메뉴 건너뛰기




Volumn 4, Issue 4, 2004, Pages 301-325

Platelet aggregation and exogenous factors from animal sources

Author keywords

Antiplatelet drugs; C type lectins; Disintegrins; Fibrinogenase; Phospholipase A2; Platelet agglutination; Platelet aggregation inducers; Platelet aggregation inhibitors; Platelet glycoproteins; Platelet receptors; Thrombin like enzymes

Indexed keywords

AGKICETIN; ANTITHROMBOCYTIC AGENT; ARGININE; ASPARTIC ACID; BOTHROJARACIN; DECORSIN; DISAGREGIN; DISINTEGRIN; ECHICETIN; EPTIFIBATIDE; FIBRINOGEN; FIBRINOGEN RECEPTOR; FIBRINOGEN RECEPTOR ANTAGONIST; GLYCINE; LECTIN; MAMBIN; ORNATIN A2; ORNATIN A3; ORNATIN B; ORNATIN C; ORNATIN D; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 INHIBITOR; SAVIGNYGRIN; SERINE PROTEINASE; SNAKE VENOM; TRIPEPTIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VARIABILIN; VITRONECTIN RECEPTOR;

EID: 9544254847     PISSN: 15680061     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568006043335835     Document Type: Review
Times cited : (22)

References (315)
  • 1
    • 0024594947 scopus 로고
    • Platelet aggregation measured by the photometric method
    • Zucker, M. B. Platelet aggregation measured by the photometric method. Meth. Enzymol., 1989, 169, 117-133.
    • (1989) Meth. Enzymol. , vol.169 , pp. 117-133
    • Zucker, M.B.1
  • 2
    • 0019497464 scopus 로고
    • Present concepts on the mechanisms of platelet aggregation
    • Vargaftig, B. B., Chignard, M., Benveniste, J. Present concepts on the mechanisms of platelet aggregation. Biochem. Pharmacol., 1981, 30, 263-271.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 263-271
    • Vargaftig, B.B.1    Chignard, M.2    Benveniste, J.3
  • 4
    • 0022137588 scopus 로고
    • The platelet fibrinogen receptor
    • Peerschke, E. I. B. The platelet fibrinogen receptor. Semin. Hematol., 1985, 22, 241-259.
    • (1985) Semin. Hematol. , vol.22 , pp. 241-259
    • Peerschke, E.I.B.1
  • 7
    • 0022704534 scopus 로고
    • Platelet activation: Role of an ADP receptor
    • Colman, R. W. Platelet activation: role of an ADP receptor. Semin. Hematol., 1986, 23, 119-128.
    • (1986) Semin. Hematol. , vol.23 , pp. 119-128
    • Colman, R.W.1
  • 8
    • 0022600067 scopus 로고
    • Molecular mechanisms of platelet aggregation
    • Leung, L. and Nachman, R. Molecular mechanisms of platelet aggregation. Ann. Rev. Med., 1986, 37, 179-186.
    • (1986) Ann. Rev. Med. , vol.37 , pp. 179-186
    • Leung, L.1    Nachman, R.2
  • 9
    • 0022594320 scopus 로고
    • Von Willebrand factor and platelet function
    • Moroose, R., Hoyer, L. W. Von Willebrand factor and platelet function. Ann. Rev. Med., 1986, 37, 157-163.
    • (1986) Ann. Rev. Med. , vol.37 , pp. 157-163
    • Moroose, R.1    Hoyer, L.W.2
  • 12
    • 0023062783 scopus 로고
    • Platelet membrane components and receptors
    • Niewiarowski, S. Platelet membrane components and receptors. Hematologia, 1987, 20, 3-14.
    • (1987) Hematologia , vol.20 , pp. 3-14
    • Niewiarowski, S.1
  • 13
    • 38149143393 scopus 로고
    • Blood platelet shape change ABCs
    • Derenleau, D. A. Blood platelet shape change ABCs. Trends Biochem. Sci., 1987, 12, 439-442.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 439-442
    • Derenleau, D.A.1
  • 14
    • 0003816885 scopus 로고
    • Platelet Membrane Receptors: Molecular Biology, Immunology, Biochemistry, and Pathology. Alan R. Liss: New York
    • Jamieson, G. A. Progress in Clinical and Biological Research, Vol. 283, Platelet Membrane Receptors: Molecular Biology, Immunology, Biochemistry, and Pathology. Alan R. Liss: New York, 1988.
    • (1988) Progress in Clinical and Biological Research , vol.283
    • Jamieson, G.A.1
  • 15
    • 0024371853 scopus 로고
    • Platelet membrane glycoproteins and their function: An overview
    • Kunicki, T. J. Platelet membrane glycoproteins and their function: an overview. Blut, 1989, 59, 30-34.
    • (1989) Blut , vol.59 , pp. 30-34
    • Kunicki, T.J.1
  • 16
    • 0024462290 scopus 로고
    • Review article. Biochemical mechanisms of platelet activation
    • Kroll, M., Schafer, A. I. Review article. Biochemical mechanisms of platelet activation. Blood, 1989, 74, 1181-1195.
    • (1989) Blood , vol.74 , pp. 1181-1195
    • Kroll, M.1    Schafer, A.I.2
  • 17
    • 9544239168 scopus 로고
    • Phillips, D. R., Shuman, M. A., Eds.; Academic Press: Orlando, FL
    • Shuman, M. A., Greenberg, C. S. In Biochemistry of Platelets; Phillips, D. R., Shuman, M. A., Eds.; Academic Press: Orlando, FL, 1986; pp. 319-346.
    • (1986) Biochemistry of Platelets , pp. 319-346
    • Shuman, M.A.1    Greenberg, C.S.2
  • 18
    • 9544226239 scopus 로고
    • Holmsen, H., Ed.; CRC Press: Boca Raton, FL Responses
    • Tracy, P. B., Mann, K. G. In Platelet Responses and Metabolism; Holmsen, H., Ed.; CRC Press: Boca Raton, FL, 1986; Vol. I, Responses, pp. 297-324.
    • (1986) Platelet Responses and Metabolism , vol.1 , pp. 297-324
    • Tracy, P.B.1    Mann, K.G.2
  • 19
    • 0002312258 scopus 로고
    • Phillips, D. R., Shuman, M. A., Eds.; Academic Press: Orlando, FL 1986
    • Tracy, P. B., Mann, K. G. 1986b In Biochemistry of Platelets; Phillips, D. R., Shuman, M. A., Eds.; Academic Press: Orlando, FL, 1986; pp. 295-318.
    • (1986) Biochemistry of Platelets , pp. 295-318
    • Tracy, P.B.1    Mann, K.G.2
  • 20
    • 0024228907 scopus 로고
    • Jamieson, G. A., Ed.; Alan R. Liss: New York, Platelet Membrane Receptors: Molecular Biology, Immunology, Biochemistry, and Pathology
    • Ganz, P. R., Tackaberry, E. S., Rock, G. In Progress in Clinical and Biological Research; Jamieson, G. A., Ed.; Alan R. Liss: New York, 1988; Vol. 283, Platelet Membrane Receptors: Molecular Biology, Immunology, Biochemistry, and Pathology, pp. 255-261.
    • (1988) Progress in Clinical and Biological Research , vol.283 , pp. 255-261
    • Ganz, P.R.1    Tackaberry, E.S.2    Rock, G.3
  • 22
    • 0022586122 scopus 로고
    • The role of platelets in the development and complications of atherosclerosis
    • Packham, M. A., Mustard, J. F. The role of platelets in the development and complications of atherosclerosis. Semin. Hematol., 1986, 23, 8-26.
    • (1986) Semin. Hematol. , vol.23 , pp. 8-26
    • Packham, M.A.1    Mustard, J.F.2
  • 23
    • 0018890908 scopus 로고
    • Characterization of the platelet-aggregating activity of tumor cells
    • Hara, Y., Steiner, M., Baldini, M. G. Characterization of the platelet- aggregating activity of tumor cells. Cancer Res. 1980 40, 1217-1222.
    • (1980) Cancer Res. , vol.40 , pp. 1217-1222
    • Hara, Y.1    Steiner, M.2    Baldini, M.G.3
  • 24
    • 0022522964 scopus 로고
    • Characterization of the platelet-aggregating activity of cancer cells with different metastatic potential
    • Grignani, G., Pacchiarini, L., Almasio, P., Pagliarino, M., Gamba, G., Rizzo, S. C., Ascari, E. Characterization of the platelet-aggregating activity of cancer cells with different metastatic potential. Eur. J. Cancer, 1986, 38, 237-244.
    • (1986) Eur. J. Cancer , vol.38 , pp. 237-244
    • Grignani, G.1    Pacchiarini, L.2    Almasio, P.3    Pagliarino, M.4    Gamba, G.5    Rizzo, S.C.6    Ascari, E.7
  • 25
    • 0020631722 scopus 로고
    • A new mechanism for tumor-induced platelet aggregation. Comparison with mechanisms shared by other tumors with possible pharmacologic strategy toward prevention of metastases
    • Lerner, W. A., Pearlstein, E., Ambrogio, C., Karpatkin, S. A new mechanism for tumor-induced platelet aggregation. Comparison with mechanisms shared by other tumors with possible pharmacologic strategy toward prevention of metastases. Eur. J. Cancer, 1983, 31 463-469.
    • (1983) Eur. J. Cancer , vol.31 , pp. 463-469
    • Lerner, W.A.1    Pearlstein, E.2    Ambrogio, C.3    Karpatkin, S.4
  • 27
    • 0023195437 scopus 로고
    • Platelet aggregating activity mediated by thrombin generation in the NCG human neuroblastoma cell line
    • Esumi, N., Todo, S., Imashuku, S. Platelet aggregating activity mediated by thrombin generation in the NCG human neuroblastoma cell line. Cancer Res., 1987, 47, 2129-2135.
    • (1987) Cancer Res. , vol.47 , pp. 2129-2135
    • Esumi, N.1    Todo, S.2    Imashuku, S.3
  • 28
    • 0023270485 scopus 로고
    • Tumor-cell-induced platelet aggregation is a glycoprotein-dependent and lipooxygenase-associated process
    • Bastida, E., Almirall, L., Ordinas, A. Tumor-cell-induced platelet aggregation is a glycoprotein-dependent and lipooxygenase-associated process. Int. J. Cancer, 1987, 39 760-763.
    • (1987) Int. J. Cancer , vol.39 , pp. 760-763
    • Bastida, E.1    Almirall, L.2    Ordinas, A.3
  • 29
    • 0024345543 scopus 로고
    • Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation
    • Sakai, T., Lund-Hansen, T., Paborsky, L., Pedersen, A. H., Kisiel, W. Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation. J. Biol. Chem., 1989, 264, 9980-9988.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9980-9988
    • Sakai, T.1    Lund-Hansen, T.2    Paborsky, L.3    Pedersen, A.H.4    Kisiel, W.5
  • 30
    • 0017139411 scopus 로고
    • Anticoagulants in the treatment of cancer
    • Hilgard, P., Thornes, R. D. Anticoagulants in the treatment of cancer. Eur. J. Cancer, 1976, 12, 755-762.
    • (1976) Eur. J. Cancer , vol.12 , pp. 755-762
    • Hilgard, P.1    Thornes, R.D.2
  • 31
    • 0019820999 scopus 로고
    • Role of platelets in tumor cell metastases
    • Karpatkin, S., Pearlstein, E. Role of platelets in tumor cell metastases. Ann. Inter. Med., 1981, 95, 636-641.
    • (1981) Ann. Inter. Med. , vol.95 , pp. 636-641
    • Karpatkin, S.1    Pearlstein, E.2
  • 32
    • 0019940957 scopus 로고
    • Platelet aggregation inhibitors and cancer
    • Gastpar, H. Platelet aggregation inhibitors and cancer. Ann. Chir. Gynaec., 1982, 71, 142-150.
    • (1982) Ann. Chir. Gynaec. , vol.71 , pp. 142-150
    • Gastpar, H.1
  • 33
    • 0020961939 scopus 로고
    • Activation of blood coagulation in cancer: Trousseau's syndrome revisited
    • Rickles, F. R., Edwards, R. L. Activation of blood coagulation in cancer: Trousseau's syndrome revisited. Blood, 1983, 62, 14-31.
    • (1983) Blood , vol.62 , pp. 14-31
    • Rickles, F.R.1    Edwards, R.L.2
  • 34
    • 0023508475 scopus 로고
    • H. Fibrinogen, fibrinogen receptors, and the peptides that inhibit these interactions
    • Plow, E. F., Marguerie, G., Ginsberg, M. H, Fibrinogen, fibrinogen receptors, and the peptides that inhibit these interactions. Biochem. Pharmac., 1987, 36, 4035-4040.
    • (1987) Biochem. Pharmac. , vol.36 , pp. 4035-4040
    • Plow, E.F.1    Marguerie, G.2    Ginsberg, M.3
  • 35
    • 0023604572 scopus 로고
    • Thrombospondin: A modular adhesive glycoprotein of platelets and nucleated cells
    • Frazier, W, A. Thrombospondin: a modular adhesive glycoprotein of platelets and nucleated cells. J. Cell Biol., 1987, 105, 625-632.
    • (1987) J. Cell Biol. , vol.105 , pp. 625-632
    • Frazier, W.A.1
  • 36
    • 0005795408 scopus 로고
    • Immunologic relationship between platelet membrane glycoprotein GP IIb/IIIa and cell surface molecules expressed by a variety of cells
    • Plow, E. F., Loftus, J. C., Levin, E. G., Fair, D. S., Dixon, D., Forsyth, J., Ginsberg, M. H. Immunologic relationship between platelet membrane glycoprotein GP IIb/IIIa and cell surface molecules expressed by a variety of cells. Proc. Natl. Acad. Sci. U. S. A., 1986, 83, 6002-6006.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6002-6006
    • Plow, E.F.1    Loftus, J.C.2    Levin, E.G.3    Fair, D.S.4    Dixon, D.5    Forsyth, J.6    Ginsberg, M.H.7
  • 37
    • 1842284730 scopus 로고
    • Platelet glycoproteins IIb and IIIa: Evidence for a family of immunologically and structurally related glycoproteins in mammalian cells
    • Charo, I. F., Fitzgerald, L. A., Steiner, B., Rall, Jr. S. C., Bekeart, L. S., Phillips, D. R. Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells. Proc. Natl. Acad. Sci. U S. A., 1986, 83, 8351-8355.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8351-8355
    • Charo, I.F.1    Fitzgerald, L.A.2    Steiner, B.3    Rall Jr., S.C.4    Bekeart, L.S.5    Phillips, D.R.6
  • 38
    • 0028202201 scopus 로고
    • Inventory of exogenous factors affecting platelet aggregation isolated from plant sources
    • Teng, C. M., Ko, F. N., Yu, S. M. Inventory of exogenous factors affecting platelet aggregation isolated from plant sources. Thromb. Haemost., 1994, 71, 517-519.
    • (1994) Thromb. Haemost. , vol.71 , pp. 517-519
    • Teng, C.M.1    Ko, F.N.2    Yu, S.M.3
  • 39
    • 0032428124 scopus 로고    scopus 로고
    • Antiplatelet agents isolated from medicinal plants
    • Teng, C. M., Ko, F. N. Antiplatelet agents isolated from medicinal plants. Res. Commun. Mol. Pathol. Pharmacol., 1998, 102, 211-225.
    • (1998) Res. Commun. Mol. Pathol. Pharmacol. , vol.102 , pp. 211-225
    • Teng, C.M.1    Ko, F.N.2
  • 40
    • 0025741002 scopus 로고
    • Inventory of exogenous platelet-aggregating agents derived from venoms
    • Smith, S. C., Brinkhous, K. M. Inventory of exogenous platelet-aggregating agents derived from venoms. Thromb. Haemost., 1991, 66, 259-263.
    • (1991) Thromb. Haemost. , vol.66 , pp. 259-263
    • Smith, S.C.1    Brinkhous, K.M.2
  • 41
    • 0031932317 scopus 로고    scopus 로고
    • Thrombin-like enzymes from snake venoms: An updated inventory
    • Pirkle, H. Thrombin-like enzymes from snake venoms: an updated inventory. Thromb. Haemost., 1998, 79, 675-683.
