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Volumn 59, Issue 4, 2012, Pages 497-506

From snake venom toxins to therapeutics - Cardiovascular examples

Author keywords

Anti cancer; Anti hypertensive agents; Antithrombotic agents; Drug design; Drug discovery; Toxins to drugs; Toxins to therapeutics

Indexed keywords

ALFIMEPRASE; ANCROD; BATROXOBIN; BRADYKININ; CALCISEPTINE; CALCIUM CHANNEL L TYPE; CAPTOPRIL; CONTORTROSTATIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; DISINTEGRIN; EPTIFIBATIDE; FIBRINOGEN; NATRIURETIC FACTOR; NESIRITIDE; NIFEDIPINE; SNAKE VENOM; TEPROTIDE; THROMBIN; TIROFIBAN; TRIFLAVIN;

EID: 80053639612     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2011.03.017     Document Type: Review
Times cited : (163)

References (139)
  • 3
    • 0020063851 scopus 로고
    • Thrombin-like and fibrinolytic enzymes in the venoms from the Gaboon viper (Bitis gabonica), eastern cottonmouth moccasin (Agkistrodon p. piscivorus) and southern copperhead (Agkistrodon c. contortrix) snakes
    • Bajwa S.S., Kirakossian H., Reddy K.N., Markland F.S. Thrombin-like and fibrinolytic enzymes in the venoms from the Gaboon viper (Bitis gabonica), eastern cottonmouth moccasin (Agkistrodon p. piscivorus) and southern copperhead (Agkistrodon c. contortrix) snakes. Toxicon 1982, 20:427-432.
    • (1982) Toxicon , vol.20 , pp. 427-432
    • Bajwa, S.S.1    Kirakossian, H.2    Reddy, K.N.3    Markland, F.S.4
  • 5
    • 0037271306 scopus 로고    scopus 로고
    • Scientific and therapeutic advances in antiplatelet therapy
    • Bhatt D.L., Topol E.J. Scientific and therapeutic advances in antiplatelet therapy. Nat. Rev. Drug Discov. 2003, 2:15-28.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 15-28
    • Bhatt, D.L.1    Topol, E.J.2
  • 6
    • 0029795769 scopus 로고    scopus 로고
    • The rationale for thrombolytic therapy
    • Califf R.M. The rationale for thrombolytic therapy. Eur. Heart J. 1996, 17(Suppl. E):2-8.
    • (1996) Eur. Heart J. , vol.17 , Issue.SUPPL. E , pp. 2-8
    • Califf, R.M.1
  • 7
    • 0037065736 scopus 로고    scopus 로고
    • The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3, and alpha5beta1 integrins
    • Calvete J.J., Fox J.W., Agelan A., Niewiarowski S., Marcinkiewicz C. The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3, and alpha5beta1 integrins. Biochemistry 2002, 41:2014-2021.
    • (2002) Biochemistry , vol.41 , pp. 2014-2021
    • Calvete, J.J.1    Fox, J.W.2    Agelan, A.3    Niewiarowski, S.4    Marcinkiewicz, C.5
  • 10
    • 0037130758 scopus 로고    scopus 로고
    • Natriuretic peptide receptors and neutral endopeptidase in mediating the renal actions of a new therapeutic synthetic natriuretic peptide dendroaspis natriuretic peptide
    • Chen H.H., Lainchbury J.G., Burnett J.C. Natriuretic peptide receptors and neutral endopeptidase in mediating the renal actions of a new therapeutic synthetic natriuretic peptide dendroaspis natriuretic peptide. J. Am. Coll. Cardiol. 2002, 40:1186-1191.
    • (2002) J. Am. Coll. Cardiol. , vol.40 , pp. 1186-1191
    • Chen, H.H.1    Lainchbury, J.G.2    Burnett, J.C.3
  • 11
    • 0026322267 scopus 로고
    • Proton NMR assignments and secondary structure of the snake venom protein echistatin
    • Chen Y., Pitzenberger S.M., Garsky V.M., Lumma P.K., Sanyal G., Baum J. Proton NMR assignments and secondary structure of the snake venom protein echistatin. Biochemistry 1991, 30:11625-11636.
    • (1991) Biochemistry , vol.30 , pp. 11625-11636
    • Chen, Y.1    Pitzenberger, S.M.2    Garsky, V.M.3    Lumma, P.K.4    Sanyal, G.5    Baum, J.6
  • 12
    • 0022392041 scopus 로고
    • Structure-function studies on the bradykinin potentiating peptide from Chinese snake venom (Agkistrodon halys Pallas)
    • Chi C.W., Wang S.Z., Xu L.G., Wang M.Y., Lo S.S., Huang W.D. Structure-function studies on the bradykinin potentiating peptide from Chinese snake venom (Agkistrodon halys Pallas). Peptides 1985, 6(Suppl. 3):339-342.
