메뉴 건너뛰기




Volumn 13, Issue 28, 2007, Pages 2935-2950

Trends in snakebite envenomation therapy: Scientific, technological and public health considerations

Author keywords

Antivenom; Hemorrhage; Inflammation; Metalloproteinase inhibitors; Necrosis; Phospholipase A2 inhibitors; Snake venom

Indexed keywords

ADRENALIN; ANTIHISTAMINIC AGENT; ARISTOLOCHIC ACID; AUROTHIOMALATE; BATIMASTAT; COMPLEMENTARY DNA; CROMOGLYCATE DISODIUM; CROTOXIN; ENZYME INHIBITOR; HYALURONIDASE ANTIBODY; IMMUNOGLOBULIN F(AB')2 FRAGMENT; IMMUNOGLOBULIN G; IMMUNOLOGICAL ADJUVANT; MARIMASTAT; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; MONOCLONAL ANTIBODY; MYOTOXIN INHIBITOR; NEUROTOXIN; NEUTRALIZING ANTIBODY; PHOSPHOLIPASE A2 INHIBITOR; PLASMID DNA; RECOMBINANT DNA; SNAKE VENOM; STEROID; SURAMIN; TETRACYCLINE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VENOM ANTISERUM; VIPERID;

EID: 38449100299     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161207782023784     Document Type: Review
Times cited : (127)

References (230)
  • 1
    • 0002304931 scopus 로고
    • Snakebite mortality in the world
    • Swaroop S, Grab B. Snakebite mortality in the world. Bull WHO 1954; 10: 35-76.
    • (1954) Bull WHO , vol.10 , pp. 35-76
    • Swaroop, S.1    Grab, B.2
  • 2
    • 0032428679 scopus 로고    scopus 로고
    • Snake-bites: Appraisal of the global situation
    • Chippaux JP. Snake-bites: appraisal of the global situation. Bull WHO 1998; 76: 515-24.
    • (1998) Bull WHO , vol.76 , pp. 515-524
    • Chippaux, J.P.1
  • 3
    • 0017050696 scopus 로고
    • The importance of bites by the saw-scaled or carpet viper (Echis carinatus). Epidemiological studies in Nigeria and a review of the world literature
    • Warrell DA, Arnett C. The importance of bites by the saw-scaled or carpet viper (Echis carinatus). Epidemiological studies in Nigeria and a review of the world literature. Acta Trop 1976; 33: 307-41.
    • (1976) Acta Trop , vol.33 , pp. 307-341
    • Warrell, D.A.1    Arnett, C.2
  • 5
    • 0000860011 scopus 로고
    • Gopalakrishnakone P, Tan CK Eds, Singapore, National University of Singapore
    • Warrell DA. In: Gopalakrishnakone P, Tan CK Eds. Recent Advances in Toxinology Research. Singapore, National University of Singapore 1992; 121-53.
    • (1992) Recent Advances in Toxinology Research , pp. 121-153
    • Warrell, D.A.1
  • 10
    • 0002414874 scopus 로고    scopus 로고
    • Bon C, Goyffon M Eds, Lyon, Fondation Marcel Mérieux
    • Warrell DA. In: Bon C, Goyffon M Eds. Envenomings and Their Treatments. Lyon, Fondation Marcel Mérieux 1996; 63-76.
    • (1996) Envenomings and Their Treatments , pp. 63-76
    • Warrell, D.A.1
  • 11
    • 0022256097 scopus 로고
    • Myonecrosis, myoglobinuria and acute renal failure induced by South American rattlesnake (Crotalus durissus terrificus) envenomation in Brazil
    • Azevedo-Marques MM, Cupo P, Coimbra TM, Hering SE, Rossi MA, Laure CJ. Myonecrosis, myoglobinuria and acute renal failure induced by South American rattlesnake (Crotalus durissus terrificus) envenomation in Brazil. Toxicon 1985; 23: 631-6.
    • (1985) Toxicon , vol.23 , pp. 631-636
    • Azevedo-Marques, M.M.1    Cupo, P.2    Coimbra, T.M.3    Hering, S.E.4    Rossi, M.A.5    Laure, C.J.6
  • 13
    • 0002923627 scopus 로고    scopus 로고
    • Bon C, Goyffon M Eds, Lyon, Fondation Marcel Mérieux
    • Bon C. In: Bon C, Goyffon M Eds. Envenomings and Their Treatments. Lyon, Fondation Marcel Mérieux 1996; 3-9.
    • (1996) Envenomings and Their Treatments , pp. 3-9
    • Bon, C.1
  • 14
    • 0345130918 scopus 로고
    • History of the primordia of snake-bite accident serotherapy
    • Vital Brazil O. History of the primordia of snake-bite accident serotherapy. Mem Inst Butantan 1987; 49: 7-20.
    • (1987) Mem Inst Butantan , vol.49 , pp. 7-20
    • Vital Brazil, O.1
  • 17
    • 42249105517 scopus 로고    scopus 로고
    • Raw I, Guidolin R, Higashi HG, Kelen EMA. In: Tu AT Ed. Handbook of Natural Toxins, 5, Reptile Venoms and Toxins. New York, Marcel Dekker, Inc 1991; 557-81.
    • Raw I, Guidolin R, Higashi HG, Kelen EMA. In: Tu AT Ed. Handbook of Natural Toxins, Vol 5, Reptile Venoms and Toxins. New York, Marcel Dekker, Inc 1991; 557-81.
  • 18
    • 42249110848 scopus 로고    scopus 로고
    • Pope CG. The action of proteolytic enzymes on the antitoxins and proteins in immune sera. II. Heat denaturation after partial enzyme action. Br J Exp Pathol 1939; 20: 201-12.
    • Pope CG. The action of proteolytic enzymes on the antitoxins and proteins in immune sera. II. Heat denaturation after partial enzyme action. Br J Exp Pathol 1939; 20: 201-12.
  • 20
    • 0037376769 scopus 로고    scopus 로고
    • A protocol for 'enhanced pepsin digestion': A step by step method for obtaining pure antibody fragments in high yield from serum
    • Jones RG, Landon J. A protocol for 'enhanced pepsin digestion': a step by step method for obtaining pure antibody fragments in high yield from serum. J Immunol Methods 2003; 275: 239-50.
    • (2003) J Immunol Methods , vol.275 , pp. 239-250
    • Jones, R.G.1    Landon, J.2
  • 21
    • 0026763864 scopus 로고
    • An affinity purified ovine antivenom for he treatment of Vipera berus envenoming
    • Smith DC, Reddi KR, Laing G, Theakston RG, Landon J. An affinity purified ovine antivenom for he treatment of Vipera berus envenoming. Toxicon 1992; 30: 865-71.
    • (1992) Toxicon , vol.30 , pp. 865-871
    • Smith, D.C.1    Reddi, K.R.2    Laing, G.3    Theakston, R.G.4    Landon, J.5
  • 23
    • 0028295746 scopus 로고
    • Caprylic acid fractionation of hyperimmune horse plasma: Description of a simple procedure for antivenom production
    • Rojas G, Jiménez JM, Gutiérrez JM. Caprylic acid fractionation of hyperimmune horse plasma: description of a simple procedure for antivenom production. Toxicon 1994; 32: 351-63.
    • (1994) Toxicon , vol.32 , pp. 351-363
    • Rojas, G.1    Jiménez, J.M.2    Gutiérrez, J.M.3
  • 24
    • 0027270501 scopus 로고
    • Randomized comparative trial of three antivenoms in the treatment of envenoming by lance-headed vipers (Bothrops jararaca) in Sao Paulo, Brazil
    • Cardoso JLC, Fan HW, Franca FOS, Jorge MT, Leite RP, Nishioka SA, et al. Randomized comparative trial of three antivenoms in the treatment of envenoming by lance-headed vipers (Bothrops jararaca) in Sao Paulo, Brazil. Q J Med 1993; 86: 315-25.
    • (1993) Q J Med , vol.86 , pp. 315-325
    • Cardoso, J.L.C.1    Fan, H.W.2    Franca, F.O.S.3    Jorge, M.T.4    Leite, R.P.5    Nishioka, S.A.6
  • 25
    • 0345313645 scopus 로고    scopus 로고
    • Otero R, Gutiérrez JM, Rojas G, Núñez V, Díaz A, Miranda E, et al. A randomized blinded clinical trial of two antivenoms, prepared by caprylic acid or ammonium sulphate fractionation of IgG, in Bothrops and Porthidium snake bites in Colombia. Correlation between safety and biochemical characteristics of antivenoms. Toxicon 1999; 37: 895-908.
    • Otero R, Gutiérrez JM, Rojas G, Núñez V, Díaz A, Miranda E, et al. A randomized blinded clinical trial of two antivenoms, prepared by caprylic acid or ammonium sulphate fractionation of IgG, in Bothrops and Porthidium snake bites in Colombia. Correlation between safety and biochemical characteristics of antivenoms. Toxicon 1999; 37: 895-908.
  • 26
    • 8744224506 scopus 로고    scopus 로고
    • Crotaline snake bite in the Ecuadorian Amazon: Randomised double blind comparative trial of three South American poly-specific antivenoms
    • Smalligan R, Cole J, Brito N, Laing GD, Mertz BL, Manock S, et al. Crotaline snake bite in the Ecuadorian Amazon: randomised double blind comparative trial of three South American poly-specific antivenoms. BMJ 2004; 329: 1129-35.
    • (2004) BMJ , vol.329 , pp. 1129-1135
    • Smalligan, R.1    Cole, J.2    Brito, N.3    Laing, G.D.4    Mertz, B.L.5    Manock, S.6
  • 27
    • 0004286397 scopus 로고
    • Harvey AL Ed, New York, Pergamon Press
    • Ménez A. In: Harvey AL Ed. Snake Toxins. New York, Pergamon Press 1991; 35-90.
    • (1991) Snake Toxins , pp. 35-90
    • Ménez, A.1
  • 28
    • 0042122760 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic relationships of immunoglobulin therapy for envenomation
    • Gutiérrez JM, Leén G, Lomonte B. Pharmacokinetic-pharmacodynamic relationships of immunoglobulin therapy for envenomation. Clin Pharmacokinet 2003; 42: 721-41.
