메뉴 건너뛰기




Volumn 45, Issue 8, 2005, Pages 1051-1061

Snake venom probes of platelet adhesion receptors and their ligands

Author keywords

C type lectin; Metalloproteinase disintegrin; Platelet; Snake venom; Thromsosis

Indexed keywords

AGGLUCETIN; AGGRETIN; ALBOAGGREGIN A; ALBOAGGREGIN B; ALBOLUXIN; ALBORHAGIN; ATROLYSIN A; BILINEXIN; BITISCETIN; BOTROCETIN; COLLAGEN; CONVULXIN; ECHICETIN; FIBRINOGEN; FLAVOCETIN A; GLYCOPROTEIN IB; HALYSASE; INTEGRIN; JARACETIN; JARARHAGIN; KAOUTHIAGIN; LEBECETIN; LECTIN; MOCARHAGIN; MONOCROTALINE; MUCETIN; MUROCETIN; OPHIOLUXIN; PADGEM PROTEIN; PROTEIN; PROTEIN SUBUNIT; RHODOCETIN; SALMOSIN; SNAKE VENOM; STEJNULXIN; THROMBOCYTE RECEPTOR; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 19544386458     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2005.02.025     Document Type: Article
Times cited : (51)

References (95)
  • 1
    • 0033980343 scopus 로고    scopus 로고
    • Snake venom modulators of platelet adhesion receptors and their ligands
    • R.K. Andrews, and M.C. Berndt Snake venom modulators of platelet adhesion receptors and their ligands Toxicon 38 2000 775 791
    • (2000) Toxicon , vol.38 , pp. 775-791
    • Andrews, R.K.1    Berndt, M.C.2
  • 2
    • 19544364854 scopus 로고    scopus 로고
    • Mocarhagin
    • A.J. Barrett N.D. Rawlings F.J. Woessner second ed. Elsevier London
    • R.K. Andrews, and M.C. Berndt Mocarhagin A.J. Barrett N.D. Rawlings F.J. Woessner Handbook of Proteolytic Enzymes second ed. 2004 Elsevier London 696 699
    • (2004) Handbook of Proteolytic Enzymes , pp. 696-699
    • Andrews, R.K.1    Berndt, M.C.2
  • 3
    • 0029816492 scopus 로고    scopus 로고
    • Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet activation
    • R.K. Andrews, M.H. Kroll, C.M. Ward, J.W. Rose, R.M. Scarborough, A.I. Smith, J.A. Lopez, and M.C. Berndt Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet activation Biochemistry 35 1996 12629 12639
    • (1996) Biochemistry , vol.35 , pp. 12629-12639
    • Andrews, R.K.1    Kroll, M.H.2    Ward, C.M.3    Rose, J.W.4    Scarborough, R.M.5    Smith, A.I.6    Lopez, J.A.7    Berndt, M.C.8
  • 5
    • 0035742227 scopus 로고    scopus 로고
    • The use of snake venom toxins as tools to study the platelet receptors for collagen and von Willebrand factor
    • R.K. Andrews, A. Kamiguti, O. Berlanga, M. Leduc, R.D.G. Theakston, and S.P. Watson The use of snake venom toxins as tools to study the platelet receptors for collagen and von Willebrand factor Haemostasis 31 2001 155 172
    • (2001) Haemostasis , vol.31 , pp. 155-172
    • Andrews, R.K.1    Kamiguti, A.2    Berlanga, O.3    Leduc, M.4    Theakston, R.D.G.5    Watson, S.P.6
  • 8
    • 1142292610 scopus 로고    scopus 로고
    • Structure-activity relationships of snake toxins targeting platelet receptors, glycoprotein Ib-IX-V and glycoprotein VI
    • R.K. Andrews, E.E. Gardiner, Y. Shen, and M.C. Berndt Structure-activity relationships of snake toxins targeting platelet receptors, glycoprotein Ib-IX-V and glycoprotein VI Curr. Med. Chem.: Cardiovasc. Hematol. Agents 1 2003 143 149
    • (2003) Curr. Med. Chem.: Cardiovasc. Hematol. Agents , vol.1 , pp. 143-149
    • Andrews, R.K.1    Gardiner, E.E.2    Shen, Y.3    Berndt, M.C.4
  • 10
    • 6044238041 scopus 로고    scopus 로고
    • The use of snake toxins to study platelet function
    • Mahaut-Smith, M.P., Gibbins, J.M. (Eds.), Humana Press Inc., UK
    • Andrews, R.K., Gardiner, E.E., Berndt, M.C., 2004b. The use of snake toxins to study platelet function. In: Mahaut-Smith, M.P., Gibbins, J.M. (Eds.), Platelets and Megakaryocytes. Methods and Protocols, Humana Press Inc., UK 335-348.
