메뉴 건너뛰기




Volumn 26, Issue 1, 2007, Pages 25-46

Interaction of snake-venom proteins with blood coagulation factors: Mechanisms of anticoagulant activity

Author keywords

Anticoagulant; Hemostatic system; Snake venom proteins

Indexed keywords

BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 9; BOTHROJARACIN; PHOSPHOLIPASE A2; PROTEIN; PROTHROMBIN; SALMORIN; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 33846982589     PISSN: 15569543     EISSN: 15569551     Source Type: Journal    
DOI: 10.1080/15569540600567412     Document Type: Review
Times cited : (16)

References (80)
  • 1
  • 2
    • 0034595843 scopus 로고    scopus 로고
    • Role of proexosite I in factor Va-dependent substrate interactions of prothrombin activation
    • Anderson, P. J., Nesset, A., Dharmawardana, K. R., Bock, P. E. (2000b). Role of proexosite I in factor Va-dependent substrate interactions of prothrombin activation. J. Biol. Chem. 275(22):16435-16442.
    • (2000) J. Biol. Chem , vol.275 , Issue.22 , pp. 16435-16442
    • Anderson, P.J.1    Nesset, A.2    Dharmawardana, K.R.3    Bock, P.E.4
  • 3
    • 0030201175 scopus 로고    scopus 로고
    • 2 - a structural review
    • 2 - a structural review. Toxicon 34(8):827-842.
    • (1996) Toxicon , vol.34 , Issue.8 , pp. 827-842
    • Arni, R.K.1    Ward, R.J.2
  • 4
    • 0029979990 scopus 로고    scopus 로고
    • Bothrojaracin: A potent two-site-directed thrombin inhibitor
    • Arocas, V., Zingali, R. B., Guillin, M. C., Bon, C., Jandrot-Perus, M. (1996). Bothrojaracin: a potent two-site-directed thrombin inhibitor. Biochemistry 35(28):9083-9089.
    • (1996) Biochemistry , vol.35 , Issue.28 , pp. 9083-9089
    • Arocas, V.1    Zingali, R.B.2    Guillin, M.C.3    Bon, C.4    Jandrot-Perus, M.5
  • 5
    • 0030930829 scopus 로고    scopus 로고
    • Molecular cloning and expression of bothrojaracin, a potent thrombin inhibitor from snake venom
    • Arocas, V., Castro, H. C., Zingali, R. B., Guillin, M. C., Jandrot-Perrus, M., Bon, C., Wisner, A. (1997). Molecular cloning and expression of bothrojaracin, a potent thrombin inhibitor from snake venom. Eur. J. Biochem. 248(2):550-557.
    • (1997) Eur. J. Biochem , vol.248 , Issue.2 , pp. 550-557
    • Arocas, V.1    Castro, H.C.2    Zingali, R.B.3    Guillin, M.C.4    Jandrot-Perrus, M.5    Bon, C.6    Wisner, A.7
  • 7
    • 0024807865 scopus 로고
    • A novel blood coagulation factor IX/factor Xbinding protein with anticoagulant activity from the venom of Trimeresurus flavoviridis (Habu snake): Isolation and characterization
    • Atoda, H., Morita, T. (1989). A novel blood coagulation factor IX/factor Xbinding protein with anticoagulant activity from the venom of Trimeresurus flavoviridis (Habu snake): isolation and characterization. J. Biochem. 106(5):808-813.
    • (1989) J. Biochem , vol.106 , Issue.5 , pp. 808-813
    • Atoda, H.1    Morita, T.2
  • 8
    • 0025874671 scopus 로고
    • The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin
    • Atoda, H., Hyuga, M., Morita, T. (1991). The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin. Eur. J. Biol. Chem. 266(23):14903-14911.
    • (1991) Eur. J. Biol. Chem , vol.266 , Issue.23 , pp. 14903-14911
    • Atoda, H.1    Hyuga, M.2    Morita, T.3
  • 9
    • 0028016085 scopus 로고
    • Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis
    • Atoda, H., Yoshida, N., Ishikawa, M., Morita, T. (1994). Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Eur. J. Biochem. 224(2):703-708.