    • (2003) Clin Pharmacokinet , vol.42 , pp. 721-741
    • Gutiérrez, J.M.1    Leén, G.2    Lomonte, B.3
  • 29
    • 0344447110 scopus 로고    scopus 로고
    • Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom
    • Gutiérrez JM, León G, Rojas G, Lomonte B, Rucavado A, Chaves F. Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom. Toxicon 1998; 36: 1529-39.
    • (1998) Toxicon , vol.36 , pp. 1529-1539
    • Gutiérrez, J.M.1    León, G.2    Rojas, G.3    Lomonte, B.4    Rucavado, A.5    Chaves, F.6
  • 30
    • 0021253366 scopus 로고
    • Pathogenesis of myonecrosis induced by crude venom and a myotoxin of Bothrops asper
    • Gutiérrez JM, Ownby CL, Odell GV. Pathogenesis of myonecrosis induced by crude venom and a myotoxin of Bothrops asper. Exp Mol Pathol 1984; 40: 367-79.
    • (1984) Exp Mol Pathol , vol.40 , pp. 367-379
    • Gutiérrez, J.M.1    Ownby, C.L.2    Odell, G.V.3
  • 31
    • 0026490009 scopus 로고
    • Ultrastructural alterations in mouse capillary blood vessels after experimental injection of venom from the snake Bothrops asper (terciopelo)
    • Moreira L, Gutiérrez JM, Borkow G, Ovadia M. Ultrastructural alterations in mouse capillary blood vessels after experimental injection of venom from the snake Bothrops asper (terciopelo). Exp Mol Pathol 1992; 57: 124-33.
    • (1992) Exp Mol Pathol , vol.57 , pp. 124-133
    • Moreira, L.1    Gutiérrez, J.M.2    Borkow, G.3    Ovadia, M.4
  • 32
    • 0027976994 scopus 로고
    • The dynamics of local tissue damage induced by Bothrops asper snake venom and myotoxin II on the mouse cremaster muscle: An intravital and electron microscopic study
    • Lomonte B, Lundgren J, Johansson B, Bagge U. The dynamics of local tissue damage induced by Bothrops asper snake venom and myotoxin II on the mouse cremaster muscle: an intravital and electron microscopic study. Toxicon 1994; 32: 41-55.
    • (1994) Toxicon , vol.32 , pp. 41-55
    • Lomonte, B.1    Lundgren, J.2    Johansson, B.3    Bagge, U.4
  • 33
    • 0347296052 scopus 로고    scopus 로고
    • Assessment of efficacy on bothropic antivenom therapy on microcirculatory effects induced by Bothrops jararaca snake venom
    • Battellino C, Piazza R, da Silva AMM, Cury Y, Farsky SHP. Assessment of efficacy on bothropic antivenom therapy on microcirculatory effects induced by Bothrops jararaca snake venom. Toxicon 2003; 41: 583-93.
    • (2003) Toxicon , vol.41 , pp. 583-593
    • Battellino, C.1    Piazza, R.2    da Silva, A.M.M.3    Cury, Y.4    Farsky, S.H.P.5
  • 34
    • 8044224042 scopus 로고    scopus 로고
    • Moreno ME & the regional group on antivenom therapy research. A randomized double-blind clinical trial of two antivenoms in patients bitten by Bothrops atrox in Colombia
    • Otero R, Gutiérrez JM, Núñez V, Robles A, Estrada R, Segura E, et al. Moreno ME & the regional group on antivenom therapy research. A randomized double-blind clinical trial of two antivenoms in patients bitten by Bothrops atrox in Colombia. Trans Royal Soc Trop Med Hyg 1996; 90: 696-700.
    • (1996) Trans Royal Soc Trop Med Hyg , vol.90 , pp. 696-700
    • Otero, R.1    Gutiérrez, J.M.2    Núñez, V.3    Robles, A.4    Estrada, R.5    Segura, E.6
  • 35
    • 0024504960 scopus 로고
    • Pharmacological evaluation of rat paw oedema induced by Bothrops jararaca venom
    • Trebien HA, Calixto JB. Pharmacological evaluation of rat paw oedema induced by Bothrops jararaca venom. Agents Actions 1989; 26: 292-300.
    • (1989) Agents Actions , vol.26 , pp. 292-300
    • Trebien, H.A.1    Calixto, J.B.2
  • 36
    • 0028963003 scopus 로고
    • Pharmacological study of edema induced by venom of the snake Bothrops asper (terciopelo)
    • Chaves F, Barboza M, Gutiérrez JM. Pharmacological study of edema induced by venom of the snake Bothrops asper (terciopelo). Toxicon 1995; 33: 31-9.
    • (1995) Toxicon , vol.33 , pp. 31-39
    • Chaves, F.1    Barboza, M.2    Gutiérrez, J.M.3
  • 37
    • 28544433408 scopus 로고    scopus 로고
    • Envenoming bites by kraits: The biological basis of treatment-resistant neuromuscular paralysis
    • Prasampun S, Walsh J, Awad SS, Harris JB. Envenoming bites by kraits: the biological basis of treatment-resistant neuromuscular paralysis. Brain 2005; 128: 2987-2996.
    • (2005) Brain , vol.128 , pp. 2987-2996
    • Prasampun, S.1    Walsh, J.2    Awad, S.S.3    Harris, J.B.4
  • 39
    • 0028131307 scopus 로고
    • Antibody treatment of toxin poisoning-Recent advances
    • Scherrmann JM. Antibody treatment of toxin poisoning-Recent advances. Clin Toxicol 1994; 32: 363-75.
    • (1994) Clin Toxicol , vol.32 , pp. 363-375
    • Scherrmann, J.M.1
  • 40
    • 0030923071 scopus 로고    scopus 로고
    • Effect of antivenom on venom pharmacokinetics in experimentally envenomed rabbits: Toward an optimization of antivenom therapy
    • Riviere G, Choumet V, Audebert F, Sabouraud A, Debray M, Scherrmann JM, et al. Effect of antivenom on venom pharmacokinetics in experimentally envenomed rabbits: toward an optimization of antivenom therapy. J Pharmacol Exp Ther 1997; 281: 1-8.
    • (1997) J Pharmacol Exp Ther , vol.281 , pp. 1-8
    • Riviere, G.1    Choumet, V.2    Audebert, F.3    Sabouraud, A.4    Debray, M.5    Scherrmann, J.M.6
  • 41
    • 0037239966 scopus 로고    scopus 로고
    • Pharmacokinetics of venom toxins and their modification by antivenom therapy
    • Bon C. Pharmacokinetics of venom toxins and their modification by antivenom therapy. J Toxicol Toxin Rev 2003; 22: 129-38.
    • (2003) J Toxicol Toxin Rev , vol.22 , pp. 129-138
    • Bon, C.1
  • 42
    • 0025931518 scopus 로고
    • Snake venom variability: Methods of study, results and interpretation
    • Chippaux JP, Williams V, White J. Snake venom variability: methods of study, results and interpretation. Toxicon 1991; 29: 1279-303.
    • (1991) Toxicon , vol.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, V.2    White, J.3
  • 44
    • 0029063285 scopus 로고
    • Ability of six Latin American antivenoms to neutralize the venom of mapaná equis (Bothrops atrox) from Antioquia and Chocó (Colombia)
    • Otero R, Núñez V, Osorio RG, Gutiérrez JM, Giraldo CA, Posada LE. Ability of six Latin American antivenoms to neutralize the venom of mapaná equis (Bothrops atrox) from Antioquia and Chocó (Colombia). Toxicon 1995; 33: 809-15.
    • (1995) Toxicon , vol.33 , pp. 809-815
    • Otero, R.1    Núñez, V.2    Osorio, R.G.3    Gutiérrez, J.M.4    Giraldo, C.A.5    Posada, L.E.6
  • 45
    • 0034029451 scopus 로고    scopus 로고
    • Neutralization of crotaline snake venoms from Central and South America by antivenoms produced in Brazil and Costa Rica
    • Bogarín G, Morais JF, Yamaguchi IK, Stephano MA, Marcelino JR, Nishikawa AK, et al. Neutralization of crotaline snake venoms from Central and South America by antivenoms produced in Brazil and Costa Rica. Toxicon 2000; 38: 1429-41.
    • (2000) Toxicon , vol.38 , pp. 1429-1441
    • Bogarín, G.1    Morais, J.F.2    Yamaguchi, I.K.3    Stephano, M.A.4    Marcelino, J.R.5    Nishikawa, A.K.6
  • 47
    • 0036490361 scopus 로고    scopus 로고
    • Geographic and ontogenic variability in the venom of the neotropical rattlesnake Crotalus durissus: Pathophysiological and therapeutic implications
    • Saravia P, Rojas E, Arce V, Guevara C, López JC, Chaves E, et al. Geographic and ontogenic variability in the venom of the neotropical rattlesnake Crotalus durissus: Pathophysiological and therapeutic implications. Rev Biol Trop 2002; 50: 337-46.
    • (2002) Rev Biol Trop , vol.50 , pp. 337-346
    • Saravia, P.1    Rojas, E.2    Arce, V.3    Guevara, C.4    López, J.C.5    Chaves, E.6
  • 48
    • 0002455725 scopus 로고    scopus 로고
    • Bon C, Goyffon M Eds, Lyon, Fondation Marcel Mérieux
    • Theakston RDG. In: Bon C, Goyffon M Eds. Envenomings and Their Treatments. Lyon, Fondation Marcel Mérieux 1996; 117-26.
    • (1996) Envenomings and Their Treatments , pp. 117-126
    • Theakston, R.D.G.1
  • 49
    • 42249109346 scopus 로고    scopus 로고
    • Fan HW. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clinica e Terapeutica. Sao Paulo, Sarvier 2003; 380-93.
    • Fan HW. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clinica e Terapeutica. Sao Paulo, Sarvier 2003; 380-93.
  • 50
    • 0033381296 scopus 로고    scopus 로고
    • 2: Results of a clinical trial in northern Cameroon
    • 2: Results of a clinical trial in northern Cameroon. Am J Trop Med Hyg 1999; 61: 1017-18.
    • (1999) Am J Trop Med Hyg , vol.61 , pp. 1017-1018
    • Chippaux, J.P.1
  • 52
    • 0347117586 scopus 로고    scopus 로고
    • Parallel infusion of hydrocortisone +/- chlorpheniramine bolus injection to prevent acute adverse reactions to antivenom for snakebites
    • Gawarammana IB, Kularatne SA, Dissanayabe WP, Kumarasiri RP, Senanayake N, Ariyasena H. Parallel infusion of hydrocortisone +/- chlorpheniramine bolus injection to prevent acute adverse reactions to antivenom for snakebites. Med J Aust 2004; 180: 20-3.
