. 24, pp. 1585–1595, 1988. View at Scopus
68. F. S. Markland, J. J. Bookstein, and T. Machado, “In vivo fibrinolytic activity of fibrolase, a metalloproteinase from the venom of Agkistrodon contortrix contortrix,” Thrombosis and Haemostasis, vol. 62, article 121, 1989.
69. T. W. Willis, A. T. Tu, and C. W. Miller, “Thrombolysis with a snake venom protease in a rat model of venous thrombosis,” Thrombosis Research, vol. 53, no. 1, pp. 19–29, 1989. View at Scopus
70. N. K. Ahmed, R. R. Gaddis, K. D. Tennant, and J. P. Lacz, “Biological and thrombolytic properties of fibrolase—a new fibrinolytic protease from snake venom,” Haemostasis, vol. 20, no. 6, pp. 334–340, 1990. View at Scopus
71. H. Abel, “Thrombolysis: the logical approach for the treatment of vascular occlusions,” Acta Cardiologica, vol. 47, no. 4, pp. 287–295, 1992. View at Scopus
72. M. Verstraete, H. R. Lijnen, and D. Collen, “Thrombolytic agents in development,” Drugs, vol. 50, no. 1, pp. 29–42, 1995. View at Scopus
73. N. A. Marsh and T. L. Fyffe, “Practical applications of snake venom toxins in haemostasis,” Bollettino della Società Italiana di Biologia Sperimentale, vol. 72, no. 9-10, pp. 263–278, 1996. View at Scopus
74. A. Gasmi, A. Chabchoub, S. Guermazi, H. Karoui, M. Elayeb, and K. Dellagi, “Further characterization and thrombolytic activity in a rat model of a fibrinogenase from Vipera lebetina venom,” Thrombosis Research, vol. 86, no. 3, pp. 233–242, 1997. View at Publisher · View at Google Scholar · View at Scopus
75. E. S. Garcia, J. A. Guimaraes, and J. L. Prado, “Purification and characterization of a sulfhydryl-dependent protease from Rhodnius prolixus midgut,” Archives of Biochemistry and Biophysics, vol. 188, no. 2, pp. 315–322, 1978. View at Scopus
76. J. R. F. Sousa, R. Q. Monteiro, H. C. Castro, and R. B. Zingali, “Proteolytic action of Bothrops jararaca venom upon its own constituents,” Toxicon, vol. 39, no. 6, pp. 787–792, 2001. View at Publisher · View at Google Scholar · View at Scopus
77. S. Iwanaga and T. Suzuki, “Enzymes in snake venoms,” in Snake Venom: Handbook of Experimental Pharmacology, C. Y. Lee, Ed., vol. 52, pp. 61–158, Springer, Berlin, Germany, 1979.
78. S. Terada, J. Hori, S. Fujimura, and E. Kimoto, “Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom,” Journal of Biochemistry, vol. 125, no. 1, pp. 64–69, 1999. View at Scopus