    • (1994) Eur. J. Biochem , vol.224 , Issue.2 , pp. 703-708
    • Atoda, H.1    Yoshida, N.2    Ishikawa, M.3    Morita, T.4
  • 10
    • 0028889413 scopus 로고
    • Blood coagulation factor IX-binding protein from the venom of Trimeresurus flavoviridis: Purification and characterization
    • Atoda, H., Ishikawa, M., Yoshihara, E., Sekiya, F., Morita, T. (1995). Blood coagulation factor IX-binding protein from the venom of Trimeresurus flavoviridis: purification and characterization. J. Biochem. 118(5):965-973.
    • (1995) J. Biochem , vol.118 , Issue.5 , pp. 965-973
    • Atoda, H.1    Ishikawa, M.2    Yoshihara, E.3    Sekiya, F.4    Morita, T.5
  • 11
    • 0032534863 scopus 로고    scopus 로고
    • Coagulation factor Xbinding protein from Deinagkistrodon acutus venom is a Gla domain-binding protein
    • Atoda, H., Ishikawa, M., Mizuno, H., Morita, T. (1998). Coagulation factor Xbinding protein from Deinagkistrodon acutus venom is a Gla domain-binding protein. Biochemistry 37(50):17361-17370.
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17361-17370
    • Atoda, H.1    Ishikawa, M.2    Mizuno, H.3    Morita, T.4
  • 12
    • 0037032426 scopus 로고    scopus 로고
    • Calcium-binding analysis and molecular modeling reveal Echis coagulation factor IX/factor Xbinding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins
    • Atoda, H., Kaneko, H., Mizuno, H., Morita, T. (2002). Calcium-binding analysis and molecular modeling reveal Echis coagulation factor IX/factor Xbinding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins. FEBS Lett. 531(2):229-234.
    • (2002) FEBS Lett , vol.531 , Issue.2 , pp. 229-234
    • Atoda, H.1    Kaneko, H.2    Mizuno, H.3    Morita, T.4
  • 13
    • 0028318556 scopus 로고
    • 2 from Vipera russelli snake venom by guanidination of lysine residues
    • 2 from Vipera russelli snake venom by guanidination of lysine residues. Toxicon 32(6):749-752.
    • (1994) Toxicon , vol.32 , Issue.6 , pp. 749-752
    • Babu, A.S.1    Gowda, T.V.2
  • 14
    • 0034731905 scopus 로고    scopus 로고
    • Not just an active site
    • Banner, D. W. (2000). Not just an active site. Nature 404(6777):449-450.
    • (2000) Nature , vol.404 , Issue.6777 , pp. 449-450
    • Banner, D.W.1
  • 15
    • 0017099577 scopus 로고
    • 2 with anticoagulant activity. II. inhibition of the phospholiped activity in coagulation
    • 2 with anticoagulant activity. II. inhibition of the phospholiped activity in coagulation. Biochim. Biophys. Acta 429(3):839-852.
    • (1976) Biochim. Biophys. Acta , vol.429 , Issue.3 , pp. 839-852
    • Boffa, M.C.1    Boffa, G.A.2
  • 16
    • 0033741151 scopus 로고    scopus 로고
    • Snake venom proteins acting on hemostasis
    • Braud, S., Bon, C., Wisner, A. (2000). Snake venom proteins acting on hemostasis. Biochimie 82(9-10):851-859.
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 851-859
    • Braud, S.1    Bon, C.2    Wisner, A.3
  • 17
    • 0032400791 scopus 로고    scopus 로고
    • Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus
    • Castro, H. C., Dutra, D. L. S., Oliveira-Carvalho, A. L., Zingali, R. B. (1998). Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus. Toxicon 36(12):1903-1912.
    • (1998) Toxicon , vol.36 , Issue.12 , pp. 1903-1912
    • Castro, H.C.1    Dutra, D.L.S.2    Oliveira-Carvalho, A.L.3    Zingali, R.B.4
  • 18
    • 0032989046 scopus 로고    scopus 로고
    • Identification of bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta
    • Castro, H. C., Fernandes, M., Zingali, R. B. (1999). Identification of bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta. Toxicon 37(10):1403-1416.