    • (2004) Med J Aust , vol.180 , pp. 20-23
    • Gawarammana, I.B.1    Kularatne, S.A.2    Dissanayabe, W.P.3    Kumarasiri, R.P.4    Senanayake, N.5    Ariyasena, H.6
  • 54
    • 0033614682 scopus 로고    scopus 로고
    • Sequential randomised and double blind trial of promethazine prophylaxis against early anaphylactic reactions to antivenom for Rothrops snakebites
    • Fan HW, Marcopito LF, Cardoso JL, Franca FO, Malaque CM, Ferrari RA, et al. Sequential randomised and double blind trial of promethazine prophylaxis against early anaphylactic reactions to antivenom for Rothrops snakebites. BMJ 1999; 318: 1451-2.
    • (1999) BMJ , vol.318 , pp. 1451-1452
    • Fan, H.W.1    Marcopito, L.F.2    Cardoso, J.L.3    Franca, F.O.4    Malaque, C.M.5    Ferrari, R.A.6
  • 55
    • 0033577475 scopus 로고    scopus 로고
    • Low dose subcutaneous adrenaline to prevent acute adverse reactions to antivenom serum in people bitten by snakes: Randomized, placebo controlled trial
    • Premawardhena AP, de Silva CE, Fonseka MMD, Gunatilake SB, de Silva HJ. Low dose subcutaneous adrenaline to prevent acute adverse reactions to antivenom serum in people bitten by snakes: randomized, placebo controlled trial. BMJ 1999; 318: 1041-3.
    • (1999) BMJ , vol.318 , pp. 1041-1043
    • Premawardhena, A.P.1    de Silva, C.E.2    Fonseka, M.M.D.3    Gunatilake, S.B.4    de Silva, H.J.5
  • 56
    • 0017656477 scopus 로고
    • Serum reactions. An analysis of commercial antivenoms and the possible role of anticomplementary
    • Sutherland SK. Serum reactions. An analysis of commercial antivenoms and the possible role of anticomplementary. Med J Aust 1977; 1: 613-15.
    • (1977) Med J Aust , vol.1 , pp. 613-615
    • Sutherland, S.K.1
  • 57
    • 0022655993 scopus 로고
    • Prediction, prevention and mechanism of early (anahylactic) antivenom ractions in victim of snake bites
    • Malasit P, Warrell DA, Chantavanich P, Viravan C, Mongkilsapaya J, Singhthong B, et al. Prediction, prevention and mechanism of early (anahylactic) antivenom ractions in victim of snake bites. BMJ 1986; 292:17-20.
    • (1986) BMJ , vol.292 , pp. 17-20
    • Malasit, P.1    Warrell, D.A.2    Chantavanich, P.3    Viravan, C.4    Mongkilsapaya, J.5    Singhthong, B.6
  • 58
    • 0003191090 scopus 로고
    • Efecto del suero antiofidico sobre la actividad hemolitica del complemento humano (in vitro) y de conejo (in vitro e in vivo)
    • Montero J, Trejos M, Lomonte B. Efecto del suero antiofidico sobre la actividad hemolitica del complemento humano (in vitro) y de conejo (in vitro e in vivo). Rev Costarric Cienc Méd 1989; 10: 1-10.
    • (1989) Rev Costarric Cienc Méd , vol.10 , pp. 1-10
    • Montero, J.1    Trejos, M.2    Lomonte, B.3
  • 60
    • 0035188813 scopus 로고    scopus 로고
    • 2 polyvalent antivenoms: Neutralization of systemic effects induced by Bothrops asper venom in mice, extravasation to muscle tissue, and potential of adverse reactions
    • 2 polyvalent antivenoms: neutralization of systemic effects induced by Bothrops asper venom in mice, extravasation to muscle tissue, and potential of adverse reactions. Toxicon 2001; 39: 793-801.
    • (2001) Toxicon , vol.39 , pp. 793-801
    • León, G.1    Monge, M.2    Rojas, E.3    Lomonte, B.4    Gutiérrez, J.M.5
  • 61
    • 9744249493 scopus 로고    scopus 로고
    • Anticomplementary activity of equine whole IgG antivenoms: Comparison of three fractionation protocols
    • León G, Lomonte B, Gutiérrez JM. Anticomplementary activity of equine whole IgG antivenoms: comparison of three fractionation protocols. Toxicon 2005; 45: 123-8.
    • (2005) Toxicon , vol.45 , pp. 123-128
    • León, G.1    Lomonte, B.2    Gutiérrez, J.M.3
  • 62
    • 33749063834 scopus 로고    scopus 로고
    • Efficacy and safety of two whole IgG polyvalent antivenoms, refined by caprylic acid fractionation with or without β-propiolactone, in the treatment of Bothrops asper bites in Colombia
    • Otero R, León G, Gutiérrez JM, Rojas G, Toro MF, Barona J, et al. Efficacy and safety of two whole IgG polyvalent antivenoms, refined by caprylic acid fractionation with or without β-propiolactone, in the treatment of Bothrops asper bites in Colombia. Trans R Soc Trop Med Hyg 2006; 100: 1173-82.
    • (2006) Trans R Soc Trop Med Hyg , vol.100 , pp. 1173-1182
    • Otero, R.1    León, G.2    Gutiérrez, J.M.3    Rojas, G.4    Toro, M.F.5    Barona, J.6
  • 63
    • 0031771071 scopus 로고    scopus 로고
    • The development and use of immunotherapy in Africa
    • Chippaux JP. The development and use of immunotherapy in Africa. Toxicon 1998; 36: 1503-6.
    • (1998) Toxicon , vol.36 , pp. 1503-1506
    • Chippaux, J.P.1
  • 64
    • 6844258211 scopus 로고    scopus 로고
    • A randomized, blinded, comparative trial of one pepsindigested and two whole IgG antivenoms for Bothrops snake bites in Urabá, Colombia
    • Otero-Patiño R, Cardoso JLC, Higashi HG, Núñez V, Diaz A, Toro MF, et al. A randomized, blinded, comparative trial of one pepsindigested and two whole IgG antivenoms for Bothrops snake bites in Urabá, Colombia. Am J Trop Med Hyg 1998; 59: 183-9.
    • (1998) Am J Trop Med Hyg , vol.59 , pp. 183-189
    • Otero-Patiño, R.1    Cardoso, J.L.C.2    Higashi, H.G.3    Núñez, V.4    Diaz, A.5    Toro, M.F.6
  • 65
    • 0030213310 scopus 로고    scopus 로고
    • Heterologous antisera and antivenins are essential biologicals: Perspectives on a worldwide crisis
    • Wilde H, Thipkong P, Sitprija V, Chaiyabutr N. Heterologous antisera and antivenins are essential biologicals: perspectives on a worldwide crisis. Ann Intern Med 1996; 125: 233-6.
    • (1996) Ann Intern Med , vol.125 , pp. 233-236
    • Wilde, H.1    Thipkong, P.2    Sitprija, V.3    Chaiyabutr, N.4
  • 66
    • 0034676806 scopus 로고    scopus 로고
    • Crisis in snake antivenom supply for Africa
    • Theakston RDG, Warrell DA. Crisis in snake antivenom supply for Africa. Lancet 2000; 356: 2104.
    • (2000) Lancet , vol.356 , pp. 2104
    • Theakston, R.D.G.1    Warrell, D.A.2
  • 67
    • 0037401660 scopus 로고    scopus 로고
    • Report of a WHO workshop on the standardization and control of antivenoms
    • Theakston RDG, Warrell DA, Griffiths E. Report of a WHO workshop on the standardization and control of antivenoms. Toxicon 2003; 41: 541-57.
    • (2003) Toxicon , vol.41 , pp. 541-557
    • Theakston, R.D.G.1    Warrell, D.A.2    Griffiths, E.3
  • 70
    • 0024152153 scopus 로고
    • Factors contributing to fatal snake bite in the rural tropics: Analysis of 46 cases in Thailand
    • Looarcesuwan S, Vimvan C, Warrell DA. Factors contributing to fatal snake bite in the rural tropics: analysis of 46 cases in Thailand. Trans R Soc Trop Med Hyg 1988; 82: 930-4.
    • (1988) Trans R Soc Trop Med Hyg , vol.82 , pp. 930-934
    • Looarcesuwan, S.1    Vimvan, C.2    Warrell, D.A.3
  • 71
    • 33745617121 scopus 로고    scopus 로고
    • Confronting the neglected problem of snake bite envenoming: The need for a global partnership
    • Gutiérrez; JM, Theakston RDG, Warrell DA. Confronting the neglected problem of snake bite envenoming: the need for a global partnership. PLoS Med 2006; 3: 727-31.
    • (2006) PLoS Med , vol.3 , pp. 727-731
    • Gutiérrez, J.M.1    Theakston, R.D.G.2    Warrell, D.A.3
  • 72
    • 13844310831 scopus 로고    scopus 로고
    • A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics
    • Serrano SMT, Shannon JD, Wand D, Camargo ACM, Fox JW. A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: an approach to understanding venom proteomics. Proteomics 2005; 5: 501-10.
    • (2005) Proteomics , vol.5 , pp. 501-510
    • Serrano, S.M.T.1    Shannon, J.D.2    Wand, D.3    Camargo, A.C.M.4    Fox, J.W.5
  • 73
    • 1842584426 scopus 로고    scopus 로고
    • Development of venom toxin-specific antibodies by DNA immunization: Rationale and strategies to improve therapy of viper envenoming
    • Harrison RA. Development of venom toxin-specific antibodies by DNA immunization: rationale and strategies to improve therapy of viper envenoming. Vaccine 2004; 22: 1648-55.
    • (2004) Vaccine , vol.22 , pp. 1648-1655
    • Harrison, R.A.1
  • 74
    • 0033842555 scopus 로고    scopus 로고
    • Antibody from mice immunized with DNA encoding the carboxyl-disintegrin and cysteine-rich domain (JD9) of the hemorrhagic metalloproteinase, jararhagin, inhibits the main lethal component of viper venom
    • Harrison RA, Moura-da-Silva AM, Laing GD, Wu Y, Richards, A, Broadhead A, et al. Antibody from mice immunized with DNA encoding the carboxyl-disintegrin and cysteine-rich domain (JD9) of the hemorrhagic metalloproteinase, jararhagin, inhibits the main lethal component of viper venom. Clin Exp Immunol 2000; 121: 358-63.
