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Volumn 45, Issue 8, 2005, Pages 1115-1132

Snake venom serine proteinases: Sequence homology vs. substrate specificity, a paradox to be solved

Author keywords

3D structure activity relationships; Blood clotting; Factor V activation; Kinin release; Molecular modeling; Molecular recognition; Platelet aggregation; Protein C activation; Snake venom serine proteinases

Indexed keywords

SERINE PROTEINASE; SNAKE VENOM;

EID: 19544394247     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2005.02.020     Document Type: Article
Times cited : (267)

References (116)
  • 1
    • 0029945766 scopus 로고    scopus 로고
    • Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom
    • A.S. Aguiar, C.R. Alves, A. Melgarejo, and S. Giovanni-de-Simone Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom Toxicon 34 1996 555 565
    • (1996) Toxicon , vol.34 , pp. 555-565
    • Aguiar, A.S.1    Alves, C.R.2    Melgarejo, A.3    Giovanni-de-Simone, S.4
  • 2
    • 0023692248 scopus 로고
    • Gyroxin, a toxin from the venom of Crotalus durissus terrificus, is a thrombin-like enzyme
    • G. Alexander, J. Grothusen, H. Zepeda, and R.J. Schwartzman Gyroxin, a toxin from the venom of Crotalus durissus terrificus, is a thrombin-like enzyme Toxicon 26 1988 953 960
    • (1988) Toxicon , vol.26 , pp. 953-960
    • Alexander, G.1    Grothusen, J.2    Zepeda, H.3    Schwartzman, R.J.4
  • 3
    • 0034702767 scopus 로고    scopus 로고
    • A novel venombin B from Agkistrodon contortrix contortrix: Evidence for recognition properties in the surface around the primary specificity pocket different from thrombin
    • G. Amiconi, A. Amoresano, G. Boumis, A. Brancaccio, R. De Cristofaro, A. De Pascalis, S. Di Girolamo, B. Maras, and A. Scaloni A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin Biochemistry 39 2000 10294 10308
    • (2000) Biochemistry , vol.39 , pp. 10294-10308
    • Amiconi, G.1    Amoresano, A.2    Boumis, G.3    Brancaccio, A.4    De Cristofaro, R.5    De Pascalis, A.6    Di Girolamo, S.7    Maras, B.8    Scaloni, A.9
  • 4
    • 0033956272 scopus 로고    scopus 로고
    • Serine proteinase inhibition by the active site titrant N alpha-(N, N-dimethylcarbamoyl)-alpha-azaornithine p-nitrophenyl ester A comparative study
    • P. Ascenzi, G. Balliano, C. Gallina, F. Polticelli, and M. Bolognesi Serine proteinase inhibition by the active site titrant N alpha-(N, N-dimethylcarbamoyl)-alpha-azaornithine p-nitrophenyl ester A comparative study Eur. J. Biochem. 267 2000 1239 1246
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1239-1246
    • Ascenzi, P.1    Balliano, G.2    Gallina, C.3    Polticelli, F.4    Bolognesi, M.5
  • 5
    • 0027201808 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma
    • L.C. Au, S.B. Lin, J.S. Chou, G.W. Teh, K.J. Chang, and C.M. Shih Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma Biochem. J. 294 1993 387 390
    • (1993) Biochem. J. , vol.294 , pp. 387-390
    • Au, L.C.1    Lin, S.B.2    Chou, J.S.3    Teh, G.W.4    Chang, K.J.5    Shih, C.M.6
  • 8
    • 0030668908 scopus 로고    scopus 로고
    • Defibrinogenating enzymes
    • W.R. Bell Jr Defibrinogenating enzymes Drugs 54 1997 18 30
    • (1997) Drugs , vol.54 , pp. 18-30
    • Bell W.R. Jr1
  • 9
    • 0034695486 scopus 로고    scopus 로고
    • The contribution of residues 192 and 193 to the specificity of snake venom serine proteinases
    • S. Braud, M.A. Parry, R. Maroun, C. Bon, and A. Wisner The contribution of residues 192 and 193 to the specificity of snake venom serine proteinases J. Biol. Chem. 275 2000 1823 1828
    • (2000) J. Biol. Chem. , vol.275 , pp. 1823-1828
    • Braud, S.1    Parry, M.A.2    Maroun, R.3    Bon, C.4    Wisner, A.5
  • 10
    • 0037007972 scopus 로고    scopus 로고
    • The stratagem utilized by the plasminogen activator from the snake Trimeresurus stejnegeri to escape serpins
    • S. Braud, B.F. Le Bonniec, C. Bon, and A. Wisner The stratagem utilized by the plasminogen activator from the snake Trimeresurus stejnegeri to escape serpins Biochemistry 41 2002 8478 8484
    • (2002) Biochemistry , vol.41 , pp. 8478-8484
    • Braud, S.1    Le Bonniec, B.F.2    Bon, C.3    Wisner, A.4
  • 11
    • 0026503083 scopus 로고
    • 3rd. Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma
    • W. Burkhart, G.F. Smith, J.L. Su, I. Parikh, and H. LeVine 3rd. Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma FEBS Lett. 297 1992 297 301
    • (1992) FEBS Lett. , vol.297 , pp. 297-301
    • Burkhart, W.1    Smith, G.F.2    Su, J.L.3    Parikh, I.4    LeVine, H.5
  • 12
    • 0035844698 scopus 로고    scopus 로고
    • Structural features of a snake venom thrombin-like enzyme: Thrombin and trypsin on a single catalytic platform?