    • (1985) Peptides , vol.6 , Issue.SUPPL. 3 , pp. 339-342
    • Chi, C.W.1    Wang, S.Z.2    Xu, L.G.3    Wang, M.Y.4    Lo, S.S.5    Huang, W.D.6
  • 13
    • 0028037889 scopus 로고
    • Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation
    • Clark E.A., Trikha M., Markland F.S., Brugge J.S. Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation. J. Biol. Chem. 1994, 269:21940-21943.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21940-21943
    • Clark, E.A.1    Trikha, M.2    Markland, F.S.3    Brugge, J.S.4
  • 14
    • 42249105887 scopus 로고    scopus 로고
    • Platelet GPIb complex as a target for anti-thrombotic drug development
    • Clemetson K.J., Clemetson J.M. Platelet GPIb complex as a target for anti-thrombotic drug development. Thromb. Haemost 2008, 99:473-479.
    • (2008) Thromb. Haemost , vol.99 , pp. 473-479
    • Clemetson, K.J.1    Clemetson, J.M.2
  • 15
    • 38449104060 scopus 로고    scopus 로고
    • Snake venom proteins affecting platelets and their applications to anti-thrombotic research
    • Clemetson K.J., Lu Q., Clemetson J.M. Snake venom proteins affecting platelets and their applications to anti-thrombotic research. Curr. Pharm. Des 2007, 13:2887-2892.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2887-2892
    • Clemetson, K.J.1    Lu, Q.2    Clemetson, J.M.3
  • 17
    • 0025881724 scopus 로고
    • History of the design of captopril and related inhibitors of angiotensin converting enzyme
    • Cushman D.W., Ondetti M.A. History of the design of captopril and related inhibitors of angiotensin converting enzyme. Hypertension 1991, 17:589-592.
    • (1991) Hypertension , vol.17 , pp. 589-592
    • Cushman, D.W.1    Ondetti, M.A.2
  • 18
    • 0032828165 scopus 로고    scopus 로고
    • Design of angiotensin converting enzyme inhibitors
    • Cushman D.W., Ondetti M.A. Design of angiotensin converting enzyme inhibitors. Nat. Med. 1999, 5:1110-1113.
    • (1999) Nat. Med. , vol.5 , pp. 1110-1113
    • Cushman, D.W.1    Ondetti, M.A.2
  • 21
    • 0026337077 scopus 로고
    • The coagulation cascade: initiation, maintenance, and regulation
    • Davie E.W., Fujikawa K., Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991, 30:10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 22
    • 0019352579 scopus 로고
    • A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats
    • de Bold A.J., Borenstein H.B., Veress A.T., Sonnenberg H. A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats. Life Sci. 1981, 28:89-94.
    • (1981) Life Sci. , vol.28 , pp. 89-94
    • de Bold, A.J.1    Borenstein, H.B.2    Veress, A.T.3    Sonnenberg, H.4
  • 23
    • 0025759993 scopus 로고
    • The hypotensive activity of Crotalus atrox (western diamondback rattlesnake) venom: identification of its origin
    • de Mesquita L.C., Selistre H.S., Giglio J.R. The hypotensive activity of Crotalus atrox (western diamondback rattlesnake) venom: identification of its origin. Am. J. Trop. Med. Hyg. 1991, 44:345-353.
    • (1991) Am. J. Trop. Med. Hyg. , vol.44 , pp. 345-353
    • de Mesquita, L.C.1    Selistre, H.S.2    Giglio, J.R.3
  • 24
    • 0026057992 scopus 로고
    • Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel
    • de Weille J.R., Schweitz H., Maes P., Tartar A., Lazdunski M. Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:2437-2440.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2437-2440
    • de Weille, J.R.1    Schweitz, H.2    Maes, P.3    Tartar, A.4    Lazdunski, M.5
  • 25
    • 33646765794 scopus 로고    scopus 로고
    • Non-clinical and clinical characterization of a novel acting thrombolytic: alfimeprase
    • Deitcher S.R., Toombs C.F. Non-clinical and clinical characterization of a novel acting thrombolytic: alfimeprase. Pathophysiol. Haemost. Thromb. 2005, 34:215-220.
    • (2005) Pathophysiol. Haemost. Thromb. , vol.34 , pp. 215-220
    • Deitcher, S.R.1    Toombs, C.F.2
  • 26
    • 58049211379 scopus 로고    scopus 로고
    • Novel bifunctional natriuretic peptides as potential therapeutics
    • Dickey D.M., Burnett J.C., Potter L.R. Novel bifunctional natriuretic peptides as potential therapeutics. J. Biol. Chem. 2008, 283:35003-35009.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35003-35009
    • Dickey, D.M.1    Burnett, J.C.2    Potter, L.R.3
  • 28
    • 34250877386 scopus 로고    scopus 로고
    • Combined antiplatelet and anticoagulant therapy: clinical benefits and risks
    • Eikelboom J.W., Hirsh J. Combined antiplatelet and anticoagulant therapy: clinical benefits and risks. J. Thromb. Haemost 2007, 5(Suppl. 1):255-263.
    • (2007) J. Thromb. Haemost , vol.5 , Issue.SUPPL. 1 , pp. 255-263
    • Eikelboom, J.W.1    Hirsh, J.2
  • 30
    • 30744449235 scopus 로고    scopus 로고
    • Angiogenesis as a therapeutic target
    • Ferrara N., Kerbel R.S. Angiogenesis as a therapeutic target. Nature 2005, 438:967-974.
