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Volumn , Issue , 2009, Pages 789-812

P-III Metalloproteinase (Leucurolysin-B) from Bothrops leucurus Venom: Isolation and Possible Inhibition

Author keywords

Inhibition of proteolytic activity of leuc B by Brazilian commercial antivenoms; P III metalloproteinase (Leucurolysin B) from Bothrops leucurus venom; Proteolytic specificity of SVMPs on oxidized insulin B chain

Indexed keywords


EID: 79957667633     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470508169.ch33     Document Type: Chapter
Times cited : (4)

References (67)
  • 1
    • 0023125054 scopus 로고
    • The origin of snakes and evolution of the venom apparatus
    • Kochva, E. The origin of snakes and evolution of the venom apparatus. Toxicon 1987, 25, 65-106.
    • (1987) Toxicon , vol.25 , pp. 65-106
    • Kochva, E.1
  • 2
    • 3042614116 scopus 로고    scopus 로고
    • Snakebites in Central and South America: epidemiology, clinical features, and clinical management
    • In The Venomous Reptiles of the Western Hemisphere; Campbell, J. A.; Lamar, W. W., Cornell University Press: Ithaca, NY
    • Warrell, D. A. Snakebites in Central and South America: epidemiology, clinical features, and clinical management. In The Venomous Reptiles of the Western Hemisphere; Campbell, J. A.; Lamar, W. W., Cornell University Press: Ithaca, NY, 2004; pp 709-761.
    • (2004) , pp. 709-761
    • Warrell, D.A.1
  • 3
    • 0002645946 scopus 로고
    • Locally acting agents: myotoxins, hemorrhagic toxins and dermonecrotic factors
    • In Handbook of Toxinology; Shier, W. T.; Mebs, D., Eds.; Marcel Dekker: New York
    • Ownby, C. L. Locally acting agents: myotoxins, hemorrhagic toxins and dermonecrotic factors. In Handbook of Toxinology; Shier, W. T.; Mebs, D., Eds.; Marcel Dekker: New York, 1990; pp 602-654.
    • (1990) , pp. 602-654
    • Ownby, C.L.1
  • 4
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason, J. B.; Fox, J. W. Hemorrhagic metalloproteinases from snake venoms. Pharmacol. Ther. 1994, 62, 325-372.
    • (1994) Pharmacol. Ther. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 5
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
    • Gutierrez, J. M.; Rucavado, A.; Escalante, T.; Diaz, 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
    • Gutierrez, J.M.1    Rucavado, A.2    Escalante, T.3    Diaz, C.4
  • 6
    • 33750605786 scopus 로고    scopus 로고
    • Mutalysins. In Handbook of Proteolytic Enzymes
    • 2nd ed.; Barrett, A. J.; Rawlings, N.; Woessner, F. J., Eds.; Elsevier Academic Press
    • Sanchez, E. F. Mutalysins. In Handbook of Proteolytic Enzymes, 2nd ed.; Barrett, A. J.; Rawlings, N.; Woessner, F. J., Eds.; Elsevier Academic Press, 2004; pp 692-694.
    • (2004) , pp. 692-694
    • Sanchez, E.F.1
  • 7
    • 0002720322 scopus 로고    scopus 로고
    • Phospholipase A2 myotoxins from Bothrops snake venoms
    • In Venom Phospholipase A2 Enzymes. Structure, Function and Mechanism; Kini, R. M., Ed.; John Wiley & Sons, Ltd
    • Gutierrez, J. M.; Lamonte, B. Phospholipase A2 myotoxins from Bothrops snake venoms. In Venom Phospholipase A2 Enzymes. Structure, Function and Mechanism; Kini, R. M., Ed.; John Wiley & Sons, Ltd., 1997; pp 321-352.
    • (1997) , pp. 321-352
    • Gutierrez, J.M.1    Lamonte, B.2
  • 8
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland, F. S. Snake venoms and the hemostatic system. Toxicon 1998, 36, 1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 9
    • 0342359205 scopus 로고    scopus 로고
    • Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems
    • Estevao-Costa, M. I.; Diniz, C. R.; Magalhaes, A.; Markland, F. S.; Sanchez, E. F. Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems. Thromb. Res. 2000, 99, 363-376.