    • H.C. Castro, D.M. Silva, C. Craik, and R.B. Zingali Structural features of a snake venom thrombin-like enzyme: thrombin and trypsin on a single catalytic platform? Biochim. Biophys. Acta. 1547 2001 183 195
    • (2001) Biochim. Biophys. Acta. , vol.1547 , pp. 183-195
    • Castro, H.C.1    Silva, D.M.2    Craik, C.3    Zingali, R.B.4
  • 13
    • 0029096066 scopus 로고
    • Characterization of a thrombin-like enzyme, grambin, from the venom of Trimeresurus gramineus and its in vivo antithrombotic effect
    • M.C. Chang, and T.F. Huang Characterization of a thrombin-like enzyme, grambin, from the venom of Trimeresurus gramineus and its in vivo antithrombotic effect Toxicon 33 1995 1087 1098
    • (1995) Toxicon , vol.33 , pp. 1087-1098
    • Chang, M.C.1    Huang, T.F.2
  • 14
    • 0029785840 scopus 로고    scopus 로고
    • +-induced allosteric regulation of catalytic activity in serine proteases
    • +-induced allosteric regulation of catalytic activity in serine proteases Proc. Natl Acad. Sci. USA 93 1996 10653 10656
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10653-10656
    • Dang, O.D.1    Di Cera, E.2
  • 15
    • 0029014036 scopus 로고
    • An allosteric switch controls the procoagulant and anticoagulant activities of thrombin
    • O.D. Dang, A. Vindigni, and E. Di Cera An allosteric switch controls the procoagulant and anticoagulant activities of thrombin Proc. Natl Acad. Sci. USA 92 1995 5977 5981
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5977-5981
    • Dang, O.D.1    Vindigni, A.2    Di Cera, E.3
  • 16
    • 0024373445 scopus 로고
    • A gyroxin analog from the venom of the bushmaster (Lachesis muta muta)
    • N.J. da Silva, S.D. Aird, C. Seebart, and I.I. Kaiser A gyroxin analog from the venom of the bushmaster (Lachesis muta muta) Toxicon 27 1989 763 771
    • (1989) Toxicon , vol.27 , pp. 763-771
    • Da Silva, N.J.1    Aird, S.D.2    Seebart, C.3    Kaiser, I.I.4
  • 17
    • 0041317466 scopus 로고    scopus 로고
    • Molecular cloning and expression of a functional snake venom serine proteinase, with platelet aggregating activity, from the Cerastes cerastes viper
    • H. Dekhil, A. Wisner, N. Marrakchi, M. El Ayeb, C. Bon, and H. Karoui Molecular cloning and expression of a functional snake venom serine proteinase, with platelet aggregating activity, from the Cerastes cerastes viper Biochemistry 42 2003 10609 10618
    • (2003) Biochemistry , vol.42 , pp. 10609-10618
    • Dekhil, H.1    Wisner, A.2    Marrakchi, N.3    El Ayeb, M.4    Bon, C.5    Karoui, H.6
  • 19
    • 0343969324 scopus 로고
    • The coagulation of blood by snake venoms and its physiological significance
    • H. Eagle The coagulation of blood by snake venoms and its physiological significance J. Exp. Med. 65 1937 613 639
    • (1937) J. Exp. Med. , vol.65 , pp. 613-639
    • Eagle, H.1
  • 20
    • 0000650903 scopus 로고
    • Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • C.T. Esmon, and W.G. Owen Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C Proc. Natl Acad. Sci. USA 78 1981 2249 2252
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 2249-2252
    • Esmon, C.T.1    Owen, W.G.2
  • 21
    • 0024492650 scopus 로고
    • Characterization of cerastobin, a thrombin-like enzyme from the venom of Cerastes vipera (Sahara sand viper)
    • T.M. Farid, A.T. Tu, and M.F. el-Asmar Characterization of cerastobin, a thrombin-like enzyme from the venom of Cerastes vipera (Sahara sand viper) Biochemistry 28 1989 371 377
    • (1989) Biochemistry , vol.28 , pp. 371-377
    • Farid, T.M.1    Tu, A.T.2    El-Asmar, M.F.3
  • 22
    • 0025093043 scopus 로고
    • Effect of cerastobin, a thrombinlike enzyme from Cerastes vipera (Egyptian sand snake) venom, on human platelets
    • T.M. Farid, A.T. Tu, and M.F. el-Asmar Effect of cerastobin, a thrombinlike enzyme from Cerastes vipera (Egyptian sand snake) venom, on human platelets Haemostasis 20 1990 296 304
    • (1990) Haemostasis , vol.20 , pp. 296-304
    • Farid, T.M.1    Tu, A.T.2    El-Asmar, M.F.3
  • 24
    • 0030727073 scopus 로고    scopus 로고
    • Purification, properties, and N-terminal amino acid sequence of a kallikrein-like enzyme from the venom of Lachesis muta rhombeata (Bushmaster)
    • S. Giovanni-De-Simone, A.S. Aguiar, A.R. Gimenez, K. Novellino, and R.S. de Moura Purification, properties, and N-terminal amino acid sequence of a kallikrein-like enzyme from the venom of Lachesis muta rhombeata (Bushmaster) J. Protein Chem. 16 1997 809 818
    • (1997) J. Protein Chem. , vol.16 , pp. 809-818
    • Giovanni-De-Simone, S.1    Aguiar, A.S.2    Gimenez, A.R.3    Novellino, K.4    De Moura, R.S.5
  • 26
    • 0035543209 scopus 로고    scopus 로고
    • Cloning and functional expression of the mucrosobin protein, a beta-fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu)
    • Y.W. Guo, T.Y. Chang, K.T. Lin, H.W. Liu, K.C. Shih, and S.H. Cheng Cloning and functional expression of the mucrosobin protein, a beta-fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu) Protein Exp. Purif. 23 2001 483 490
    • (2001) Protein Exp. Purif. , vol.23 , pp. 483-490
    • Guo, Y.W.1    Chang, T.Y.2    Lin, K.T.3    Liu, H.W.4    Shih, K.C.5    Cheng, S.H.6
  • 27
    • 0030015031 scopus 로고    scopus 로고
    • Purification and molecular cloning of calobin, a thrombin-like enzyme from Agkistrodon caliginosus (Korean viper)
    • B.S. Hahn, K.Y. Yang, E.M. Park, I.M. Chang, and Y.S. Kim Purification and molecular cloning of calobin, a thrombin-like enzyme from Agkistrodon caliginosus (Korean viper) J. Biochem. (Tokyo) 119 1996 835 843
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 835-843
    • Hahn, B.S.1    Yang, K.Y.2    Park, E.M.3    Chang, I.M.4    Kim, Y.S.5
  • 28
    • 0032400779 scopus 로고    scopus 로고