    • (2005) Nature , vol.438 , pp. 967-974
    • Ferrara, N.1    Kerbel, R.S.2
  • 31
    • 0031949097 scopus 로고    scopus 로고
    • Isolation: analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom
    • Ferreira L.A., Galle A., Raida M., Schrader M., Lebrun I., Habermehl G. Isolation: analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom. J. Protein Chem. 1998, 17:285-289.
    • (1998) J. Protein Chem. , vol.17 , pp. 285-289
    • Ferreira, L.A.1    Galle, A.2    Raida, M.3    Schrader, M.4    Lebrun, I.5    Habermehl, G.6
  • 32
    • 0028883991 scopus 로고
    • Structure and effects of a kinin potentiating fraction F (AppF) isolated from Agkistrodon piscivorus piscivorus venom
    • Ferreira L.A., Mollring T., Lebrun F.L., Raida M., Znottka R., Habermehl G.G. Structure and effects of a kinin potentiating fraction F (AppF) isolated from Agkistrodon piscivorus piscivorus venom. Toxicon 1995, 33:1313-1319.
    • (1995) Toxicon , vol.33 , pp. 1313-1319
    • Ferreira, L.A.1    Mollring, T.2    Lebrun, F.L.3    Raida, M.4    Znottka, R.5    Habermehl, G.G.6
  • 33
    • 84873780743 scopus 로고
    • A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca
    • Ferreira S.H. A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca. Br. J. Pharmacol. Chemother. 1965, 24:163-169.
    • (1965) Br. J. Pharmacol. Chemother. , vol.24 , pp. 163-169
    • Ferreira, S.H.1
  • 34
    • 0014959663 scopus 로고
    • Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom
    • Ferreira S.H., Bartelt D.C., Greene L.J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry 1970, 9:2583-2593.
    • (1970) Biochemistry , vol.9 , pp. 2583-2593
    • Ferreira, S.H.1    Bartelt, D.C.2    Greene, L.J.3
  • 35
    • 38449110166 scopus 로고    scopus 로고
    • Approaching the golden age of natural product pharmaceuticals from venom libraries: an overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications
    • Fox J.W., Serrano S.M. Approaching the golden age of natural product pharmaceuticals from venom libraries: an overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications. Curr. Pharm. Des 2007, 13:2927-2934.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2927-2934
    • Fox, J.W.1    Serrano, S.M.2
  • 37
    • 12344315863 scopus 로고    scopus 로고
    • Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): isolation, chemical and biological characterisation
    • Fry B.G., Wickramaratana J.C., Lemme S., Beuve A., Garbers D., Hodgson W.C., Alewood P. Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): isolation, chemical and biological characterisation. Biochem. Biophys. Res. Commun. 2005, 327:1011-1015.
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 1011-1015
    • Fry, B.G.1    Wickramaratana, J.C.2    Lemme, S.3    Beuve, A.4    Garbers, D.5    Hodgson, W.C.6    Alewood, P.7
  • 38
    • 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
  • 41
    • 0030781570 scopus 로고    scopus 로고
    • Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus
    • Ho P.L., Soares M.B., Maack T., Gimenez I., Puorto G., Furtado M.F., Raw I. Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus. Eur. J. Biochem. 1997, 250:144-149.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 144-149
    • Ho, P.L.1    Soares, M.B.2    Maack, T.3    Gimenez, I.4    Puorto, G.5    Furtado, M.F.6    Raw, I.7
  • 42
    • 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
  • 44
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: roles in cancer development and as treatment targets
    • Jin H., Varner J. Integrins: roles in cancer development and as treatment targets. Br. J. Cancer 2004, 90:561-565.
    • (2004) Br. J. Cancer , vol.90 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 46
    • 0019333503 scopus 로고
    • The complete primary structures of two reduced and S-carboxymethylated Angusticeps-type toxins from Dendroaspis angusticeps (green mamba) venom
    • Joubert F.J., Taljaard N. The complete primary structures of two reduced and S-carboxymethylated Angusticeps-type toxins from Dendroaspis angusticeps (green mamba) venom. Biochim. Biophys. Acta 1980, 623:449-456.
    • (1980) Biochim. Biophys. Acta , vol.623 , pp. 449-456
    • Joubert, F.J.1    Taljaard, N.2
  • 47
    • 0019189878 scopus 로고
    • The primary structure of a short neurotoxin homologue (S4C8) from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom
    • Joubert F.J., Taljaard N. The primary structure of a short neurotoxin homologue (S4C8) from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Int. J. Biochem. 1980, 12:567-574.
    • (1980) Int. J. Biochem. , vol.12 , pp. 567-574
    • Joubert, F.J.1    Taljaard, N.2
  • 48
    • 0034683048 scopus 로고    scopus 로고
    • Suppressive mechanism of salmosin, a novel disintegrin in B16 melanoma cell metastasis
    • Kang I.C., Kim D.S., Jang Y., Chung K.H. Suppressive mechanism of salmosin, a novel disintegrin in B16 melanoma cell metastasis. Biochem. Biophys. Res. Commun. 2000, 275:169-173.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 169-173
    • Kang, I.C.1    Kim, D.S.2    Jang, Y.3    Chung, K.H.4
  • 49
    • 0033178713 scopus 로고    scopus 로고
    • A novel disintegrin salmosin inhibits tumor angiogenesis
    • Kang I.C., Lee Y.D., Kim D.S. A novel disintegrin salmosin inhibits tumor angiogenesis. Cancer Res. 1999, 59:3754-3760.