    • (2000) Thromb. Res. , vol.99 , pp. 363-376
    • Estevao-Costa, M.I.1    Diniz, C.R.2    Magalhaes, A.3    Markland, F.S.4    Sanchez, E.F.5
  • 10
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zincpeptidases
    • Stöcker,W.; Grams, F.; Baumann, U.; Reinemer, P.; Gomis-Rüth, F. X.; McKay, D. B.; Bode, W. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zincpeptidases. Protein Sci. 1995, 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.X.5    McKay, D.B.6    Bode, W.7
  • 11
    • 0039122255 scopus 로고    scopus 로고
    • Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor a convertase inhibitor
    • Gomis-Rüth, F. X.; Meyer, E. F.; Kress, L. F.; Politi, V. Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor a convertase inhibitor. Protein Sci. 1998, 7, 283-292.
    • (1998) Protein Sci. , vol.7 , pp. 283-292
    • Gomis-Rüth, F.X.1    Meyer, E.F.2    Kress, L.F.3    Politi, V.4
  • 12
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metaloprotease domain-multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg, T. G.; Primakoff, P.; Myles, D. G.; White, J. M. ADAM, a novel family of membrane proteins containing a disintegrin and metaloprotease domain-multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 1995, 131, 275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 13
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox, J. W.; Serrano, S. M. T. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45, 969-985.
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.T.2
  • 14
    • 33644843824 scopus 로고    scopus 로고
    • A snake venom metalloproteinase that inhibited cell proliferation and induced morphological changes of ECV304 cells
    • Wan, S. G.; Jin, Y.; Lee, W. H.; Zhang, Y. A snake venom metalloproteinase that inhibited cell proliferation and induced morphological changes of ECV304 cells. Toxicon 2006, 47, 480-489.
    • (2006) Toxicon , vol.47 , pp. 480-489
    • Wan, S.G.1    Jin, Y.2    Lee, W.H.3    Zhang, Y.4
  • 15
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atroxlysin A
    • Jia, L. G.; Wang, X. M.; Shannon, G. D.; Bjarnason, J. B.; Fox, J. W. Function of disintegrin-like/cysteine-rich domains of atroxlysin A. J. Biol. Chem. 1997, 272, 13094-13102.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13094-13102
    • Jia, L.G.1    Wang, X.M.2    Shannon, G.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 18
    • 27944497471 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed-jararaca) snake venom
    • Bello, C.A.; Hermogenes, A. L.; Magalhaes, A.;Veiga, S. S.; Gremski, L. H.; Richardson, M.; Sanchez, E. F. Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed-jararaca) snake venom. Biochimie 2006, 88, 189-200.
    • (2006) Biochimie , vol.88 , pp. 189-200
    • Bello, C.A.1    Hermogenes, A.L.2    Magalhaes, A.3    Veiga, S.S.4    Gremski, L.H.5    Richardson, M.6    Sanchez, E.F.7
  • 20
    • 34249733674 scopus 로고    scopus 로고
    • Cytotoxic, thrombolytic, and edematogenic activities of leucurolysin-a, a metalloproteinase from Bothrops leucurus snake venom
    • Gremski, L. H.; Chaim, O. M.; Paludo, K. S.; Sade, Y. B.; Otuki, M. F.; Richardson, M.; Gremski, W.; Sanchez, E. F.; Veiga, S. S. Cytotoxic, thrombolytic, and edematogenic activities of leucurolysin-a, a metalloproteinase from Bothrops leucurus snake venom. Toxicon 2007, 50, 120-134.
    • (2007) Toxicon , vol.50 , pp. 120-134
    • Gremski, L.H.1    Chaim, O.M.2    Paludo, K.S.3    Sade, Y.B.4    Otuki, M.F.5    Richardson, M.6    Gremski, W.7    Sanchez, E.F.8    Veiga, S.S.9
  • 21
    • 27644597567 scopus 로고    scopus 로고
    • Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom
    • Wang, W. J.; Shih, Ch.; Huang, T. F. Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom. Biochimie 2005, 87, 1065-1077.