    • (2004) Platelets and Megakaryocytes. Methods and Protocols , pp. 335-348
    • Andrews, R.K.1    Gardiner, E.E.2    Berndt, M.C.3
  • 14
    • 0345688868 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors improve recovery and hemostatic function of in vitro-aged or -injured mouse platelets
    • W. Bergmeier, P.C. Burger, C.L. Piffath, K.M. Hoffmeister, J.H. Hartwig, B. Nieswandt, and D.D. Wagner Metalloproteinase inhibitors improve recovery and hemostatic function of in vitro-aged or -injured mouse platelets Blood 102 2003 4229 4235
    • (2003) Blood , vol.102 , pp. 4229-4235
    • Bergmeier, W.1    Burger, P.C.2    Piffath, C.L.3    Hoffmeister, K.M.4    Hartwig, J.H.5    Nieswandt, B.6    Wagner, D.D.7
  • 15
    • 0029055393 scopus 로고
    • Snake venom metalloendopeptidases: Reprolysins
    • J.B. Bjarnason, and J.W. Fox Snake venom metalloendopeptidases: reprolysins Methods Enzymol. 248 1995 345 368
    • (1995) Methods Enzymol. , vol.248 , pp. 345-368
    • Bjarnason, J.B.1    Fox, J.W.2
  • 16
    • 0035783370 scopus 로고    scopus 로고
    • Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C
    • M.B. Bolger, S. Swenson, and F.S. Markland Jr. Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C AAPS Pharm. Sci. 3 2001 E16
    • (2001) AAPS Pharm. Sci. , vol.3 , pp. 16
    • Bolger, M.B.1    Swenson, S.2    Markland Jr., F.S.3
  • 17
    • 0032472805 scopus 로고    scopus 로고
    • Adhesion of activated platelets to endothelial cells: Evidence for a GPIIb-IIIa-dependent bridging mechanism and novel roles for endothelial intercellular adhesion molecule 1 (ICAM-1), αvβ3 integrin, and GPIbα
    • T. Bombeli, B.R. Schwartz, and J.M. Harlan Adhesion of activated platelets to endothelial cells: evidence for a GPIIb-IIIa-dependent bridging mechanism and novel roles for endothelial intercellular adhesion molecule 1 (ICAM-1), αvβ3 integrin, and GPIbα J. Exp. Med. 187 1998 329 339
    • (1998) J. Exp. Med. , vol.187 , pp. 329-339
    • Bombeli, T.1    Schwartz, B.R.2    Harlan, J.M.3
  • 18
    • 0141737510 scopus 로고    scopus 로고
    • A new protein structure of P-II class snake venom metalloproteinases: It comprises metalloproteinase and disintegrin domains
    • R.Q. Chen, Y. Jin, J.B. Wu, X.D. Zhou, Q.M. Lu, W.Y. Wang, and Y.L. Xiong A new protein structure of P-II class snake venom metalloproteinases: it comprises metalloproteinase and disintegrin domains Biochem. Biophys. Res. Commun. 310 2003 182 187
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 182-187
    • Chen, R.Q.1    Jin, Y.2    Wu, J.B.3    Zhou, X.D.4    Lu, Q.M.5    Wang, W.Y.6    Xiong, Y.L.7
  • 19
    • 0034811684 scopus 로고    scopus 로고
    • Aggretin, a C-type lectin protein, induces platelet aggregation via integrin α2β1 and GP Ib in a phosphatidylinositol 3-kinase independent pathway
    • C.-H. Chung, H.-C. Peng, and T.-F. Huang Aggretin, a C-type lectin protein, induces platelet aggregation via integrin α2β1 and GP Ib in a phosphatidylinositol 3-kinase independent pathway Biochem. Biophys. Res. Commun. 285 2001 689 695
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 689-695
    • Chung, C.-H.1    Peng, H.-C.2    Huang, T.-F.3
  • 20
    • 0043171125 scopus 로고    scopus 로고