    • Molecular cloning of capillary permeability-increasing enzyme-2 from Agkistrodon caliginosus (Korean viper)
    • B.S. Hahn, K. Baek, W.S. Kim, C.S. Lee, I.L. Chang, and Y.S. Kim Molecular cloning of capillary permeability-increasing enzyme-2 from Agkistrodon caliginosus (Korean viper) Toxicon 36 1998 1887 1893
    • (1998) Toxicon , vol.36 , pp. 1887-1893
    • Hahn, B.S.1    Baek, K.2    Kim, W.S.3    Lee, C.S.4    Chang, I.L.5    Kim, Y.S.6
  • 29
    • 0004582738 scopus 로고    scopus 로고
    • Introduction: Serine peptidases and their clans
    • A.J. Barrett N.D. Rawlings J.F. Woessner Academic Press London
    • S. Halfon, and C.S. Craik A.J. Barrett N.D. Rawlings J.F. Woessner Introduction: serine peptidases and their clans Handbook of Proteolytic Enzymes 1998 Academic Press London 3 4
    • (1998) Handbook of Proteolytic Enzymes , pp. 3-4
    • Halfon, S.1    Craik, C.S.2
  • 30
    • 0013688696 scopus 로고
    • Partial purification of the blood-clotting factor from the venom of Bothrops jararaca
    • O.B. Henriques, M. Fichman, and S.B. Henriques Partial purification of the blood-clotting factor from the venom of Bothrops jararaca Biochem. J. 75 1960 551 556
    • (1960) Biochem. J. , vol.75 , pp. 551-556
    • Henriques, O.B.1    Fichman, M.2    Henriques, S.B.3
  • 31
    • 0032918274 scopus 로고    scopus 로고
    • Crotalase, a fibrinogen-clotting snake venom enzyme: Primary structure and evidence for a fibrinogen recognition exosite different from thrombin
    • A.H. Henschen-Edman, I. Theodor, B.F. Edwards, and H. Pirkle Crotalase, a fibrinogen-clotting snake venom enzyme: primary structure and evidence for a fibrinogen recognition exosite different from thrombin Thromb. Haemost. 81 1999 81 86
    • (1999) Thromb. Haemost. , vol.81 , pp. 81-86
    • Henschen-Edman, A.H.1    Theodor, I.2    Edwards, B.F.3    Pirkle, H.4
  • 32
    • 0014854261 scopus 로고
    • Studies on a procoagulant fraction of southern copperhead snake venom: The preferential release of fibrinopeptide B
    • R.H. Herzig, O.D. Ratnoff, and J.R. Shainoff Studies on a procoagulant fraction of southern copperhead snake venom: the preferential release of fibrinopeptide B J. Lab. Clin. Med. 76 1970 451 465
    • (1970) J. Lab. Clin. Med. , vol.76 , pp. 451-465
    • Herzig, R.H.1    Ratnoff, O.D.2    Shainoff, J.R.3
  • 33
    • 0028030369 scopus 로고
    • Isolation of multiple isoforms of alpha-fibrinogenase from the Western diamondback rattlesnake Crotalus atrox: N-terminal sequence homology with ancrod, an antithrombotic agent from Malayan viper
    • C.C. Hung, and S.H. Chiou Isolation of multiple isoforms of alpha-fibrinogenase from the Western diamondback rattlesnake Crotalus atrox: N-terminal sequence homology with ancrod, an antithrombotic agent from Malayan viper Biochem. Biophys. Res. Commun. 201 1994 1414 1423
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1414-1423
    • Hung, C.C.1    Chiou, S.H.2
  • 34
    • 0034618677 scopus 로고    scopus 로고
    • Expression of a kallikrein-like protease from the snake venom: Engineering of autocatalytic site in the fusion protein to facilitate protein refolding
    • C.C. Hung, and S.H. Chiou Expression of a kallikrein-like protease from the snake venom: engineering of autocatalytic site in the fusion protein to facilitate protein refolding Biochem. Biophys. Res. Commun. 275 2000 924 930
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 924-930
    • Hung, C.C.1    Chiou, S.H.2
  • 35
    • 0037387204 scopus 로고    scopus 로고
    • The molecular basis of thrombin allostery revealed by a 1.8 A structure of the 'slow' form
    • J.A. Huntington, and C.T. Esmon The molecular basis of thrombin allostery revealed by a 1.8 A structure of the 'slow' form Structure (Cambridge) 11 2003 469 479
    • (2003) Structure (Cambridge) , vol.11 , pp. 469-479
    • Huntington, J.A.1    Esmon, C.T.2
  • 36
    • 0023644641 scopus 로고
    • Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme
    • N. Itoh, N. Tanaka, S. Mihashi, and I. Yamashina Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme J. Biol. Chem. 262 1987 3132 3135
    • (1987) J. Biol. Chem. , vol.262 , pp. 3132-3135
    • Itoh, N.1    Tanaka, N.2    Mihashi, S.3    Yamashina, I.4
  • 37
    • 0024278701 scopus 로고
    • Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family
    • N. Itoh, N. Tanaka, I. Funakoshi, T. Kawasaki, S. Mihashi, and I. Yamashina Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family J. Biol. Chem. 263 1988 7628 7631
    • (1988) J. Biol. Chem. , vol.263 , pp. 7628-7631
    • Itoh, N.1    Tanaka, N.2    Funakoshi, I.3    Kawasaki, T.4    Mihashi, S.5    Yamashina, I.6
  • 38
    • 0023816167 scopus 로고
    • The complete nucleotide sequence of the gene for batroxobin, a thrombin-like snake venom enzyme
    • N. Itoh, N. Tanaka, I. Funakoshi, T. Kawasaki, S. Mihashi, and I. Yamashina The complete nucleotide sequence of the gene for batroxobin, a thrombin-like snake venom enzyme Nucleic Acids Res. 16 1988 10377 10378
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10377-10378
    • Itoh, N.1    Tanaka, N.2    Funakoshi, I.3    Kawasaki, T.4    Mihashi, S.5    Yamashina, I.6
  • 39
    • 0037121083 scopus 로고    scopus 로고
    • A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs)
    • I.L. Junqueira-de-Azevedo, and P.L. Ho A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs) Gene 299 2002 279 291
    • (2002) Gene , vol.299 , pp. 279-291
    • Junqueira-de-Azevedo, I.L.1    Ho, P.L.2
  • 40
    • 0015528135 scopus 로고
    • Studies on blood coagulation factor V, VI. Changes of molecular weight accompanying activation of factor V by thrombin and the procoagulant protein of Russell's viper venom