    • (1999) Cancer Res. , vol.59 , pp. 3754-3760
    • Kang, I.C.1    Lee, Y.D.2    Kim, D.S.3
  • 51
    • 0014950435 scopus 로고
    • Structure of bradykinin-potentiating peptide containing tryptophan from the venom of Agkistrodon halys blomhoffii
    • Kato H., Suzuki T. Structure of bradykinin-potentiating peptide containing tryptophan from the venom of Agkistrodon halys blomhoffii. Experientia 1970, 26:1205-1206.
    • (1970) Experientia , vol.26 , pp. 1205-1206
    • Kato, H.1    Suzuki, T.2
  • 52
    • 0015228658 scopus 로고
    • Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffi. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C
    • Kato H., Suzuki T. Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffi. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C. Biochemistry 1971, 10:972-980.
    • (1971) Biochemistry , vol.10 , pp. 972-980
    • Kato, H.1    Suzuki, T.2
  • 53
    • 0031740746 scopus 로고    scopus 로고
    • Proline brackets and identification of potential functional sites in proteins: toxins to therapeutics
    • Kini R.M. Proline brackets and identification of potential functional sites in proteins: toxins to therapeutics. Toxicon 1998, 36:1659-1670.
    • (1998) Toxicon , vol.36 , pp. 1659-1670
    • Kini, R.M.1
  • 54
    • 9544254847 scopus 로고    scopus 로고
    • Platelet aggregation and exogenous factors from animal sources
    • Kini R.M. Platelet aggregation and exogenous factors from animal sources. Curr. Drug Targets Cardiovasc. Haematol. Disord. 2004, 4:301-325.
    • (2004) Curr. Drug Targets Cardiovasc. Haematol. Disord. , vol.4 , pp. 301-325
    • Kini, R.M.1
  • 55
    • 33646780927 scopus 로고    scopus 로고
    • Serine proteases affecting blood coagulation and fibrinolysis from snake venoms
    • Kini R.M. Serine proteases affecting blood coagulation and fibrinolysis from snake venoms. Pathophysiol. Haemost. Thromb. 2005, 34:200-204.
    • (2005) Pathophysiol. Haemost. Thromb. , vol.34 , pp. 200-204
    • Kini, R.M.1
  • 56
    • 33746885464 scopus 로고    scopus 로고
    • Anticoagulant proteins from snake venoms: structure, function and mechanism
    • Kini R.M. Anticoagulant proteins from snake venoms: structure, function and mechanism. Biochem. J. 2006, 397:377-387.
    • (2006) Biochem. J. , vol.397 , pp. 377-387
    • Kini, R.M.1
  • 58
    • 0029089655 scopus 로고
    • A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites
    • Kini R.M., Evans H.J. A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites. Biochem. Biophys. Res. Commun. 1995, 212:1115-1124.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 1115-1124
    • Kini, R.M.1    Evans, H.J.2
  • 59
    • 0029930504 scopus 로고    scopus 로고
    • Prediction of potential protein-protein interaction sites from amino acid sequence. Identification of a fibrin polymerization site
    • Kini R.M., Evans H.J. Prediction of potential protein-protein interaction sites from amino acid sequence. Identification of a fibrin polymerization site. FEBS Lett. 1996, 385:81-86.
    • (1996) FEBS Lett. , vol.385 , pp. 81-86
    • Kini, R.M.1    Evans, H.J.2
  • 61
    • 0024462290 scopus 로고
    • Biochemical mechanisms of platelet activation
    • Kroll M.H., Schafer A.I. Biochemical mechanisms of platelet activation. Blood 1989, 74:1181-1195.
    • (1989) Blood , vol.74 , pp. 1181-1195
    • Kroll, M.H.1    Schafer, A.I.2
  • 62
    • 34250358937 scopus 로고    scopus 로고
    • Natriuretic peptides and therapeutic applications
    • Lee C.Y., Burnett J.C. Natriuretic peptides and therapeutic applications. Heart Fail. Rev. 2007, 12:131-142.
    • (2007) Heart Fail. Rev. , vol.12 , pp. 131-142
    • Lee, C.Y.1    Burnett, J.C.2
  • 63
    • 67149084605 scopus 로고    scopus 로고
    • Pharmacodynamics of a novel designer natriuretic peptide, CD-NP, in a first-in-human clinical trial in healthy subjects
    • Lee C.Y., Chen H.H., Lisy O., Swan S., Cannon C., Lieu H.D., Burnett J.C. Pharmacodynamics of a novel designer natriuretic peptide, CD-NP, in a first-in-human clinical trial in healthy subjects. J. Clin. Pharmacol. 2009, 49:668-673.
    • (2009) J. Clin. Pharmacol. , vol.49 , pp. 668-673
    • Lee, C.Y.1    Chen, H.H.2    Lisy, O.3    Swan, S.4    Cannon, C.5    Lieu, H.D.6    Burnett, J.C.7
  • 64
    • 0022600067 scopus 로고
    • Molecular mechanisms of platelet aggregation
    • Leung L., Nachman R. Molecular mechanisms of platelet aggregation. Annu. Rev. Med. 1986, 37:179-186.