    • (1998) Thromb. Haemost. , vol.79 , pp. 675-683
    • Pirkle, H.1
  • 42
    • 0023911738 scopus 로고
    • Comparison of the platelet aggregation induced by three thrombin-like enzymes of snake venoms and thrombin
    • Teng, C. M., Ko, F. N. Comparison of the platelet aggregation induced by three thrombin-like enzymes of snake venoms and thrombin. Thromb. Haemost., 1988, 59, 304-309.
    • (1988) Thromb. Haemost. , vol.59 , pp. 304-309
    • Teng, C.M.1    Ko, F.N.2
  • 44
    • 0025093043 scopus 로고
    • Effect of cerastobin, a thrombin-like enzyme from Cerastes vipera (Egyptian sand snake) venom, on human platelets
    • Farid, T. M., Tu, A. T., El Asmar, M. F. Effect of cerastobin, a thrombin-like enzyme from Cerastes vipera (Egyptian sand snake) venom, on human platelets. Haemostasis, 1990, 20, 296-304.
    • (1990) Haemostasis , vol.20 , pp. 296-304
    • Farid, T.M.1    Tu, A.T.2    El Asmar, M.F.3
  • 45
    • 0029060817 scopus 로고
    • Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes
    • Marrakchi, N., Zingali, R. B., Karoui, H., Bon, C., El Ayeb, M. Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes. Biochim. Biophys. Acta, 1995, 1244, 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
  • 46
    • 0030857042 scopus 로고    scopus 로고
    • Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties
    • Marrakchi, N., Barbouche, R., Guermazi, S., Karoui, H., Bon, C., El Ayeb, M. Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties. Eur. J. Biochem., 1997, 247, 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
  • 47
    • 0029058747 scopus 로고
    • Characterization of a potent platelet aggregation inducer from Cerastes cerastes (Egyptian sand viper) venom
    • Basheer, A. R., El Asmar, M. F., Soslau, G. Characterization of a potent platelet aggregation inducer from Cerastes cerastes (Egyptian sand viper) venom. Biochim. Biophys. Acta, 1995, 1250, 97-109.
    • (1995) Biochim. Biophys. Acta , vol.1250 , pp. 97-109
    • Basheer, A.R.1    El Asmar, M.F.2    Soslau, G.3
  • 48
    • 0028973481 scopus 로고
    • Afaâcytin, an αβ-fibrinogenase from Cerastes cerastes (horned viper) venom, activates purified factor X and induces serotonin release from human blood platelets
    • Djebari, L. F., Martin Eauclaire, M. F., Mauco, G., Marchot, P. Afaâcytin, an αβ-fibrinogenase from Cerastes cerastes (horned viper) venom, activates purified factor X and induces serotonin release from human blood platelets. Eur. J. Biochem., 1995, 233, 756-765.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 756-765
    • Djebari, L.F.1    Martin Eauclaire, M.F.2    Mauco, G.3    Marchot, P.4
  • 49
    • 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
    • Serrano, S, M., Matos, M. F., Mandelbaum, F. R., Sampaio, C. A. 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, 1993 31, 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
  • 50
    • 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
    • Serrano, S. M., Mentele, R., Sampaio, C. A., Fink, E. Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca. Biochemistry, 1995, 34, 7186-7193.
    • (1995) Biochemistry , vol.34 , pp. 7186-7193
    • Serrano, S.M.1    Mentele, R.2    Sampaio, C.A.3    Fink, E.4
  • 51
    • 0018749203 scopus 로고
    • The action mechanism of the purified platelet aggregation principle of Trimeresurus mucrosquamatus venom
    • Ouyang, C., Teng, C. M. The action mechanism of the purified platelet aggregation principle of Trimeresurus mucrosquamatus venom. Thromb. Haemost., 1979, 41, 475-490.
    • (1979) Thromb. Haemost. , vol.41 , pp. 475-490
    • Ouyang, C.1    Teng, C.M.2
  • 53
    • 0021200644 scopus 로고
    • 2 from snake and bee venoms on rabbit platelet function
    • 2 from snake and bee venoms on rabbit platelet function. Toxicon, 1984, 22, 705-718.
    • (1984) Toxicon , vol.22 , pp. 705-718
    • Ouyang, C.1    Huang, T.F.2
  • 54
    • 0021214397 scopus 로고
    • Biphasic effect on platelet aggregation by phospholipase a purified from Vipera russelli snake venom
    • Teng, C. M., Chen, Y. H., Ouyang, C. Biphasic effect on platelet aggregation by phospholipase a purified from Vipera russelli snake venom. Biochim. Biophys. Acta, 1984, 772, 393-402.
    • (1984) Biochim. Biophys. Acta , vol.772 , pp. 393-402
    • Teng, C.M.1    Chen, Y.H.2    Ouyang, C.3
  • 55
    • 0022381202 scopus 로고
    • Effect of Russell's viper venom phospholipase A on blood coagulation and platelet aggregation
    • Teng, C. M., Chen, Y. H., Ouyang, C. H. Effect of Russell's viper venom phospholipase A on blood coagulation and platelet aggregation. Semin. Thromb. Hemost., 1985, 11, 367-372.
    • (1985) Semin. Thromb. Hemost. , vol.11 , pp. 367-372
    • Teng, C.M.1    Chen, Y.H.2    Ouyang, C.H.3
  • 56
    • 0022903196 scopus 로고
    • 2 on platelet aggregation in comparison with those produced by arachidonic acid and lysophosphatidylcholine
    • 2 on platelet aggregation in comparison with those produced by arachidonic acid and lysophosphatidylcholine. Thromb. Res., 1986, 44, 875-886.
    • (1986) Thromb. Res. , vol.44 , pp. 875-886
    • Teng, C.M.1    Kuo, Y.P.2    Lee, L.G.3    Ouyang, C.4
  • 57
    • 0024371625 scopus 로고
    • 2 from the venom of Agkistrodon acutus (five pace snake) and its effect on platelet aggregation
    • 2 from the venom of Agkistrodon acutus (five pace snake) and its effect on platelet aggregation. Toxicon, 1989, 27, 675-682.
    • (1989) Toxicon , vol.27 , pp. 675-682
    • Chen, R.H.1    Chen, Y.C.2
  • 60
    • 0019174452 scopus 로고
    • Thrombolectin: A lectin isolated from Bothrops atrox venom
    • Gartner, T. K., Stocker, K., Williams, D. C. Thrombolectin: a lectin isolated from Bothrops atrox venom. FEBS Lett., 1980, 117, 13-16.
    • (1980) FEBS Lett. , vol.117 , pp. 13-16
    • Gartner, T.K.1    Stocker, K.2    Williams, D.C.3
  • 61
    • 0021646758 scopus 로고
    • 2+-dependent β-galactoside-specific lectins from snake venoms
    • 2+-dependent β-galactoside-specific lectins from snake venoms. Biochem. J., 1984, 224, 301-307.
    • (1984) Biochem. J. , vol.224 , pp. 301-307
    • Gartner, T.K.1    Ogilvie, M.L.2
  • 62
    • 0023014079 scopus 로고
    • Isolation and characterization of lactose-binding lectins from the venoms of the snakes Lachesis muta and Dendroaspis jamesonii
    • Ogilvie, M. L., Dockter, M. E., Wenz, L., Gartner, T. K. Isolation and characterization of lactose-binding lectins from the venoms of the snakes Lachesis muta and Dendroaspis jamesonii. J. Biochem. (Tokyo), 1986, 100, 1425-1431.
    • (1986) J. Biochem. (Tokyo) , vol.100 , pp. 1425-1431
    • Ogilvie, M.L.1    Dockter, M.E.2    Wenz, L.3    Gartner, T.K.4
  • 63
    • 0024450761 scopus 로고
    • Platelet-aggregation is stimulated by lactose-inhibitable snake venom lectins
    • Ogilvie, M. L., Byl, J. W., Gartner, T. K. Platelet-aggregation is stimulated by lactose-inhibitable snake venom lectins. Thromb. Haemost., 1989, 62, 704-707.
    • (1989) Thromb. Haemost. , vol.62 , pp. 704-707
    • Ogilvie, M.L.1    Byl, J.W.2    Gartner, T.K.3
  • 64
    • 0019124971 scopus 로고
    • Activation of guinea-pig platelets induced by convulxin, a substance extracted from the venom of Crotalus durissus cascavella
    • Vargaftig, B. B., Prado-Franceschi, J., Chignard, M., Lefort, J., Marlas, G. Activation of guinea-pig platelets induced by convulxin, a substance extracted from the venom of Crotalus durissus cascavella. Eur. J. Pharmacol., 1980, 68, 451-464.
    • (1980) Eur. J. Pharmacol. , vol.68 , pp. 451-464
    • Vargaftig, B.B.1    Prado-Franceschi, J.2    Chignard, M.3    Lefort, J.4    Marlas, G.5
  • 65
    • 0020566873 scopus 로고
    • Convulxin-induced activation of intact and of thrombin-degranulated rabbit platelets: Specific crossed desensitisation with collagen
    • Vargaftig, B. B., Joseph, D., Wal, F., Marlas, G., Chignard, M., Chevance, L. G. Convulxin-induced activation of intact and of thrombin-degranulated rabbit platelets: specific crossed desensitisation with collagen. Eur. J. Pharmacol., 1983, 92, 57-68.
    • (1983) Eur. J. Pharmacol. , vol.92 , pp. 57-68
    • Vargaftig, B.B.1    Joseph, D.2    Wal, F.3    Marlas, G.4    Chignard, M.5    Chevance, L.G.6
  • 66
    • 0019811115 scopus 로고
    • Effects of convulxin, a toxin from rattlesnake venom, on platelets and leukocytes of anesthetized rabbits
    • Prado-Franceschi, J., Tavares, D. Q., Hertel, R., Lobo de Araujo, A. Effects of convulxin, a toxin from rattlesnake venom, on platelets and leukocytes of anesthetized rabbits. Toxicon, 1981 19, 661-666.
    • (1981) Toxicon , vol.19 , pp. 661-666
    • Prado-Franceschi, J.1    Tavares, D.Q.2    Hertel, R.3    Lobo de Araujo, A.4
  • 67
    • 0020048375 scopus 로고
    • Purification and preliminary structure of a potent platelet aggregating glycoprotein isolated from the venom of Crotalus durissus cascavella
    • Marlas, G. Purification and preliminary structure of a potent platelet aggregating glycoprotein isolated from the venom of Crotalus durissus cascavella. Toxicon, 1982, 20, 289-290.
    • (1982) Toxicon , vol.20 , pp. 289-290
    • Marlas, G.1
  • 68
    • 0021069223 scopus 로고
    • Isolation and electron microscope studies of a potent platelet-aggregating glycoprotein from the venom of Crotalus durissus cascavella
    • Marlas, G., Joseph, D., Huet, C. I. Isolation and electron microscope studies of a potent platelet-aggregating glycoprotein from the venom of Crotalus durissus cascavella. Biochimie, 1983, 65 405-416.
    • (1983) Biochimie , vol.65 , pp. 405-416
    • Marlas, G.1    Joseph, D.2    Huet, C.I.3
  • 69
    • 0020854737 scopus 로고
    • Subunit structure of a potent platelet-activating glycoprotein isolated from the venom of Crotalus durissus cascavella
    • Marlas, G., Joseph, D., Huet, C. Subunit structure of a potent platelet-activating glycoprotein isolated from the venom of Crotalus durissus cascavella. Biochimie, 1983, 65, 619-628.
    • (1983) Biochimie , vol.65 , pp. 619-628
    • Marlas, G.1    Joseph, D.2    Huet, C.3
  • 70
    • 0028057308 scopus 로고
    • Convulxin-induced platelet aggregation is accompanied by a powerful activation of the phospholipase C pathway
    • Faili, A., Randon, J., Francischetti, I. M., Vargaftig, B. B., Hatmi, M. Convulxin-induced platelet aggregation is accompanied by a powerful activation of the phospholipase C pathway. Biochem. J., 1994, 298, 87-91.
    • (1994) Biochem. J. , vol.298 , pp. 87-91
    • Faili, A.1    Randon, J.2    Francischetti, I.M.3    Vargaftig, B.B.4    Hatmi, M.5
  • 71
    • 0030801096 scopus 로고    scopus 로고
    • Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets
    • Francischetti, I. M., Saliou, B., Leduc, M., Carlini, C. R., Hatmi, M., Randon, J., Faili, A., Bon, C. Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets. Toxicon, 1997, 35 1217-1228.
    • (1997) Toxicon , vol.35 , pp. 1217-1228
    • Francischetti, I.M.1    Saliou, B.2    Leduc, M.3    Carlini, C.R.4    Hatmi, M.5    Randon, J.6    Faili, A.7    Bon, C.8
  • 73
    • 0023011625 scopus 로고
    • Purification and characterization of a platelet aggregation inducer from Calloselasma rhodostoma (Malayan pit viper) snake venom
    • Ouyang, C., Yeh, H. I., Huang, T. F. Purification and characterization of a platelet aggregation inducer from Calloselasma rhodostoma (Malayan pit viper) snake venom. Toxicon, 1986, 24, 633-643.
    • (1986) Toxicon , vol.24 , pp. 633-643
    • Ouyang, C.1    Yeh, H.I.2    Huang, T.F.3
  • 74
    • 0029111991 scopus 로고
    • Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma rhodostoma) venom, activates phospholipase C by acting as a glycoprotein Ia/IIa agonist
    • Huang, T. F., Liu, C. Z., Yang, S. H. Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma rhodostoma) venom, activates phospholipase C by acting as a glycoprotein Ia/IIa agonist. Biochem. J., 1995, 309, 1021-1027.
    • (1995) Biochem. J. , vol.309 , pp. 1021-1027
    • Huang, T.F.1    Liu, C.Z.2    Yang, S.H.3
  • 75
    • 0032576958 scopus 로고    scopus 로고
    • Rhodocytin, a functional novel platelet agonist belonging to the heterodimeric C-type lectin family, induces platelet aggregation independently of glycoprotein Ib
    • Shin, Y., Morita, T. Rhodocytin, a functional novel platelet agonist belonging to the heterodimeric C-type lectin family, induces platelet aggregation independently of glycoprotein Ib. Biochem. Biophys. Res. Commun., 1998, 245, 741-745.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 741-745
    • Shin, Y.1    Morita, T.2
  • 76
    • 0033525708 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by glycoprotein Ia/IIa in human platelets: Comparison with those of glycoprotein VI
    • Inoue, K., Ozaki, Y., Satoh, K., Wu, Y., Yatomi, Y., Shin, Y., Morita, T. Signal transduction pathways mediated by glycoprotein Ia/IIa in human platelets: comparison with those of glycoprotein VI. Biochem. Biophys. Res. Commun., 1999, 256, 114-120.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 114-120
    • Inoue, K.1    Ozaki, Y.2    Satoh, K.3    Wu, Y.4    Yatomi, Y.5    Shin, Y.6    Morita, T.7
  • 77
    • 0018926610 scopus 로고
    • A potent platelet aggregation inducer purified from Trimeresurus mucrosquamatus snake venom
    • Ouyang, C., Wang, J. P., Teng, C. M. A potent platelet aggregation inducer purified from Trimeresurus mucrosquamatus snake venom. Biochim. Biophys. Acta, 1980, 630, 246-253.
    • (1980) Biochim. Biophys. Acta , vol.630 , pp. 246-253
    • Ouyang, C.1    Wang, J.P.2    Teng, C.M.3
  • 78
    • 0019460966 scopus 로고
    • Ultrastructure changes and release reaction of platelets induced by an aggregation inducer purified from Trimeresurus mucrosquamatus (Formosan habu) snake venom
    • Teng, C. M., Liao, K. K., Wang, J. P., Lin, H. S., Ouyang, C. Ultrastructure changes and release reaction of platelets induced by an aggregation inducer purified from Trimeresurus mucrosquamatus (Formosan habu) snake venom. Toxicon, 1981, 19, 121-130.