    • (1999) Toxicon , vol.37 , Issue.10 , pp. 1403-1416
    • Castro, H.C.1    Fernandes, M.2    Zingali, R.B.3
  • 19
    • 0029913241 scopus 로고    scopus 로고
    • Functional and sequence characterization of coagulation factor IX/factor X-binding protein from the venom of Echis carinatus leucogaster
    • Chen, Y. L., Tsai, I. H. (1996). Functional and sequence characterization of coagulation factor IX/factor X-binding protein from the venom of Echis carinatus leucogaster. Biochemistry 35(16):5264-5271.
    • (1996) Biochemistry , vol.35 , Issue.16 , pp. 5264-5271
    • Chen, Y.L.1    Tsai, I.H.2
  • 20
    • 0027130809 scopus 로고
    • Coagulation factor X inhibitor from hundred-pace snake (Deinagkistrodon acutus) venom
    • Cox, A. C. (1993). Coagulation factor X inhibitor from hundred-pace snake (Deinagkistrodon acutus) venom. Toxicon 31(11):1445-1457.
    • (1993) Toxicon , vol.31 , Issue.11 , pp. 1445-1457
    • Cox, A.C.1
  • 21
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E. W., Fujikawa, K., Kisiel, W. (1991). The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30(43):10363-10370.
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 23
    • 0041819753 scopus 로고    scopus 로고
    • Evolutionary analysis reveals collective properties and specificity in the C-type lectin-like domain superfamily
    • Ebner, S., Sharon, N., Ben-Tal, N. (2003). Evolutionary analysis reveals collective properties and specificity in the C-type lectin-like domain superfamily. Prot. Struct. Funct. Gen. 52(1):44-55.
    • (2003) Prot. Struct. Funct. Gen , vol.52 , Issue.1 , pp. 44-55
    • Ebner, S.1    Sharon, N.2    Ben-Tal, N.3
  • 26
    • 0028109290 scopus 로고
    • Membranedependent reactions in blood coagulation: Role of vitamin-K-dependent enzyme complexes
    • Kalafatis, M., Swords, N. A., Rand, M. D., Mann, K. G. (1994). Membranedependent reactions in blood coagulation: role of vitamin-K-dependent enzyme complexes. Biochim. Biophys. Acta 1227(3):113-129.
    • (1994) Biochim. Biophys. Acta , vol.1227 , Issue.3 , pp. 113-129
    • Kalafatis, M.1    Swords, N.A.2    Rand, M.D.3    Mann, K.G.4
  • 27
    • 15844371511 scopus 로고    scopus 로고
    • Complete amino acid sequence and identification of the platelet glycoprotein Ib-binding site of jararaca GPIb-BP, a snake venom protein isolated from Bothrops jararaca
    • Kawasaki, T., Fujimura, Y., Usami, Y., Suzuki, M., Miura, S., Sakurai, Y., Makita, K., Taniuchi, Y., Hirano, K., Titani, K. (1996). Complete amino acid sequence and identification of the platelet glycoprotein Ib-binding site of jararaca GPIb-BP, a snake venom protein isolated from Bothrops jararaca J. Biol. Chem. 271(18):10635-10639.
    • (1996) J. Biol. Chem , vol.271 , Issue.18 , pp. 10635-10639
    • Kawasaki, T.1    Fujimura, Y.2    Usami, Y.3    Suzuki, M.4    Miura, S.5    Sakurai, Y.6    Makita, K.7    Taniuchi, Y.8    Hirano, K.9    Titani, K.10
  • 28
    • 0033199229 scopus 로고    scopus 로고
    • 2 from Naja nigricollis venom binds to coagulation factor Xa to Inhibit the prothrombinase complex
    • 2 from Naja nigricollis venom binds to coagulation factor Xa to Inhibit the prothrombinase complex. Arch. Biochem. Biophys. 369(1);107-113.
    • (1999) Arch. Biochem. Biophys , vol.369 , Issue.1 , pp. 107-113
    • Kerns, R.T.1    Kini, R.M.2    Stefansson, S.3    Evans, H.J.4
  • 29
    • 33846975728 scopus 로고    scopus 로고
    • 2 Enzymes: Structure, Function and Mechanism, Chichester, England: John Wiley & Sons, 511.
    • 2 Enzymes: Structure, Function and Mechanism, Chichester, England: John Wiley & Sons, 511.
  • 33
    • 0029617267 scopus 로고
    • 2 isoenzymes from Naja nigricollis venom
    • 2 isoenzymes from Naja nigricollis venom. Toxicon 33(12):1585-1590.