    • M.J. Kahn, and H.C. Hemker Studies on blood coagulation factor V, VI. Changes of molecular weight accompanying activation of factor V by thrombin and the procoagulant protein of Russell's viper venom Thromb. Diath. Haemorrh. 27 1972 25 32
    • (1972) Thromb. Diath. Haemorrh. , vol.27 , pp. 25-32
    • Kahn, M.J.1    Hemker, H.C.2
  • 41
    • 0018292828 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom 1. Purification and characterization of the enzyme
    • E.P. Kirby, S. Niewiarowski, K. Stocker, C. Kettner, E. Shaw, and T.M. Brudzynski Thrombocytin, a serine protease from Bothrops atrox venom 1. Purification and characterization of the enzyme Biochemistry 18 1979 3564 3570
    • (1979) Biochemistry , vol.18 , pp. 3564-3570
    • Kirby, E.P.1    Niewiarowski, S.2    Stocker, K.3    Kettner, C.4    Shaw, E.5    Brudzynski, T.M.6
  • 42
    • 0018573970 scopus 로고
    • Molecular properties of the Factor V-activating enzyme from Russell's viper venom
    • W. Kisiel Molecular properties of the Factor V-activating enzyme from Russell's viper venom J. Biol. Chem. 254 1979 12230 12234
    • (1979) J. Biol. Chem. , vol.254 , pp. 12230-12234
    • Kisiel, W.1
  • 43
    • 0023655997 scopus 로고
    • Characterization of a protein C activator from Agkistrodon contortrix contortrix venom
    • W. Kisiel, S. Kondo, K.J. Smith, B.A. McMullen, and L.F. Smith Characterization of a protein C activator from Agkistrodon contortrix contortrix venom J. Biol. Chem. 262 1987 12607 12613
    • (1987) J. Biol. Chem. , vol.262 , pp. 12607-12613
    • Kisiel, W.1    Kondo, S.2    Smith, K.J.3    McMullen, B.A.4    Smith, L.F.5
  • 44
    • 0024268231 scopus 로고
    • Physiological and biochemical properties of a kallikrein-like enzyme from the venom of Vipera aspis aspis (aspic viper)
    • Y. Komori, and H. Sugihara Physiological and biochemical properties of a kallikrein-like enzyme from the venom of Vipera aspis aspis (aspic viper) Toxicon 6 1988 1193 1203
    • (1988) Toxicon , vol.6 , pp. 1193-1203
    • Komori, Y.1    Sugihara, H.2
  • 45
    • 0027405255 scopus 로고
    • Effect of bilineobin, a thrombin-like proteinase from the venom of common cantil (Agkistrodon bilineatus)
    • Y. Komori, T. Nikai, A. Ohara, S. Yagihashi, and H. Sugihara Effect of bilineobin, a thrombin-like proteinase from the venom of common cantil (Agkistrodon bilineatus) Toxicon 31 1993 257 270
    • (1993) Toxicon , vol.31 , pp. 257-270
    • Komori, Y.1    Nikai, T.2    Ohara, A.3    Yagihashi, S.4    Sugihara, H.5
  • 46
    • 0022639289 scopus 로고
    • Purification and some chemical properties of thrombin-like enzyme from Trimeresurus flavoviridis venom
    • T. Kosugi, Y. Ariga, M. Nakamura, and K. Kinjo Purification and some chemical properties of thrombin-like enzyme from Trimeresurus flavoviridis venom Thromb. Haemost. 55 1986 24 30
    • (1986) Thromb. Haemost. , vol.55 , pp. 24-30
    • Kosugi, T.1    Ariga, Y.2    Nakamura, M.3    Kinjo, K.4
  • 47
    • 0035876166 scopus 로고    scopus 로고
    • Molecular markers of serine protease evolution
    • M.M. Krem, and E. Di Cera Molecular markers of serine protease evolution EMBO J. 20 2001 3036 3045
    • (2001) EMBO J. , vol.20 , pp. 3036-3045
    • Krem, M.M.1    Di Cera, E.2
  • 49
    • 0034658053 scopus 로고    scopus 로고
    • cDNA cloning of brevinase, a heterogeneous two-chain fibrinolytic enzyme from Agkistrodon blomhoffii brevicaudus snake venom, by serial hybridization-polymerase chain reaction
    • J.W. Lee, and W. Park cDNA cloning of brevinase, a heterogeneous two-chain fibrinolytic enzyme from Agkistrodon blomhoffii brevicaudus snake venom, by serial hybridization-polymerase chain reaction Arch. Biochem. Biophys. 377 2000 234 240
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 234-240
    • Lee, J.W.1    Park, W.2
  • 50
    • 0033554030 scopus 로고    scopus 로고
    • Purification and characterization of brevinase, a heterogeneous two-chain fibrinolytic enzyme from the venom of Korean snake, Agkistrodon blomhoffii brevicaudus
    • J.W. Lee, J.H. Seu, I.K. Rhee, I. Jin, Y. Kawamura, and W. Park Purification and characterization of brevinase, a heterogeneous two-chain fibrinolytic enzyme from the venom of Korean snake, Agkistrodon blomhoffii brevicaudus Biochem. Biophys. Res. Commun. 260 1999 665 670
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 665-670
    • Lee, J.W.1    Seu, J.H.2    Rhee, I.K.3    Jin, I.4    Kawamura, Y.5    Park, W.6
  • 51
    • 0023494401 scopus 로고
    • Degradation of coagulation proteins by an enzyme from Malayan pit viper (Akistrodon rhodostoma) venom
    • P. Lollar, C.G. Parker, P.J. Kajenski, R.D. Litwiller, and D.N. Fass Degradation of coagulation proteins by an enzyme from Malayan pit viper (Akistrodon rhodostoma) venom Biochemistry 26 1987 7627 7736
    • (1987) Biochemistry , vol.26 , pp. 7627-7736
    • Lollar, P.1    Parker, C.G.2    Kajenski, P.J.3    Litwiller, R.D.4    Fass, D.N.5
  • 53
    • 0027305178 scopus 로고
    • The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta)
    • A. Magalhaes, B.C. Da Fonseca, C.R. Diniz, J. Gilroy, and M. Richardson The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta) FEBS Lett. 329 1993 116 120
    • (1993) FEBS Lett. , vol.329 , pp. 116-120
    • Magalhaes, A.1    Da Fonseca, B.C.2    Diniz, C.R.3    Gilroy, J.4    Richardson, M.5
  • 54
    • 0000705433 scopus 로고
    • Studies on the active center of trypsin; the binding of amidines and guanidines as models of the substrate side chain
    • M. Mares-Guia, and E. Shaw Studies on the active center of trypsin; the binding of amidines and guanidines as models of the substrate side chain J. Biol. Chem. 240 1965 1579 1585
    • (1965) J. Biol. Chem. , vol.240 , pp. 1579-1585
    • Mares-Guia, M.1    Shaw, E.2
  • 56
    • 0030714651 scopus 로고    scopus 로고
    • Snake venoms