    • (1981) Toxicon , vol.19 , pp. 121-130
    • Teng, C.M.1    Liao, K.K.2    Wang, J.P.3    Lin, H.S.4    Ouyang, C.5
  • 79
    • 0027534716 scopus 로고
    • Trimucytin: A collagen-like aggregating inducer isolated from Trimeresurus mucrosquamatus snake venom
    • Teng, C. M., Ko, F. N., Tsai, I. H., Hung, M. L., Huang, T. F. Trimucytin: A collagen-like aggregating inducer isolated from Trimeresurus mucrosquamatus snake venom. Thromb. Haemost., 1993, 69, 286-292.
    • (1993) Thromb. Haemost. , vol.69 , pp. 286-292
    • Teng, C.M.1    Ko, F.N.2    Tsai, I.H.3    Hung, M.L.4    Huang, T.F.5
  • 80
    • 0004162857 scopus 로고
    • Activation of human platelets induced by the aggregoserpentin of Trimeresurus mucrosquamatus venom (TMVA)
    • Pirkle, H., Markland, F. S, Jr., Eds.; Marcel Dekker: New York
    • Chen, J. H., Wan, H., Ruan, C. Activation of human platelets induced by the aggregoserpentin of Trimeresurus mucrosquamatus venom (TMVA). In Hemostasis and Animal Venoms; Pirkle, H., Markland, F. S, Jr., Eds.; Marcel Dekker: New York, 1988; pp. 411-421.
    • (1988) Hemostasis and Animal Venoms , pp. 411-421
    • Chen, J.H.1    Wan, H.2    Ruan, C.3
  • 81
    • 0021023778 scopus 로고
    • A potent platelet aggregation inducer from Trimeresurus gramineus snake venom
    • Ouyang, C., Huang, T. F. A potent platelet aggregation inducer from Trimeresurus gramineus snake venom. Biochim. Biophys. Acta, 1983, 761, 126-134.
    • (1983) Biochim. Biophys. Acta , vol.761 , pp. 126-134
    • Ouyang, C.1    Huang, T.F.2
  • 82
    • 0024447287 scopus 로고
    • Triwaglerin: A potent platelet aggregation inducer purified from Trimeresurus wagleri snake venom
    • Teng, C. M., Hung, M. L., Huang, T. F., Ouyang, C. Triwaglerin: a potent platelet aggregation inducer purified from Trimeresurus wagleri snake venom. Biochim. Biophys. Acta, 1989, 992, 258-264.
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 258-264
    • Teng, C.M.1    Hung, M.L.2    Huang, T.F.3    Ouyang, C.4
  • 83
    • 0024208210 scopus 로고
    • Platelet aggregation induced by equinatoxin
    • Teng, C. M., Lee, L. G., Lee, C. Y., Ferlan, I. Platelet aggregation induced by equinatoxin. Thromb. Res., 1988, 52 401-411.
    • (1988) Thromb. Res. , vol.52 , pp. 401-411
    • Teng, C.M.1    Lee, L.G.2    Lee, C.Y.3    Ferlan, I.4
  • 84
    • 0031805437 scopus 로고    scopus 로고
    • The cDNA cloning and molecular characterization of a snake venom platelet glycoprotein lb-binding protein, mamushigin, from Agkistrodon halys blomhoffii venom
    • Sakurai, Y., Fujimura, Y., Kokubo, T., Imamura, K., Kawasaki, T., Handa, M., Suzuki, M., Matsui, T., Titani, K., Yoshioka, A. The cDNA cloning and molecular characterization of a snake venom platelet glycoprotein lb-binding protein, mamushigin, from Agkistrodon halys blomhoffii venom. Thromb. Haemost., 1998, 79, 1199-1207.
    • (1998) Thromb. Haemost. , vol.79 , pp. 1199-1207
    • Sakurai, Y.1    Fujimura, Y.2    Kokubo, T.3    Imamura, K.4    Kawasaki, T.5    Handa, M.6    Suzuki, M.7    Matsui, T.8    Titani, K.9    Yoshioka, A.10
  • 85
    • 0026328887 scopus 로고
    • Alboaggregin-B: A new platelet agonist that binds to platelet membrane glycoprotein Ib
    • Peng, M., Lu, W., Kirby, E. P. Alboaggregin-B: a new platelet agonist that binds to platelet membrane glycoprotein Ib. Biochemistry 1991, 30, 11529-11536.
    • (1991) Biochemistry , vol.30 , pp. 11529-11536
    • Peng, M.1    Lu, W.2    Kirby, E.P.3
  • 86
    • 0026723481 scopus 로고
    • Characterization of three alboaggregins purified from Trimeresurus albolabris venom
    • Peng, M., Lu, W., Kirby, E. P. Characterization of three alboaggregins purified from Trimeresurus albolabris venom. Thromb. Haemost., 1992, 67, 702-707.
    • (1992) Thromb. Haemost. , vol.67 , pp. 702-707
    • Peng, M.1    Lu, W.2    Kirby, E.P.3
  • 88
    • 0027212250 scopus 로고
    • Echicetin: A snake venom protein that inhibits binding of von Willebrand factor and alboaggregins to platelet glycoprotein Ib
    • Peng, M., Lu, W., Beviglia, L., Niewiarowski, S., Kirby, E. P. Echicetin: a snake venom protein that inhibits binding of von Willebrand factor and alboaggregins to platelet glycoprotein Ib. Blood 1993, 81, 2321-2328.
    • (1993) Blood , vol.81 , pp. 2321-2328
    • Peng, M.1    Lu, W.2    Beviglia, L.3    Niewiarowski, S.4    Kirby, E.P.5
  • 89
    • 0029004231 scopus 로고
    • Functional and sequence characterization of agkicetin, a new glycoprotein Ib antagonist isolated from Agkistrodon acutus venom
    • Chen, Y. L., Tsai, J. H. Functional and sequence characterization of agkicetin, a new glycoprotein Ib antagonist isolated from cAgkistrodon acutus venom. Biochem. Biophys. Res. Commun. 1995, 210, 472-477.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 472-477
    • Chen, Y.L.1    Tsai, J.H.2
  • 90
    • 0028998182 scopus 로고
    • Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress
    • Taniuchi, Y., Kawasaki, T., Fujimura, Y., Suzuki, M., Titani, K., Sakai, Y., Kaku, S., Hisamichi, N., Satoh, N., Takenaka, T., Handa, M., Sawai, Y. Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. Biochim. Biophys. Acta, 1995, 1244, 331-338.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 331-338
    • Taniuchi, Y.1    Kawasaki, T.2    Fujimura, Y.3    Suzuki, M.4    Titani, K.5    Sakai, Y.6    Kaku, S.7    Hisamichi, N.8    Satoh, N.9    Takenaka, T.10    Handa, M.11    Sawai, Y.12
  • 91
  • 93
    • 0013493426 scopus 로고
    • Venom coagglutinin: An activator of platelet aggregation dependent on von Willebrand factor
    • Read, M. S., Shermer, R. W., Brinkhous, K. M. Venom coagglutinin: an activator of platelet aggregation dependent on von Willebrand factor. Proc. Natl. Acad. Sci. U. S. A., 1978, 75, 4514-4518.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 4514-4518
    • Read, M.S.1    Shermer, R.W.2    Brinkhous, K.M.3
  • 94
    • 0020692553 scopus 로고
    • Venom coagglutinin for detection of von Willebrand factor activity in animal plasmas
    • Read, M. S., Potter, J. Y., Brinkhous, K. M. Venom coagglutinin for detection of von Willebrand factor activity in animal plasmas. J. Lab. Clin. Med., 1983, 101, 74-82.
    • (1983) J. Lab. Clin. Med. , vol.101 , pp. 74-82
    • Read, M.S.1    Potter, J.Y.2    Brinkhous, K.M.3
  • 95
    • 0024353508 scopus 로고
    • Role of botrocetin in platelet agglutination: Formation of an activated complex of botrocetin and von Willebrand factor
    • Read, M. S., Smith, S. V., Lamb, M. A., Brinkhous, K. M. Role of botrocetin in platelet agglutination: formation of an activated complex of botrocetin and von Willebrand factor. Blood, 1989, 74, 1031-1035.
    • (1989) Blood , vol.74 , pp. 1031-1035
    • Read, M.S.1    Smith, S.V.2    Lamb, M.A.3    Brinkhous, K.M.4
  • 96
    • 0019866867 scopus 로고
    • Von Willebrand syndrome induced by a Bothrops venom factor: Bioassay for venom coagglutinin
    • Brinkhous, K. M., Barnes, D. S., Potter, J. Y., Read, M. S. Von Willebrand syndrome induced by a Bothrops venom factor: bioassay for venom coagglutinin. Proc. Natl. Acad Sci. U S. A., 1981, 78, 3230-3234.
    • (1981) Proc. Natl. Acad. Sci. U S. A. , vol.78 , pp. 3230-3234
    • Brinkhous, K.M.1    Barnes, D.S.2    Potter, J.Y.3    Read, M.S.4
  • 97
    • 0020967787 scopus 로고
    • Botrocetin (venom coagglutinin): Reaction with a broad spectrum of multimeric forms of factor VIII macromolecular complex
    • Brinkhous, K. M., Read, M. S., Fricke, W. A., Wagner, R. H. Botrocetin (venom coagglutinin): reaction with a broad spectrum of multimeric forms of factor VIII macromolecular complex. Proc. Natl. Acad. Sci. U. S. A., 1983, 80, 1463-1466.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 1463-1466
    • Brinkhous, K.M.1    Read, M.S.2    Fricke, W.A.3    Wagner, R.H.4
  • 98
    • 0021273941 scopus 로고
    • The agglutination of human platelets by botrocetin: Evidence that botrocetin and ristocetin act at different sites on the factor VIII molecule and platelet membrane
    • Howard, M. A., Perkin, J., Salem, H. H., Firkin, B. G. The agglutination of human platelets by botrocetin: evidence that botrocetin and ristocetin act at different sites on the factor VIII molecule and platelet membrane. Br. J. Haematol., 1984, 57, 25-35.
    • (1984) Br. J. Haematol. , vol.57 , pp. 25-35
    • Howard, M.A.1    Perkin, J.2    Salem, H.H.3    Firkin, B.G.4
  • 99
    • 0022000541 scopus 로고
    • Botrocetin- and polybrene-induced platelet aggregation in platelet-type von Willebrand disease
    • Takahashi, H., Nagayama, R., Hattori, A., Shibata, A. Botrocetin- and polybrene-induced platelet aggregation in platelet-type von Willebrand disease. Am. J. Hematol., 1985, 18, 179-189.
    • (1985) Am. J. Hematol. , vol.18 , pp. 179-189
    • Takahashi, H.1    Nagayama, R.2    Hattori, A.3    Shibata, A.4
  • 100
    • 0023611358 scopus 로고
    • The von willebrand factor domain-mediating botrocetin-induced binding to glycoprotein IB lies between Val449 and Lys728
    • Fujimura, Y., Holland, L. Z., Ruggeri, Z. M., Zimmerman, T. S. The von willebrand factor domain-mediating botrocetin-induced binding to glycoprotein IB lies between Val449 and Lys728. Blood, 1987 70, 985-988.
    • (1987) Blood , vol.70 , pp. 985-988
    • Fujimura, Y.1    Holland, L.Z.2    Ruggeri, Z.M.3    Zimmerman, T.S.4
  • 101
    • 0024446932 scopus 로고
    • Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex
    • Andrews, R. K., Booth, W. J., Gorman, J. J., Castaldi, P. A., Berndt, M. C. Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex. Biochemistry, 1989, 28, 8317-8326.
    • (1989) Biochemistry , vol.28 , pp. 8317-8326
    • Andrews, R.K.1    Booth, W.J.2    Gorman, J.J.3    Castaldi, P.A.4    Berndt, M.C.5
  • 102
    • 0030568869 scopus 로고    scopus 로고
    • Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans snake venom
    • Hamako, J., Matsui, T., Suzuki, M., Ito, M., Makita, K., Fujimura, Y., Ozeki, Y., Titani, K. Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans snake venom. Biochem. Biophys. Res. Commun., 1996 226, 273-279.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 273-279
    • Hamako, J.1    Matsui, T.2    Suzuki, M.3    Ito, M.4    Makita, K.5    Fujimura, Y.6    Ozeki, Y.7    Titani, K.8
  • 103
    • 0021816420 scopus 로고
    • Characterization of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom
    • Ouyang, C. H., Ma, Y. H., Jih, H. C., Teng, C. M. Characterization of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom. Biochim. Biophys. Acta, 1985 841, 1-7.
    • (1985) Biochim. Biophys. Acta , vol.841 , pp. 1-7
    • Ouyang, C.H.1    Ma, Y.H.2    Jih, H.C.3    Teng, C.M.4
  • 104
    • 0021810615 scopus 로고
    • Action mechanism of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom
    • Teng, C. M., Ma, Y. H., Ouyang, C. H. Action mechanism of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom. Biochim. Biophys. Acta, 1985, 841, 8-14.
    • (1985) Biochim. Biophys. Acta , vol.841 , pp. 8-14
    • Teng, C.M.1    Ma, Y.H.2    Ouyang, C.H.3
  • 105
    • 0022589875 scopus 로고
    • Plasma cofactors necessary for Enhydrina schistosa (beaked sea snake) venom to induce platelet aggregation
    • Marshall, L. R., Herrmann, R. P. Plasma cofactors necessary for Enhydrina schistosa (beaked sea snake) venom to induce platelet aggregation. Thromb. Res., 1986, 43, 229-235.
    • (1986) Thromb. Res. , vol.43 , pp. 229-235
    • Marshall, L.R.1    Herrmann, R.P.2
  • 106
    • 0024234712 scopus 로고
    • Plasma components are required for platelet activation by the toxin of Loxosceles reclusa
    • Rees, R. S., Gates, C., Timmons, S., Des Prez, R. M., King, L. E., Jr. Plasma components are required for platelet activation by the toxin of Loxosceles reclusa. Toxicon, 1988, 26, 1035-1045.
    • (1988) Toxicon , vol.26 , pp. 1035-1045
    • Rees, R.S.1    Gates, C.2    Timmons, S.3    Des Prez, R.M.4    King Jr., L.E.5
  • 107
    • 0014490405 scopus 로고
    • The isolation of a component of the venom of Trimeresurus okinavensis that causes the aggregation of blood platelets
    • Davey, M. G., Esnouf, M. P. The isolation of a component of the venom of Trimeresurus okinavensis that causes the aggregation of blood platelets. Biochem. J., 1969, 111, 733-743.
    • (1969) Biochem. J. , vol.111 , pp. 733-743
    • Davey, M.G.1    Esnouf, M.P.2
  • 108
    • 0023878541 scopus 로고
    • Mechanism of rabbit platelet agglutination induced by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka
    • Li. J. Z., Lian, E. C. Mechanism of rabbit platelet agglutination induced by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka. Thromb. Haemost., 1988, 59 432-434.
    • (1988) Thromb. Haemost. , vol.59 , pp. 432-434
    • Li, J.Z.1    Lian, E.C.2
  • 109
    • 0023875679 scopus 로고
    • Aggregation of human platelets by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka
    • Li. J. Z., Lian, E. C. Aggregation of human platelets by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka. Thromb. Haemost., 1988b, 59, 435-439.
    • (1988) Thromb. Haemost. , vol.59 , pp. 435-439
    • Li, J.Z.1    Lian, E.C.2
  • 110
    • 0025147709 scopus 로고
    • Review article: Effects of snake venom proteins on blood platelets
    • Kini, R.M., Evans, H.J. Review article: Effects of snake venom proteins on blood platelets. Toxicon, 1990, 28, 1387-1422.
    • (1990) Toxicon , vol.28 , pp. 1387-1422
    • Kini, R.M.1    Evans, H.J.2
  • 111
    • 0026713194 scopus 로고
    • Characterization of snake venom components acting on blood coagulation and platelet function
    • Ouyang, C., Teng, C. M., Huang, T. F. Characterization of snake venom components acting on blood coagulation and platelet function. Toxicon, 1992, 30, 945-966.