    • (1995) Toxicon , vol.33 , Issue.12 , pp. 1585-1590
    • Kini, R.M.1    Evans, H.J.2
  • 34
    • 0034663075 scopus 로고    scopus 로고
    • Purification and cDNA cloning of salmorin that inhibits fibrinogen clotting
    • Koh, Y., Chung, K., Kim, D. (2000). Purification and cDNA cloning of salmorin that inhibits fibrinogen clotting. Thromb. Res. 99(4):389-398.
    • (2000) Thromb. Res , vol.99 , Issue.4 , pp. 389-398
    • Koh, Y.1    Chung, K.2    Kim, D.3
  • 35
    • 0035998328 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of halyxin, a heterogeneous three-chain anticoagulant protein from the venom of Agkistrodon halys brevicaudus
    • Koo, B. H., Sohn, Y. D., Hwang, K. C., Jang, Y., Kim, D. S., Chung, K. H. (2002). Characterization and cDNA cloning of halyxin, a heterogeneous three-chain anticoagulant protein from the venom of Agkistrodon halys brevicaudus. Toxicon 40(7):947-957.
    • (2002) Toxicon , vol.40 , Issue.7 , pp. 947-957
    • Koo, B.H.1    Sohn, Y.D.2    Hwang, K.C.3    Jang, Y.4    Kim, D.S.5    Chung, K.H.6
  • 36
    • 0026346977 scopus 로고
    • Proteolytic formation of either of the two prothrombin activation intermediates results in formation of a hirugen-binding site
    • Liu, L. W., Ye, J., Johnson, A. E., Esmon, C. T. (1991). Proteolytic formation of either of the two prothrombin activation intermediates results in formation of a hirugen-binding site. J. Biol. Chem. 266(35):23632-23636.
    • (1991) J. Biol. Chem , vol.266 , Issue.35 , pp. 23632-23636
    • Liu, L.W.1    Ye, J.2    Johnson, A.E.3    Esmon, C.T.4
  • 37
    • 0343442450 scopus 로고    scopus 로고
    • Coagulant and anticoagulant activities of Bothrops lanceolatus (Fer-de-lance) venom
    • Lôbo de Araújo, A., Kamiguti, A., Bon, C. (2001). Coagulant and anticoagulant activities of Bothrops lanceolatus (Fer-de-lance) venom. Toxicon 39(2-3):371-375.
    • (2001) Toxicon , vol.39 , Issue.2-3 , pp. 371-375
    • Lôbo de Araújo, A.1    Kamiguti, A.2    Bon, C.3
  • 38
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland, F. S. (1998). Snake venoms and the hemostatic system. Toxicon 36(12):1749-1800.
    • (1998) Toxicon , vol.36 , Issue.12 , pp. 1749-1800
    • Markland, F.S.1
  • 39
    • 0030979409 scopus 로고    scopus 로고
    • Structure of coagulation factors IX/X-binding protein, a heterodimer of Ctype lectin domains
    • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., Morita, T. (1997). Structure of coagulation factors IX/X-binding protein, a heterodimer of Ctype lectin domains. Nat. Struct. Biol. 4(6):438-441.
    • (1997) Nat. Struct. Biol , vol.4 , Issue.6 , pp. 438-441
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, T.6
  • 40
    • 0033612377 scopus 로고    scopus 로고
    • Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A.: Implication of central loop swapping based on deletion in the linker region
    • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., Morita, T. (1999). Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A.: implication of central loop swapping based on deletion in the linker region. J. Mol. Biol. 289(1):103-112.
    • (1999) J. Mol. Biol , vol.289 , Issue.1 , pp. 103-112
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, T.6
  • 41
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with Gla domain of factor X
    • Mizuno, H., Fujimoto, Z., Atoda, H., Morita, T. (2001). Crystal structure of an anticoagulant protein in complex with Gla domain of factor X. Proc. Natl. Acad. Sci. USA. 98(13):7230-7234.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.13 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 42
    • 0034307023 scopus 로고    scopus 로고
    • Inhibition of prothrombin activation by bothrojaracin, a C-type lectin from Bothrops jararaca venom
    • Monteiro, R. Q., Zingali, R. B. (2000). Inhibition of prothrombin activation by bothrojaracin, a C-type lectin from Bothrops jararaca venom. Arch. Biochem. Biophys. 382(1):123-128.