    • (2000) Clin Exp Immunol , vol.121 , pp. 358-363
    • Harrison, R.A.1    Moura-da-Silva, A.M.2    Laing, G.D.3    Wu, Y.4    Richards, A.5    Broadhead, A.6
  • 75
    • 0242289639 scopus 로고    scopus 로고
    • Fractionation of equine antivenom using caprylic acid precipitation in combination with cationic ion-exchange chromatography
    • Raweerith R, Ratanabanangkoon K. Fractionation of equine antivenom using caprylic acid precipitation in combination with cationic ion-exchange chromatography. J Immunol Methods 2003; 282: 63-72.
    • (2003) J Immunol Methods , vol.282 , pp. 63-72
    • Raweerith, R.1    Ratanabanangkoon, K.2
  • 78
    • 11944274516 scopus 로고
    • Rattlesnake and scorpion antivenoms from the egg yolks of immunized hens
    • Thalley BT, Carroll SB. Rattlesnake and scorpion antivenoms from the egg yolks of immunized hens. Biotechnology 1990; 8: 934-8.
    • (1990) Biotechnology , vol.8 , pp. 934-938
    • Thalley, B.T.1    Carroll, S.B.2
  • 79
    • 1642493838 scopus 로고    scopus 로고
    • Meddeb-Mouelhi F, Bouhaouala-Zahar B, Benlasfar Z, Hammadi M, Mejri T, 'Moslah M, et al. Immunized camel sera and derived immunoglobulin subclasses neutralizing Androctonus austrans hector scorpion toxins. Toxicon 2003; 42: 785-91.
    • Meddeb-Mouelhi F, Bouhaouala-Zahar B, Benlasfar Z, Hammadi M, Mejri T, 'Moslah M, et al. Immunized camel sera and derived immunoglobulin subclasses neutralizing Androctonus austrans hector scorpion toxins. Toxicon 2003; 42: 785-91.
  • 80
    • 33644512108 scopus 로고    scopus 로고
    • Neutralisation of venom-induced haemorrhage by IgG, from camels and llamas immunized with viper venom and also by endogenous, non-IgG components in camelid sera
    • Harrison RA, Hasson SS, Harmsen M, Laing GD, Conrath K, Theakston RDG. Neutralisation of venom-induced haemorrhage by IgG, from camels and llamas immunized with viper venom and also by endogenous, non-IgG components in camelid sera. Toxicon 2006; 47: 364-8.
    • (2006) Toxicon , vol.47 , pp. 364-368
    • Harrison, R.A.1    Hasson, S.S.2    Harmsen, M.3    Laing, G.D.4    Conrath, K.5    Theakston, R.D.G.6
  • 82
    • 27444442720 scopus 로고    scopus 로고
    • Factors associated with adverse reactions induced by caprylic acid-fractionated whole IgG preparations: Comparison between horse, sheep and camel IgGs
    • Herrera M, León G, Segura A, Meneses F, Lomonte B, Chippaux JP, et al. Factors associated with adverse reactions induced by caprylic acid-fractionated whole IgG preparations: comparison between horse, sheep and camel IgGs. Toxicon 2005; 46: 775-81.
    • (2005) Toxicon , vol.46 , pp. 775-781
    • Herrera, M.1    León, G.2    Segura, A.3    Meneses, F.4    Lomonte, B.5    Chippaux, J.P.6
  • 83
    • 42249110847 scopus 로고    scopus 로고
    • Cardoso DF, Yamaguchi IK, Moura da Silva AM. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clínica e Terapeutica. Sao Paulo, Sarvier 2003; 367-79.
    • Cardoso DF, Yamaguchi IK, Moura da Silva AM. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clínica e Terapeutica. Sao Paulo, Sarvier 2003; 367-79.
  • 84
    • 0030806376 scopus 로고    scopus 로고
    • Biologically active human anticrotoxin scFv isolated from a semisynthetic phage library
    • Lafaye P, Chournet V, Demangel C, Bon C, Mazie JC. Biologically active human anticrotoxin scFv isolated from a semisynthetic phage library. Immunotechnology 1997; 3: 117-25.
    • (1997) Immunotechnology , vol.3 , pp. 117-125
    • Lafaye, P.1    Chournet, V.2    Demangel, C.3    Bon, C.4    Mazie, J.C.5
  • 85
    • 9344223986 scopus 로고    scopus 로고
    • Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library
    • Vaughan TJ, Williams AJ, Pritchard K, Osbourn JK, Pope AR, Earnshaw JC, et al. Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library. Nat Biothechnol 1996; 14: 309-14.
    • (1996) Nat Biothechnol , vol.14 , pp. 309-314
    • Vaughan, T.J.1    Williams, A.J.2    Pritchard, K.3    Osbourn, J.K.4    Pope, A.R.5    Earnshaw, J.C.6
  • 88
    • 0042430527 scopus 로고    scopus 로고
    • Antibody engineering for therapeutics
    • Presta L. Antibody engineering for therapeutics. Curr Opin Struct Biol 2003; 13: 519-25.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 519-525
    • Presta, L.1
  • 89
    • 0030890761 scopus 로고    scopus 로고
    • First clinical experiences with a new ovine Fab Echis ocellatus snake bite antivenom in Nigeria: Randomized comparative trial with Institute Pasteur Serum (Ipser) Africa antivenom
    • Meyer WP, Habib AG, Onayade AA, Yakubu A, Smith DC, Nasidi A, et al. First clinical experiences with a new ovine Fab Echis ocellatus snake bite antivenom in Nigeria: randomized comparative trial with Institute Pasteur Serum (Ipser) Africa antivenom. Am J Trop Med Hyg 1997; 56: 291-300.
    • (1997) Am J Trop Med Hyg , vol.56 , pp. 291-300
    • Meyer, W.P.1    Habib, A.G.2    Onayade, A.A.3    Yakubu, A.4    Smith, D.C.5    Nasidi, A.6
  • 90
    • 0035955926 scopus 로고    scopus 로고
    • A randomized multicenter trial of crotalinae polyvalent immune Fab (ovine) antivenom for the treatment for crotaline snakebite in the United States
    • Dart RC, Seifert SA, Boyer LV, Clark RF, Hall E, McKinney P, et al. A randomized multicenter trial of crotalinae polyvalent immune Fab (ovine) antivenom for the treatment for crotaline snakebite in the United States. Arch Intern Med 2001; 161: 2030-6.
    • (2001) Arch Intern Med , vol.161 , pp. 2030-2036
    • Dart, R.C.1    Seifert, S.A.2    Boyer, L.V.3    Clark, R.F.4    Hall, E.5    McKinney, P.6
  • 91
    • 0021061641 scopus 로고
    • Development of simple standard assay procedures for the characterization of snake venoms
    • Theakston RDG, Reid HA. Development of simple standard assay procedures for the characterization of snake venoms. Bull WHO 1983; 61: 949-56.
    • (1983) Bull WHO , vol.61 , pp. 949-956
    • Theakston, R.D.G.1    Reid, H.A.2
  • 92
  • 93
    • 0035814646 scopus 로고    scopus 로고
    • Defining and refining international donor support for combating the AIDS pandemic
    • Attaran A, Sachs J. Defining and refining international donor support for combating the AIDS pandemic. Lancet 2001; 357: 57-61.
    • (2001) Lancet , vol.357 , pp. 57-61
    • Attaran, A.1    Sachs, J.2
  • 94
    • 0035038385 scopus 로고    scopus 로고
    • A new global commitment to disease control in Africa
    • Sachs J. A new global commitment to disease control in Africa. Nat Med 2001; 7: 521-3.
    • (2001) Nat Med , vol.7 , pp. 521-523
    • Sachs, J.1
  • 95
    • 42249093296 scopus 로고    scopus 로고
    • Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil
    • Sao Paulo, Sarvier
    • Gutiérrez JM, Lomonte B. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clínica e Terapeutica. Sao Paulo, Sarvier 2003; 310-23.
    • (2003) Biologia, Clínica e Terapeutica , pp. 310-323
    • Gutiérrez, J.M.1    Lomonte, B.2
  • 96
    • 0033731921 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Their role in the pathogenesis of local tissue damage
    • Gutiérrez J, Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 2000; 82: 841-59.
    • (2000) Biochimie , vol.82 , pp. 841-859
    • Gutiérrez, J.1    Rucavado, A.2
  • 97
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH land Met-turn) and topologies an should be grouped into a common family, the 'metzincins'
    • Bode W, Gomis-Ruth FX, Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH land Met-turn) and topologies an should be grouped into a common family, the 'metzincins'. FEBS Lett 1993; 331: 134-40.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 98
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox JW, Serrano SMT. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005; 45: 969-85.
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.T.2
  • 99
    • 0028176523 scopus 로고
    • Refined 2 Å X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin
    • Gomis-Ruth FX, Kress LF, Kellerman J, Mayr I, Lee X, Huber R, et al. Refined 2 Å X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin. J Mol Biol 1994; 239: 513-44.
    • (1994) J Mol Biol , vol.239 , pp. 513-544
    • Gomis-Ruth, F.X.1    Kress, L.F.2    Kellerman, J.3    Mayr, I.4    Lee, X.5    Huber, R.6
  • 100
    • 10744232219 scopus 로고    scopus 로고
    • Amino acid sequence and crystal structure of BaPI, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities
    • Watanabe L, Shannon JD, Valente RH, Rucavado A, Alape-Girón A, Kamiguti AS, et al. Amino acid sequence and crystal structure of BaPI, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities. Protein Sci 2003; 12: 2273-81.
    • (2003) Protein Sci , vol.12 , pp. 2273-2281
    • Watanabe, L.1    Shannon, J.D.2    Valente, R.H.3    Rucavado, A.4    Alape-Girón, A.5    Kamiguti, A.S.6
  • 101
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason JB, Fox JW. Hemorrhagic metalloproteinases from snake venoms. Pharmacol Ther 1994; 62: 325-72.
    • (1994) Pharmacol Ther , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 102
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: Structure, assembly and role in tumor angiogenesis
    • Kallury R. Basement membranes: structure, assembly and role in tumor angiogenesis. Nat Rev Cancer 2003; 3: 422-33.