    • (1992) Toxicon , vol.30 , pp. 945-966
    • Ouyang, C.1    Teng, C.M.2    Huang, T.F.3
  • 112
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski, S., McLane, M. A., Kloczewiak, M., Stewart, G. J. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol., 1994, 31, 289-300.
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 113
    • 0033741151 scopus 로고    scopus 로고
    • Snake venom proteins acting on hemostasis
    • Braud, S., Bon, C., Wisner, A. Snake venom proteins acting on hemostasis. Biochimie, 2000, 82, 851-859.
    • (2000) Biochimie , vol.82 , pp. 851-859
    • Braud, S.1    Bon, C.2    Wisner, A.3
  • 114
    • 0025729301 scopus 로고
    • Inventory of exogenous inhibitors of platelet aggregation
    • Teng, CM, Huang, TF. Inventory of exogenous inhibitors of platelet aggregation. Thrombos. Haemostas., 1991, 65, 624-626.
    • (1991) Thrombos. Haemostas. , vol.65 , pp. 624-626
    • Teng, C.M.1    Huang, T.F.2
  • 115
    • 0035167442 scopus 로고    scopus 로고
    • Exogenous inhibitors of platelet aggregation from animal sources
    • Kini, R.M., Chow, G. Exogenous inhibitors of platelet aggregation from animal sources. Thrombos. Haemostas., 2001, 85, 179-181.
    • (2001) Thrombos. Haemostas. , vol.85 , pp. 179-181
    • Kini, R.M.1    Chow, G.2
  • 116
    • 0023915420 scopus 로고
    • The platelet membrane glycoprotein IIb-IIIa complex
    • Phillips, D. R., Charo, I. F., Parise, L. V., Fitzgerald, L. A. The platelet membrane glycoprotein IIb-IIIa complex. Blood, 1988, 71, 831-843.
    • (1988) Blood , vol.71 , pp. 831-843
    • Phillips, D.R.1    Charo, I.F.2    Parise, L.V.3    Fitzgerald, L.A.4
  • 117
    • 0029763215 scopus 로고    scopus 로고
    • Analysis of GPIIb/GPIIIa receptor number by quantification of 7E3 binding to human platelets
    • Wagner, C. L., Mascelli, M. A., Neblock, D. S., Weisman, H. F., Coller, B. S., Jordan, R. E. Analysis of GPIIb/GPIIIa receptor number by quantification of 7E3 binding to human platelets. Blood, 1996 88, 907-914.
    • (1996) Blood , vol.88 , pp. 907-914
    • Wagner, C.L.1    Mascelli, M.A.2    Neblock, D.S.3    Weisman, H.F.4    Coller, B.S.5    Jordan, R.E.6
  • 118
    • 0020438172 scopus 로고
    • Purification of glycoproteins IIb and III from human platelet plasma membranes and characterization of a calcium-dependent glycoprotein IIb-III complex
    • Jennings, L. K., Phillips, D. R. Purification of glycoproteins IIb and III from human platelet plasma membranes and characterization of a calcium-dependent glycoprotein IIb-III complex. J. Biol. Chem., 1982, 257, 10458-10466.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10458-10466
    • Jennings, L.K.1    Phillips, D.R.2
  • 119
    • 0021028111 scopus 로고
    • Calcium cation regulation of glycoprotein IIb-IIIa complex formation in platelet plasma membranes
    • Fujimura, K., Phillips, D. R. Calcium cation regulation of glycoprotein IIb-IIIa complex formation in platelet plasma membranes. J. Biol. Chem., 1983, 258, 10247-10252.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10247-10252
    • Fujimura, K.1    Phillips, D.R.2
  • 120
    • 0022221860 scopus 로고
    • Calcium regulation of the platelet membrane glycoprotein IIb-IIIa complex
    • Fitzgerald, L. A., Phillips, D. R. Calcium regulation of the platelet membrane glycoprotein IIb-IIIa complex. J. Biol. Chem., 1985, 260, 11366-11374.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11366-11374
    • Fitzgerald, L.A.1    Phillips, D.R.2
  • 121
    • 0023865294 scopus 로고
    • Identity of saturable calcium-binding sites on blood platelets and their involvement in platelet aggregation
    • Johnston, G. I., Heptinstall, S. Identity of saturable calcium-binding sites on blood platelets and their involvement in platelet aggregation. Thrombos. Haemos., 1988, 58, 54-61.
    • (1988) Thrombos. Haemos. , vol.58 , pp. 54-61
    • Johnston, G.I.1    Heptinstall, S.2
  • 122
    • 0025908304 scopus 로고
    • Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins. Effects of lipids and temperature
    • Rivas, G. A., Gonzalez-Rodriguez, J. Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins. Effects of lipids and temperature. Biochem. J., 1991, 276 35-40.
    • (1991) Biochem. J. , vol.276 , pp. 35-40
    • Rivas, G.A.1    Gonzalez-Rodriguez, J.2
  • 123
    • 0029062761 scopus 로고
    • Platelet glycoprotein IIb/IIIa receptors in cardiovascular medicine
    • Lefkovits, J., Plow, E. F., Topol, E. J. Platelet glycoprotein IIb/IIIa receptors in cardiovascular medicine. N. Engl. J. Med., 1995, 332, 1553-1559.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1553-1559
    • Lefkovits, J.1    Plow, E.F.2    Topol, E.J.3
  • 126
    • 0035099426 scopus 로고    scopus 로고
    • Inhibition of platelet aggregation of a mutant proinsulin molecule engineered by introduction of a native Arg-Gly-Asp sequence
    • Yang, Z. H., Jing, J., Tang, J. G. Inhibition of platelet aggregation of a mutant proinsulin molecule engineered by introduction of a native Arg-Gly-Asp sequence. Appl. Biochem. Biotechnol., 2001 90, 1-10.
    • (2001) Appl. Biochem. Biotechnol. , vol.90 , pp. 1-10
    • Yang, Z.H.1    Jing, J.2    Tang, J.G.3
  • 128
    • 0028052961 scopus 로고
    • Binding of recombinant fibrinogen mutants to platelets
    • Farrell, D. H., Thiagarajan, P. Binding of recombinant fibrinogen mutants to platelets. J. Biol, Chem., 1994, 269 226-231.
    • (1994) J. Biol, Chem. , vol.269 , pp. 226-231
    • Farrell, D.H.1    Thiagarajan, P.2
  • 130
    • 0024206252 scopus 로고
    • Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus
    • Gan, Z. R., Gould, R. J., Jacobs, J. W., Friedman, P. A., Polokoff, M. A. Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus. J. Biol. Chem., 1988 263, 19827-19832.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19827-19832
    • Gan, Z.R.1    Gould, R.J.2    Jacobs, J.W.3    Friedman, P.A.4    Polokoff, M.A.5
  • 131
    • 0024557652 scopus 로고
    • Trigramin: Primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets
    • Huang, T. F., Holt, J. C., Kirby, E. P., Niewiarowski, S. Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets. Biochemistry, 1989, 28, 661-666.
    • (1989) Biochemistry , vol.28 , pp. 661-666
    • Huang, T.F.1    Holt, J.C.2    Kirby, E.P.3    Niewiarowski, S.4
  • 132
    • 0025289449 scopus 로고
    • Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins: RGD-containing peptides from viper venoms
    • Musial, J., Niewiarowski, S., Rucinski, B., Stewart, G. J., Cook, J. J., Williams, J. A., Edmunds, L. H., Jr. Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins: RGD-containing peptides from viper venoms. Circulation, 1990, 82, 261-273.
    • (1990) Circulation , vol.82 , pp. 261-273
    • Musial, J.1    Niewiarowski, S.2    Rucinski, B.3    Stewart, G.J.4    Cook, J.J.5    Williams, J.A.6    Edmunds Jr., L.H.7
  • 134
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • Kini, R. M., Evans, H. J. Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon, 1992, 30, 265-293.
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 135
    • 0026748687 scopus 로고
    • Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: Evidence for signal, zymogen, and disintegrin-like structures
    • Hite, L. A., Shannon, J. D., Bjarnason, J. B., Fox, J. W. Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures. Biochemistry, 1992, 31 6203-6211.
    • (1992) Biochemistry , vol.31 , pp. 6203-6211
    • Hite, L.A.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 136
    • 0028337108 scopus 로고
    • cDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • Hite, L. A., Bjarnason, J. B., Fox, J. W. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys., 1994, 308, 182-191.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Bjarnason, J.B.2    Fox, J.W.3
  • 137
    • 0026623540 scopus 로고
    • Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains
    • Takeya, H., Nishida, S., Miyata, T., Kawada, S., Saisaka, Y., Morita, T., Iwanaga, S. Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains. J. Biol. Chem., 1992, 267, 14109-14117.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14109-14117
    • Takeya, H.1    Nishida, S.2    Miyata, T.3    Kawada, S.4    Saisaka, Y.5    Morita, T.6    Iwanaga, S.7
  • 138
    • 0027193420 scopus 로고
    • Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes
    • Takeya, H., Nishida, S., Nishino, N., Makinose, Y., Omori-Satoh, T., Nikai, T., Sugihara, H., Iwanaga, S. Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes. J. Biochem., 1993, 113, 473-483.
    • (1993) J. Biochem. , vol.113 , pp. 473-483
    • Takeya, H.1    Nishida, S.2    Nishino, N.3    Makinose, Y.4    Omori-Satoh, T.5    Nikai, T.6    Sugihara, H.7    Iwanaga, S.8
  • 139
    • 0026495409 scopus 로고
    • Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloproteinase, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family
    • Paine, M. J. I., Desmond, H. P., Theakston, R. D. G., Crampton, J. M. Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloproteinase, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. J. Biol. Chem., 1992, 267, 22869-22876.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22869-22876
    • Paine, M.J.I.1    Desmond, H.P.2    Theakston, R.D.G.3    Crampton, J.M.4
  • 140
    • 0027964650 scopus 로고
    • Cloning of metalloproteinase genes in the carpet viper (Echis pyramidum leakeyi). Further members of the metalloprotease/disintegrin gene family
    • Paine, M. J. I., Moura-de-Silva, A. M., Theakston, R. D. G., Crampton, J. M. Cloning of metalloproteinase genes in the carpet viper (Echis pyramidum leakeyi). Further members of the metalloprotease/disintegrin gene family. Eur. J. Biochem., 1994 224, 483-488.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 483-488
    • Paine, M.J.I.1    Moura-de-Silva, A.M.2    Theakston, R.D.G.3    Crampton, J.M.4
  • 141
    • 0027254333 scopus 로고
    • Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom
    • Au, L. C., Chou, J. S., Chang, K. J., Teh, G. W., Lin, S. B. Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom. Biochim. Biophys. Acta, 1993 1173, 243-245.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 243-245
    • Au, L.C.1    Chou, J.S.2    Chang, K.J.3    Teh, G.W.4    Lin, S.B.5
  • 143
    • 0033049456 scopus 로고    scopus 로고
    • Ussuristatin 2, a novel KGD-bearing disintegrin from Agkistrodon ussuriensis venom
    • Oshikawa, K., Terada, S. Ussuristatin 2, a novel KGD-bearing disintegrin from Agkistrodon ussuriensis venom. J. Biochem., 1999, 125, 31-35.
    • (1999) J. Biochem. , vol.125 , pp. 31-35
    • Oshikawa, K.1    Terada, S.2
  • 144
    • 0034854834 scopus 로고    scopus 로고
    • Purification and characterization of a new RGD/KGD-containing dimeric disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus piscivorus: The unique effect of piscivostatin on platelet aggregation
    • Okuda, D., Morita, T. Purification and characterization of a new RGD/KGD-containing dimeric disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus piscivorus: the unique effect of piscivostatin on platelet aggregation. J. Biochem., 2001, 130, 407-415.
    • (2001) J. Biochem. , vol.130 , pp. 407-415
    • Okuda, D.1    Morita, T.2
  • 146
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist
    • Adler, M., Lazarus, R. A., Dennis, M. S., Wagner, G. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist. Science, 1991, 253, 445-448.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis, M.S.3    Wagner, G.4
  • 147
    • 0025786742 scopus 로고
    • Three-dimensional structure of echistatin, the smallest active RGD protein
    • Saudek, V., Atkinson, R. A., Pelton, J. T. Three-dimensional structure of echistatin, the smallest active RGD protein. Biochemistry 1991, 30, 7369-7372.
    • (1991) Biochemistry , vol.30 , pp. 7369-7372
    • Saudek, V.1    Atkinson, R.A.2    Pelton, J.T.3
  • 148
    • 0026709490 scopus 로고
    • The solution structure of echistatin: Evidence for disulfide bond rearrangement in homologous snake toxins
    • Cooke, R. M., Carter, B. G., Murray-Rust, P., Hartshorn, M. J., Herzyk, P., Hubbard, R. E. The solution structure of echistatin: evidence for disulfide bond rearrangement in homologous snake toxins. Protein Engg., 1992, 5, 473-477.
    • (1992) Protein Engg. , vol.5 , pp. 473-477
    • Cooke, R.M.1    Carter, B.G.2    Murray-Rust, P.3    Hartshorn, M.J.4    Herzyk, P.5    Hubbard, R.E.6
  • 149
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor
    • Senn, H., Klaus, W. The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor. J. Mol. Biol., 1993, 232, 907-925.
    • (1993) J. Mol. Biol. , vol.232 , pp. 907-925
    • Senn, H.1    Klaus, W.2
  • 151
    • 0028568947 scopus 로고
    • 3 with immobilized glycoprotein ligands by snake-venom RGD (Arg-Gly-Asp) proteins. Evidence supporting a functional role for the amino acid residues flanking the tripeptide RGD in determining the inhibitory properties of snake-venom RGD proteins
    • 3 with immobilized glycoprotein ligands by snake-venom RGD (Arg-Gly-Asp) proteins. Evidence supporting a functional role for the amino acid residues flanking the tripeptide RGD in determining the inhibitory properties of snake-venom RGD proteins. Biochem. J., 1994, 304, 929-936.
    • (1994) Biochem. J. , vol.304 , pp. 929-936
    • Lu, X.1    Williams, J.A.2    Deadman, J.J.3    Salmon, G.P.4    Kakkar, V.V.5    Wilkinson, J.M.6    Baruch, D.7    Authi, K.S.8    Rahman, S.9
  • 152
    • 0030042941 scopus 로고    scopus 로고
    • Substitutions of Proline 42 to Alanine and Methionine 46 to Asparagine around RGD domain of the neurotoxin dendroaspin alter its preferential antagonism to that resembling the disintegrin elagantin
    • Lu, X., Rahman, S., Kakkar, V. V., Authi, K. S. Substitutions of Proline 42 to Alanine and Methionine 46 to Asparagine around RGD domain of the neurotoxin dendroaspin alter its preferential antagonism to that resembling the disintegrin elagantin. J. Biol. Chem., 1996 271, 289-294.
    • (1996) J. Biol. Chem. , vol.271 , pp. 289-294
    • Lu, X.1    Rahman, S.2    Kakkar, V.V.3    Authi, K.S.4
  • 153
    • 0035339577 scopus 로고    scopus 로고
    • Evaluation of the role of Proline residues flanking the RGD motif of dendroaspin, an inhibitor of platelet aggregation and cell adhesion
    • Lu, X., Sun, Y., Shang, D., Wattam, B., Egglezou, S., Hughes, T., Hyde, E., Scully, M., Kakkar, V. Evaluation of the role of Proline residues flanking the RGD motif of dendroaspin, an inhibitor of platelet aggregation and cell adhesion. Biochem. J., 2001, 355, 633-638.
    • (2001) Biochem. J. , vol.355 , pp. 633-638
    • Lu, X.1    Sun, Y.2    Shang, D.3    Wattam, B.4    Egglezou, S.5    Hughes, T.6    Hyde, E.7    Scully, M.8    Kakkar, V.9
  • 154
    • 0028972312 scopus 로고
    • 3 contains distinct and interacting binding sites for snake-venom RGD (Arg-Gly-Asp) proteins. Evidence that the receptor-binding characteristics of snake-venom RGD proteins are related to the amino acid environment flanking the sequence RGD
    • 3 contains distinct and interacting binding sites for snake-venom RGD (Arg-Gly-Asp) proteins. Evidence that the receptor-binding characteristics of snake-venom RGD proteins are related to the amino acid environment flanking the sequence RGD. Biochem. J. 1995, 312, 223-232.