    • (2000) Arch. Biochem. Biophys , vol.382 , Issue.1 , pp. 123-128
    • Monteiro, R.Q.1    Zingali, R.B.2
  • 43
    • 0036166459 scopus 로고    scopus 로고
    • Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated prothrombin activation
    • Monteiro, R. Q., Zingali, R. B. (2002). Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated prothrombin activation. Thromb. Haemost. 87(2):288-293.
    • (2002) Thromb. Haemost , vol.87 , Issue.2 , pp. 288-293
    • Monteiro, R.Q.1    Zingali, R.B.2
  • 44
    • 0030998805 scopus 로고    scopus 로고
    • Distinct bothojaracin isoforms produced by individual jararaca (Bothrops jararaca) snakes
    • Monteiro, R. Q., Carlini, C. R., Guimarães, J. A., Zingali, R. B. (1997). Distinct bothojaracin isoforms produced by individual jararaca (Bothrops jararaca) snakes. Toxicon 35(5):649-657.
    • (1997) Toxicon , vol.35 , Issue.5 , pp. 649-657
    • Monteiro, R.Q.1    Carlini, C.R.2    Guimarães, J.A.3    Zingali, R.B.4
  • 46
    • 0345493916 scopus 로고    scopus 로고
    • Allosteric changes of thrombin catalytic site induced by interaction of bothrojaracin with anion-binding exosities I and II
    • Monteiro, R. Q., Rapôso, J. G., Wisner, A., Guimarães, J. A., Bon, C., Zingali, R. B. (1999). Allosteric changes of thrombin catalytic site induced by interaction of bothrojaracin with anion-binding exosities I and II. Biochem. Biophys. Res. Comm. 262(3):819-822.
    • (1999) Biochem. Biophys. Res. Comm , vol.262 , Issue.3 , pp. 819-822
    • Monteiro, R.Q.1    Rapôso, J.G.2    Wisner, A.3    Guimarães, J.A.4    Bon, C.5    Zingali, R.B.6
  • 47
    • 0037457949 scopus 로고    scopus 로고
    • Subunit dissociation, unfolding, and inactivation of bothrojaracin, a C-type lectin-like protein from snake venom
    • Monteiro, R. Q., Foguel, D., Castro, H. C., Zingali, R. B. (2003). Subunit dissociation, unfolding, and inactivation of bothrojaracin, a C-type lectin-like protein from snake venom. Biochemistry 42(2):509-515.
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 509-515
    • Monteiro, R.Q.1    Foguel, D.2    Castro, H.C.3    Zingali, R.B.4
  • 48
    • 0035742201 scopus 로고    scopus 로고
    • 2: Protein versus phospholipid dependent mechanism of action
    • 2: protein versus phospholipid dependent mechanism of action. Haemostasis 31(3-6):279-287.
    • (2001) Haemostasis , vol.31 , Issue.3-6 , pp. 279-287
    • Mounier, C.M.1    Bon, C.2    Kini, R.M.3
  • 51
    • 9744281932 scopus 로고    scopus 로고
    • Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
    • Ogawa, T., Chijiwa, T., Oda-Ueda, N., Ohno, M. (2005). Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon 45(1):1-14.
    • (2005) Toxicon , vol.45 , Issue.1 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 52
    • 0016690687 scopus 로고
    • Purification and properties of the anticoagulant principle of Trimeresurus gramineus venom
    • Ouyang, C., Yang, F. Y. (1975). Purification and properties of the anticoagulant principle of Trimeresurus gramineus venom. Biochim. Biophys. Acta 386(2):479-492.
    • (1975) Biochim. Biophys. Acta , vol.386 , Issue.2 , pp. 479-492
    • Ouyang, C.1    Yang, F.Y.2
  • 53
    • 0019434362 scopus 로고
    • Mechanism of the anticoagulant action of phospholipase A purified from Trimeresurus mucrosquamatus (Formosan Habu) snake venom
    • Ouyang, C., Jy, W., Zan, Y. P., Teng, C. M. (1981). Mechanism of the anticoagulant action of phospholipase A purified from Trimeresurus mucrosquamatus (Formosan Habu) snake venom. Toxicon 19(1):113-120.