    • (1986) Annu. Rev. Med. , vol.37 , pp. 179-186
    • Leung, L.1    Nachman, R.2
  • 66
    • 0029010357 scopus 로고
    • Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors
    • Linz W., Wiemer G., Gohlke P., Unger T., Scholkens B.A. Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors. Pharmacol. Rev. 1995, 47:25-49.
    • (1995) Pharmacol. Rev. , vol.47 , pp. 25-49
    • Linz, W.1    Wiemer, G.2    Gohlke, P.3    Unger, T.4    Scholkens, B.A.5
  • 70
    • 39749109478 scopus 로고    scopus 로고
    • Triggers, targets and treatments for thrombosis
    • Mackman N. Triggers, targets and treatments for thrombosis. Nature 2008, 451:914-918.
    • (2008) Nature , vol.451 , pp. 914-918
    • Mackman, N.1
  • 71
    • 0030750415 scopus 로고    scopus 로고
    • Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site
    • Marcinkiewicz C., Vijay-Kumar S., McLane M.A., Niewiarowski S. Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site. Blood 1997, 90:1565-1575.
    • (1997) Blood , vol.90 , pp. 1565-1575
    • Marcinkiewicz, C.1    Vijay-Kumar, S.2    McLane, M.A.3    Niewiarowski, S.4
  • 73
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland F.S. Snake venoms and the hemostatic system. Toxicon 1998, 36:1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 74
    • 0035742117 scopus 로고    scopus 로고
    • A novel snake venom disintegrin that inhibits human ovarian cancer dissemination and angiogenesis in an orthotopic nude mouse model
    • Markland F.S., Shieh K., Zhou Q., Golubkov V., Sherwin R.P., Richters V., Sposto R. A novel snake venom disintegrin that inhibits human ovarian cancer dissemination and angiogenesis in an orthotopic nude mouse model. Haemostasis 2001, 31:183-191.
    • (2001) Haemostasis , vol.31 , pp. 183-191
    • Markland, F.S.1    Shieh, K.2    Zhou, Q.3    Golubkov, V.4    Sherwin, R.P.5    Richters, V.6    Sposto, R.7
  • 75
    • 79960652099 scopus 로고    scopus 로고
    • Fibrolase and its evolution to clinical trials: a long and winding road
    • Springer, Dordrecht, R.M. Kini, K.J. Clemetson, F.S. Markland, M.A. McLane, T. Morita (Eds.)
    • Markland F.S., Swenson S. Fibrolase and its evolution to clinical trials: a long and winding road. Toxins and Hemostasis: From Bench to Bedside 2010, 409-427. Springer, Dordrecht. R.M. Kini, K.J. Clemetson, F.S. Markland, M.A. McLane, T. Morita (Eds.).
    • (2010) Toxins and Hemostasis: From Bench to Bedside , pp. 409-427
    • Markland, F.S.1    Swenson, S.2
  • 76
    • 0017798369 scopus 로고
    • The effects of snake venoms on the cardiovascular and haemostatic mechanisms
    • Marsh N., Whaler B. The effects of snake venoms on the cardiovascular and haemostatic mechanisms. Int. J. Biochem. 1978, 9:217-220.
    • (1978) Int. J. Biochem. , vol.9 , pp. 217-220
    • Marsh, N.1    Whaler, B.2
  • 78
    • 0030570733 scopus 로고    scopus 로고
    • Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 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 recognition of alpha IIb beta 3 and alpha v beta 3 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
  • 80
    • 33646794420 scopus 로고    scopus 로고
    • Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent
    • Minea R., Swenson S., Costa F., Chen T.C., Markland F.S. Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent. Pathophysiol. Haemost. Thromb. 2005, 34:177-183.
    • (2005) Pathophysiol. Haemost. Thromb. , vol.34 , pp. 177-183
    • Minea, R.1    Swenson, S.2    Costa, F.3    Chen, T.C.4    Markland, F.S.5
  • 81
    • 33745995088 scopus 로고    scopus 로고
    • Phase II trial of alfimeprase, a novel-acting fibrin degradation agent, for occluded central venous access devices
    • Moll S., Kenyon P., Bertoli L., De Maio J., Homesley H., Deitcher S.R. Phase II trial of alfimeprase, a novel-acting fibrin degradation agent, for occluded central venous access devices. J. Clin. Oncol. 2006, 24:3056-3060.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 3056-3060
    • Moll, S.1    Kenyon, P.2    Bertoli, L.3    De Maio, J.4    Homesley, H.5    Deitcher, S.R.6
  • 83
    • 0036679895 scopus 로고    scopus 로고
    • Anti-integrin as novel drug-discovery targets: potential therapeutic and diagnostic implications
    • Mousa S.A. Anti-integrin as novel drug-discovery targets: potential therapeutic and diagnostic implications. Curr. Opin. Chem. Biol. 2002, 6:534-541.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 534-541
    • Mousa, S.A.1
  • 85
    • 0017243179 scopus 로고
    • Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
    • Nolan C., Hall L.S., Barlow G.H. Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom. Methods Enzymol. 1976, 45:205-213.