    • (1995) Biochem. J. , vol.312 , pp. 223-232
    • Rahman, S.1    Lu, X.2    Kakkar, V.V.3    Authi, K.S.4
  • 155
    • 0030570733 scopus 로고    scopus 로고
    • Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for the recognition of α IIβ3 and αvβ3 integrins
    • McLane, M. A., Vijay-Kumar, S., Marcinkiewicz, C., Calvete, J. J., Niewiarowski, S. Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for the recognition of αIIβ3 and αvβ3 integrins. FEBS Lett., 1996, 391, 139-143.
    • (1996) FEBS Lett. , vol.391 , pp. 139-143
    • McLane, M.A.1    Vijay-Kumar, S.2    Marcinkiewicz, C.3    Calvete, J.J.4    Niewiarowski, S.5
  • 156
    • 0037070206 scopus 로고    scopus 로고
    • Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus
    • Smith, J. B., Theakston, R. D. G., Coelho, A. L. J., Barja-Fidalgo, C., Calvete, J. J., Marcinkiewicz, C. Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus. FEBS Lett., 2002, 512, 111-115.
    • (2002) FEBS Lett. , vol.512 , pp. 111-115
    • Smith, J.B.1    Theakston, R.D.G.2    Coelho, A.L.J.3    Barja-Fidalgo, C.4    Calvete, J.J.5    Marcinkiewicz, C.6
  • 158
    • 0034916180 scopus 로고    scopus 로고
    • Platelet aggregation inhibition with glycoprotein IIb - IIIa inhibitors
    • Proimos, G. Platelet aggregation inhibition with glycoprotein IIb - IIIa inhibitors. J. Thromb. Thrombolysis, 2001, 11 99-110.
    • (2001) J. Thromb. Thrombolysis , vol.11 , pp. 99-110
    • Proimos, G.1
  • 159
    • 0030863733 scopus 로고    scopus 로고
    • Clinical pharmacology of eptifibatide
    • Phillips, D. R., Scarborough, R. M. Clinical pharmacology of eptifibatide. Am. J. Cardiol., 1997, 80 (Suppl. 4A), 11B-20B.
    • (1997) Am. J. Cardiol. , vol.80 , Issue.SUPPL. 4A
    • Phillips, D.R.1    Scarborough, R.M.2
  • 161
    • 0028371958 scopus 로고
    • Triflavin, an antiplatelet peptide inhibits tumor cell-extracellular matrix adhesion via an RGD-dependent mechanism
    • Sheu, J. R., Lin, C. H., Huang, T. F. Triflavin, an antiplatelet peptide inhibits tumor cell-extracellular matrix adhesion via an RGD-dependent mechanism. J. Lab. Clin. Med., 1994, 123, 256-263.
    • (1994) J. Lab. Clin. Med. , vol.123 , pp. 256-263
    • Sheu, J.R.1    Lin, C.H.2    Huang, T.F.3
  • 162
    • 0029879229 scopus 로고    scopus 로고
    • Platelet glycoprotein IIb/IIIa receptor antagonists in
    • Lefkovits, J., Topol, E. J. Platelet glycoprotein IIb/IIIa receptor antagonists in coronary artery disease. Eur. Heart J., 1996, 17, 9-18.
    • (1996) Eur. Heart J. , vol.17 , pp. 9-18
    • Lefkovits, J.1    Topol, E.J.2
  • 163
    • 0029759912 scopus 로고    scopus 로고
    • Triflavin, an Arg-Gly-Asp containing peptide, inhibits the adhesion of tumor cells to matrix proteins via binding to multiple integrin receptors expressed on human hepatoma cells
    • Sheu, J. R., Lin, C. H., Peng, H. C., Huang, T. F. Triflavin, an Arg-Gly-Asp containing peptide, inhibits the adhesion of tumor cells to matrix proteins via binding to multiple integrin receptors expressed on human hepatoma cells. Proc. Soc. Exp. Biol. Med., 1996, 213, 71-79.
    • (1996) Proc. Soc. Exp. Biol. Med. , vol.213 , pp. 71-79
    • Sheu, J.R.1    Lin, C.H.2    Peng, H.C.3    Huang, T.F.4
  • 164
    • 0028838003 scopus 로고
    • Arg-Gly-Asp containing peptide, rhodostomin, inhibits in vitro cell adhesion to extracellular matrices and platelet aggregation caused by Sao-2 human osteosarcoma cells
    • Chiang, H. S., Yang, R. S., Huang, T. F. Arg-Gly-Asp containing peptide, rhodostomin, inhibits in vitro cell adhesion to extracellular matrices and platelet aggregation caused by Sao-2 human osteosarcoma cells. Br. J. Cancer, 1995, 71, 265-270.
    • (1995) Br. J. Cancer , vol.71 , pp. 265-270
    • Chiang, H.S.1    Yang, R.S.2    Huang, T.F.3
  • 165
    • 0026039146 scopus 로고
    • Inhibition of routine melanoma cell-matrix adhesion and experimental metastasis by albolabrin, an RGD-containing peptide isolated from the venom of Trimeresurus albolabris
    • Soszka, T., Knudsen, K. A., Beviglia, L., Rossi, C., Poggi, A., Niewiarowski, S. Inhibition of routine melanoma cell-matrix adhesion and experimental metastasis by albolabrin, an RGD-containing peptide isolated from the venom of Trimeresurus albolabris. Exp. Cell Res., 1991, 196, 6-12.
    • (1991) Exp. Cell Res. , vol.196 , pp. 6-12
    • Soszka, T.1    Knudsen, K.A.2    Beviglia, L.3    Rossi, C.4    Poggi, A.5    Niewiarowski, S.6
  • 166
    • 0026795394 scopus 로고
    • Triflavin, an Arg-Gly-Asp containing peptide inhibits cell-substratum adhesion and melanoma cell-induced lung colonization
    • Sheu, J. R., Lin, C. H., Chuang, J. L., Teng, C. M., Huang, T. F. Triflavin, an Arg-Gly-Asp containing peptide inhibits cell-substratum adhesion and melanoma cell-induced lung colonization. Jpn. J. Cancer Res., 1992, 83, 885-893.
    • (1992) Jpn. J. Cancer Res. , vol.83 , pp. 885-893
    • Sheu, J.R.1    Lin, C.H.2    Chuang, J.L.3    Teng, C.M.4    Huang, T.F.5
  • 167
    • 0028111866 scopus 로고
    • 1 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis
    • 1 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis. Cancer Res., 1994, 54, 4993-4998.
    • (1994) Cancer Res. , vol.54 , pp. 4993-4998
    • Trikha, M.1    De Clerck, Y.A.2    Markland, F.S.3
  • 169
    • 0026633893 scopus 로고
    • Triflavin, an Arg-Gly-Asp containing peptide, inhibits aggregation of human platelets induced by human hepatoma cell line
    • Sheu, J. R., Lin, C. H., Chuang, J. L., Teng, C. M., Huang, T. F. Triflavin, an Arg-Gly-Asp containing peptide, inhibits aggregation of human platelets induced by human hepatoma cell line. Thrombos. Res. 1992, 66, 679-691.
    • (1992) Thrombos. Res. , vol.66 , pp. 679-691
    • Sheu, J.R.1    Lin, C.H.2    Chuang, J.L.3    Teng, C.M.4    Huang, T.F.5
  • 171
    • 0001562465 scopus 로고    scopus 로고
    • 3 antagonist and inducing apoptosis
    • 3 antagonist and inducing apoptosis. Blood, 1998 92, 3268-3276.
    • (1998) Blood , vol.92 , pp. 3268-3276
    • Yeh, C.H.1    Peng, H.C.2    Huang, T.F.3
  • 172
    • 0036179582 scopus 로고    scopus 로고
    • Snake venom disintegrin, saxatilin, inhibits platelet aggregation, human umbilical vein endothelial cell proliferation, and smooth muscle cell migration
    • Hong, S. Y., Koh, Y. S., Chung, K. H., Kim, D. S. Snake venom disintegrin, saxatilin, inhibits platelet aggregation, human umbilical vein endothelial cell proliferation, and smooth muscle cell migration. Thrombos, Res., 2002, 105, 79-86.
    • (2002) Thrombos. Res. , vol.105 , pp. 79-86
    • Hong, S.Y.1    Koh, Y.S.2    Chung, K.H.3    Kim, D.S.4
  • 173
    • 0028046746 scopus 로고
    • Blockade of osteoclast-mediated bone resorption through occupancy of the integrin receptor: A potential approach to the therapy of osteoporosis
    • Dresner-Pollak, R., Rosenblatt, M. Blockade of osteoclast-mediated bone resorption through occupancy of the integrin receptor: a potential approach to the therapy of osteoporosis. J. Cell. Biochem., 1994, 56, 323-330.
    • (1994) J. Cell Biochem. , vol.56 , pp. 323-330
    • Dresner-Pollak, R.1    Rosenblatt, M.2
  • 176
    • 0031793624 scopus 로고    scopus 로고
    • Histomorphometric evidence for echistatin inhibition of bone resorption in mice with secondary hyperparathyroidism
    • Masarachia, P., Yamamoto, M., Len, C. T., Rodan, G., Duong, L. Histomorphometric evidence for echistatin inhibition of bone resorption in mice with secondary hyperparathyroidism. Endocrinology 1998, 139, 1401-1410.
    • (1998) Endocrinology , vol.139 , pp. 1401-1410
    • Masarachia, P.1    Yamamoto, M.2    Len, C.T.3    Rodan, G.4    Duong, L.5
  • 178
    • 0026650803 scopus 로고
    • Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins
    • McDowell, R. S., Dennis, M. S., Louie, A., Shuster, M., Mulkerrin, M. G., Lazarus, R. A. Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry, 1992, 31, 4766-4772.
    • (1992) Biochemistry , vol.31 , pp. 4766-4772
    • McDowell, R.S.1    Dennis, M.S.2    Louie, A.3    Shuster, M.4    Mulkerrin, M.G.5    Lazarus, R.A.6
  • 179
    • 0028533579 scopus 로고
    • Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin
    • Sutcliffe, M. J., Jaseja, M., Hyde, E. I., Lu, X., Williams, J. A. Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin. Nat. Struct. Biol., 1994, 1, 802-807.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 802-807
    • Sutcliffe, M.J.1    Jaseja, M.2    Hyde, E.I.3    Lu, X.4    Williams, J.A.5
  • 180
    • 0036381024 scopus 로고    scopus 로고
    • Molecular molds with multiple missions: Functional sites in three-finger toxins
    • Kini, R. M. Molecular molds with multiple missions: functional sites in three-finger toxins. Clinic. Exptl. Pharmacol. Physiol., 2002, 29, 815-822.
    • (2002) Clinic Exptl. Pharmacol. Physiol. , vol.29 , pp. 815-822
    • Kini, R.M.1
  • 181
    • 0025329916 scopus 로고
    • Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
    • Seymour, J. L., Henzel, W. J., Nevins, B., Stults, J. T., Lazarus, R. A. Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J. Biol. Chem., 1990, 265, 10143-10147.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10143-10147
    • Seymour, J.L.1    Henzel, W.J.2    Nevins, B.3    Stults, J.T.4    Lazarus, R.A.5
  • 182
    • 0026331936 scopus 로고
    • Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata
    • Mazur, P., Henzel, W. J., Seymour, J. L., Lazarus, R. A. Ornatins: potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur. J. Biochem., 1991, 202, 1073-1082.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1073-1082
    • Mazur, P.1    Henzel, W.J.2    Seymour, J.L.3    Lazarus, R.A.4
  • 183
    • 0028017504 scopus 로고
    • Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting
    • Krezel, A. M., Wagner, G., Seymour-Ulmer, J., Lazarus, R. A. Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting. Science, 1994, 264, 1944-1947.
    • (1994) Science , vol.264 , pp. 1944-1947
    • Krezel, A.M.1    Wagner, G.2    Seymour-Ulmer, J.3    Lazarus, R.A.4
  • 184
    • 0028217639 scopus 로고
    • Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata
    • Karczewski, J., Endris, R., Connolly, T. M. Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata. J. Biol. Chem., 1994, 269, 6702-6708.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6702-6708
    • Karczewski, J.1    Endris, R.2    Connolly, T.M.3
  • 185
    • 0037077268 scopus 로고    scopus 로고
    • Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the kunitz-BPTI fold
    • Mans, B. J., Louw, A. I., Neitz, A. W. H. Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the kunitz-BPTI fold. J. Biol. Chem., 2002, 277, 21371-21378.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21371-21378
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.H.3
  • 186
    • 0029898540 scopus 로고    scopus 로고
    • Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis
    • Wang, X., Coons, L. B., Taylor, D. B., Stevens, S. E. Jr., Gartner, T. K. Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis. J. Biol. Chem., 1996, 271, 17785-17790.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17785-17790
    • Wang, X.1    Coons, L.B.2    Taylor, D.B.3    Stevens Jr., S.E.4    Gartner, T.K.5
  • 187
    • 0023603317 scopus 로고
    • Structure-function relationship of human von Willebrand factor
    • Girma J.-P., Meyer, D., Verweij, C. L., Pannekoek, H., Sixma, J. J. Structure-function relationship of human von Willebrand factor. Blood, 1987, 70, 605-611.
    • (1987) Blood , vol.70 , pp. 605-611
    • Girma, J.-P.1    Meyer, D.2    Verweij, C.L.3    Pannekoek, H.4    Sixma, J.J.5
  • 188
    • 0026323664 scopus 로고
    • Von Willebrand factor
    • Sadler, J. E. von Willebrand factor. J. Biol. Chem., 1991, 266, 18172-18178.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18172-18178
    • Sadler, J.E.1
  • 189
    • 0028037555 scopus 로고
    • Isolation, characterization and amino acid sequence of echicetin β subunit, a specific inhibitor of von Willebrand factor and thrombin interaction with glycoprotein Ib
    • Peng, M., Holt, J. C., Niewiarowski, S. Isolation, characterization and amino acid sequence of echicetin β subunit, a specific inhibitor of von Willebrand factor and thrombin interaction with glycoprotein Ib. Biochem. Biophys. Res. Commun., 1994, 205 68-72.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 68-72
    • Peng, M.1    Holt, J.C.2    Niewiarowski, S.3
  • 190
    • 0029129139 scopus 로고
    • Interaction of echicetin with a high affinity thrombin binding site on platelet glycoprotein GPIb
    • Peng, M., Emig, F. A., Mao, A., Lu, W., Kirby, E. P., Niewiarowski, S., Kowalska, M. A. Interaction of echicetin with a high affinity thrombin binding site on platelet glycoprotein GPIb. Thromb. Haemost., 1995, 74, 954-957.
    • (1995) Thromb. Haemost. , vol.74 , pp. 954-957
    • Peng, M.1    Emig, F.A.2    Mao, A.3    Lu, W.4    Kirby, E.P.5    Niewiarowski, S.6    Kowalska, M.A.7
  • 191
    • 9544250197 scopus 로고    scopus 로고
    • C-type lectin-related proteins. Current Drug Targets
    • this issue
    • Morita, T. C-type lectin-related proteins. Current Drug Targets, this issue.
    • Morita, T.1
  • 192
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X
    • Mizuno, H., Fujimoto, Z., Atoda, H., Morita, T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc. Natl. Acad. Sci. U S. A., 2001, 98, 7230-7234.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 194
    • 0141844485 scopus 로고    scopus 로고
    • Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: Insight into glycoprotein Ibα binding mechanism induced by snake venom proteins
    • Maita, N., Nishio, K., Nishimoto, E., Matsui, T., Shikamoto, Y., Morita, T., Sadler, J. E., Mizuno, H. Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibα binding mechanism induced by snake venom proteins. J. Biol. Chem., 2003, 278, 37777-37781.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37777-37781
    • Maita, N.1    Nishio, K.2    Nishimoto, E.3    Matsui, T.4    Shikamoto, Y.5    Morita, T.6    Sadler, J.E.7    Mizuno, H.8
  • 195
    • 0030979409 scopus 로고    scopus 로고
    • Structure of Coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains
    • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., Morita, H. Structure of Coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains. Nature Struc. Biol., 1997 4, 438-441.