    • BaG, a new dimeric metalloproteinase/disintegrin from the Bothrops alternatus snake venom that interacts with α5β1 integrin
    • M.R. Cominetti, J.U. Ribeiro, J.W. Fox, and H.S. Selistre-de-Araujo BaG, a new dimeric metalloproteinase/disintegrin from the Bothrops alternatus snake venom that interacts with α5β1 integrin Arch. Biochem. Biophys. 416 2003 171 179
    • (2003) Arch. Biochem. Biophys. , vol.416 , pp. 171-179
    • Cominetti, M.R.1    Ribeiro, J.U.2    Fox, J.W.3    Selistre-de-Araujo, H.S.4
  • 22
    • 0028807440 scopus 로고
    • A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature N terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding
    • M. De Luca, L.C. Dunlop, R.K. Andrews, J.V. Flannery Jr, R. Ettling, D.A. Cumming, G.M. Veldman, and M.C. Berndt A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature N terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding J. Biol. Chem. 270 1995 26734 26737
    • (1995) J. Biol. Chem. , vol.270 , pp. 26734-26737
    • De Luca, M.1    Dunlop, L.C.2    Andrews, R.K.3    Flannery J.V. Jr4    Ettling, R.5    Cumming, D.A.6    Veldman, G.M.7    Berndt, M.C.8
  • 23
    • 0028900697 scopus 로고
    • Jararhagin and jaracetin: Novel snake venom inhibitors of the integrin collagen receptor, α2β1
    • M. De Luca, C.M. Ward, K. Ohmori, R.K. Andrews, and M.C. Berndt Jararhagin and jaracetin: novel snake venom inhibitors of the integrin collagen receptor, α2β1 Biochem. Biophys. Res. Commun. 206 1995 570 576
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 570-576
    • De Luca, M.1    Ward, C.M.2    Ohmori, K.3    Andrews, R.K.4    Berndt, M.C.5
  • 24
    • 0035174016 scopus 로고    scopus 로고
    • Ristocetin-dependent, but not botrocetin-dependent, binding of von Willebrand factor to the platelet glycoprotein Ib-IX-V complex correlates with shear-dependent interactions
    • J.-F. Dong, M.C. Berndt, A. Schade, L.V. McIntire, R.K. Andrews, and J.A. Lopez Ristocetin-dependent, but not botrocetin-dependent, binding of von Willebrand factor to the platelet glycoprotein Ib-IX-V complex correlates with shear-dependent interactions Blood 97 2001 162 168
    • (2001) Blood , vol.97 , pp. 162-168
    • Dong, J.-F.1    Berndt, M.C.2    Schade, A.3    McIntire, L.V.4    Andrews, R.K.5    Lopez, J.A.6
  • 25
    • 0035865596 scopus 로고    scopus 로고
    • Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib
    • D. Dormann, J.M. Clemetson, A. Navdaev, B.E. Kehrel, and K.J. Clemetson Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib Blood 97 2001 929 936
    • (2001) Blood , vol.97 , pp. 929-936
    • Dormann, D.1    Clemetson, J.M.2    Navdaev, A.3    Kehrel, B.E.4    Clemetson, K.J.5
  • 26
    • 0035159441 scopus 로고    scopus 로고
    • Bilinexin, a snake C-type lectin from Agkistrodon bilineatus venom agglutinates platelets via GPIb and α2β1
    • X.Y. Du, A. Navdaev, J.M. Clemetson, E. Magnenat, T.N. Wells, and K.J. Clemetson Bilinexin, a snake C-type lectin from Agkistrodon bilineatus venom agglutinates platelets via GPIb and α2β1 Thromb. Haemost. 86 2001 1277 1283
    • (2001) Thromb. Haemost. , vol.86 , pp. 1277-1283
    • Du, X.Y.1    Navdaev, A.2    Clemetson, J.M.3    Magnenat, E.4    Wells, T.N.5    Clemetson, K.J.6
  • 27
    • 0036219334 scopus 로고    scopus 로고