    • F.S. Markland Jr Snake venoms Drugs 54 1997 1 10
    • (1997) Drugs , vol.54 , pp. 1-10
    • Markland F.S. Jr1
  • 57
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • F.S. Markland Jr Snake venoms and the hemostatic system Toxicon 36 1998 1749 1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland F.S. Jr1
  • 59
    • 0035743546 scopus 로고    scopus 로고
    • Molecular basis for the partition of the essential functions of thrombin among snake venom serine proteinases: The case of thrombin-like enzymes
    • R.C. Maroun Molecular basis for the partition of the essential functions of thrombin among snake venom serine proteinases: the case of thrombin-like enzymes Haemostasis 31 2001 247 256
    • (2001) Haemostasis , vol.31 , pp. 247-256
    • Maroun, R.C.1
  • 60
    • 1242276724 scopus 로고    scopus 로고
    • Identification of the substrate-binding exosites of two snake venom serine proteinases: Molecular basis for the partition of two essential functions of thrombin
    • R.C. Maroun, and S.M. Serrano Identification of the substrate-binding exosites of two snake venom serine proteinases: molecular basis for the partition of two essential functions of thrombin J. Mol. Recognit. 17 2004 51 61
    • (2004) J. Mol. Recognit. , vol.17 , pp. 51-61
    • Maroun, R.C.1    Serrano, S.M.2
  • 61
    • 0029060817 scopus 로고
    • Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes
    • N. Marrakchi, R.B. Zingali, H. Karoui, C. Bon, and M. el Ayeb Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes Biochim. Biophys. Acta 1244 1995 147 156
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 147-156
    • Marrakchi, N.1    Zingali, R.B.2    Karoui, H.3    Bon, C.4    El Ayeb, M.5
  • 62
    • 0030857042 scopus 로고    scopus 로고
    • Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties
    • N. Marrakchi, R. Barbouche, S. Guermazi, H. Karoui, C. Bon, and M. El Ayeb Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties Eur. J. Biochem. 247 1997 121 128
    • (1997) Eur. J. Biochem. , vol.247 , pp. 121-128
    • Marrakchi, N.1    Barbouche, R.2    Guermazi, S.3    Karoui, H.4    Bon, C.5    El Ayeb, M.6
  • 63
    • 0031471083 scopus 로고    scopus 로고
    • Insights into the three-dimensional structure of crotalase: Implications for biological activity and substrate specificity
    • I. Massova, H. Pirkle, B.F.P. Edwards, and S. Mobashery Insights into the three-dimensional structure of crotalase: implications for biological activity and substrate specificity Bioorg. Med. Chem. Lett. 24 1997 3139 3144
    • (1997) Bioorg. Med. Chem. Lett. , vol.24 , pp. 3139-3144
    • Massova, I.1    Pirkle, H.2    Edwards, B.F.P.3    Mobashery, S.4
  • 64
    • 6844240861 scopus 로고    scopus 로고
    • Purification and amino acid sequence of halystase from snake venom of Agkistrodon halys blomhoffii, a serine protease that cleaves specifically fibrinogen and kininogen
    • T. Matsui, Y. Sakurai, Y. Fujimura, I. Hayashi, S. Oh-Ishi, M. Suzuki, J. Hamako, Y. Yamamoto, J. Yamazaki, M. Kinoshita, and K. Titani Purification and amino acid sequence of halystase from snake venom of Agkistrodon halys blomhoffii, a serine protease that cleaves specifically fibrinogen and kininogen Eur. J. Biochem. 252 1998 569 575
    • (1998) Eur. J. Biochem. , vol.252 , pp. 569-575
    • Matsui, T.1    Sakurai, Y.2    Fujimura, Y.3    Hayashi, I.4    Oh-Ishi, S.5    Suzuki, M.6    Hamako, J.7    Yamamoto, Y.8    Yamazaki, J.9    Kinoshita, M.10    Titani, K.11
  • 65
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • T. Matsui, Y. Fujimura, and K. Titani Snake venom proteases affecting hemostasis and thrombosis Biochim. Biophys. Acta 1477 2000 146 156
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 66
    • 0024494030 scopus 로고
    • Primary structure of a protein C activator from Agkistrodon contortrix contortrix venom
    • B.A. McMullen, K. Fujikawa, and W. Kisiel Primary structure of a protein C activator from Agkistrodon contortrix contortrix venom Biochemistry 28 1989 674 679
    • (1989) Biochemistry , vol.28 , pp. 674-679
    • McMullen, B.A.1    Fujikawa, K.2    Kisiel, W.3
  • 67
    • 0642307040 scopus 로고    scopus 로고
    • The unusual high molecular mass of Bothrops protease A, a trypsin-like serine peptidase from the venom of Bothrops jararaca, is due to its high carbohydrate content
    • N. Murayama, K. Saguchi, R. Mentele, M.T. Assakura, H. Ohi, Y. Fujita, A.C. Camargo, S. Higuchi, and S.M. Serrano The unusual high molecular mass of Bothrops protease A, a trypsin-like serine peptidase from the venom of Bothrops jararaca, is due to its high carbohydrate content Biochim. Biophys. Acta 1652 2003 1 6
    • (2003) Biochim. Biophys. Acta , vol.1652 , pp. 1-6
    • Murayama, N.1    Saguchi, K.2    Mentele, R.3    Assakura, M.T.4    Ohi, H.5    Fujita, Y.6    Camargo, A.C.7    Higuchi, S.8    Serrano, S.M.9
  • 68
    • 0017623226 scopus 로고
    • Throbocytin-a novel platelet activating enzyme from Bothrops atrox venom
    • S. Niewiarowski, E.P. Kirby, and K. Stocker Throbocytin-a novel platelet activating enzyme from Bothrops atrox venom Thromb. Res. 10 1977 863 869
    • (1977) Thromb. Res. , vol.10 , pp. 863-869
    • Niewiarowski, S.1    Kirby, E.P.2    Stocker, K.3
  • 69
    • 0018646786 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom 2. Interaction with platelets and plasma-clotting factors
    • S. Niewiarowski, E.P. Kirby, T.M. Brudzynski, and K. Stocker Thrombocytin, a serine protease from Bothrops atrox venom 2. Interaction with platelets and plasma-clotting factors Biochemistry 18 1979 3570 3577
    • (1979) Biochemistry , vol.18 , pp. 3570-3577
    • Niewiarowski, S.1    Kirby, E.P.2    Brudzynski, T.M.3    Stocker, K.4
  • 70
    • 0028947353 scopus 로고
    • Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon bilineatus venom
    • T. Nikai, A. Ohara, Y. Komori, J.W. Fox, and H. Sugihara Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon bilineatus venom Arch. Biochem. Biophys. 318 1995 89 96
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 89-96
    • Nikai, T.1    Ohara, A.2    Komori, Y.3    Fox, J.W.4    Sugihara, H.5
  • 72
    • 0017243179 scopus 로고
    • Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
    • C. Nolan, L.S. Hall, and G.H. Barlow Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom Methods Enzymol. 45 1976 205 213
    • (1976) Methods Enzymol. , vol.45 , pp. 205-213
    • Nolan, C.1    Hall, L.S.2    Barlow, G.H.3
  • 74
    • 0024278452 scopus 로고
    • Characterization of a protein C activator from the venom of Agkistrodon contortrix contortrix
    • C.L. Orthner, P. Bhattacharya, and D.K. Strickland Characterization of a protein C activator from the venom of Agkistrodon contortrix contortrix Biochemistry 27 1988 2558 2564
    • (1988) Biochemistry , vol.27 , pp. 2558-2564
    • Orthner, C.L.1    Bhattacharya, P.2    Strickland, D.K.3
  • 75
    • 0037401417 scopus 로고    scopus 로고
    • Purification and characterization of a thrombin like enzyme, elegaxobin II, with lys-bradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu)
    • E. Oyama, and H. Takahashi Purification and characterization of a thrombin like enzyme, elegaxobin II, with lys-bradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu) Toxicon 41 2003 559 568
    • (2003) Toxicon , vol.41 , pp. 559-568
    • Oyama, E.1    Takahashi, H.2
  • 77
    • 0032403414 scopus 로고    scopus 로고
    • Expression and characterization of a novel plasminogen activator from Agkistrodon halys venom
    • D. Park, H. Kim, K. Chung, D.S. Kim, and Y. Yun Expression and characterization of a novel plasminogen activator from Agkistrodon halys venom Toxicon 36 1998 1807 1819
    • (1998) Toxicon , vol.36 , pp. 1807-1819
    • Park, D.1    Kim, H.2    Chung, K.3    Kim, D.S.4    Yun, Y.5
  • 78
    • 0032530323 scopus 로고    scopus 로고
    • The crystal structure of the novel snake venom plasminogen activator TSV-PA: A prototype structure for snake venom serine proteinases
    • M.A. Parry, U. Jacob, R. Huber, A. Wisner, C. Bon, and W. Bode The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases Structure 6 1998 1195 1206
    • (1998) Structure , vol.6 , pp. 1195-1206
    • Parry, M.A.1    Jacob, U.2    Huber, R.3    Wisner, A.4    Bon, C.5    Bode, W.6
  • 79
    • 0031932317 scopus 로고    scopus 로고
    • Thrombin-like enzymes from snake venoms: An updated inventory
    • H. Pirkle Thrombin-like enzymes from snake venoms: an updated inventory Thromb. Haemost. 79 1998 675 683
    • (1998) Thromb. Haemost. , vol.79 , pp. 675-683
    • Pirkle, H.1
  • 80
    • 0023010367 scopus 로고
    • Thrombin-like enzyme from the venom of Bitis gabonica Purification, properties, and coagulant actions
    • H. Pirkle, I. Theodor, D. Miyada, and G. Simmons Thrombin-like enzyme from the venom of Bitis gabonica Purification, properties, and coagulant actions J. Biol. Chem. 261 1986 8830 8835
    • (1986) J. Biol. Chem. , vol.261 , pp. 8830-8835
    • Pirkle, H.1    Theodor, I.2    Miyada, D.3    Simmons, G.4
  • 81
    • 6844236231 scopus 로고
    • Separation of the bradykinin releasing enzymes from the clotting factor in venom from Bothrops jararaca. Naunyn-Schmiedeberg's
    • H.W. Raudonat, and M. Rocha e Silva Separation of the bradykinin releasing enzymes from the clotting factor in venom from Bothrops jararaca. Naunyn-Schmiedeberg's Arch. Exp. Path. Pharmak. 243 1962 237 253
    • (1962) Arch. Exp. Path. Pharmak. , vol.243 , pp. 237-253
    • Raudonat, H.W.1    Rocha E Silva, M.2
  • 82
    • 0020959547 scopus 로고
    • Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca)
    • A.P. Reichl, M.T. Assakura, and F.R. Mandelbaum Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca) Toxicon 21 1983 421 427
    • (1983) Toxicon , vol.21 , pp. 421-427
    • Reichl, A.P.1    Assakura, M.T.2    Mandelbaum, F.R.3
  • 83
    • 0014216684 scopus 로고
    • The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin
    • K.C. Robbins, L. Summaria, B. Hsieh, and R.J. Shah The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin J. Biol. Chem. 242 1967 2333 2342
    • (1967) J. Biol. Chem. , vol.242 , pp. 2333-2342
    • Robbins, K.C.1    Summaria, L.2    Hsieh, B.3    Shah, R.J.4
  • 84
    • 84931128415 scopus 로고
    • Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and trypsin
    • M. Rocha e Silva, W.T. Beraldo, and G. Rosenfeld Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and trypsin Am. J. Physiol. 156 1949 261 273
    • (1949) Am. J. Physiol. , vol.156 , pp. 261-273
    • Rocha E Silva, M.1    Beraldo, W.T.2    Rosenfeld, G.3
  • 85
    • 10944229005 scopus 로고
    • Bradykininogen levels following Crotalus envenomation
    • F.E. Russel Bradykininogen levels following Crotalus envenomation Toxicon 69 1965 277 279
    • (1965) Toxicon , vol.69 , pp. 277-279
    • Russel, F.E.1
  • 86
    • 0036027966 scopus 로고    scopus 로고
    • Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom
    • M. Samel, J. Subbi, J. Siigur, and E. Siigur Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom Toxicon 40 2002 51 54
    • (2002) Toxicon , vol.40 , pp. 51-54
    • Samel, M.1    Subbi, J.2    Siigur, J.3    Siigur, E.4
  • 87
    • 0034698270 scopus 로고    scopus 로고
    • Interaction of viper venom serine peptidases with thrombin receptors on human platelets
    • B.F. Santos, S.M. Serrano, A. Kuliopulos, and S. Niewiarowski Interaction of viper venom serine peptidases with thrombin receptors on human platelets FEBS Lett. 477 2000 199 202
    • (2000) FEBS Lett. , vol.477 , pp. 199-202