    • (1997) Nature Struc. Biol. , vol.4 , pp. 438-441
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, H.6
  • 196
    • 0035856557 scopus 로고    scopus 로고
    • Crystal structure of bitiscetin, a von Willebrand factor-dependent platelet aggregation inducer
    • Hirotsu, S., Mizuno, H., Fukuda, K., Qi, M. C., Matsui, T., Hamako, J., Morita, T., Titani, K. Crystal structure of bitiscetin, a von Willebrand factor-dependent platelet aggregation inducer. Biochemistry 2001, 40, 13592-13597.
    • (2001) Biochemistry , vol.40 , pp. 13592-13597
    • Hirotsu, S.1    Mizuno, H.2    Fukuda, K.3    Qi, M.C.4    Matsui, T.5    Hamako, J.6    Morita, T.7    Titani, K.8
  • 198
    • 0026102853 scopus 로고
    • Calin - A platelet adhesion inhibitor from the saliva of the medicinal leech
    • Munro, R., Jones, C. P., Sawyer, R. T. Calin - a platelet adhesion inhibitor from the saliva of the medicinal leech. Blood Coagul. Fibrinolysis, 1991, 2, 179-184.
    • (1991) Blood Coagul. Fibrinolysis , vol.2 , pp. 179-184
    • Munro, R.1    Jones, C.P.2    Sawyer, R.T.3
  • 199
    • 0026733452 scopus 로고
    • An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. I. Identification, isolation, and characterization
    • Connolly, T. M., Jacobs, J. W., Condra, C. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. I. Identification, isolation, and characterization. J. Biol. Chem., 1992, 267, 6893-6898.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6893-6898
    • Connolly, T.M.1    Jacobs, J.W.2    Condra, C.3
  • 200
    • 0026705756 scopus 로고
    • An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. II. Cloning of the cDNA and expression
    • Keller, P. M., Schultz, L. D., Condra, C., Karczewski, J., Connolly, T. M. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. II. Cloning of the cDNA and expression. J. Biol. Chem., 1992, 267, 6899-6904.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6899-6904
    • Keller, P.M.1    Schultz, L.D.2    Condra, C.3    Karczewski, J.4    Connolly, T.M.5
  • 201
    • 0027520772 scopus 로고
    • Cloning of the cDNA and expression of moubatin, an inhibitor of platelet aggregation
    • Keller, P. M., Waxman, L., Arnold, B. A., Schultz, L. D., Condra, C., Connolly, T. M. Cloning of the cDNA and expression of moubatin, an inhibitor of platelet aggregation. J. Biol. Chem., 1993, 268, 5450-5456.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5450-5456
    • Keller, P.M.1    Waxman, L.2    Arnold, B.A.3    Schultz, L.D.4    Condra, C.5    Connolly, T.M.6
  • 202
    • 0027418305 scopus 로고
    • Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata
    • Waxman, L., Connolly, T. M. Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata. J. Biol. Chem., 1993, 268, 5445-5449.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5445-5449
    • Waxman, L.1    Connolly, T.M.2
  • 203
    • 0028233804 scopus 로고
    • A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation
    • Usami, Y., Fujimura, Y., Miura, S., Shima, H., Yoshida, E., Yoshioka, A., Hirano, K., Suzuki, M., Titani, K. A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation. Biochem. Biophys. Res. Commun., 1994, 201, 331-339.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 331-339
    • Usami, Y.1    Fujimura, Y.2    Miura, S.3    Shima, H.4    Yoshida, E.5    Yoshioka, A.6    Hirano, K.7    Suzuki, M.8    Titani, K.9
  • 204
    • 0028986726 scopus 로고
    • An inhibitor from the argasid tick Ornithodoros moubata of cell adhesion to collagen
    • Karczewski, J., Waxman, L., Endris, R. G., Connolly, T. M. An inhibitor from the argasid tick Ornithodoros moubata of cell adhesion to collagen. Biochem. Biophys. Res. Commun., 1995, 208, 532-541.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 532-541
    • Karczewski, J.1    Waxman, L.2    Endris, R.G.3    Connolly, T.M.4
  • 205
    • 0029917707 scopus 로고    scopus 로고
    • The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain
    • Zhou, Q., Dangelmaier, C., Smith, J. B. The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain. Biochem. Biophys. Res. Commun., 1996, 19,720-726.
    • (1996) Biochem. Biophys. Res. Commun. , vol.19 , pp. 720-726
    • Zhou, Q.1    Dangelmaier, C.2    Smith, J.B.3
  • 206
    • 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
  • 207
    • 0031568217 scopus 로고    scopus 로고
    • Crovidisin, a collagen-binding protein isolated from snake venom of Crotalus viridis, prevents platelet-collagen interaction
    • Liu, C. Z., Huang, T. F. Crovidisin, a collagen-binding protein isolated from snake venom of Crotalus viridis, prevents platelet-collagen interaction. Arch. Biochem. Biophys., 1997, 337, 291-299.
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 291-299
    • Liu, C.Z.1    Huang, T.F.2
  • 209
    • 0028905848 scopus 로고
    • Expression of active recombinant pallidin, a novel platelet aggregation inhibitor, in the periplasm of Escherichia coli
    • Haendler, B., Becker, A., Noeske-Jungblut, C., Krätzschmar, J., Donner, P., Schleuning, W. D. Expression of active recombinant pallidin, a novel platelet aggregation inhibitor, in the periplasm of Escherichia coli. Biochem. J., 1995, 307, 465-470.
    • (1995) Biochem. J. , vol.307 , pp. 465-470
    • Haendler, B.1    Becker, A.2    Noeske-Jungblut, C.3    Krätzschmar, J.4    Donner, P.5    Schleuning, W.D.6
  • 210
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists
    • Jia, L. G., Wang, X. M., Shannon, J. D., Bjarnason, J. B., Fox, J. W. Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists. 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, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 211
    • 0001673324 scopus 로고    scopus 로고
    • Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin
    • Kamiguti, A. S., Moura da Silva, A. M., Laing, G. D., Knapp, T., Zuzel, M., Crampton, J. M., Theakston, R. D. Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin. Biochim. Biophys. Acta, 1997, 1335, 209-217.
    • (1997) Biochim. Biophys. Acta , vol.1335 , pp. 209-217
    • Kamiguti, A.S.1    Mourada Silva, A.M.2    Laing, G.D.3    Knapp, T.4    Zuzel, M.5    Crampton, J.M.6    Theakston, R.D.7
  • 212
    • 0029949611 scopus 로고    scopus 로고
    • 1-integrin by the snake venom metalloproteinase jararhagin
    • 1-integrin by the snake venom metalloproteinase jararhagin. Biochem. J., 1996, 320, 635-641.
    • (1996) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.2    Zuzel, M.3
  • 213
    • 0026102830 scopus 로고
    • Thrombin structure and function: Why thrombin is the primary target for antithrombotics
    • Fenton, J. W., Ofosu, F. A., Moon, D. G., Maraganore, J. M. Thrombin structure and function: why thrombin is the primary target for antithrombotics. Blood Coagul. Fibrinolysis, 1991, 2, 69-75.
    • (1991) Blood Coagul. Fibrinolysis , vol.2 , pp. 69-75
    • Fenton, J.W.1    Ofosu, F.A.2    Moon, D.G.3    Maraganore, J.M.4
  • 214
    • 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. Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: characterization and mechanism of thrombin inhibition. Biochemistry, 1993, 32, 10794-10802.
    • (1993) Biochemistry , vol.32 , pp. 10794-10802
    • Zingali, R.B.1    Jandrot-Perrus, M.2    Guillin, M.C.3    Bon, C.4
  • 215
    • 0032400791 scopus 로고    scopus 로고
    • Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus
    • Castro, H. C., Dutra, D. L., Oliveira-Carvalho, A. L., Zingali, R. B. Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus. Toxicon, 1998, 36, 1903-1912.
    • (1998) Toxicon , vol.36 , pp. 1903-1912
    • Castro, H.C.1    Dutra, D.L.2    Oliveira-Carvalho, A.L.3    Zingali, R.B.4
  • 217
  • 218
    • 0030837756 scopus 로고    scopus 로고
    • Inhibition of thrombin-mediated cellular effects by triabin, a highly potent anion-binding exosite thrombin inhibitor
    • Glusa, E., Bretschneider, E., Daum, J., Noeske-Jungblut, C. Inhibition of thrombin-mediated cellular effects by triabin, a highly potent anion-binding exosite thrombin inhibitor. Thromb. Haemost., 1997, 77, 1196-1200.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1196-1200
    • Glusa, E.1    Bretschneider, E.2    Daum, J.3    Noeske-Jungblut, C.4
  • 219
    • 0345493916 scopus 로고    scopus 로고
    • Allosteric changes of thrombin catalytic site induced by interaction of bothrojaracin with anion-binding exosites I and II
    • Monteiro, R. Q., Raposo, J. G., Wisner, A., Guimaraes, J. A., Bon, C., Zingali, R. B. Allosteric changes of thrombin catalytic site induced by interaction of bothrojaracin with anion-binding exosites I and II. Biochem. Biophys. Res. Commun., 1999, 262, 819-822.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 819-822
    • Monteiro, R.Q.1    Raposo, J.G.2    Wisner, A.3    Guimaraes, J.A.4    Bon, C.5    Zingali, R.B.6
  • 220
    • 0035743555 scopus 로고    scopus 로고
    • Interaction of bothrojaracin with prothrombin
    • Zingali, R. B., Bianconi, M. L., Monteiro, R. Q. Interaction of bothrojaracin with prothrombin. Haemostasis, 2001, 31 273-278.
    • (2001) Haemostasis , vol.31 , pp. 273-278
    • Zingali, R.B.1    Bianconi, M.L.2    Monteiro, R.Q.3
  • 221
    • 0030593658 scopus 로고    scopus 로고
    • Novel anti-platelet aggregation polypeptides from Vipera lebetina venom: Isolation and characterization
    • Barbouche, R., Marrakchi, N., Mansuelle, P., Krifi, M., Fenouillet, E., Rochat, H., El Ayeb, M. Novel anti-platelet aggregation polypeptides from Vipera lebetina venom: isolation and characterization. FEBS Lett., 1996, 392, 6-10.
    • (1996) FEBS Lett. , vol.392 , pp. 6-10
    • Barbouche, R.1    Marrakchi, N.2    Mansuelle, P.3    Krifi, M.4    Fenouillet, E.5    Rochat, H.6    El Ayeb, M.7
  • 222
    • 0032402121 scopus 로고    scopus 로고
    • Anti-platelet activity of the peptides composing the lebetin 1 family, a new class of inhibitors of platelet aggregation
    • Barbouche, R., Marrakchi, N., Mabrouk, K., Krifi, M. N., Van Rietschoten, J., Fenouillet, E., El Ayeb, M., Rochat, H. Anti-platelet activity of the peptides composing the lebetin 1 family, a new class of inhibitors of platelet aggregation. Toxicon, 1998. 36, 1939-1947.
    • (1998) Toxicon , vol.36 , pp. 1939-1947
    • Barbouche, R.1    Marrakchi, N.2    Mabrouk, K.3    Krifi, M.N.4    Van Rietschoten, J.5    Fenouillet, E.6    El Ayeb, M.7    Rochat, H.8
  • 225
    • 0021038657 scopus 로고
    • Inhibition of platelet aggregation by 5′-nucleotidase purified from Trimeresurus gramineus snake venom
    • Ouyang, C., Huang, T. F. Inhibition of platelet aggregation by 5′-nucleotidase purified from Trimeresurus gramineus snake venom. Toxicon, 1983, 21, 491-501.
    • (1983) Toxicon , vol.21 , pp. 491-501
    • Ouyang, C.1    Huang, T.F.2
  • 226
    • 0022998890 scopus 로고
    • Platelet aggregation inhibitors from Agkistrodon acutus snake venom
    • Ouyang, C., Huang, T. F. Platelet aggregation inhibitors from Agkistrodon acutus snake venom. Toxicon, 1986, 24 1099-1106.
    • (1986) Toxicon , vol.24 , pp. 1099-1106
    • Ouyang, C.1    Huang, T.F.2
  • 227
    • 0016148838 scopus 로고
    • Correlations between the enzymatic and factors active on blood coagulation and platelet aggregation from the venom of Vipera aspis
    • Boffa, M. C., Boffa, G. A. Correlations between the enzymatic and factors active on blood coagulation and platelet aggregation from the venom of Vipera aspis. Biochim. Biophys. Acta, 1974, 354 275-290.
    • (1974) Biochim. Biophys. Acta , vol.354 , pp. 275-290
    • Boffa, M.C.1    Boffa, G.A.2
  • 230
    • 0021077064 scopus 로고
    • A potent platelet aggregation inhibitor purified from Agkistrodon halys (mamushi) snake venom
    • Ouyang, C., Yeh, H. I., Huang, T. F. A potent platelet aggregation inhibitor purified from Agkistrodon halys (mamushi) snake venom. Toxicon, 1983, 21, 797-804.
    • (1983) Toxicon , vol.21 , pp. 797-804
    • Ouyang, C.1    Yeh, H.I.2    Huang, T.F.3
  • 231
    • 0023771337 scopus 로고
    • 2 isoenzymes, from Naja nigricollis venom
    • 2 isoenzymes, from Naja nigricollis venom. Thromb. Haemost., 1988, 60, 170-173.
    • (1988) Thromb. Haemost. , vol.60 , pp. 170-173
    • Kini, R.M.1    Evans, H.J.2
  • 234
    • 0017231072 scopus 로고
    • Fibrinogenolytic enzymes of Trimeresurus venom
    • Ouyang, C., Teng, C. M. Fibrinogenolytic enzymes of Trimeresurus venom. Biochim. Biophys. Acta, 1976, 420 298-308.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 298-308
    • Ouyang, C.1    Teng, C.M.2
  • 235
    • 0018742326 scopus 로고
    • Properties of fibrinogen degradation products produced by α- and β- fibrinogenases of Trimeresurus mucrosquamatus snake venom
    • Ouyang, C., Teng, C. M., Chen, Y. C. Properties of fibrinogen degradation products produced by α- and β- fibrinogenases of Trimeresurus mucrosquamatus snake venom. Toxicon, 1979, 17, 121-126.
    • (1979) Toxicon , vol.17 , pp. 121-126
    • Ouyang, C.1    Teng, C.M.2    Chen, Y.C.3
  • 236
    • 0025996086 scopus 로고
    • Inhibition of platelet aggregation by a fibrinogenase from Naja nigricollis venom is independent of fibrinogen degradation
    • Kini, R. M., Evans, H. J. Inhibition of platelet aggregation by a fibrinogenase from Naja nigricollis venom is independent of fibrinogen degradation. Biochim. Biophys. Acta, 1991, 1095 117-121.
    • (1991) Biochim. Biophys. Acta , vol.1095 , pp. 117-121
    • Kini, R.M.1    Evans, H.J.2
  • 237
    • 0027444873 scopus 로고
    • Antiplatelet protease, kistomin, selectively cleaves human platelet glycoprotein Ib
    • Huang, T. F., Chang, M. C., Teng, C. M. Antiplatelet protease, kistomin, selectively cleaves human platelet glycoprotein Ib. Biochim. Biophys. Acta, 1993, 1158, 293-299.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 293-299
    • Huang, T.F.1    Chang, M.C.2    Teng, C.M.3
  • 238
    • 0035657710 scopus 로고    scopus 로고
    • Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox
    • Wu, W. B., Peng, H. C., Huang, T. F. Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox. Thromb. Haemost., 2001, 86, 1501-1511.