    • (1981) Toxicon , vol.19 , Issue.1 , pp. 113-120
    • Ouyang, C.1    Jy, W.2    Zan, Y.P.3    Teng, C.M.4
  • 54
    • 0019209304 scopus 로고
    • 2: A fluorescence study of their binding to phospholipid vesicles and correlation with anticoagulant activities
    • 2: a fluorescence study of their binding to phospholipid vesicles and correlation with anticoagulant activities. J. Biol. Act. 255(16):7734-7739.
    • (1980) J. Biol. Act , vol.255 , Issue.16 , pp. 7734-7739
    • Prigent-Dachary, J.1    Boffa, M.C.2    Boiseau, M.R.3    Dufourcq, J.4
  • 55
    • 0018907213 scopus 로고
    • The role of phospholipids and factor Va in the prothrombinase complex
    • Rosing, J., Tans, G., Govers-Riemslag, J. W., Zwaal, R. F., Hemker, H. C. (1980). The role of phospholipids and factor Va in the prothrombinase complex. J. Biol. Chem. 255(1):274-283.
    • (1980) J. Biol. Chem , vol.255 , Issue.1 , pp. 274-283
    • Rosing, J.1    Tans, G.2    Govers-Riemslag, J.W.3    Zwaal, R.F.4    Hemker, H.C.5
  • 56
    • 0034792723 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom
    • Sakurai, Y., Takatsuka, H., Yoshioka, A., Matsui, T., Suzuki, M., Titani, K., Fujimura, Y. (2001). Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. Toxicon 39(12):1827-1833.
    • (2001) Toxicon , vol.39 , Issue.12 , pp. 1827-1833
    • Sakurai, Y.1    Takatsuka, H.2    Yoshioka, A.3    Matsui, T.4    Suzuki, M.5    Titani, K.6    Fujimura, Y.7
  • 57
    • 0041620465 scopus 로고    scopus 로고
    • Anticoagulant activity of M-LAO, L-amino acid oxidase purified from Agkistrodon halys blomhoffii, through selective inhibition of factor IX
    • Sakurai, Y., Shima, M., Matsumoto, T., Takatsuka, H., Nishiya, K., Kasuda, S., Fujimura, Y., Yoshioka, A. (2003). Anticoagulant activity of M-LAO, L-amino acid oxidase purified from Agkistrodon halys blomhoffii, through selective inhibition of factor IX. Biochim. Biophys. Acta 1649(1):51-57.
    • (2003) Biochim. Biophys. Acta , vol.1649 , Issue.1 , pp. 51-57
    • Sakurai, Y.1    Shima, M.2    Matsumoto, T.3    Takatsuka, H.4    Nishiya, K.5    Kasuda, S.6    Fujimura, Y.7    Yoshioka, A.8
  • 58
    • 0027185530 scopus 로고
    • Isolation and characterization of an anticoagulant protein homologous to botrocetin from the venom of Bothrops jararaca
    • Sekiya, F., Atoda, H., Morita, T. (1993). Isolation and characterization of an anticoagulant protein homologous to botrocetin from the venom of Bothrops jararaca. Biochemistry 32(27):6892-6897.
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 6892-6897
    • Sekiya, F.1    Atoda, H.2    Morita, T.3
  • 59
    • 0029128896 scopus 로고
    • Role of calcium(II) ions in the recognition of coagulation factors IX and X by IX/X-bp, an anticoagulant from snake venom
    • Sekiya, F., Yamashita, T., Morita, T. (1995). Role of calcium(II) ions in the recognition of coagulation factors IX and X by IX/X-bp, an anticoagulant from snake venom. Biochemistry 34(31):10043-10047.
    • (1995) Biochemistry , vol.34 , Issue.31 , pp. 10043-10047
    • Sekiya, F.1    Yamashita, T.2    Morita, T.3
  • 60
    • 0028332939 scopus 로고
    • Molecular mapping of the heparin-binding exosite of thrombin
    • Sheehan, J. P., Sadler, J. E. (1994). Molecular mapping of the heparin-binding exosite of thrombin. Proc. Natl. Acad. Sci. USA 91(12):5518-5522.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.12 , pp. 5518-5522
    • Sheehan, J.P.1    Sadler, J.E.2
  • 61
    • 33646356275 scopus 로고
    • Isolation of coagulant and anticoagulant principles from the venom of Trimeresurus gramineus
    • Shiau, S. Y., Ouyang C. (1965). Isolation of coagulant and anticoagulant principles from the venom of Trimeresurus gramineus. Toxicon 69:213-220.