    • (1976) Methods Enzymol. , vol.45 , pp. 205-213
    • Nolan, C.1    Hall, L.S.2    Barlow, G.H.3
  • 86
    • 50849130572 scopus 로고    scopus 로고
    • Structure and activity of plasmin and other direct thrombolytic agents
    • Novokhatny V. Structure and activity of plasmin and other direct thrombolytic agents. Thromb. Res. 2008, 122(Suppl. 3):S3-S8.
    • (2008) Thromb. Res. , vol.122 , Issue.SUPPL. 3
    • Novokhatny, V.1
  • 88
    • 0004919656 scopus 로고
    • Structural relationships of angiotensin converting-enzyme inhibitors to pharmacologic activity
    • Ondetti M.A. Structural relationships of angiotensin converting-enzyme inhibitors to pharmacologic activity. Circulation 1988, 77:I74-I78.
    • (1988) Circulation , vol.77
    • Ondetti, M.A.1
  • 89
    • 0021152476 scopus 로고
    • Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions
    • Ondetti M.A., Cushman D.W. Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions. CRC Crit. Rev. Biochem. 1984, 16:381-411.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 381-411
    • Ondetti, M.A.1    Cushman, D.W.2
  • 90
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents
    • Ondetti M.A., Rubin B., Cushman D.W. Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents. Science 1977, 196:441-444.
    • (1977) Science , vol.196 , pp. 441-444
    • Ondetti, M.A.1    Rubin, B.2    Cushman, D.W.3
  • 92
    • 67849090560 scopus 로고    scopus 로고
    • Novel interactions in platelet biology: CLEC-2/podoplanin and laminin/GPVI
    • Ozaki Y., Suzuki-Inoue K., Inoue O. Novel interactions in platelet biology: CLEC-2/podoplanin and laminin/GPVI. J. Thromb. Haemost. 2009, 7(Suppl. 1):191-194.
    • (2009) J. Thromb. Haemost. , vol.7 , Issue.SUPPL. 1 , pp. 191-194
    • Ozaki, Y.1    Suzuki-Inoue, K.2    Inoue, O.3
  • 93
    • 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
  • 94
    • 0021743751 scopus 로고
    • The chemistry of enalapril
    • Panchett A.A. The chemistry of enalapril. Br. J. Clin. Pharmacol. 1984, 18(Suppl. 2):201S-207S.
    • (1984) Br. J. Clin. Pharmacol. , vol.18 , Issue.SUPPL. 2
    • Panchett, A.A.1
  • 95
    • 1542343914 scopus 로고    scopus 로고
    • From viper's venom to drug design: treating hypertension
    • Patlak M. From viper's venom to drug design: treating hypertension. FASEB J. 2004, 18:421.
    • (2004) FASEB J. , vol.18 , pp. 421
    • Patlak, M.1
  • 98
    • 0029183978 scopus 로고
    • A novel analgesic toxin (hannalgesin) from the venom of king cobra (Ophiophagus hannah)
    • Pu X.C., Wong P.T., Gopalakrishnakone P. A novel analgesic toxin (hannalgesin) from the venom of king cobra (Ophiophagus hannah). Toxicon 1995, 33:1425-1431.
    • (1995) Toxicon , vol.33 , pp. 1425-1431
    • Pu, X.C.1    Wong, P.T.2    Gopalakrishnakone, P.3
  • 100
    • 0027081926 scopus 로고
    • Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom
    • Randolph A., Chamberlain S.H., Chu H.L., Retzios A.D., Markland F.S., Masiarz F.R. Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom. Protein Sci. 1992, 1:590-600.
    • (1992) Protein Sci. , vol.1 , pp. 590-600
    • Randolph, A.1    Chamberlain, S.H.2    Chu, H.L.3    Retzios, A.D.4    Markland, F.S.5    Masiarz, F.R.6
  • 101
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken D.C., Lijnen H.R. New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost 2009, 7:4-13.
    • (2009) J. Thromb. Haemost , vol.7 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 102
    • 0017664337 scopus 로고
    • Bradykinin potentiating and sensitizing activities of new synthetic analogues of snake venom peptides
    • Sabia E.B., Tominaga M., Paiva A.C., Paiva T.B. Bradykinin potentiating and sensitizing activities of new synthetic analogues of snake venom peptides. J. Med. Chem. 1977, 20:1679-1681.
    • (1977) J. Med. Chem. , vol.20 , pp. 1679-1681
    • Sabia, E.B.1    Tominaga, M.2    Paiva, A.C.3    Paiva, T.B.4
  • 103
    • 17144392493 scopus 로고    scopus 로고
    • Short-term risk of death after treatment with nesiritide for decompensated heart failure: a pooled analysis of randomized controlled trials
    • Sackner-Bernstein J.D., Kowalski M., Fox M., Aaronson K. Short-term risk of death after treatment with nesiritide for decompensated heart failure: a pooled analysis of randomized controlled trials. JAMA 2005, 293:1900-1905.