    • (2003) Nat Rev Cancer , vol.3 , pp. 422-433
    • Kallury, R.1
  • 103
    • 0027494603 scopus 로고
    • Type IV collagen: Structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis
    • Hudson BG, Reeders ST, Tryggvason K. Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis. J Biol Chem 1993; 268: 26033-6.
    • (1993) J Biol Chem , vol.268 , pp. 26033-26036
    • Hudson, B.G.1    Reeders, S.T.2    Tryggvason, K.3
  • 104
    • 0018088785 scopus 로고
    • Hemorrhagic toxins from rattle-snake ( Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins
    • Ownby CL, Bjarnason JB, Tu AT. Hemorrhagic toxins from rattle-snake ( Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins. Am J Pathol 1978; 93: 201-18.
    • (1978) Am J Pathol , vol.93 , pp. 201-218
    • Ownby, C.L.1    Bjarnason, J.B.2    Tu, A.T.3
  • 105
    • 0027933353 scopus 로고
    • Pathological changes induced by BaH1, a hemorrhagic proteinase isolated from Bothrops asper (terciopelo) snake venom, on mouse capillary blood vessels
    • Moreira L, Borkow G, Ovadia M, Gutiérrez JM. Pathological changes induced by BaH1, a hemorrhagic proteinase isolated from Bothrops asper (terciopelo) snake venom, on mouse capillary blood vessels. Toxicon 1994; 32: 977-87.
    • (1994) Toxicon , vol.32 , pp. 977-987
    • Moreira, L.1    Borkow, G.2    Ovadia, M.3    Gutiérrez, J.M.4
  • 106
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • Gutiérrez JM, Rucavado A, Escalante T, Díaz C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005; 45: 997-1011.
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutiérrez, J.M.1    Rucavado, A.2    Escalante, T.3    Díaz, C.4
  • 107
    • 31744450623 scopus 로고    scopus 로고
    • Blood flow is required for rapid endothelial cell damage induced by a snake venom hemorrhagic metalloproteinase
    • Gutiérrez JM, Núñez J, Escalante T, Rucavado A. Blood flow is required for rapid endothelial cell damage induced by a snake venom hemorrhagic metalloproteinase. Microvasc Res 2006; 71: 55-63.
    • (2006) Microvasc Res , vol.71 , pp. 55-63
    • Gutiérrez, J.M.1    Núñez, J.2    Escalante, T.3    Rucavado, A.4
  • 108
    • 0028270563 scopus 로고
    • Activity of hemorrhagic metalloproteinase BaH-1 and myotoxin II from Bothrops asper snake venom on capillary endothelial cells in vitro
    • Lomonte B, Gutiérrez JM, Borkow G, Ovadia M, Tarkowski A, Hanson LÅ. Activity of hemorrhagic metalloproteinase BaH-1 and myotoxin II from Bothrops asper snake venom on capillary endothelial cells in vitro. Toxicon 1994; 32: 505-10.
    • (1994) Toxicon , vol.32 , pp. 505-510
    • Lomonte, B.1    Gutiérrez, J.M.2    Borkow, G.3    Ovadia, M.4    Tarkowski, A.5    Hanson, L.Å.6
  • 109
    • 19544391618 scopus 로고    scopus 로고
    • Characterization of events associated with apoptosis/anoikis induced by snake venom metalloproteinase BaP1 on human endothelial cells
    • Díaz C, Valverde L, Brenes O, Rucavado A, Gutiérrez JM. Characterization of events associated with apoptosis/anoikis induced by snake venom metalloproteinase BaP1 on human endothelial cells. J Cell Biochem 2005; 94: 520-8.
    • (2005) J Cell Biochem , vol.94 , pp. 520-528
    • Díaz, C.1    Valverde, L.2    Brenes, O.3    Rucavado, A.4    Gutiérrez, J.M.5
  • 110
    • 23944464005 scopus 로고    scopus 로고
    • Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells
    • Tanjoni I, Weinlich R, Della-Casa MS, Clissa PB, Saldanha-Gama RF, de Freitas MS, et al. Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells. Apoptosis 2005; 10: 851-61.
    • (2005) Apoptosis , vol.10 , pp. 851-861
    • Tanjoni, I.1    Weinlich, R.2    Della-Casa, M.S.3    Clissa, P.B.4    Saldanha-Gama, R.F.5    de Freitas, M.S.6
  • 112
    • 0029949611 scopus 로고    scopus 로고
    • 1-integrin by the snake venom metalloproteinase jararhagin
    • 1-integrin by the snake venom metalloproteinase jararhagin. Biochem J 1996; 320: 635-41.
    • (1996) Biochem J , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.M.2    Zuzel, M.3
  • 113
    • 0025583295 scopus 로고
    • Muscle necrosis caused by snake venoms and toxins
    • Harris JB, Cullen MJ. Muscle necrosis caused by snake venoms and toxins. Electron Microsc Rev 1990; 3: 183-211.
    • (1990) Electron Microsc Rev , vol.3 , pp. 183-211
    • Harris, J.B.1    Cullen, M.J.2
  • 114
    • 1042287114 scopus 로고    scopus 로고
    • 2: Insights into the mechanisms of local and systemic myotoxicity
    • 2: insights into the mechanisms of local and systemic myotoxicity. Toxicon 2003; 42: 915-31.
    • (2003) Toxicon , vol.42 , pp. 915-931
    • Gutiérrez, J.M.1    Ownby, C.L.2
  • 115
    • 0029905805 scopus 로고    scopus 로고
    • Myotoxic activity of the toxic phospholipase, notexin, from the venom of the Australian tiger snake
    • Dixon RW, Harris JB. Myotoxic activity of the toxic phospholipase, notexin, from the venom of the Australian tiger snake. J Neuropathol Exp Neurol 1996; 55: 1230-7.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1230-1237
    • Dixon, R.W.1    Harris, J.B.2
  • 116
    • 1442359944 scopus 로고    scopus 로고
    • Membrane depolarization is the initial action of crotoxin on isolated murine skeletal muscle
    • Melo PA, Burns CF, Blankemeyer JT, Ownby CL. Membrane depolarization is the initial action of crotoxin on isolated murine skeletal muscle. Toxicon 2004; 43: 111-9.
    • (2004) Toxicon , vol.43 , pp. 111-119
    • Melo, P.A.1    Burns, C.F.2    Blankemeyer, J.T.3    Ownby, C.L.4
  • 121
    • 1042264060 scopus 로고    scopus 로고
    • 2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action
    • 2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action. Toxicon 2003; 42: 885-901.
    • (2003) Toxicon , vol.42 , pp. 885-901
    • Lomonte, B.1    Angulo, Y.2    Calderón, L.3
  • 122
    • 1042287120 scopus 로고    scopus 로고
    • 2 by sequence analysis and site directed mutagenesis
    • 2 by sequence analysis and site directed mutagenesis. Toxicon 2003; 42: 869-83.
    • (2003) Toxicon , vol.42 , pp. 869-883
    • Chioato, L.1    Ward, R.J.2
  • 123
    • 0028848625 scopus 로고
    • Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (terciopelo)
    • Gutiérrez JM, Romero M, Núñez J, Chaves F, Borkow G, Ovadia M. Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (terciopelo). Exp Mol Pathol 1995; 62: 28-41.
    • (1995) Exp Mol Pathol , vol.62 , pp. 28-41
    • Gutiérrez, J.M.1    Romero, M.2    Núñez, J.3    Chaves, F.4    Borkow, G.5    Ovadia, M.6
  • 124
    • 4344696667 scopus 로고    scopus 로고
    • Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil
    • Sao Paulo, Sarvier
    • Franca FOS, Málaque CMS. In: Cardoso JLC, Franca FOS, Fan HW, Málaque CMS, Haddad V. Animais Peconhentos no Brasil. Biologia, Clínica e Terapeutica. Sao Paulo, Sarvier 2003; 72-86.
    • (2003) Biologia, Clínica e Terapeutica , pp. 72-86
    • Franca, F.O.S.1    Málaque, C.M.S.2
  • 125
    • 0031661318 scopus 로고    scopus 로고
    • Blister formation and skin damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Rucavado A, Núñez J, Gutiérrez JM. Blister formation and skin damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Int J Exp Pathol 1998; 79: 245-54.
    • (1998) Int J Exp Pathol , vol.79 , pp. 245-254
    • Rucavado, A.1    Núñez, J.2    Gutiérrez, J.M.3
  • 126
    • 0029432140 scopus 로고
    • Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (terciopelo) snake venom
    • Rucavado A, Lomonte B, Ovadia M, Gutiérrez JM. Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (terciopelo) snake venom. Exp Mol Pathol 1995; 63: 186-99.
    • (1995) Exp Mol Pathol , vol.63 , pp. 186-199
    • Rucavado, A.1    Lomonte, B.2    Ovadia, M.3    Gutiérrez, J.M.4
  • 127
    • 0036027944 scopus 로고    scopus 로고
    • Neutralization of a snake venom hemorrhagic metalloproteinase prevents coagulopathy after subcutaneous injection of Bothrops jararaca venom in rats
    • Anai K, Sugiki M, Yoshida E, Maruyama M. Neutralization of a snake venom hemorrhagic metalloproteinase prevents coagulopathy after subcutaneous injection of Bothrops jararaca venom in rats. Toxicon 2002; 40: 63-8.
    • (2002) Toxicon , vol.40 , pp. 63-68
    • Anai, K.1    Sugiki, M.2    Yoshida, E.3    Maruyama, M.4
  • 128
    • 0021001085 scopus 로고
    • Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor
    • Tu AT, Hendon RR. Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor. Comp Biochem Physiol B 1983; 76: 377-83.
    • (1983) Comp Biochem Physiol B , vol.76 , pp. 377-383
    • Tu, A.T.1    Hendon, R.R.2
  • 129
    • 2342462926 scopus 로고    scopus 로고
    • Isolation and characterization of hyaluronidase, a "spreading factor" from Indian cobra (Naja naja) venom
    • Giris KS, Shashidharamurthy R, Nagaraju S, Gowda TV, Kemparaju K. Isolation and characterization of hyaluronidase, a "spreading factor" from Indian cobra (Naja naja) venom. Biochimie 2004; 86: 193-202.