    • (2001) Thromb. Haemost. , vol.86 , pp. 1501-1511
    • Wu, W.B.1    Peng, H.C.2    Huang, T.F.3
  • 239
    • 0032527059 scopus 로고    scopus 로고
    • Isolation, sequence analysis, and biological activity of atrolysin E/D the non-RGD disintegrin domain from Crotalus atrox venom
    • Shimokawa, K., Jia, L. G., Shannon, J. D., Fox, J. W. Isolation, sequence analysis, and biological activity of atrolysin E/D the non-RGD disintegrin domain from Crotalus atrox venom. Arch. Biochem. Biophys., 1998, 354, 239-246.
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 239-246
    • Shimokawa, K.1    Jia, L.G.2    Shannon, J.D.3    Fox, J.W.4
  • 240
    • 0035164296 scopus 로고    scopus 로고
    • Exogenous factors from animal sources that induce platelet aggregation
    • Chow, G., Kini, R. M. Exogenous factors from animal sources that induce platelet aggregation. Thrombos. Haemostas., 2001, 85, 177-178.
    • (2001) Thrombos. Haemostas. , vol.85 , pp. 177-178
    • Chow, G.1    Kini, R.M.2
  • 241
    • 0019212576 scopus 로고
    • Crotalocytin: Recognition and purification of a timber rattlesnake platelet aggregating protein
    • Schmaier, A. H., Claypool, W., Colman, R. W. Crotalocytin: recognition and purification of a timber rattlesnake platelet aggregating protein. Blood, 1980, 56, 1013-1019.
    • (1980) Blood , vol.56 , pp. 1013-1019
    • Schmaier, A.H.1    Claypool, W.2    Colman, R.W.3
  • 242
    • 0019171408 scopus 로고
    • Crotalocytin: Characterization of the timber rattlesnake platelet activating protein
    • Schmaier, A. H., Colman, R. W. Crotalocytin: characterization of the timber rattlesnake platelet activating protein. Blood, 1980, 56, 1020-1028.
    • (1980) Blood , vol.56 , pp. 1020-1028
    • Schmaier, A.H.1    Colman, R.W.2
  • 243
    • 0024367339 scopus 로고
    • Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombin
    • Hill-Eubanks, D. C., Parker, C. G., Lollar, P. Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombin. Proc. Natl. Acad. Sci. U. S. A., 1989, 86, 6508-6512.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6508-6512
    • Hill-Eubanks, D.C.1    Parker, C.G.2    Lollar, P.3
  • 244
    • 0017623226 scopus 로고
    • Thrombocytin - A novel platelet activating enzyme from Bothrops atrox venom
    • Niewiarowski, S., Kirby, E. P., Stocker, K. Thrombocytin - a novel platelet activating enzyme from Bothrops atrox venom. Thromb. Res., 1977, 10, 863-869.
    • (1977) Thromb. Res. , vol.10 , pp. 863-869
    • Niewiarowski, S.1    Kirby, E.P.2    Stocker, K.3
  • 245
    • 0018292828 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom. 1. Purification and characterization of the enzyme
    • Kirby, E. P., Niewiarowski, S., Stocker, K., Kettner, C., Shaw, E., Budzynski, T, M. Thrombocytin, a serine protease from Bothrops atrox venom. 1. Purification and characterization of the enzyme. Biochemistry, 1979, 18, 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    Budzynski, T.M.6
  • 246
    • 0018646786 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom. 2. Interaction with platelets and plasma-clotting factors
    • Niewiarowski, S., Kirby, E. P., Brudzynski, T. M., Stocker. K. Thrombocytin, a serine protease from Bothrops atrox venom. 2. Interaction with platelets and plasma-clotting factors. Biochemistry 1979, 18, 3570-3577.
    • (1979) Biochemistry , vol.18 , pp. 3570-3577
    • Niewiarowski, S.1    Kirby, E.P.2    Brudzynski, T.M.3    Stocker, K.4
  • 247
    • 0021319973 scopus 로고
    • Investigations on the effect of thrombocytin on platelets
    • Kubisz, P., Arabi, A., Seghier, F., Cronberg, S. Investigations on the effect of thrombocytin on platelets. Thromb. Res., 1984, 33, 225-227.
    • (1984) Thromb. Res. , vol.33 , pp. 225-227
    • Kubisz, P.1    Arabi, A.2    Seghier, F.3    Cronberg, S.4
  • 248
    • 0014854261 scopus 로고
    • Studies on a procoagulant fraction of southern copperhead snake venom: The preferential release of fibrinopeptide B
    • Herzig, R. H., Ratnoff, O. D., Shainoff, J, R. Studies on a procoagulant fraction of southern copperhead snake venom: the preferential release of fibrinopeptide B. J. Lab. Clin. Med., 1970, 76, 451-465.
    • (1970) J. Lab. Clin. Med. , vol.76 , pp. 451-465
    • Herzig, R.H.1    Ratnoff, O.D.2    Shainoff, J.R.3
  • 249
    • 0013847362 scopus 로고
    • Actions of some coagulant snake venom on blood platelets
    • Davey, M. G., Luscher, E. F. Actions of some coagulant snake venom on blood platelets. Nature, 1965, 207, 730-732.
    • (1965) Nature , vol.207 , pp. 730-732
    • Davey, M.G.1    Luscher, E.F.2
  • 250
    • 0031831363 scopus 로고    scopus 로고
    • Severe coagulopathy after a bite of a green bush viper (Atheris squamiger): Case report and biochemical analysis of the venom
    • Mebs, D., Holada, K., Kornalik, F., Simak, J., Vanková, H., Muller, D., Schoenemann, H., Lange, H., Herrmann, H. W. Severe coagulopathy after a bite of a green bush viper (Atheris squamiger : case report and biochemical analysis of the venom. Toxicon, 1998, 36, 1333-1340.
    • (1998) Toxicon , vol.36 , pp. 1333-1340
    • Mebs, D.1    Holada, K.2    Kornalik, F.3    Simak, J.4    Vanková, H.5    Muller, D.6    Schoenemann, H.7    Lange, H.8    Herrmann, H.W.9
  • 251
    • 0016170422 scopus 로고
    • Effects of puff-adder venom on coagulation, fibrinolysis and platelet aggregation in the baboon
    • Brink, S., Steytler, J. G. Effects of puff-adder venom on coagulation, fibrinolysis and platelet aggregation in the baboon. S. Afr. Med. J., 1974, 48, 1205-1213.
    • (1974) S. Afr. Med. J. , vol.48 , pp. 1205-1213
    • Brink, S.1    Steytler, J.G.2
  • 252
    • 0015883752 scopus 로고
    • Effects of puff adder venom on the coagulation mechanism. I. In vivo
    • Phillips, L. L., Weiss, H. J., Pessar, L., Christy, N. P. Effects of puff adder venom on the coagulation mechanism. I. In vivo. Toxicon, 1973, 11, 423-431.
    • (1973) Toxicon , vol.11 , pp. 423-431
    • Phillips, L.L.1    Weiss, H.J.2    Pessar, L.3    Christy, N.P.4
  • 253
    • 0015743161 scopus 로고
    • Effects of puff adder venom on the coagulation mechanism. II. In vitro
    • Phillips, L. L., Weiss, H. J., Christy, N. P. Effects of puff adder venom on the coagulation mechanism. II. In vitro. Thromb. Diath. Haemorrh., 1973, 30, 499-508.
    • (1973) Thromb. Diath. Haemorrh. , vol.30 , pp. 499-508
    • Phillips, L.L.1    Weiss, H.J.2    Christy, N.P.3
  • 254
    • 0014899318 scopus 로고
    • Effects of the venom of the rhinoceros horned viper (Bitis nasicornis) on blood coagulation, platelet aggregation, andfibrinolysis
    • MacKay, N., Ferguson, J. C., McNicol, G. P. Effects of the venom of the rhinoceros horned viper (Bitis nasicornis) on blood coagulation, platelet aggregation, andfibrinolysis. J. Clin. Pathol. 1970, 23, 789-796.
    • (1970) J. Clin. Pathol. , vol.23 , pp. 789-796
    • MacKay, N.1    Ferguson, J.C.2    McNicol, G.P.3
  • 255
    • 0020066792 scopus 로고
    • Envenomation by the Northern black tail rattlesnake (Crotalus molossus molossus): Report of two cases and the in vitro effects of the venom on fibrinolysis and platelet aggregation
    • Hardy, D. L., Jeter, M., Corrigan, J. J., Jr., Envenomation by the Northern black tail rattlesnake (Crotalus molossus molossus : report of two cases and the in vitro effects of the venom on fibrinolysis and platelet aggregation. Toxicon, 1982, 20 487-493.
    • (1982) Toxicon , vol.20 , pp. 487-493
    • Hardy, D.L.1    Jeter, M.2    Corrigan Jr., J.J.3
  • 256
    • 0024373025 scopus 로고
    • Australian snake venoms and their in vitro effect on human platelets
    • Marshall, L. R., Herrmann, R. P. Australian snake venoms and their in vitro effect on human platelets. Thromb. Res., 1989, 54, 269-275.
    • (1989) Thromb. Res. , vol.54 , pp. 269-275
    • Marshall, L.R.1    Herrmann, R.P.2
  • 257
    • 0015690903 scopus 로고
    • Effects of green pit viper (Trimeresurus erythrurus and Trimeresurus popeorum) venoms on blood coagulation, platelets and the fibrinolytic enzyme systems: Studies in vivo and in vitro
    • Mitrakul, C. Effects of green pit viper (Trimeresurus erythrurus and Trimeresurus popeorum) venoms on blood coagulation, platelets and the fibrinolytic enzyme systems: studies in vivo and in vitro. Am. J. Clin. Pathol., 1973, 60, 654-662.
    • (1973) Am. J. Clin. Pathol. , vol.60 , pp. 654-662
    • Mitrakul, C.1
  • 258
    • 0022735702 scopus 로고
    • Biological properties of the venom of the red-necked keel-back snake (Rhabdophis subminiatus)
    • Iddon, D., Theakston, R. D. Biological properties of the venom of the red-necked keel-back snake (Rhabdophis subminiatus). Ann. Trop. Med. Parasitol., 1986, 80, 339-344.
    • (1986) Ann. Trop. Med. Parasitol. , vol.80 , pp. 339-344
    • Iddon, D.1    Theakston, R.D.2
  • 259
    • 0025333470 scopus 로고
    • Elegantin and albolabrin purified peptides from viper venoms: Homologies with the RGDS domain of fibrinogen and von Willebrand factor
    • Williams, J, Rucinski, B., Holt, J., Niewiarowski, S. Elegantin and albolabrin purified peptides from viper venoms: homologies with the RGDS domain of fibrinogen and von Willebrand factor. Biochim. Biophys. Acta, 1990, 1039, 81-89.
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 81-89
    • Williams, J.1    Rucinski, B.2    Holt, J.3    Niewiarowski, S.4
  • 261
    • 0025290037 scopus 로고
    • Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb-IIIa complex inhibits receptor function
    • Savage, B., Marzec, U. M., Chao, B. H., Harker, L. A., Maraganore, J. M., Ruggeri, Z. M. Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb-IIIa complex inhibits receptor function. J. Biol. Chem., 1990, 265, 11766-11772.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11766-11772
    • Savage, B.1    Marzec, U.M.2    Chao, B.H.3    Harker, L.A.4    Maraganore, J.M.5    Ruggeri, Z.M.6
  • 262
    • 0025753506 scopus 로고
    • Purification and characterization of an antiplatelet peptide, arietin, from Bitis arietans venom
    • Huang, T. F., Wang, W. J., Teng, C. M., Liu, C. S., Ouyang, C. Purification and characterization of an antiplatelet peptide, arietin, from Bitis arietans venom. Biochim. Biophys. Acta, 1991 1074, 136-143.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 136-143
    • Huang, T.F.1    Wang, W.J.2    Teng, C.M.3    Liu, C.S.4    Ouyang, C.5
  • 263
    • 0025804870 scopus 로고
    • Mechanism of action of the antiplatelet peptide, arietin, from Bitis arietans venom
    • Huang, T. F., Wang, W. J., Teng, C. M., Ouyang, C. Mechanism of action of the antiplatelet peptide, arietin, from Bitis arietans venom. Biochim. Biophys. Acta, 1991, 1074, 144-150.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 144-150
    • Huang, T.F.1    Wang, W.J.2    Teng, C.M.3    Ouyang, C.4
  • 264
    • 0024997061 scopus 로고
    • Batroxostatin, an Arg-Gly-Asp-containing peptide from Bothrops atrox, is a potent inhibitor of platelet aggregation and cell interaction with fibronectin
    • Rucinski, B., Niewiarowski, S., Holt, J. C., Soszka, T., Knudsen, K. A. Batroxostatin, an Arg-Gly-Asp-containing peptide from Bothrops atrox, is a potent inhibitor of platelet aggregation and cell interaction with fibronectin. Biochim. Biophys. Acta, 1990, 1054, 257-262.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 257-262
    • Rucinski, B.1    Niewiarowski, S.2    Holt, J.C.3    Soszka, T.4    Knudsen, K.A.5
  • 266
    • 0024852988 scopus 로고
    • Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans
    • Shebuski, R. J., Ramjit, D. R., Bencen, G. H., Polokoff, M. A. Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans. J. Biol. Chem., 1989, 264, 21550-21556.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21550-21556
    • Shebuski, R.J.1    Ramjit, D.R.2    Bencen, G.H.3    Polokoff, M.A.4
  • 267
    • 0031018096 scopus 로고    scopus 로고
    • Cerastatin, a new potent inhibitor of platelet aggregation from the venom of the Tunisian viper, Cerastes cerastes
    • Marrakchi, N., Barbouche, R., Bon, C., El Ayeb, M. Cerastatin, a new potent inhibitor of platelet aggregation from the venom of the Tunisian viper, Cerastes cerastes. Toxicon, 1997, 35, 125-135.
    • (1997) Toxicon , vol.35 , pp. 125-135
    • Marrakchi, N.1    Barbouche, R.2    Bon, C.3    El Ayeb, M.4
  • 268
    • 0028880595 scopus 로고
    • Crotavirin, a potent platelet aggregation inhibitor purified from the venom of the snake Crotalus viridis
    • Liu, C. Z., Peng, H. C., Huang, T. F. Crotavirin, a potent platelet aggregation inhibitor purified from the venom of the snake Crotalus viridis. Toxicon, 1995, 33, 1289-1298.
    • (1995) Toxicon , vol.33 , pp. 1289-1298
    • Liu, C.Z.1    Peng, H.C.2    Huang, T.F.3
  • 269
    • 0028168017 scopus 로고
    • Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets
    • McLane, M. A., Kowalska, M. A., Silver, L., Shattil, S. J., Niewiarowski, S. Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets. Biochem. J., 1994, 301, 429-436.
    • (1994) Biochem. J. , vol.301 , pp. 429-436
    • McLane, M.A.1    Kowalska, M.A.2    Silver, L.3    Shattil, S.J.4    Niewiarowski, S.5
  • 270
    • 0028817868 scopus 로고
    • A comparison of the effect of decorsin and two disintegrins, albolabrin and eristostatin, on platelet function
    • McLane, M. A., Gabbeta, J., Rao, A. K., Beviglia, L., Lazarus, R. A., Niewiarowski, S. A comparison of the effect of decorsin and two disintegrins, albolabrin and eristostatin, on platelet function. Thromb. Haemost., 1995, 74, 1316-1322.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1316-1322
    • McLane, M.A.1    Gabbeta, J.2    Rao, A.K.3    Beviglia, L.4    Lazarus, R.A.5    Niewiarowski, S.6
  • 272
    • 0030995291 scopus 로고    scopus 로고
    • Isolation and amino acid sequence of flavostatin, a novel disintegrin from the venom of Trimeresurus flavoviridis
    • Maruyama, K., Kawasaki, T., Sakai, Y., Taniuchi, Y., Shimizu, M., Kawashima, H., Takenaka, T. Isolation and amino acid sequence of flavostatin, a novel disintegrin from the venom of Trimeresurus flavoviridis. Peptides, 1997, 18, 73-78.