    • (2005) Biochimie , vol.87 , pp. 1065-1077
    • Wang, W.J.1    Shih, C.H.2    Huang, T.F.3
  • 23
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: evidences that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from common precursor
    • Kini, R. M.; Evans, H. J. Structural domains in venom proteins: evidences that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from common precursor. Toxicon 1992, 30, 265-293.
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 24
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zincdependent metalloproteinases
    • Jongeneel, C. V.; Bouvier, J.; Bairoch, A. A unique signature identifies a family of zincdependent metalloproteinases. FEBS Lett. 1989, 242, 211-214.
    • (1989) FEBS Lett. , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 25
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of of zincpeptidases
    • Stöcker,W.; Grams, F.; Baumann, U.; Reinemer, P.; Gomis-Rüth, F. -X.; McKey, D. B.; Bode, W. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of of zincpeptidases. Protein Sci. 1995, 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.-X.5    McKey, D.B.6    Bode, W.7
  • 26
    • 0032847562 scopus 로고    scopus 로고
    • MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes
    • Roberts, C. M.; Tani, P. H.; Bridges, L. C.; Laszik, Z. MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. J. Biol. Chem. 1999, 274, 29251-29259.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29251-29259
    • Roberts, C.M.1    Tani, P.H.2    Bridges, L.C.3    Laszik, Z.4
  • 27
    • 22144440164 scopus 로고    scopus 로고
    • Snake venom metalloproteinase containing a disintegrinlike domain, its structure-activity relationships at interacting with integrins
    • Lu, X.; Lu, M. F.; Kakkar, V. V. Snake venom metalloproteinase containing a disintegrinlike domain, its structure-activity relationships at interacting with integrins. Curr. Med. Chem.-Cardiovasc. Hematol. Agents 2005, 3, 249-260.
    • (2005) Curr. Med. Chem.-Cardiovasc. Hematol. Agents , vol.3 , pp. 249-260
    • Lu, X.1    Lu, M.F.2    Kakkar, V.V.3
  • 28
    • 0031195282 scopus 로고    scopus 로고
    • Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom
    • Shimokawa, K.; Shannon, J. D.; Jia, L. -G.; Fox, J.W. Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom. Arch. Biochem. Biophys. 1997, 343, 35-43.
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 35-43
    • Shimokawa, K.1    Shannon, J.D.2    Jia, L.-G.3    Fox, J.W.4
  • 29
    • 0034213348 scopus 로고    scopus 로고
    • Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
    • Nikai, T.; Taniguchi, K.; Komori, Y.; Masuda, K.; Fox, J. W.; Sugihara, H. Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch. Biochem. Biophys. 2000, 378, 6-15.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 6-15
    • Nikai, T.1    Taniguchi, K.2    Komori, Y.3    Masuda, K.4    Fox, J.W.5    Sugihara, H.6
  • 30
    • 34247572893 scopus 로고    scopus 로고
    • Isolation and cloning of a metalloproteinase from king cobra snake venom
    • Guo, X. -X.; Zeng, L.; Lee, W. H.; Zhang, Y.; Jin, Y. Isolation and cloning of a metalloproteinase from king cobra snake venom. Toxicon 2007, 48, 954-965.
    • (2007) Toxicon , vol.48 , pp. 954-965
    • Guo, X.-X.1    Zeng, L.2    Lee, W.H.3    Zhang, Y.4    Jin, Y.5
  • 31
    • 0035836453 scopus 로고    scopus 로고
    • Complete amino acid sequence of kaouthiagin, a novel cobra venom metalloproteinase with two disintegrin-like sequences
    • Ito, M.; Hamako, J.; Sakurai, Y.; Matsumoto, M.; Fujimura, Y.; Suzuki, M.; Hashimoto, K.; Titani, K.; Matsui, T. Complete amino acid sequence of kaouthiagin, a novel cobra venom metalloproteinase with two disintegrin-like sequences. Biochemistry 2001, 40, 4503-4511.