    • Alboluxin, a snake C-type lectin from Trimeresurus albolabris venom is a potent platelet agonist acting via GPIb and GPVI
    • X.-Y. Du, E. Magnenat, T.N. Wells, and K.J. Clemetson Alboluxin, a snake C-type lectin from Trimeresurus albolabris venom is a potent platelet agonist acting via GPIb and GPVI Thromb. Haemost. 87 2002 692 698
    • (2002) Thromb. Haemost. , vol.87 , pp. 692-698
    • Du, X.-Y.1    Magnenat, E.2    Wells, T.N.3    Clemetson, K.J.4
  • 28
    • 0037144572 scopus 로고    scopus 로고
    • Ophioluxin, a convulxin-like C-type lectin from Ophiophagus hannah (king cobra) is a powerful platelet activator via glycoprotein VI
    • X.-Y. Du, J.M. Clemetson, A. Navdaev, E.M. Magnenat, T.N. Wells, and K.J. Clemetson Ophioluxin, a convulxin-like C-type lectin from Ophiophagus hannah (king cobra) is a powerful platelet activator via glycoprotein VI J. Biol. Chem. 277 2002 35124 35132
    • (2002) J. Biol. Chem. , vol.277 , pp. 35124-35132
    • Du, X.-Y.1    Clemetson, J.M.2    Navdaev, A.3    Magnenat, E.M.4    Wells, T.N.5    Clemetson, K.J.6
  • 29
    • 0035853796 scopus 로고    scopus 로고
    • α2β1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen
    • J.A. Eble, B. Beermann, H.J. Hinz, and A. Schmidt-Hederich α2β1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen J. Biol. Chem. 276 2001 12274 12284
    • (2001) J. Biol. Chem. , vol.276 , pp. 12274-12284
    • Eble, J.A.1    Beermann, B.2    Hinz, H.J.3    Schmidt-Hederich, A.4
  • 30
    • 0036860535 scopus 로고    scopus 로고
    • Rhodocetin antagonizes stromal tumor invasion in vitro and other α2β1 integrin-mediated cell functions
    • J.A. Eble, S. Niland, A. Dennes, A. Schmidt-Hederich, P. Bruckner, and G. Brunner Rhodocetin antagonizes stromal tumor invasion in vitro and other α2β1 integrin-mediated cell functions Matrix Biol. 21 2002 547 558
    • (2002) Matrix Biol. , vol.21 , pp. 547-558
    • Eble, J.A.1    Niland, S.2    Dennes, A.3    Schmidt-Hederich, A.4    Bruckner, P.5    Brunner, G.6
  • 31
    • 0344309120 scopus 로고    scopus 로고
    • The α2β1 integrin inhibitor rhodocetin binds to the A-domain of the integrin α2 subunit proximal to the collagen-binding site
    • J.A. Eble, and D.S. Tuckwell The α2β1 integrin inhibitor rhodocetin binds to the A-domain of the integrin α2 subunit proximal to the collagen-binding site Biochem. J. 376 2003 77 85
    • (2003) Biochem. J. , vol.376 , pp. 77-85
    • Eble, J.A.1    Tuckwell, D.S.2
  • 32
    • 12444303861 scopus 로고    scopus 로고
    • Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin
    • S. Falati, Q. Liu, P. Gross, G. Merrill-Skoloff, J. Chou, E. Vandendries, A. Celi, K. Croce, B.C. Furie, and B. Furie Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin J. Exp. Med. 197 2003 1585 1598
    • (2003) J. Exp. Med. , vol.197 , pp. 1585-1598
    • Falati, S.1    Liu, Q.2    Gross, P.3    Merrill-Skoloff, G.4    Chou, J.5    Vandendries, E.6    Celi, A.7    Croce, K.8    Furie, B.C.9    Furie, B.10
  • 33
    • 0029119149 scopus 로고
    • Platelets roll on stimulated endothelium in vivo: An interaction mediated by endothelial P-selectin
    • P.S. Frenette, R.C. Johnson, R.O. Hynes, and D.D. Wagner Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin Proc. Natl Acad. Sci. USA 92 1995 7450 7454