    • (2004) Biochimie , vol.86 , pp. 193-202
    • Giris, K.S.1    Shashidharamurthy, R.2    Nagaraju, S.3    Gowda, T.V.4    Kemparaju, K.5
  • 130
    • 6944227500 scopus 로고    scopus 로고
    • Membrane independent activation of fibroblast proMMP-2 by snake venom: Novel roles for venom proteinases
    • Saravia-Otten P, Frisan T, Thelestam M, Gutiérrez JM. Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases. Toxicon 2004; 44: 749-64.
    • (2004) Toxicon , vol.44 , pp. 749-764
    • Saravia-Otten, P.1    Frisan, T.2    Thelestam, M.3    Gutiérrez, J.M.4
  • 132
    • 0027534529 scopus 로고
    • Host response to Bothrops asper snake venom: Analysis of edema formation, inflammatory cells, and cytokine release in a mouse model
    • Lomonte B, Tarkowski A, Hanson LÅ. Host response to Bothrops asper snake venom: analysis of edema formation, inflammatory cells, and cytokine release in a mouse model. Inflammation 1993; 17: 93-105.
    • (1993) Inflammation , vol.17 , pp. 93-105
    • Lomonte, B.1    Tarkowski, A.2    Hanson, L.Å.3
  • 133
    • 0036096413 scopus 로고    scopus 로고
    • Increments in cytokines and matrix metalloproteinases in skeletal muscle after injection of tissue-damaging toxins from the venom of the snake Bothrops asper
    • Rucavado A, Escalante T, Teixeira CFP, Fernandes CM, Díaz C, Gutiérrez JM. Increments in cytokines and matrix metalloproteinases in skeletal muscle after injection of tissue-damaging toxins from the venom of the snake Bothrops asper. Mediat Inflamm 2002; 11: 121-8.
    • (2002) Mediat Inflamm , vol.11 , pp. 121-128
    • Rucavado, A.1    Escalante, T.2    Teixeira, C.F.P.3    Fernandes, C.M.4    Díaz, C.5    Gutiérrez, J.M.6
  • 135
    • 0034894386 scopus 로고    scopus 로고
    • Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo
    • Zamunér SR, Gutiérrez JM, Muscará MN, Teixeira SA, Teixeira CFP. Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo. Toxicon 2001; 39: 1505-13.
    • (2001) Toxicon , vol.39 , pp. 1505-1513
    • Zamunér, S.R.1    Gutiérrez, J.M.2    Muscará, M.N.3    Teixeira, S.A.4    Teixeira, C.F.P.5
  • 136
    • 27444434730 scopus 로고    scopus 로고
    • Inflammation induced by Bothrops asper venom: Release of proinflammatory cytokines and eicosanoids, and role of adhesion molecules in leukocyte infiltration
    • Zamunér SR, Zuliani JP, Fernandes CM, Gutiérrez JM, Teixeira CFP. Inflammation induced by Bothrops asper venom: release of proinflammatory cytokines and eicosanoids, and role of adhesion molecules in leukocyte infiltration. Toxicon 2005; 46: 806-13.
    • (2005) Toxicon , vol.46 , pp. 806-813
    • Zamunér, S.R.1    Zuliani, J.P.2    Fernandes, C.M.3    Gutiérrez, J.M.4    Teixeira, C.F.P.5
  • 138
    • 33748492712 scopus 로고    scopus 로고
    • Role of nitric oxide in the local and systemic pathophysiological effects induced by Bothrops asper snake venom in mice
    • Chaves F, Teixeira CFP, Gutiérrez JM. Role of nitric oxide in the local and systemic pathophysiological effects induced by Bothrops asper snake venom in mice. Inflanim Res 2006; 55: 245-53.
    • (2006) Inflanim Res , vol.55 , pp. 245-253
    • Chaves, F.1    Teixeira, C.F.P.2    Gutiérrez, J.M.3
  • 139
    • 0035072511 scopus 로고    scopus 로고
    • Pharmacological modulation of hyperalgesia induced by Bothrops asper (terciopelo) snake venom
    • Chacur M, Picolo G, Gutiérrez JM, Teixeira CFP, Cury Y. Pharmacological modulation of hyperalgesia induced by Bothrops asper (terciopelo) snake venom. Toxicon 2001; 39: 1173-81.
    • (2001) Toxicon , vol.39 , pp. 1173-1181
    • Chacur, M.1    Picolo, G.2    Gutiérrez, J.M.3    Teixeira, C.F.P.4    Cury, Y.5
  • 141
    • 0031081512 scopus 로고    scopus 로고
    • Leukocyte response induced by Bothrops jararaca crude venom: In vivo and in vitro studies
    • Farsky SHP, Walber J, Costa-Cruz M, Cury Y, Teixeira CFP. Leukocyte response induced by Bothrops jararaca crude venom: in vivo and in vitro studies. Toxicon 1997; 35: 185-93.
    • (1997) Toxicon , vol.35 , pp. 185-193
    • Farsky, S.H.P.1    Walber, J.2    Costa-Cruz, M.3    Cury, Y.4    Teixeira, C.F.P.5
  • 142
    • 23944488766 scopus 로고    scopus 로고
    • Role of the snake venom toxin jararhagin in proinflammatory pathogenesis: In vitro and in vivo gene expression analysis of the effects of the toxin
    • Gallagher P, Bao Y, Serrano SMT, Laing GD, Theakston RDG, Gutiérrez JM, et al. Role of the snake venom toxin jararhagin in proinflammatory pathogenesis: in vitro and in vivo gene expression analysis of the effects of the toxin. Arch Biochem Biophys 2005; 441: 1-15.
    • (2005) Arch Biochem Biophys , vol.441 , pp. 1-15
    • Gallagher, P.1    Bao, Y.2    Serrano, S.M.T.3    Laing, G.D.4    Theakston, R.D.G.5    Gutiérrez, J.M.6
  • 143
    • 0034898736 scopus 로고    scopus 로고
    • The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on proinflammatory cytokines released by murine peritoneal adherent cells
    • Clissa PB, Laing GD, Theakston RDG, Mota I, Taylor MJ, Mourada-Silva AM. The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on proinflammatory cytokines released by murine peritoneal adherent cells. Toxicon 2001; 39: 1567-73.
    • (2001) Toxicon , vol.39 , pp. 1567-1573
    • Clissa, P.B.1    Laing, G.D.2    Theakston, R.D.G.3    Mota, I.4    Taylor, M.J.5    Mourada-Silva, A.M.6
  • 144
    • 24344440254 scopus 로고    scopus 로고
    • 2. Toxicon 2005; 46: 523-32.
    • 2. Toxicon 2005; 46: 523-32.
  • 145
    • 30944463623 scopus 로고    scopus 로고
    • Wei JF, Mo Y2, Quiao LY, Wei XL, Chen HQ, Xie H, et al. Potent histamine-releasing activity of atrahagin, a novel snake venom metalloproteinase. Int J Biochem Cell Biol 2006; 38: 510-20.
    • Wei JF, Mo Y2, Quiao LY, Wei XL, Chen HQ, Xie H, et al. Potent histamine-releasing activity of atrahagin, a novel snake venom metalloproteinase. Int J Biochem Cell Biol 2006; 38: 510-20.
  • 146
    • 15044346270 scopus 로고    scopus 로고
    • 2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line
    • 2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line. Toxicon 2005; 45: 651-60.
    • (2005) Toxicon , vol.45 , pp. 651-660
    • Mora, R.1    Valverde, B.2    Díaz, C.3    Lomonte, B.4    Gutiérrez, J.M.5
  • 148
    • 0023915259 scopus 로고
    • Leukocyte depletion attenuates vascular injury in postischemic skeletal muscle
    • Korthuis RJ, Grisham MB, Granger DN. Leukocyte depletion attenuates vascular injury in postischemic skeletal muscle. Am J Physiol 1988; 254: H823-7.
    • (1988) Am J Physiol , vol.254
    • Korthuis, R.J.1    Grisham, M.B.2    Granger, D.N.3
  • 150
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong VW, Power C, Edwards DR. Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci 2001; 2: 502-11.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Edwards, D.R.3
  • 151
    • 0141592399 scopus 로고    scopus 로고
    • Neutrophils do not contribute to local tissue damage, but play a key role in skeletal muscle regenerarion, in mice injected with Bothrops asper snake venom
    • Teixeira CFP, Zamuner SR, Zuliani JP, Fernandes CM, Cruz-Hofling MA, Fernandes I, et al. Neutrophils do not contribute to local tissue damage, but play a key role in skeletal muscle regenerarion, in mice injected with Bothrops asper snake venom. Muscle Nerve 2003; 28: 449-59.
    • (2003) Muscle Nerve , vol.28 , pp. 449-459
    • Teixeira, C.F.P.1    Zamuner, S.R.2    Zuliani, J.P.3    Fernandes, C.M.4    Cruz-Hofling, M.A.5    Fernandes, I.6
  • 152
    • 11144234882 scopus 로고    scopus 로고
    • Role of TNF-α, IL-1β and IL-6 in the local tissue damage induced by Bothrops asper snake venom: An experimental assessment in mice
    • Chaves F, Teixeira CFP, Gutiérrez JM. Role of TNF-α, IL-1β and IL-6 in the local tissue damage induced by Bothrops asper snake venom: an experimental assessment in mice. Toxicon 2005; 45: 171-8.
    • (2005) Toxicon , vol.45 , pp. 171-178
    • Chaves, F.1    Teixeira, C.F.P.2    Gutiérrez, J.M.3
  • 153
    • 17144388980 scopus 로고    scopus 로고
    • Effects of neutrophil depletion in the local pathological alterations and muscle regeneration in mice injected with Bothrops jararaca snake venom
    • Teixeira CFP, Chaves F, Zamunér SR, Fernandes CM, Zuliani JP, Cruz-Hofling MA, et al. Effects of neutrophil depletion in the local pathological alterations and muscle regeneration in mice injected with Bothrops jararaca snake venom. Int J Exp Pathol 2005; 86: 107-15.
    • (2005) Int J Exp Pathol , vol.86 , pp. 107-115
    • Teixeira, C.F.P.1    Chaves, F.2    Zamunér, S.R.3    Fernandes, C.M.4    Zuliani, J.P.5    Cruz-Hofling, M.A.6
  • 154
    • 1142309648 scopus 로고    scopus 로고
    • The complement system is involved in acute inflammation but not in the hemorrhage produced by a Bothrops atrox snake venom low molecular mass proteinase
    • Rodrigues FG, Petretski JH, Kanashiro MM, Lemos L, Dias da Silva W, Kipnis TL. The complement system is involved in acute inflammation but not in the hemorrhage produced by a Bothrops atrox snake venom low molecular mass proteinase. Mol Immunol 2004; 40: 1149-56.