    • (2001) Biochemistry , vol.40 , pp. 4503-4511
    • Ito, M.1    Hamako, J.2    Sakurai, Y.3    Matsumoto, M.4    Fujimura, Y.5    Suzuki, M.6    Hashimoto, K.7    Titani, K.8    Matsui, T.9
  • 32
    • 0033958729 scopus 로고    scopus 로고
    • Function of the cysteine-rich domain of the hemorrhagic metalloproteinase atrolysin A: collagen targeting and inhibition of platelet aggregation
    • Jia, L. G.; Bjarnason, J. B.; Fox, J. W. Function of the cysteine-rich domain of the hemorrhagic metalloproteinase atrolysin A: collagen targeting and inhibition of platelet aggregation. Arch. Biochem. Biophys. 2000, 373, 281-286.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 281-286
    • Jia, L.G.1    Bjarnason, J.B.2    Fox, J.W.3
  • 33
    • 0042564783 scopus 로고    scopus 로고
    • Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function
    • Kamiguti, A. S.; Gallagher, P.; Marcinkiewicz, C.; Theakston, R. D. G.; Zuzel, M.; Fox, J. W. Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function. FEBS Lett. 2003, 549, 129-134.
    • (2003) FEBS Lett. , vol.549 , pp. 129-134
    • Kamiguti, A.S.1    Gallagher, P.2    Marcinkiewicz, C.3    Theakston, R.D.G.4    Zuzel, M.5    Fox, J.W.6
  • 35
    • 0029095156 scopus 로고
    • Proteolytic specificity of two hemorrhagic factors, LHF-I and LHF-II, isolated from the venom of the bushmaster snake (Lachesis muta muta)
    • Sanchez, E. F.; Cordeiro, M. N.; Oliveira, E. B.; Juliano, L.; Prado, E. S.; Diniz, C. R. Proteolytic specificity of two hemorrhagic factors, LHF-I and LHF-II, isolated from the venom of the bushmaster snake (Lachesis muta muta). Toxicon 1995, 33, 1061-1069.
    • (1995) Toxicon , vol.33 , pp. 1061-1069
    • Sanchez, E.F.1    Cordeiro, M.N.2    Oliveira, E.B.3    Juliano, L.4    Prado, E.S.5    Diniz, C.R.6
  • 37
    • 0020575296 scopus 로고
    • Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom
    • Civello, D. J.; Duong, H. L.; Geren, C. R. Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom. Biochemistry 1983, 22, 749-755.
    • (1983) Biochemistry , vol.22 , pp. 749-755
    • Civello, D.J.1    Duong, H.L.2    Geren, C.R.3
  • 38
    • 0021986185 scopus 로고
    • Isolation and characterization of hemorrhagic factors a and b from the venom of the Chinese habu snake (Trimeresurus mucrosquamatus)
    • Nikai, T.; Mori, N.; Kishida, Y.; Kato, Ch.; Takenata, T.; Murakami, S.; Shigezane, H.; Sugihara, H. Isolation and characterization of hemorrhagic factors a and b from the venom of the Chinese habu snake (Trimeresurus mucrosquamatus). Biochim. Biophys. Acta. 1985, 838, 122-131.
    • (1985) Biochim. Biophys. Acta. , vol.838 , pp. 122-131
    • Nikai, T.1    Mori, N.2    Kishida, Y.3    Kato, C.H.4    Takenata, T.5    Murakami, S.6    Shigezane, H.7    Sugihara, H.8
  • 39
    • 0024010806 scopus 로고
    • Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom
    • Bjarnason, J. B.; Hamilton, D.; Fox, J. W. Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom. Biol. Chem. Hoppe-Seyler 1988, 369, 121-129.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 121-129
    • Bjarnason, J.B.1    Hamilton, D.2    Fox, J.W.3
  • 40
    • 0024452930 scopus 로고
    • Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases
    • Baramova, E. N.; Shannon, J. D.; Bjarnason, J. B.; Fox, J.W. Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch. Biochem. Biophys. 1989, 275, 63-71.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 63-71
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 41
    • 0032412785 scopus 로고    scopus 로고
    • Hemorrhagic factors from snake venoms. II, structures of hemorrhagic factors and types and mechanisms of hemorrhage
    • Mashiko, H.; Takahashi, H. Hemorrhagic factors from snake venoms. II, structures of hemorrhagic factors and types and mechanisms of hemorrhage. J. Toxicol. Toxin Rev. 1998, 17, 493-512.