    • (1997) Peptides , vol.18 , pp. 73-78
    • Maruyama, K.1    Kawasaki, T.2    Sakai, Y.3    Taniuchi, Y.4    Shimizu, M.5    Kawashima, H.6    Takenaka, T.7
  • 274
    • 0025880046 scopus 로고
    • Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist
    • Huang, T. F., Liu, C. Z., Ouyang, C. H., Teng, C. M. Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist. Biochem. Pharmacol., 1991, 42, 1209-1219.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1209-1219
    • Huang, T.F.1    Liu, C.Z.2    Ouyang, C.H.3    Teng, C.M.4
  • 275
    • 0027954377 scopus 로고
    • Purification and characterization of platelet aggregation inhibitors from snake venoms
    • Trikha, M., Rote, W. E., Manley, P. J., Lucchesi, B. R., Markland, F. S. Purification and characterization of platelet aggregation inhibitors from snake venoms. Thromb. Res., 1994, 73, 39-52.
    • (1994) Thromb. Res. , vol.73 , pp. 39-52
    • Trikha, M.1    Rote, W.E.2    Manley, P.J.3    Lucchesi, B.R.4    Markland, F.S.5
  • 276
    • 0032527808 scopus 로고    scopus 로고
    • Purification and molecular cloning of a platelet aggregation inhibitor from the snake (Agkistrodon halys brevicaudus) venom
    • Kang, I. C., Chung, K. H., Lee, S. J., Yuri, Y., Moon, H. M., Kim, D. S. Purification and molecular cloning of a platelet aggregation inhibitor from the snake (Agkistrodon halys brevicaudus) venom. Thromb. Res., 1998, 91, 65-73.
    • (1998) Thromb. Res. , vol.91 , pp. 65-73
    • Kang, I.C.1    Chung, K.H.2    Lee, S.J.3    Yuri, Y.4    Moon, H.M.5    Kim, D.S.6
  • 277
    • 0032585108 scopus 로고    scopus 로고
    • Cloning and characterization of novel disintegrins from Agkistrodon halys venom
    • Park, D., Kang, I., Kim, H., Chung, K., Kim, D. S., Yun, Y. Cloning and characterization of novel disintegrins from Agkistrodon halys venom. Mol. Cells, 1998, 8, 578-584.
    • (1998) Mol. Cells , vol.8 , pp. 578-584
    • Park, D.1    Kang, I.2    Kim, H.3    Chung, K.4    Kim, D.S.5    Yun, Y.6
  • 278
    • 0025861078 scopus 로고
    • A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom
    • Huang, T. F., Sheu, J. R., Teng, C. M. A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom. Biochem. J., 1991, 277, 351-357.
    • (1991) Biochem. J. , vol.277 , pp. 351-357
    • Huang, T.F.1    Sheu, J.R.2    Teng, C.M.3
  • 279
    • 0026099011 scopus 로고
    • Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex
    • Huang, T. F., Sheu, J. R., Teng, C. M., Chen, S. W., Liu, C. S. Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex. J. Biochem., 1991, 109, 328-334.
    • (1991) J. Biochem. , vol.109 , pp. 328-334
    • Huang, T.F.1    Sheu, J.R.2    Teng, C.M.3    Chen, S.W.4    Liu, C.S.5
  • 280
    • 0023639428 scopus 로고
    • Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex
    • Huang, T. F., Holt, J. C., Lukasiewicz, H., Niewiarowski, S. Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. J. Biol. Chem., 1987, 262, 16157-16163.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16157-16163
    • Huang, T.F.1    Holt, J.C.2    Lukasiewicz, H.3    Niewiarowski, S.4
  • 281
    • 0027958796 scopus 로고
    • Characterization of a cDNA encoding the precursor of platelet aggregation inhibition and metalloproteinase from Trimeresurus mucrosquamatus venom
    • Tsai, I. H., Wang, Y. M., Lee, Y. H. Characterization of a cDNA encoding the precursor of platelet aggregation inhibition and metalloproteinase from Trimeresurus mucrosquamatus venom. Biochim. Biophys. Acta, 1994, 1200, 337-340.
    • (1994) Biochim. Biophys. Acta , vol.1200 , pp. 337-340
    • Tsai, I.H.1    Wang, Y.M.2    Lee, Y.H.3
  • 282
    • 0023651330 scopus 로고
    • Characterization of a potent platelet aggregation inhibitor from Agkistrodon rhodostoma snake venom
    • Huang, T. F., Wu, Y. J., Ouyang, C. Characterization of a potent platelet aggregation inhibitor from Agkistrodon rhodostoma snake venom. Biochim. Biophys. Acta, 1987, 925, 248-257.
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 248-257
    • Huang, T.F.1    Wu, Y.J.2    Ouyang, C.3
  • 283
    • 0027423538 scopus 로고
    • Salivary gland extracts from the deerfly contain a potent inhibitor of platelet aggregation
    • Grevelink, S. A., Youssef, D. E., Loscalzo, J., Lerner, E. A. Salivary gland extracts from the deerfly contain a potent inhibitor of platelet aggregation. Proc. Natl. Acad. Sci. U. S. A., 1993, 90, 9155-9158.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9155-9158
    • Grevelink, S.A.1    Youssef, D.E.2    Loscalzo, J.3    Lerner, E.A.4
  • 284
    • 4243844689 scopus 로고
    • Purification and characterization of potent inhibitors of von Willebrand factor binding to glycoprotein (GP) 1b from the venom of timber rattlesnake, Crotalus h. horridus
    • Scarborough, R. M., Hsu, M. A., Teng, W., Nannizzi, L., Rose, J. W. Purification and characterization of potent inhibitors of von Willebrand factor binding to glycoprotein (GP) 1b from the venom of timber rattlesnake, Crotalus h. horridus. Blood, 1991, 78 1568.
    • (1991) Blood , vol.78 , pp. 1568
    • Scarborough, R.M.1    Hsu, M.A.2    Teng, W.3    Nannizzi, L.4    Rose, J.W.5
  • 285
    • 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. 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., 1996, 271, 10635-10639.
    • (1996) J. Biol. Chem. , vol.271 , 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
  • 286
    • 0032526556 scopus 로고    scopus 로고
    • Purification, characterization, and amino acid sequence determination of acanthins, potent inhibitors of platelet aggregation from Acanthophis antarcticus (common death adder) venom
    • Chow, G., Subburaju, S., Kini, R. M. Purification, characterization, and amino acid sequence determination of acanthins, potent inhibitors of platelet aggregation from Acanthophis antarcticus (common death adder) venom. Arch. Biochem. Biophys., 1998, 354, 232-238.
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 232-238
    • Chow, G.1    Subburaju, S.2    Kini, R.M.3
  • 287
    • 0032472768 scopus 로고    scopus 로고
    • Purification and preliminary characterisation of praelongin phospholipases, antiplatelet agents from the snake venom of Acanthophis praelongus
    • Sim, K. L. Purification and preliminary characterisation of praelongin phospholipases, antiplatelet agents from the snake venom of Acanthophis praelongus. Biochim. Biophys. Acta, 1998, 1379 198-206.
    • (1998) Biochim. Biophys. Acta , vol.1379 , pp. 198-206
    • Sim, K.L.1
  • 288
    • 0021332353 scopus 로고
    • Mechanism of action of the platelet aggregation inhibitor purified from Agkistrodon halys (mamushi) snake venom
    • Huang, T. F., Yeh, H. I., Ouyang, C. Mechanism of action of the platelet aggregation inhibitor purified from Agkistrodon halys (mamushi) snake venom. Toxicon, 1984, 22, 243-251.
    • (1984) Toxicon , vol.22 , pp. 243-251
    • Huang, T.F.1    Yeh, H.I.2    Ouyang, C.3
  • 291
    • 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. Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects. Toxicon, 1997, 35, 1239-1250.
    • (1997) Toxicon , vol.35 , pp. 1239-1250
    • Subburaju, S.1    Kini, R.M.2
  • 292
    • 0034653921 scopus 로고    scopus 로고
    • 2 with platelet aggregation inhibitor activity from Austrelaps superbus venom: Protein purification and cDNA cloning
    • 2 with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning. Arch. Biochem. Biophys., 2000, 375, 289-303.
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 289-303
    • Singh, B.S.1    Armugam, A.2    Kini, R.M.3    Jeyaseelan, K.4
  • 297
    • 0020632120 scopus 로고
    • Potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom
    • Ouyang, C., Huang, T. F. Potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom. Biochim. Biophys. Acta, 1983, 757, 332-341.
    • (1983) Biochim. Biophys. Acta , vol.757 , pp. 332-341
    • Ouyang, C.1    Huang, T.F.2
  • 298
    • 0021319204 scopus 로고
    • Action mechanism of the potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom
    • Huang, T. F., Ouyang, C. Action mechanism of the potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom. Thromb. Res., 1984, 33, 125-138.
    • (1984) Thromb. Res. , vol.33 , pp. 125-138
    • Huang, T.F.1    Ouyang, C.2
  • 300
    • 0029914764 scopus 로고    scopus 로고
    • A platelet aggregation inhibitor phospholipase A'2 from Russell's viper (Vipera russelli) venom: Isolation and characterization
    • Prasad, B. N., Kemparaju, K., Bhatt, K. G., Gowda, T. V. A platelet aggregation inhibitor phospholipase A'2 from Russell's viper ( Vipera russelli) venom: isolation and characterization. Toxicon, 1996, 34, 1173-1185.
    • (1996) Toxicon , vol.34 , pp. 1173-1185
    • Prasad, B.N.1    Kemparaju, K.2    Bhatt, K.G.3    Gowda, T.V.4
  • 301
    • 0022412464 scopus 로고
    • A platelet function inhibitor purified from Vipera russelli siamensis (Smith) snake venom
    • Li, Y. S., Liu, K. F., Wang, Q. C., Ran, Y. L., Tu, G. C. A platelet function inhibitor purified from Vipera russelli siamensis (Smith) snake venom. Toxicon, 1985, 23, 895-903.
    • (1985) Toxicon , vol.23 , pp. 895-903
    • Li, Y.S.1    Liu, K.F.2    Wang, Q.C.3    Ran, Y.L.4    Tu, G.C.5
  • 302
    • 0023001103 scopus 로고
    • Mechanism of action of the platelet function inhibitor from Vipera russelli siamensis snake venom
    • Li, Y. S., Liu, K. F., Wang, Q. C. Mechanism of action of the platelet function inhibitor from Vipera russelli siamensis snake venom. Toxicon, 1986, 24, 875-883.
    • (1986) Toxicon , vol.24 , pp. 875-883
    • Li, Y.S.1    Liu, K.F.2    Wang, Q.C.3
  • 303
    • 0027980074 scopus 로고
    • 2 purified from Heloderma horridum (beaded lizard) venom
    • 2 purified from Heloderma horridum (beaded lizard) venom. Biochim. Biophys. Acta, 1994, 1211 61-68.
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 61-68
    • Huang, T.F.1    Chiang, H.S.2
  • 304
    • 0020596757 scopus 로고
    • α-Fibrogenase from Agkistrodon rhodostoma (Malayan pit viper) snake venom
    • Ouyang, C., Hwang, L. J., Huang, T. F. α-Fibrogenase from Agkistrodon rhodostoma (Malayan pit viper) snake venom. Toxicon, 1983, 21, 25-33.
    • (1983) Toxicon , vol.21 , pp. 25-33
    • Ouyang, C.1    Hwang, L.J.2    Huang, T.F.3
  • 305
    • 0022366055 scopus 로고
    • Inhibition of rabbit platelet aggregation by α-fibrogenase purified from Calloselasma rhodostoma (Malayan pit viper) venom
    • Ouyang, C., Hwang, L. J., Huang, T. F. Inhibition of rabbit platelet aggregation by α-fibrogenase purified from Calloselasma rhodostoma (Malayan pit viper) venom. J. Formosan. Med. Assoc., 1985, 84, 1197-1206.
    • (1985) J. Formosan. Med. Assoc. , vol.84 , pp. 1197-1206
    • Ouyang, C.1    Hwang, L.J.2    Huang, T.F.3
  • 306
    • 0017348382 scopus 로고
    • Physicochemical properties of α- and β-fibrinogenases of Trimeresurus mucrosquamatus venom
    • Ouyang, C., Teng, C. M., Chen, Y. C. Physicochemical properties of α- and β-fibrinogenases of Trimeresurus mucrosquamatus venom. Biochim. Biophys. Acta, 1977, 481, 622-630.
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 622-630
    • Ouyang, C.1    Teng, C.M.2    Chen, Y.C.3
  • 307
    • 0025832323 scopus 로고
    • Purification and characterization of a fibrinogenase from Vipera lebetina (desert adder) venom
    • Gasmi, A., Karoui, M., Benlasfar, Z., Karoui, H., El Ayeb, M., Dellagi, K. Purification and characterization of a fibrinogenase from Vipera lebetina (desert adder) venom. Toxicon, 1991, 29, 827-836.
    • (1991) Toxicon , vol.29 , pp. 827-836
    • Gasmi, A.1    Karoui, M.2    Benlasfar, Z.3    Karoui, H.4    El Ayeb, M.5    Dellagi, K.6
  • 308
    • 0010301339 scopus 로고
    • Effect of a fibrinogenase from Vipera lebetina venom on human blood coagulation factors and platelets
    • Gasmi, A., Guermazi, S., Chabchoub, A., Makni, K., Karoui, H., El Ayeb, M., Dellagi, K. Effect of a fibrinogenase from Vipera lebetina venom on human blood coagulation factors and platelets. Toxicon, 1993, 31, 520.
    • (1993) Toxicon , vol.31 , pp. 520
    • Gasmi, A.1    Guermazi, S.2    Chabchoub, A.3    Makni, K.4    Karoui, H.5    El Ayeb, M.6    Dellagi, K.7
  • 309
    • 0027978509 scopus 로고
    • Properties of fibrinogen cleaved by Jararhagin, a metalloproteinase from the venom of Bothrops jararaca
    • Kamiguti, A. S., Slupsky, J. R., Zuzel, M., Hay, C. R. Properties of fibrinogen cleaved by Jararhagin, a metalloproteinase from the venom of Bothrops jararaca. Thromb. Haemost., 1994, 72 244-249.
    • (1994) Thromb. Haemost. , vol.72 , pp. 244-249
    • Kamiguti, A.S.1    Slupsky, J.R.2    Zuzel, M.3    Hay, C.R.4
  • 310
    • 0027053899 scopus 로고
    • A novel α-type fibrinogenase from Agkistrodon rhodostoma snake venom
    • Huang, T. F., Chang, M. C., Peng, H. C., Teng, C. M. A novel α-type fibrinogenase from Agkistrodon rhodostoma snake venom. Biochim. Biophys. Acta, 1992, 1160, 262-268.
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 262-268
    • Huang, T.F.1    Chang, M.C.2    Peng, H.C.3    Teng, C.M.4
  • 311
    • 0028836750 scopus 로고
    • Purification and characterization of a non-hemorrhagic metalloproteinase from Agkistrodon halys brevicaudus venom
    • Fujimura, S., Rikimara, T., Baba, S., Hori, J., Hao, X. Q., Terada, S., Kimoto, E. Purification and characterization of a non-hemorrhagic metalloproteinase from Agkistrodon halys brevicaudus venom. Biochim. Biophys. Acta, 1995, 1243, 94-100.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 94-100
    • Fujimura, S.1    Rikimara, T.2    Baba, S.3    Hori, J.4    Hao, X.Q.5    Terada, S.6    Kimoto, E.7
  • 312
    • 0021687769 scopus 로고
    • Purification and properties of a fibrinogenase from the venom of Naja nigricollis
    • Evans, H. J. Purification and properties of a fibrinogenase from the venom of Naja nigricollis. Biochim. Biophys. Acta, 1984 802, 49-54.
    • (1984) Biochim. Biophys. Acta , vol.802 , pp. 49-54
    • Evans, H.J.1
  • 313
    • 0029105096 scopus 로고
    • Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen
    • Zhou, Q., Smith, J. B., Grossman, M. H. Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem. J., 1995, 307, 411-417.
    • (1995) Biochem. J. , vol.307 , pp. 411-417
    • Zhou, Q.1    Smith, J.B.2    Grossman, M.H.3
  • 314
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.