    • Santos, B.F.1    Serrano, S.M.2    Kuliopulos, A.3    Niewiarowski, S.4
  • 88
    • 0014211618 scopus 로고
    • On the size of the active site in proteases I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 89
    • 0019171408 scopus 로고
    • Crotalocytin: Characterization of the timber rattlesnake platelet activating protein
    • A.H. Schmaier, and R.W. Colman Crotalocytin: characterization of the timber rattlesnake platelet activating protein Blood 56 1980 1020 1028
    • (1980) Blood , vol.56 , pp. 1020-1028
    • Schmaier, A.H.1    Colman, R.W.2
  • 91
    • 0018960511 scopus 로고
    • Purification of gyroxin from a South American rattlesnake (Crotalus durissus terrificus) venom
    • C. Seki, J.C. Vidal, and A. Barrio Purification of gyroxin from a South American rattlesnake (Crotalus durissus terrificus) venom Toxicon 18 1980 235 247
    • (1980) Toxicon , vol.18 , pp. 235-247
    • Seki, C.1    Vidal, J.C.2    Barrio, A.3
  • 92
    • 0027418603 scopus 로고
    • Basic proteinases from Bothrops moojeni (caissaca) venom-I Isolation and activity of two serine proteinases, MSP 1 and MSP 2, on synthetic substrates and on platelet aggregation
    • S.M. Serrano, M.F. Matos, F.R. Mandelbaum, and C.A. Sampaio Basic proteinases from Bothrops moojeni (caissaca) venom-I Isolation and activity of two serine proteinases, MSP 1 and MSP 2, on synthetic substrates and on platelet aggregation Toxicon 31 1993 471 481
    • (1993) Toxicon , vol.31 , pp. 471-481
    • Serrano, S.M.1    Matos, M.F.2    Mandelbaum, F.R.3    Sampaio, C.A.4
  • 93
    • 0029005343 scopus 로고
    • Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca
    • S.M. Serrano, R. Mentele, C.A. Sampaio, and E. Fink Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca Biochemistry 34 1995 7186 7193
    • (1995) Biochemistry , vol.34 , pp. 7186-7193
    • Serrano, S.M.1    Mentele, R.2    Sampaio, C.A.3    Fink, E.4
  • 94
    • 0032005943 scopus 로고    scopus 로고
    • Purification and characterization of a kinin-releasing and fibrinogen-clotting serine proteinase (KN-BJ) from the venom of Bothrops jararaca, and molecular cloning and sequence analysis of its cDNA
    • S.M. Serrano, Y. Hagiwara, N. Murayama, S. Higuchi, R. Mentele, C.A. Sampaio, A.C. Camargo, and E. Fink Purification and characterization of a kinin-releasing and fibrinogen-clotting serine proteinase (KN-BJ) from the venom of Bothrops jararaca, and molecular cloning and sequence analysis of its cDNA Eur. J. Biochem. 251 1998 845 853
    • (1998) Eur. J. Biochem. , vol.251 , pp. 845-853
    • Serrano, S.M.1    Hagiwara, Y.2    Murayama, N.3    Higuchi, S.4    Mentele, R.5    Sampaio, C.A.6    Camargo, A.C.7    Fink, E.8
  • 95
    • 0034098978 scopus 로고    scopus 로고
    • A novel fibrinogen-clotting enzyme, TL-BJ, from the venom of the snake Bothrops jararaca: Purification and characterization
    • S.M. Serrano, C.A. Sampaio, R. Mentele, A.C. Camargo, and E. Fink A novel fibrinogen-clotting enzyme, TL-BJ, from the venom of the snake Bothrops jararaca: purification and characterization Thromb. Haemost. 83 2000 438 444
    • (2000) Thromb. Haemost. , vol.83 , pp. 438-444
    • Serrano, S.M.1    Sampaio, C.A.2    Mentele, R.3    Camargo, A.C.4    Fink, E.5
  • 96
    • 0022384286 scopus 로고
    • Purification and characterization of a coagulant enzyme from Trimeresurus flavoviridis venom
    • T.C. Shieh, S. Tanaka, H. Kihara, M. Ohno, and S. Makisumi Purification and characterization of a coagulant enzyme from Trimeresurus flavoviridis venom J. Biochem. (Tokyo) 98 1985 713 721
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 713-721
    • Shieh, T.C.1    Tanaka, S.2    Kihara, H.3    Ohno, M.4    Makisumi, S.5
  • 97
    • 0023883275 scopus 로고
    • Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom
    • T.C. Shieh, S. Kawabata, H. Kihara, M. Ohno, and S. Iwanaga Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom J. Biochem. (Tokyo) 103 1988 596 605
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 596-605
    • Shieh, T.C.1    Kawabata, S.2    Kihara, H.3    Ohno, M.4    Iwanaga, S.5
  • 98
    • 0027368585 scopus 로고
    • Purification of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi)
    • K. Shimokawa, and H. Takahashi Purification of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi) Toxicon 31 1993 1213 1219
    • (1993) Toxicon , vol.31 , pp. 1213-1219
    • Shimokawa, K.1    Takahashi, H.2
  • 99
    • 0027369828 scopus 로고
    • Some properties of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi)
    • K. Shimokawa, and H. Takahashi Some properties of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi) Toxicon 31 1993 1221 1227
    • (1993) Toxicon , vol.31 , pp. 1221-1227
    • Shimokawa, K.1    Takahashi, H.2
  • 100
    • 0030976517 scopus 로고    scopus 로고
    • Capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (kankoku-mamushi): Activity resulting from the release of peptides from fibrinogen
    • K. Shimokawa, and H. Takahashi Capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (kankoku-mamushi): activity resulting from the release of peptides from fibrinogen Toxicon 35 1997 597 605
    • (1997) Toxicon , vol.35 , pp. 597-605
    • Shimokawa, K.1    Takahashi, H.2
  • 101
    • 0032436007 scopus 로고    scopus 로고
    • Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (Levantine viper) snake venom
    • E. Siigur, M. Samel, K. Tonismagi, J. Subbi, T. Reintamm, and J. Siigur Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (Levantine viper) snake venom Biochim. Biophys. Acta 1429 1998 239 248
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 239-248
    • Siigur, E.1    Samel, M.2    Tonismagi, K.3    Subbi, J.4    Reintamm, T.5    Siigur, J.6
  • 102