    • (2005) JAMA , vol.293 , pp. 1900-1905
    • Sackner-Bernstein, J.D.1    Kowalski, M.2    Fox, M.3    Aaronson, K.4
  • 104
    • 16344377117 scopus 로고    scopus 로고
    • Risk of worsening renal function with nesiritide in patients with acutely decompensated heart failure
    • Sackner-Bernstein J.D., Skopicki H.A., Aaronson K.D. Risk of worsening renal function with nesiritide in patients with acutely decompensated heart failure. Circulation 2005, 111:1487-1491.
    • (2005) Circulation , vol.111 , pp. 1487-1491
    • Sackner-Bernstein, J.D.1    Skopicki, H.A.2    Aaronson, K.D.3
  • 105
  • 106
    • 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
  • 111
    • 0021176415 scopus 로고
    • Hypotensive and hemostatic properties of rattlesnake (Crotalus viridis helleri) venom and venom fractions in dogs
    • Schaeffer R.C., Briston C., Chilton S.M., Carlson R.W. Hypotensive and hemostatic properties of rattlesnake (Crotalus viridis helleri) venom and venom fractions in dogs. J. Pharmacol. Exp. Ther. 1984, 230:393-398.
    • (1984) J. Pharmacol. Exp. Ther. , vol.230 , pp. 393-398
    • Schaeffer, R.C.1    Briston, C.2    Chilton, S.M.3    Carlson, R.W.4
  • 112
    • 0031226165 scopus 로고    scopus 로고
    • Comparative molecular modelling study of the calcium channel blockers nifedipine and black mamba toxin FS2
    • Schleifer K.J. Comparative molecular modelling study of the calcium channel blockers nifedipine and black mamba toxin FS2. J. Comput. Aided Mol. Des 1997, 11:491-501.
    • (1997) J. Comput. Aided Mol. Des , vol.11 , pp. 491-501
    • Schleifer, K.J.1
  • 113
    • 0026776795 scopus 로고
    • A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)
    • Schweitz H., Vigne P., Moinier D., Frelin C., Lazdunski M. A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps). J. Biol. Chem. 1992, 267:13928-13932.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13928-13932
    • Schweitz, H.1    Vigne, P.2    Moinier, D.3    Frelin, C.4    Lazdunski, M.5
  • 114
    • 34247594281 scopus 로고    scopus 로고
    • Drug evaluation: alfimeprase, a plasminogen-independent thrombolytic
    • Shah A.R., Scher L. Drug evaluation: alfimeprase, a plasminogen-independent thrombolytic. IDrugs 2007, 10:329-335.
    • (2007) IDrugs , vol.10 , pp. 329-335
    • Shah, A.R.1    Scher, L.2
  • 115
    • 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
  • 116
    • 0034630876 scopus 로고    scopus 로고
    • Intravenous ancrod for treatment of acute ischemic stroke: the STAT study: a randomized controlled trial. Stroke treatment with Ancrod trial
    • Sherman D.G., Atkinson R.P., Chippendale T., Levin K.A., Ng K., Futrell N., Hsu C.Y., Levy D.E. Intravenous ancrod for treatment of acute ischemic stroke: the STAT study: a randomized controlled trial. Stroke treatment with Ancrod trial. JAMA 2000, 283:2395-2403.
    • (2000) JAMA , vol.283 , pp. 2395-2403
    • Sherman, D.G.1    Atkinson, R.P.2    Chippendale, T.3    Levin, K.A.4    Ng, K.5    Futrell, N.6    Hsu, C.Y.7    Levy, D.E.8
  • 117
    • 0030722126 scopus 로고    scopus 로고
    • Inhibition of angiogenesis in vitro and in vivo: comparison of the relative activities of triflavin, an Arg-Gly-Asp-containing peptide and anti-alpha(v)beta3 integrin monoclonal antibody
    • Sheu J.R., Yen M.H., Kan Y.C., Hung W.C., Chang P.T., Luk H.N. Inhibition of angiogenesis in vitro and in vivo: comparison of the relative activities of triflavin, an Arg-Gly-Asp-containing peptide and anti-alpha(v)beta3 integrin monoclonal antibody. Biochim. Biophys. Acta 1997, 1336:445-454.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 445-454
    • Sheu, J.R.1    Yen, M.H.2    Kan, Y.C.3    Hung, W.C.4    Chang, P.T.5    Luk, H.N.6
  • 118
    • 77952267932 scopus 로고    scopus 로고
    • Transcriptomic analysis of the venom gland of the red-headed krait (Bungarus flaviceps) using expressed sequence tags
    • Siang A.S., Doley R., Vonk F.J., Kini R.M. Transcriptomic analysis of the venom gland of the red-headed krait (Bungarus flaviceps) using expressed sequence tags. BMC Mol. Biol. 2010, 11:24.
    • (2010) BMC Mol. Biol. , vol.11 , pp. 24
    • Siang, A.S.1    Doley, R.2    Vonk, F.J.3    Kini, R.M.4
  • 122
    • 0015083348 scopus 로고
    • Bradykinin potentiating peptide PCA-Lys-Trp-Ala-Pro. An inhibitor of the pulmonary inactivation of bradykinin and conversion of angiotensin I to II
    • Stewart J.M., Ferreira S.H., Greene L.J. Bradykinin potentiating peptide PCA-Lys-Trp-Ala-Pro. An inhibitor of the pulmonary inactivation of bradykinin and conversion of angiotensin I to II. Biochem. Pharmacol. 1971, 20:1557-1567.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 1557-1567
    • Stewart, J.M.1    Ferreira, S.H.2    Greene, L.J.3
  • 123
    • 0017242939 scopus 로고
    • The coagulant enzyme from Bothrops atrox venom (batroxobin)
    • Stocker K., Barlow G.H. The coagulant enzyme from Bothrops atrox venom (batroxobin). Methods Enzymol. 1976, 45:214-223.