    • (1965) Toxicon , vol.69 , pp. 213-220
    • Shiau, S.Y.1    Ouyang, C.2
  • 63
    • 0034102778 scopus 로고    scopus 로고
    • Determination of the three-dimensional structure of toxins by protein crystallography
    • Souza, D. H. F., Selistre de Araujo, H. S., Garratt R. C. (2000). Determination of the three-dimensional structure of toxins by protein crystallography. Toxicon 38(10):1307-1353.
    • (2000) Toxicon , vol.38 , Issue.10 , pp. 1307-1353
    • Souza, D.H.F.1    Selistre de Araujo, H.S.2    Garratt, R.C.3
  • 65
    • 0025196592 scopus 로고
    • 2 from Naja nigicollis venom inhibits the prothrombinase complex by a novel nonenzymatic mechanism
    • 2 from Naja nigicollis venom inhibits the prothrombinase complex by a novel nonenzymatic mechanism. Biochemistry 29(33):7742-7746.
    • (1990) Biochemistry , vol.29 , Issue.33 , pp. 7742-7746
    • Stefansson, S.1    Kini, R.M.2    Evans, H.J.3
  • 66
    • 0003988350 scopus 로고
    • Stocker, K. F, ed, Boca Raton, FL: CRC Press
    • Stocker, K. F., ed. (1990). Medical Use of Snake Venom Proteins. Boca Raton, FL: CRC Press.
    • (1990) Medical Use of Snake Venom Proteins
  • 67
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs, M. T., Bode, W. (1993). A player of many parts: the spotlight falls on thrombin's structure. Thromb. Res. 69(1):1-58.
    • (1993) Thromb. Res , vol.69 , Issue.1 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 68
    • 0030610957 scopus 로고    scopus 로고
    • Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects
    • Subburaju, S., Kini, R. M. (1997). Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects .Toxicon 35(8):1239-1250.
    • (1997) Toxicon , vol.35 , Issue.8 , pp. 1239-1250
    • Subburaju, S.1    Kini, R.M.2
  • 69
    • 0036238874 scopus 로고    scopus 로고
    • Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon acutus venom
    • Tani, A., Ogawa, T., Nose, T., Nikandrov, N. N., Deshimaru, M., Chijiwa, T., Chang, C. C., Fukumaki, Y., Ohno, M. (2002). Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon acutus venom. Toxicon 40(6):803-813.
    • (2002) Toxicon , vol.40 , Issue.6 , pp. 803-813
    • Tani, A.1    Ogawa, T.2    Nose, T.3    Nikandrov, N.N.4    Deshimaru, M.5    Chijiwa, T.6    Chang, C.C.7    Fukumaki, Y.8    Ohno, M.9
  • 70
    • 0027507459 scopus 로고
    • Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca
    • Usami, Y., Fujimura, Y., Suzuki, M., Ozeki, Y., Nishio, K., Fukui, H., Titani, K. (1993). Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca. Proc. Natl. Acad. Sci. USA. 90(3):928-932.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.3 , pp. 928-932
    • Usami, Y.1    Fujimura, Y.2    Suzuki, M.3    Ozeki, Y.4    Nishio, K.5    Fukui, H.6    Titani, K.7
  • 71
    • 0033535986 scopus 로고    scopus 로고
    • Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): Synergistic and non-covalent interactions between its subunits
    • Wang, R., Kini, R. M., Chung, M. C. (1999). Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and non-covalent interactions between its subunits. Biochemistry 38(23):7584-7593.
    • (1999) Biochemistry , vol.38 , Issue.23 , pp. 7584-7593
    • Wang, R.1    Kini, R.M.2    Chung, M.C.3
  • 72
    • 0028023796 scopus 로고
    • Activation-induced exposure of the thrombin anion-binding exosite
    • Wu, Q., Picard, V., Aiach, M., Sadler, J. E. (1994). Activation-induced exposure of the thrombin anion-binding exosite. J. Biol. Chem. 269(5):3725-3730.