    • 0344500853 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a cDNA for factor V activating enzyme
    • E. Siigur, A. Aaspollu, and J. Siigur Molecular cloning and sequence analysis of a cDNA for factor V activating enzyme Biochem. Biophys. Res. Commun. 262 1999 328 332
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 328-332
    • Siigur, E.1    Aaspollu, A.2    Siigur, J.3
  • 103
    • 0024811327 scopus 로고
    • Purification and properties of the thrombin-like enzyme from the venom of Lachesis muta muta
    • A.M.V. Silveira, A. Magalhães, C.R. Diniz, and E.B. Oliveira Purification and properties of the thrombin-like enzyme from the venom of Lachesis muta muta Int. J. Biochem. 21 1989 863 871
    • (1989) Int. J. Biochem. , vol.21 , pp. 863-871
    • Silveira, A.M.V.1    Magalhães, A.2    Diniz, C.R.3    Oliveira, E.B.4
  • 104
    • 0017283234 scopus 로고
    • A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization
    • J. Stenflo A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization J. Biol. Chem. 251 1976 355 363
    • (1976) J. Biol. Chem. , vol.251 , pp. 355-363
    • Stenflo, J.1
  • 105
    • 0017242939 scopus 로고
    • The coagulant enzyme from Bothrops atrox venom (batroxobin)
    • K. Stocker, and G.H. Barlow The coagulant enzyme from Bothrops atrox venom (batroxobin) Methods Enzymol. 45 1976 214 223
    • (1976) Methods Enzymol. , vol.45 , pp. 214-223
    • Stocker, K.1    Barlow, G.H.2
  • 106
    • 0020033067 scopus 로고
    • Thrombin-like snake venom proteinases
    • K. Stocker, H. Fischer, and J. Meier Thrombin-like snake venom proteinases Toxicon 20 1982 265 273
    • (1982) Toxicon , vol.20 , pp. 265-273
    • Stocker, K.1    Fischer, H.2    Meier, J.3
  • 107
    • 0023115106 scopus 로고
    • Characterization of the protein C activator Protac from the venom of the southern copperhead (Agkistrodon contortrix) snake
    • K. Stocker, H. Fischer, J. Meier, M. Brogli, and L. Svendsen Characterization of the protein C activator Protac from the venom of the southern copperhead (Agkistrodon contortrix) snake Toxicon 25 1987 239 252
    • (1987) Toxicon , vol.25 , pp. 239-252
    • Stocker, K.1    Fischer, H.2    Meier, J.3    Brogli, M.4    Svendsen, L.5
  • 108
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin structure
    • M.T. Stubbs, and W. Bode A player of many parts: the spotlight falls on thrombin structure Thromb. Res. 69 1993 1 58
    • (1993) Thromb. Res. , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 109
    • 0022611950 scopus 로고
    • Inhibition of batroxobin, a serine proteinase from Bothrops snake venom, by derivatives of benzamidine
    • J. Sturzebecher, U. Sturzebecher, and F. Markwardt Inhibition of batroxobin, a serine proteinase from Bothrops snake venom, by derivatives of benzamidine Toxicon 24 1986 585 595
    • (1986) Toxicon , vol.24 , pp. 585-595
    • Sturzebecher, J.1    Sturzebecher, U.2    Markwardt, F.3
  • 110
    • 0024270675 scopus 로고
    • The factor V-activating enzyme (RVV-V) from Russell's viper venom Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences
    • F. Tokunaga, K. Nagasawa, S. Tamura, T. Miyata, S. Iwanaga, and W. Kisiel The factor V-activating enzyme (RVV-V) from Russell's viper venom Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences J. Biol. Chem. 263 1988 17471 17481
    • (1988) J. Biol. Chem. , vol.263 , pp. 17471-17481
    • Tokunaga, F.1    Nagasawa, K.2    Tamura, S.3    Miyata, T.4    Iwanaga, S.5    Kisiel, W.6
  • 111
    • 0035865501 scopus 로고    scopus 로고
    • Serine protease isoforms of Deinagkistrodon acutus venom: Cloning, sequencing and phylogenetic analysis
    • Y.M. Wang, S.R. Wang, and I.H. Tsai Serine protease isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis Biochem. J. 354 2001 161 168
    • (2001) Biochem. J. , vol.354 , pp. 161-168
    • Wang, Y.M.1    Wang, S.R.2    Tsai, I.H.3
  • 112
    • 0036379701 scopus 로고    scopus 로고
    • Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase
    • C. Yamamoto, D. Tsuru, N. Oda-Ueda, M. Ohno, S. Hattori, and S.T. Kim Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase Immunology 107 2002 111 117
    • (2002) Immunology , vol.107 , pp. 111-117
    • Yamamoto, C.1    Tsuru, D.2    Oda-Ueda, N.3    Ohno, M.4    Hattori, S.5    Kim, S.T.6
  • 113
    • 0036399793 scopus 로고    scopus 로고
    • Cloning, expression and purification of gussurobin, a thrombin-like enzyme from the snake venom of Gloydius ussuriensis
    • Q. Yang, X.J. Hu, X.M. Xu, L.J. An, X.D. Yuan, and Z.G. Su Cloning, expression and purification of gussurobin, a thrombin-like enzyme from the snake venom of Gloydius ussuriensis Acta Biochim. Biophys. Sinica 34 2002 6 10
    • (2002) Acta Biochim. Biophys. Sinica , vol.34 , pp. 6-10
    • Yang, Q.1    Hu, X.J.2    Xu, X.M.3    An, L.J.4    Yuan, X.D.5    Su, Z.G.6
  • 114
    • 0028899505 scopus 로고
    • A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning
    • Y. Zhang, A. Wisner, Y. Xiong, and C. Bon A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning J. Biol. Chem. 270 1995 10246 10255
    • (1995) J. Biol. Chem. , vol.270 , pp. 10246-10255
    • Zhang, Y.1    Wisner, A.2    Xiong, Y.3    Bon, C.4
  • 115
    • 0030878832 scopus 로고    scopus 로고
    • Trimeresurus stejnegeri snake venom plasminogen activator Site-directed mutagenesis and molecular modeling
    • Y. Zhang, A. Wisner, R.C. Maroun, V. Choumet, Y. Xiong, and C. Bon Trimeresurus stejnegeri snake venom plasminogen activator Site-directed mutagenesis and molecular modeling J. Biol. Chem. 272 1997 20531 20537
    • (1997) J. Biol. Chem. , vol.272 , pp. 20531-20537
    • Zhang, Y.1    Wisner, A.2    Maroun, R.C.3    Choumet, V.4    Xiong, Y.5    Bon, C.6


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