    • (1976) Methods Enzymol. , vol.45 , pp. 214-223
    • Stocker, K.1    Barlow, G.H.2
  • 124
    • 0017656265 scopus 로고
    • Snake venom toxins. The amino-acid sequence of a short-neurotoxin homologue from Dendroaspis polylepis polylepis (black mamba) venom
    • Strydom D.J. Snake venom toxins. The amino-acid sequence of a short-neurotoxin homologue from Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 1977, 76:99-106.
    • (1977) Eur. J. Biochem. , vol.76 , pp. 99-106
    • Strydom, D.J.1
  • 125
    • 0023867456 scopus 로고
    • A new natriuretic peptide in porcine brain
    • Sudoh T., Kangawa K., Minamino N., Matsuo H. A new natriuretic peptide in porcine brain. Nature 1988, 332:78-81.
    • (1988) Nature , vol.332 , pp. 78-81
    • Sudoh, T.1    Kangawa, K.2    Minamino, N.3    Matsuo, H.4
  • 126
    • 0025312570 scopus 로고
    • C-type natriuretic peptide (CNP): a new member of natriuretic peptide family identified in porcine brain
    • Sudoh T., Minamino N., Kangawa K., Matsuo H. C-type natriuretic peptide (CNP): a new member of natriuretic peptide family identified in porcine brain. Biochem. Biophys. Res. Commun. 1990, 168:863-870.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 863-870
    • Sudoh, T.1    Minamino, N.2    Kangawa, K.3    Matsuo, H.4
  • 127
    • 4444329286 scopus 로고    scopus 로고
    • Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression
    • Swenson S., Costa F., Minea R., Sherwin R.P., Ernst W., Fujii G., Yang D., Markland F.S. Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression. Mol. Cancer Ther. 2004, 3:499-511.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 499-511
    • Swenson, S.1    Costa, F.2    Minea, R.3    Sherwin, R.P.4    Ernst, W.5    Fujii, G.6    Yang, D.7    Markland, F.S.8
  • 129
    • 0031790591 scopus 로고    scopus 로고
    • The cardiovascular, coagulation and haematological effects of tiger snake (Notechis scutatus) venom
    • Tibballs J. The cardiovascular, coagulation and haematological effects of tiger snake (Notechis scutatus) venom. Anaesth. Intensive Care 1998, 26:529-535.
    • (1998) Anaesth. Intensive Care , vol.26 , pp. 529-535
    • Tibballs, J.1
  • 130
    • 0033573790 scopus 로고    scopus 로고
    • Platelet GPIIb-IIIa blockers
    • Topol E.J., Byzova T.V., Plow E.F. Platelet GPIIb-IIIa blockers. Lancet 1999, 353:227-231.
    • (1999) Lancet , vol.353 , pp. 227-231
    • Topol, E.J.1    Byzova, T.V.2    Plow, E.F.3
  • 131
    • 0028111866 scopus 로고
    • Contortrostatin, a snake venom disintegrin, inhibits beta 1 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis
    • Trikha M., De Clerck Y.A., Markland F.S. Contortrostatin, a snake venom disintegrin, inhibits beta 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
  • 133
    • 0029112787 scopus 로고
    • Smooth muscle relaxing and hypotensive activities of synthetic calciseptine and the homologous snake venom peptide FS2
    • Watanabe T.X., Itahara Y., Kuroda H., Chen Y.N., Kimura T., Sakakibara S. Smooth muscle relaxing and hypotensive activities of synthetic calciseptine and the homologous snake venom peptide FS2. Jpn. J. Pharmacol. 1995, 68:305-313.
    • (1995) Jpn. J. Pharmacol. , vol.68 , pp. 305-313
    • Watanabe, T.X.1    Itahara, Y.2    Kuroda, H.3    Chen, Y.N.4    Kimura, T.5    Sakakibara, S.6
  • 136
    • 0001562465 scopus 로고    scopus 로고
    • Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin alphavbeta3 antagonist and inducing apoptosis
    • Yeh C.H., Peng H.C., Huang T.F. Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin alphavbeta3 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
  • 137
    • 0035028334 scopus 로고    scopus 로고
    • Rhodostomin, a snake venom disintegrin, inhibits angiogenesis elicited by basic fibroblast growth factor and suppresses tumor growth by a selective alpha(v)beta(3) blockade of endothelial cells
    • Yeh C.H., Peng H.C., Yang R.S., Huang T.F. Rhodostomin, a snake venom disintegrin, inhibits angiogenesis elicited by basic fibroblast growth factor and suppresses tumor growth by a selective alpha(v)beta(3) blockade of endothelial cells. Mol. Pharmacol. 2001, 59:1333-1342.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1333-1342
    • Yeh, C.H.1    Peng, H.C.2    Yang, R.S.3    Huang, T.F.4


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