    • (1994) J. Biol. Chem , vol.269 , Issue.5 , pp. 3725-3730
    • Wu, Q.1    Picard, V.2    Aiach, M.3    Sadler, J.E.4
  • 73
    • 0033178496 scopus 로고    scopus 로고
    • Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri
    • Xu, Q., Wu, X. F., Xia, Q. C., Wang, K. Y. (1999). Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri. Biochem. J. 341(Pt 3):733-737.
    • (1999) Biochem. J , vol.341 , Issue.PART 3 , pp. 733-737
    • Xu, Q.1    Wu, X.F.2    Xia, Q.C.3    Wang, K.Y.4
  • 74
    • 0034335353 scopus 로고    scopus 로고
    • Purification and characterization of anticoagulation factors from the venom of Agkistrodon acutus
    • Xu, X., Liu, Q., Xie, Y., Wu, S. D. (2000). Purification and characterization of anticoagulation factors from the venom of Agkistrodon acutus. Toxicon 38(11):1517-1528.
    • (2000) Toxicon , vol.38 , Issue.11 , pp. 1517-1528
    • Xu, X.1    Liu, Q.2    Xie, Y.3    Wu, S.D.4
  • 75
    • 0036209197 scopus 로고    scopus 로고
    • Terbium(III) fluorescence probe studies on metal ion-binding sites in anticoagulation factor I from Agkistrodon acutus venom
    • Xu, X., Liu, Q., Liu, Y., Xie, Y. (2002a). Terbium(III) fluorescence probe studies on metal ion-binding sites in anticoagulation factor I from Agkistrodon acutus venom. J. Protein. Chem. 21(2):123-129.
    • (2002) J. Protein. Chem , vol.21 , Issue.2 , pp. 123-129
    • Xu, X.1    Liu, Q.2    Liu, Y.3    Xie, Y.4
  • 76
    • 0036129121 scopus 로고    scopus 로고
    • Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus
    • Xu, X., Liu, Q., Yu, H., Xie, Y. (2002b). Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus. Protein Sci. 11(4):944-956.
    • (2002) Protein Sci , vol.11 , Issue.4 , pp. 944-956
    • Xu, X.1    Liu, Q.2    Yu, H.3    Xie, Y.4
  • 77
    • 0037133514 scopus 로고    scopus 로고
    • Metal ion-induced stabilization and refolding of anticoagulation factor II from the venom of Agkistrodon acutus
    • Xu, X., Liu, Q., Xie, Y. (2002c). Metal ion-induced stabilization and refolding of anticoagulation factor II from the venom of Agkistrodon acutus. Biochemistry 41(11):3546-3554.
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3546-3554
    • Xu, X.1    Liu, Q.2    Xie, Y.3
  • 78
    • 0037391215 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic analysis of AHP IX-bp, a zinc ion and pH-dependent coagulation factor IX binding protein from Agkistrodon halys pallas venom
    • Zang, J., Teng, M., Niu, L. (2003). Purification, crystallization and preliminary crystallographic analysis of AHP IX-bp, a zinc ion and pH-dependent coagulation factor IX binding protein from Agkistrodon halys pallas venom. Acta Crystallogr. D Biol. Crystallogr. 59(Pt 4):730-733.
    • (2003) Acta Crystallogr. D Biol. Crystallogr , vol.59 , Issue.PART 4 , pp. 730-733
    • Zang, J.1    Teng, M.2    Niu, L.3
  • 79
    • 0027490609 scopus 로고
    • Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: Characterization and mechanism of thrombin inhibition
    • Zingali, R. B., Jandrot-Perrus, M., Guillin, M. C., Bon, C. (1993). Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: characterization and mechanism of thrombin inhibition. Biochemistry 32(40):10794-10802.
    • (1993) Biochemistry , vol.32 , Issue.40 , pp. 10794-10802
    • Zingali, R.B.1    Jandrot-Perrus, M.2    Guillin, M.C.3    Bon, C.4
  • 80
    • 0035743555 scopus 로고    scopus 로고
    • Interaction of bothrojaracin with prothrombin
    • Zingali, R. B., Bianconi, M. L., Monteiro, R. Q. (2001). Interaction of bothrojaracin with prothrombin. Haemostasis 31(3-6):273-278.
    • (2001) Haemostasis , vol.31 , Issue.3-6 , pp. 273-278
    • Zingali, R.B.1    Bianconi, M.L.2    Monteiro, R.Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.