    • (1998) J. Toxicol. Toxin Rev. , vol.17 , pp. 493-512
    • Mashiko, H.1    Takahashi, H.2
  • 42
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: structure, assembly and role in tumor angiogenesis
    • Kalluri, R. Basement membranes: structure, assembly and role in tumor angiogenesis. Nat. Rev. Cancer 2003, 3, 422-433.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 422-433
    • Kalluri, R.1
  • 43
    • 0031686026 scopus 로고    scopus 로고
    • Characterization of the hemorrhagic reaction caused by Vibrio vulnificus metalloproteinase, a member of the thermolysin family
    • Miyoshi, S. I.; Nakasawa, H.; Kawata, K.; Tomochika, K. I.; Tobe, K.; Shinoda, S. Characterization of the hemorrhagic reaction caused by Vibrio vulnificus metalloproteinase, a member of the thermolysin family. Infect. Immun. 1998, 66, 4851-4855.
    • (1998) Infect. Immun. , vol.66 , pp. 4851-4855
    • Miyoshi, S.I.1    Nakasawa, H.2    Kawata, K.3    Tomochika, K.I.4    Tobe, K.5    Shinoda, S.6
  • 45
    • 0023377705 scopus 로고
    • Laminin-nidogen complex: extraction with chelating agents and structural characterization
    • Paulsson, M.; Aumaillay, M.; Deutzmann, R.; Timpl, R.; Beck, K. Laminin-nidogen complex: extraction with chelating agents and structural characterization. Eur. J. Biochem. 1987, 166, 11-19.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumaillay, M.2    Deutzmann, R.3    Timpl, R.4    Beck, K.5
  • 46
    • 0026542959 scopus 로고
    • Basement membrane proteins: structure, assembly, and cellular interactions
    • Paulson, M. Basement membrane proteins: structure, assembly, and cellular interactions. Crit. Rev. Biochem. Mol. Biol. 1992, 27, 93-127.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 93-127
    • Paulson, M.1
  • 47
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin. Structure, assembly, and cardiovascular implications
    • Magnus, K.; Mosher, D. F. Fibronectin. Structure, assembly, and cardiovascular implications. Arterioscler. Thromb. Vasc. Biol. 1998, 18, 1363-1370.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 1363-1370
    • Magnus, K.1    Mosher, D.F.2
  • 48
    • 19544369492 scopus 로고    scopus 로고
    • Platelets as targets of snake venom metalloproteinases
    • Kamiguti, S. A. Platelets as targets of snake venom metalloproteinases. Toxicon 2005, 45, 1041-1049.
    • (2005) Toxicon , vol.45 , pp. 1041-1049
    • Kamiguti, S.A.1
  • 49
    • 19544386458 scopus 로고    scopus 로고
    • Snake venom probes of platelet adhesion receptors and their ligands
    • Wijeyewckrema, L. C.; Berndt, M. C.; Andrews, R. K. Snake venom probes of platelet adhesion receptors and their ligands. Toxicon 2005, 45, 1051-1061.
    • (2005) Toxicon , vol.45 , pp. 1051-1061
    • Wijeyewckrema, L.C.1    Berndt, M.C.2    Andrews, R.K.3
  • 50
    • 0029949611 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation as the result of cleavage of a2b1-integrin by the snake venom metalloproteinase jararhagin
    • Kamiguti, A. S.; Hay, C. M. H.; Zuzel, M. Inhibition of collagen-induced platelet aggregation as the result of cleavage of a2b1-integrin by the snake venom metalloproteinase jararhagin. Biochem. J. 1996, 320, 635-641.