    • (2004) Mol Immunol , vol.40 , pp. 1149-1156
    • Rodrigues, F.G.1    Petretski, J.H.2    Kanashiro, M.M.3    Lemos, L.4    Dias da Silva, W.5    Kipnis, T.L.6
  • 155
    • 0029840014 scopus 로고    scopus 로고
    • Processing of pro-tumor necrosis factor-α by venom metalloproteinases: A hypothesis explaining local tissue damage following snake bite
    • Moura-da-Silva AM, Laing GD, Paine MJI, Dennison JMTJ, Politi V, Crampton JM, et al. Processing of pro-tumor necrosis factor-α by venom metalloproteinases: a hypothesis explaining local tissue damage following snake bite. Eur J Immunol 1996; 26: 2000-5.
    • (1996) Eur J Immunol , vol.26 , pp. 2000-2005
    • Moura-da-Silva, A.M.1    Laing, G.D.2    Paine, M.J.I.3    Dennison, J.M.T.J.4    Politi, V.5    Crampton, J.M.6
  • 158
    • 0026016355 scopus 로고
    • Towards understanding skeletal muscle regeneration
    • Grounds M. Towards understanding skeletal muscle regeneration. Path Res Pract 1991; 187: 1-22.
    • (1991) Path Res Pract , vol.187 , pp. 1-22
    • Grounds, M.1
  • 159
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke J, Garry DJ. Myogenic satellite cells: physiology to molecular biology. J Appl Physiol 2001; 91: 534-51.
    • (2001) J Appl Physiol , vol.91 , pp. 534-551
    • Hawke, J.1    Garry, D.J.2
  • 160
    • 19244367926 scopus 로고    scopus 로고
    • Comparative study on the ability of IgG and Fab sheep antivenoms to neutralize local hemorrhage, edema and myonecrosis induced by Bothrops asper (terciopelo) snake venom
    • León G, Valverde JM, Rojas G, Lomonte B, Gutiérrez JM.
    • (2000) Toxicon , vol.38 , pp. 233-244
    • León, G.1    Valverde, J.M.2    Rojas, G.3    Lomonte, B.4    Gutiérrez, J.M.5
  • 161
    • 0030273220 scopus 로고    scopus 로고
    • 2 antivenoms in the neutralization of hemorrhagic activity of Vipera berus snake venom in mice
    • 2 antivenoms in the neutralization of hemorrhagic activity of Vipera berus snake venom in mice. Toxicon 1996; 34: 1197-202.
    • (1996) Toxicon , vol.34 , pp. 1197-1202
    • Lomonte, B.1    León, G.2    Hanson, L.Å.3
  • 162
    • 0037304467 scopus 로고    scopus 로고
    • Intramuscular administration of antivenoms in- experimental envenomation by Bothrops asper: Comparison between Fab and IgG
    • Chaves F, Loría GD, Salazar A, Gutiérrez JM. Intramuscular administration of antivenoms in- experimental envenomation by Bothrops asper: comparison between Fab and IgG. Toxicon 2003; 41: 237-44.
    • (2003) Toxicon , vol.41 , pp. 237-244
    • Chaves, F.1    Loría, G.D.2    Salazar, A.3    Gutiérrez, J.M.4
  • 163
    • 0242352551 scopus 로고    scopus 로고
    • Hyaluronidase inhibitors (sodium chromoglycate and sodium aurothiomalate) reduce the local tissue damage and prolong the survival time of mice injected with Naja kaouthia and Calloselasma rhodostoma venoms
    • Yingprasertchai S, Bunyasrisawat S, Ratanabanangkoon K. Hyaluronidase inhibitors (sodium chromoglycate and sodium aurothiomalate) reduce the local tissue damage and prolong the survival time of mice injected with Naja kaouthia and Calloselasma rhodostoma venoms. Toxicon 2003; 42: 635-46.
    • (2003) Toxicon , vol.42 , pp. 635-646
    • Yingprasertchai, S.1    Bunyasrisawat, S.2    Ratanabanangkoon, K.3
  • 164
    • 0034662380 scopus 로고    scopus 로고
    • Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Escalante T, Franceschi A, Rucavado A, Gutiérrez JM. Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Biochem Pharmacol 2000; 60: 269-74.
    • (2000) Biochem Pharmacol , vol.60 , pp. 269-274
    • Escalante, T.1    Franceschi, A.2    Rucavado, A.3    Gutiérrez, J.M.4
  • 166
    • 20444450643 scopus 로고    scopus 로고
    • Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin
    • Murakami MT, Arruda EZ, Melo PA, Martinez AB, Calil-Eliás S, Tomaz MA, et al. Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin. J Mol Biol 2005; 350: 416-26.
    • (2005) J Mol Biol , vol.350 , pp. 416-426
    • Murakami, M.T.1    Arruda, E.Z.2    Melo, P.A.3    Martinez, A.B.4    Calil-Eliás, S.5    Tomaz, M.A.6
  • 167
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF. Matrix metalloproteinases. J Biol Chem 1999; 274: 21451-4.
    • (1999) J Biol Chem , vol.274 , pp. 21451-21454
    • Nagase, H.1    Woessner, J.F.2
  • 168
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 169
    • 14044274265 scopus 로고    scopus 로고
    • Recent developments in the design of specific matrix metalloproteinase inhibitors aided by structural and computational studies
    • Rao BG. Recent developments in the design of specific matrix metalloproteinase inhibitors aided by structural and computational studies. Curr Pharm Des 2005; 11: 295-322.
    • (2005) Curr Pharm Des , vol.11 , pp. 295-322
    • Rao, B.G.1
  • 170
    • 3543090958 scopus 로고    scopus 로고
    • Chemically modified tetracyclines as inhibitors of matrix metalloproteinases
    • Acharya MR, Venitz J, Figg WD, Sparreboom A. Chemically modified tetracyclines as inhibitors of matrix metalloproteinases. Drug Resist Updat 2004; 7: 195-208.
    • (2004) Drug Resist Updat , vol.7 , pp. 195-208
    • Acharya, M.R.1    Venitz, J.2    Figg, W.D.3    Sparreboom, A.4
  • 171
    • 0035571790 scopus 로고    scopus 로고
    • A comparative docking study and the design of potentially selective MMP inhibitors
    • Hanessian S, Moitessier N, Therrien E. A comparative docking study and the design of potentially selective MMP inhibitors. J Comput Aided Mol Des 2001; 15: 873-81.
    • (2001) J Comput Aided Mol Des , vol.15 , pp. 873-881
    • Hanessian, S.1    Moitessier, N.2    Therrien, E.3
  • 172
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002; 295: 2387-92.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 173
    • 0032980326 scopus 로고    scopus 로고
    • Inhibition of adamalysin II and MMPs by phosphonate analogues of snake venom peptides
    • D'Alessio S, Gallina C, Gavuzzo E, Giordano C, Gorini B, Mazza F, et al. Inhibition of adamalysin II and MMPs by phosphonate analogues of snake venom peptides. Bioorg Med Chem 1999; 7: 389-94.
    • (1999) Bioorg Med Chem , vol.7 , pp. 389-394
    • D'Alessio, S.1    Gallina, C.2    Gavuzzo, E.3    Giordano, C.4    Gorini, B.5    Mazza, F.6
  • 174
    • 0033863530 scopus 로고    scopus 로고
    • Ongoing trials with matrix metalloproteinase inhibitors
    • Brown PD. Ongoing trials with matrix metalloproteinase inhibitors. Exp Opin Invest Drugs 2000; 9: 2167-77.
    • (2000) Exp Opin Invest Drugs , vol.9 , pp. 2167-2177
    • Brown, P.D.1
  • 175
    • 0027964860 scopus 로고
    • Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form D)
    • Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, et al. Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form D). Proc Natl Acad Sci USA 1994; 91: 8447-51.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8447-8451
    • Zhang, D.1    Botos, I.2    Gomis-Ruth, F.X.3    Doll, R.4    Blood, C.5    Njoroge, F.G.6
  • 176
    • 0029866390 scopus 로고    scopus 로고
    • Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF. Batimastat, a potent matrix metalloproteinase inhibitor, exhibits an unexpected mode of binding. Proc Natl Acad Sci USA 1996; 93: 2749-54.
    • Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF. Batimastat, a potent matrix metalloproteinase inhibitor, exhibits an unexpected mode of binding. Proc Natl Acad Sci USA 1996; 93: 2749-54.
  • 177
    • 0027171764 scopus 로고
    • Inhibition of metalloproteinases in Bothrops asper venom by endogenous peptides
    • Francis B, Kaiser II. Inhibition of metalloproteinases in Bothrops asper venom by endogenous peptides. Toxicon 1993; 31: 889-99.
    • (1993) Toxicon , vol.31 , pp. 889-899
    • Francis, B.1    Kaiser II2
  • 178
    • 0036310675 scopus 로고    scopus 로고
    • Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues
    • Huang KF, Chiou SH, Ko TP, Wang AHJ. 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 2002; 269: 3047-56.
    • (2002) Eur J Biochem , vol.269 , pp. 3047-3056
    • Huang, K.F.1    Chiou, S.H.2    Ko, T.P.3    Wang, A.H.J.4
  • 179
    • 15944366565 scopus 로고    scopus 로고
    • Presence of peptide inhibitors in rattlesnake venoms and their effects on endogenous metalloproteases
    • Munekiyo SM, Mackessy SP. Presence of peptide inhibitors in rattlesnake venoms and their effects on endogenous metalloproteases. Toxicon 2005; 45: 255-63.
    • (2005) Toxicon , vol.45 , pp. 255-263
    • Munekiyo, S.M.1    Mackessy, S.P.2
  • 181
  • 182
    • 0034830642 scopus 로고    scopus 로고
    • Cloning and characterization of BJ46a, a snake venom metalloproteinase inhibitor from Bothrops jararaca serum
    • Valente RH, Dragulev B, Perales J, Fox JW, Domont GB. Cloning and characterization of BJ46a, a snake venom metalloproteinase inhibitor from Bothrops jararaca serum. Eur J Biochem 2001; 268: 3042-52.