    • (1996) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.M.H.2    Zuzel, M.3
  • 51
    • 0037174925 scopus 로고    scopus 로고
    • The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrilar collagen agonist involved in fibroblast cell adhesion and signaling
    • Zigrino, P.; Kamiguti, A. S.; Eble, J.; Drescher, C.; Nischt, R.; Fox, J.W.; Mauch, C. The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrilar collagen agonist involved in fibroblast cell adhesion and signaling. J. Biol. Chem. 2002, 277, 40528-40535.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40528-40535
    • Zigrino, P.1    Kamiguti, A.S.2    Eble, J.3    Drescher, C.4    Nischt, R.5    Fox, J.W.6    Mauch, C.7
  • 53
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. RGD and other recognition sequences for integrins. Annu. Rev. Cell. Biol. 1996, 12, 679-715.
    • (1996) Annu. Rev. Cell. Biol. , vol.12 , pp. 679-715
    • Ruoslahti, E.1
  • 54
    • 0034841747 scopus 로고    scopus 로고
    • The molecular basis of integrin-extracellular matrix interactions
    • Eble, J. A. The molecular basis of integrin-extracellular matrix interactions. Osteoar. Cartilage 2001, 9A, S131-S140.
    • (2001) Osteoar. Cartilage , vol.9 A
    • Eble, J.A.1
  • 55
    • 28844437147 scopus 로고    scopus 로고
    • Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation
    • You,W. -K.; Jang, Y. -J.; Chung, K. -H.; Kim, D. -S. Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation. Biochem. Biophys. Res. Commun. 2006, 339, 964-970.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 964-970
    • You, W.-K.1    Jang, Y.-J.2    Chung, K.-H.3    Kim, D.-S.4
  • 56
    • 33845648870 scopus 로고    scopus 로고
    • Purification and functional characterization of AAV1, a novel P-III metalloproteinase, from Formosan Agkistrodon acutus venom
    • Wang, W. -J. Purification and functional characterization of AAV1, a novel P-III metalloproteinase, from Formosan Agkistrodon acutus venom. Biochimie 2007, 89, 105-115.
    • (2007) Biochimie , vol.89 , pp. 105-115
    • Wang, W.-J.1
  • 57
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three disulfide hemorrhagic zinc metalloproteinase from Agkistrodon acutus
    • Gong,W.; Zhu, X.; Liu, S.; Teng, M.; Niu, L. Crystal structures of acutolysin A, a three disulfide hemorrhagic zinc metalloproteinase from Agkistrodon acutus. J. Mol. Biol. 1998, 283, 657-668.
    • (1998) J. Mol. Biol. , vol.283 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 58
    • 0028892387 scopus 로고
    • Structural analysis of zinc substitutions in the active site of thermolysin
    • Holland, D. R.; Hausrath, A. C.; Juers, D.; Matthews, B. W. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci. 1995, 4, 1955-1965.
    • (1995) Protein Sci. , vol.4 , pp. 1955-1965
    • Holland, D.R.1    Hausrath, A.C.2    Juers, D.3    Matthews, B.W.4
  • 59
    • 33947302585 scopus 로고    scopus 로고
    • Neutralization of the haemorrhagic activities of viperine snake venoms and venom metalloproteinases using synthetic peptide inhibitors and chelators
    • Howes, J. M.; Theakston, R. D. G.; Laing, G. D. Neutralization of the haemorrhagic activities of viperine snake venoms and venom metalloproteinases using synthetic peptide inhibitors and chelators. Toxicon 2007, 49, 734-739.
    • (2007) Toxicon , vol.49 , pp. 734-739
    • Howes, J.M.1    Theakston, R.D.G.2    Laing, G.D.3
  • 60
    • 0020164637 scopus 로고
    • Evolution of a2-macroglobulin
    • Starkey, P. M.; Barrett, A. J. Evolution of a2-macroglobulin. Biochem. J. 1982, 205, 91-95.
    • (1982) Biochem. J. , vol.205 , pp. 91-95
    • Starkey, P.M.1    Barrett, A.J.2
  • 61
    • 0025023540 scopus 로고
    • Interaction of hemorrhagic metalloproteinases with human a2-macroglobulin
    • Baramova, E. N.; Shannon, J. D.; Bjarnason, J. B.; Gonias, S. L.; Fox, J.W. Interaction of hemorrhagic metalloproteinases with human a2-macroglobulin. Biochemistry 1990, 29, 1069-1074.
    • (1990) Biochemistry , vol.29 , pp. 1069-1074
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Gonias, S.L.4    Fox, J.W.5
  • 62
    • 0028067253 scopus 로고
    • Ineffectiveness of the inhibition of the main hemorrhagic metalloproteinase from Bothrops jararaca venom by its only plasma inhibitor a2-macroglobulin
    • Kamiguti, A. S.; Desmond, H. P.; Theakston, R. D. G.; Hay, C. R. M.; Zuzel, M. Ineffectiveness of the inhibition of the main hemorrhagic metalloproteinase from Bothrops jararaca venom by its only plasma inhibitor a2-macroglobulin. Biochim. Biophys. Acta. 1994, 1200, 307-314.
    • (1994) Biochim. Biophys. Acta. , vol.1200 , pp. 307-314
    • Kamiguti, A.S.1    Desmond, H.P.2    Theakston, R.D.G.3    Hay, C.R.M.4    Zuzel, M.5
  • 63
    • 15044351795 scopus 로고    scopus 로고
    • Antigenic relationships and relative immunogenicities of isolated metalloproteinases from Echis ocellatus venom
    • Howes, J. M.; Theakston, R. D. G.; Laing, G. D. Antigenic relationships and relative immunogenicities of isolated metalloproteinases from Echis ocellatus venom. Toxicon 2005, 45, 677-680.
    • (2005) Toxicon , vol.45 , pp. 677-680
    • Howes, J.M.1    Theakston, R.D.G.2    Laing, G.D.3
  • 64
    • 0034664687 scopus 로고    scopus 로고
    • Structural and functional characterization of neuwiedase, a nonhemorrhagic fibrinogenolytic metaloprotease from Bothrops neuwiedi snake venom
    • Rodrigues, V. M.; Soares, A. M.; Guerra-Sá, R.; Rodrigues, V.; Fontes, M. R. M.; Giglio, J. R. Structural and functional characterization of neuwiedase, a nonhemorrhagic fibrinogenolytic metaloprotease from Bothrops neuwiedi snake venom. Arch. Biochem. Biophys. 2000, 381, 213-224.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 213-224
    • Rodrigues, V.M.1    Soares, A.M.2    Guerra-Sá, R.3    Rodrigues, V.4    Fontes, M.R.M.5    Giglio, J.R.6
  • 65
    • 0036162142 scopus 로고    scopus 로고
    • Pharmacological characterization and neutralization of the venoms used in the production of Bothropic antivenom in Brazil
    • Camey, K. U.; Velarde, D. T.; Sanchez, E. F. Pharmacological characterization and neutralization of the venoms used in the production of Bothropic antivenom in Brazil. Toxicon 2002, 40, 501-509.
    • (2002) Toxicon , vol.40 , pp. 501-509
    • Camey, K.U.1    Velarde, D.T.2    Sanchez, E.F.3
  • 66
    • 0037376318 scopus 로고    scopus 로고
    • The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody
    • Harrison, R. A.;Wüster, W.; Theakston, R. D. G. The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody. Toxicon 2003, 41, 441-449.
    • (2003) Toxicon , vol.41 , pp. 441-449
    • Harrison, R.A.1    Wüster, W.2    Theakston, R.D.G.3
  • 67
    • 0028316735 scopus 로고
    • Ineficácia do antiveneno botropico na neutralização da atividade coagulante do veneno de Lachesis muta muta. Relato de caso e comprovação experimental
    • Bard, R.; de Lima, J. C.; Sa Neto, R. P.; de Oliveira, S. G.; dos Santos, M. C. Ineficácia do antiveneno botropico na neutralização da atividade coagulante do veneno de Lachesis muta muta. Relato de caso e comprovação experimental. Rev. Inst.Méd. Trop. S. Paulo 1994, 36, 77-81.
    • (1994) Rev. Inst.Méd. Trop. S. Paulo , vol.36 , pp. 77-81
    • Bard, R.1    De Lima, J.C.2    Sa Neto, R.P.3    De Oliveira, S.G.4    Dos Santos, M.C.5


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