    • (2001) Eur J Biochem , vol.268 , pp. 3042-3052
    • Valente, R.H.1    Dragulev, B.2    Perales, J.3    Fox, J.W.4    Domont, G.B.5
  • 183
    • 1642462834 scopus 로고    scopus 로고
    • Effect of the metalloproteinase inhibitor batimastat in the systemic toxicity induced by Bothrops asper snake venom: Understanding the role of metalloproteinases in envenomation
    • Rucavado A, Escalante T, Gutiérrez JM. Effect of the metalloproteinase inhibitor batimastat in the systemic toxicity induced by Bothrops asper snake venom: understanding the role of metalloproteinases in envenomation. Toxicon 2004; 43: 417-24.
    • (2004) Toxicon , vol.43 , pp. 417-424
    • Rucavado, A.1    Escalante, T.2    Gutiérrez, J.M.3
  • 184
    • 0030175550 scopus 로고    scopus 로고
    • Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases
    • Kamiguti AS, Hay CRM, Theakston RDG, Zuzel M. Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases. Toxicon 1996; 34: 627-42.
    • (1996) Toxicon , vol.34 , pp. 627-642
    • Kamiguti, A.S.1    Hay, C.R.M.2    Theakston, R.D.G.3    Zuzel, M.4
  • 185
    • 19544369492 scopus 로고    scopus 로고
    • Platelets as targets of snake venom metalloproteinases
    • Kamiguti AS. Platelets as targets of snake venom metalloproteinases. Toxicon 2005; 45: 1041-9.
    • (2005) Toxicon , vol.45 , pp. 1041-1049
    • Kamiguti, A.S.1
  • 189
    • 0030201175 scopus 로고    scopus 로고
    • 2 -a structural review
    • 2 -a structural review. Toxicon 1996; 34: 827-41.
    • (1996) Toxicon , vol.34 , pp. 827-841
    • Arni, R.K.1    Ward, R.J.2
  • 195
    • 1042275605 scopus 로고    scopus 로고
    • 2 enzymes
    • 2 enzymes. Toxicon 2003; 42: 827-40.
    • (2003) Toxicon , vol.42 , pp. 827-840
    • Kini, R.M.1
  • 197
    • 0036943741 scopus 로고    scopus 로고
    • Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera
    • Deepa M, Gowda TV. Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera. Arch Biochem Biophys 2002; 408: 42-50.
    • (2002) Arch Biochem Biophys , vol.408 , pp. 42-50
    • Deepa, M.1    Gowda, T.V.2
  • 201
    • 0023186213 scopus 로고
    • 2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid
    • 2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid. Toxicon 1987; 25: 501-15.
    • (1987) Toxicon , vol.25 , pp. 501-515
    • Vishwanath, B.S.1    Kini, R.M.2    Gowda, T.V.3
  • 203
    • 1142309590 scopus 로고    scopus 로고
    • 2 and antivenin activity of melanin extracted from Thea sinensis Linn
    • 2 and antivenin activity of melanin extracted from Thea sinensis Linn. Life Sci 2004; 74: 2037-47.
    • (2004) Life Sci , vol.74 , pp. 2037-2047
    • Hung, Y.C.1    Sava, V.2    Hong, M.Y.3    Huang, G.S.4
  • 205
  • 207
    • 0028034445 scopus 로고
    • 2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling
    • 2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling. J Biol Chem 1994; 269: 29867-73.
    • (1994) J Biol Chem , vol.269 , pp. 29867-29873
    • Lomonte, B.1    Moreno, E.2    Tarkowski, A.3    Hanson, L.Å.4    Maccarana, M.5
  • 208
    • 0027409655 scopus 로고
    • Antagonism of the myotoxic effects of Bothrops jararacussu venom and bothropstoxin by polyanions
    • Melo PA, Homsi-Brandeburgo MI, Giglio JR, Suárez-Kurtz G. Antagonism of the myotoxic effects of Bothrops jararacussu venom and bothropstoxin by polyanions. Toxicon 1993; 31: 285-91.
    • (1993) Toxicon , vol.31 , pp. 285-291
    • Melo, P.A.1    Homsi-Brandeburgo, M.I.2    Giglio, J.R.3    Suárez-Kurtz, G.4
  • 209
  • 210
    • 1042287027 scopus 로고    scopus 로고
    • 2 myotoxin inhibitor proteins from snakes, mammals and plants
    • 2 myotoxin inhibitor proteins from snakes, mammals and plants. Toxicon 2003; 42: 963-77.
    • (2003) Toxicon , vol.42 , pp. 963-977
    • Lizano, S.1    Domont, G.2    Perales, J.3
  • 211
    • 0030757947 scopus 로고    scopus 로고
    • 2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon blomhoffi siniticus
    • 2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon blomhoffi siniticus. Biochem J 1997; 325: 527-31.
    • (1997) Biochem J , vol.325 , pp. 527-531
    • Ohkura, N.1    Ohkuhara, H.2    Inoue, S.3    Ikeda, K.4    Hayashi, K.5
  • 215
    • 0027298410 scopus 로고
    • Suramin: A novel antineoplastic agent with multiple potential mechanisms of action
    • Stein CA. Suramin: a novel antineoplastic agent with multiple potential mechanisms of action. Cancer Res 1993; 53: 2239-48.
    • (1993) Cancer Res , vol.53 , pp. 2239-2248
    • Stein, C.A.1
  • 216
    • 11144293690 scopus 로고    scopus 로고
    • The use of suramin, an antifibrotic agent, to improve muscle recovery after strain injury
    • Chan YS, Li Y, Foster W, Fu FH, Huard J. The use of suramin, an antifibrotic agent, to improve muscle recovery after strain injury. Am J Sports Med 2005; 33: 43-51.
    • (2005) Am J Sports Med , vol.33 , pp. 43-51
    • Chan, Y.S.1    Li, Y.2    Foster, W.3    Fu, F.H.4    Huard, J.5
  • 217
    • 0036714237 scopus 로고    scopus 로고
    • 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure
    • 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure. Biochemistry 2002; 41: 10914-9.
    • (2002) Biochemistry , vol.41 , pp. 10914-10919
    • Chandra, V.1    Jasti, J.2    Kaur, P.3    Srinivasan, A.4    Betzel, C.5    Singh, T.P.6
  • 218
    • 0141954191 scopus 로고    scopus 로고
    • 2 from Naja naja sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-Arg-Ser (VAFRS) at 1.9 Å resolution reveals unique features
    • 2 from Naja naja sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-Arg-Ser (VAFRS) at 1.9 Å resolution reveals unique features. Biochemistry 2003; 42: 11701-6.
    • (2003) Biochemistry , vol.42 , pp. 11701-11706
    • Singh, R.K.1    Vikram, P.2    Makker, J.3    Jabeen, T.4    Sharma, S.5    Dey, S.6
  • 220
    • 32544431758 scopus 로고    scopus 로고
    • Inhibition of Naja naja venom hyaluronidase: Role in the management of poisonous bite
    • Girish KS, Kemparaju K. Inhibition of Naja naja venom hyaluronidase: role in the management of poisonous bite. Life Sci 2006; 78: 1433-40.
    • (2006) Life Sci , vol.78 , pp. 1433-1440
    • Girish, K.S.1    Kemparaju, K.2
  • 222
    • 0023332595 scopus 로고
    • Coral snake venoms: Mode of action and pathophysiology of experimental envenomation
    • Vital Brazil O. Coral snake venoms: mode of action and pathophysiology of experimental envenomation. Rev Inst Med Trop Sao Paulo 1987; 29: 119-26.
    • (1987) Rev Inst Med Trop Sao Paulo , vol.29 , pp. 119-126
    • Vital Brazil, O.1
  • 223
    • 0031797435 scopus 로고    scopus 로고
    • Local inflammation, lethality and cytokine release in mice injected with Bothrops atrox venom
    • Barros SF, Friedlanskaia I, Petricevich VL, Kipnis TL. Local inflammation, lethality and cytokine release in mice injected with Bothrops atrox venom. Mediat Inflamm 1998; 7: 339-46.
    • (1998) Mediat Inflamm , vol.7 , pp. 339-346
    • Barros, S.F.1    Friedlanskaia, I.2    Petricevich, V.L.3    Kipnis, T.L.4
  • 225
    • 0034113347 scopus 로고    scopus 로고
    • Increments in serum cytokine and nitric oxide levels in mice injected with Bothrops asper and Bothrops jararaca snake venoms
    • Petricevich VL, Teixeira CFP, Tambourgi DV, Gutiérrez JM. Increments in serum cytokine and nitric oxide levels in mice injected with Bothrops asper and Bothrops jararaca snake venoms. Toxicon 2000; 38: 1253-66.
    • (2000) Toxicon , vol.38 , pp. 1253-1266
    • Petricevich, V.L.1    Teixeira, C.F.P.2    Tambourgi, D.V.3    Gutiérrez, J.M.4
  • 226
    • 0035001310 scopus 로고    scopus 로고
    • Antagonization of TNF attenuates systemic hemodynamic manifestations of envenomation in a rat model of Vipera aspis snakebite
    • Szold O, Ben-Abraham R, Weinbroum AA, Englender TE, Ovadia D, Sorkine M, et al. Antagonization of TNF attenuates systemic hemodynamic manifestations of envenomation in a rat model of Vipera aspis snakebite. Intensive Care Med 2001; 27: 884-8.
    • (2001) Intensive Care Med , vol.27 , pp. 884-888
    • Szold, O.1    Ben-Abraham, R.2    Weinbroum, A.A.3    Englender, T.E.4    Ovadia, D.5    Sorkine, M.6
  • 227
    • 0038581262 scopus 로고    scopus 로고
    • Tumor necrosis factor as a mediator of cardiac toxicity following snake envenomation
    • Szold O, Ben-Abraham R, Frolkis I, Sorkine M, Sorkine P. Tumor necrosis factor as a mediator of cardiac toxicity following snake envenomation. Crit Care Med 2003; 31: 1449-53.
    • (2003) Crit Care Med , vol.31 , pp. 1449-1453
    • Szold, O.1    Ben-Abraham, R.2    Frolkis, I.3    Sorkine, M.4    Sorkine, P.5
  • 230
    • 0034899916 scopus 로고    scopus 로고
    • 2 from Agkistrodon piscivorus piscivorus snake venom: Synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
    • 2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities. Toxicon 2001; 39: 1587-94.
    • (2001) Toxicon , vol.39 , pp. 1587-1594
    • Núñez, C.E.1    Angulo, Y.2    Lomonte, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.