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7450-7454
    • Frenette, P.S.1    Johnson, R.C.2    Hynes, R.O.3    Wagner, D.D.4
  • 34
    • 0025727990 scopus 로고
    • Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca
    • Y. Fujimura, K. Titani, Y. Usami, M. Suzuki, R. Oyama, T. Matsui, H. Fukui, M. Sugimoto, and Z.M. Ruggeri Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca Biochemistry 30 1991 1957 1964
    • (1991) Biochemistry , vol.30 , pp. 1957-1964
    • Fujimura, Y.1    Titani, K.2    Usami, Y.3    Suzuki, M.4    Oyama, R.5    Matsui, T.6    Fukui, H.7    Sugimoto, M.8    Ruggeri, Z.M.9
  • 35
    • 0034728354 scopus 로고    scopus 로고
    • Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers
    • K. Fukuda, H. Mizuno, H. Atoda, and T. Morita Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers Biochemistry 39 2000 1915 1923
    • (2000) Biochemistry , vol.39 , pp. 1915-1923
    • Fukuda, K.1    Mizuno, H.2    Atoda, H.3    Morita, T.4
  • 37
    • 0035469896 scopus 로고    scopus 로고
    • Regulation of P-selectin binding to the neutrophil P-selectin counter-receptor P-selectin glycoprotein ligand-1 by neutrophil elastase and cathepsin G
    • E.E. Gardiner, M. De Luca, T. McNally, A.D. Michelson, R.K. Andrews, and M.C. Berndt Regulation of P-selectin binding to the neutrophil P-selectin counter-receptor P-selectin glycoprotein ligand-1 by neutrophil elastase and cathepsin G Blood 98 2001 1440 1447
    • (2001) Blood , vol.98 , pp. 1440-1447
    • Gardiner, E.E.1    De Luca, M.2    McNally, T.3    Michelson, A.D.4    Andrews, R.K.5    Berndt, M.C.6
  • 38
    • 0037047083 scopus 로고    scopus 로고
    • Involvement of glycoprotein VI in platelet thrombus formation on both collagen and von Willebrand factor surfaces under flow conditions
    • S. Goto, N. Tamura, S. Handa, M. Arai, K. Kodama, and H. Takayama Involvement of glycoprotein VI in platelet thrombus formation on both collagen and von Willebrand factor surfaces under flow conditions Circulation 106 2002 266 272
    • (2002) Circulation , vol.106 , pp. 266-272
    • Goto, S.1    Tamura, N.2    Handa, S.3    Arai, M.4    Kodama, K.5    Takayama, H.6
  • 39
    • 0345257356 scopus 로고    scopus 로고
    • Multiple integrin-ligand interactions synergize in shear-resistant platelet adhesion at sites of arterial injury in vivo
    • S. Grüner, M. Prostredna, V. Schulte, T. Krieg, B. Eckes, C. Brakebusch, and B. Nieswandt Multiple integrin-ligand interactions synergize in shear-resistant platelet adhesion at sites of arterial injury in vivo Blood 102 2003 4021 4027
    • (2003) Blood , vol.102 , pp. 4021-4027
    • Grüner, S.1    Prostredna, M.2    Schulte, V.3    Krieg, T.4    Eckes, B.5    Brakebusch, C.6    Nieswandt, B.7
  • 40
    • 0031787654 scopus 로고    scopus 로고
    • Purification and characterization of kaouthiagin, a von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom
    • J. Hamako, T. Matsui, S. Nishida, S. Nomura, Y. Fujimura, M. Ito, Y. Ozeki, and K. Titani Purification and characterization of kaouthiagin, a von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom Thromb. Haemost. 80 1998 499 505
    • (1998) Thromb. Haemost. , vol.80 , pp. 499-505
    • Hamako, J.1    Matsui, T.2    Nishida, S.3    Nomura, S.4    Fujimura, Y.5    Ito, M.6    Ozeki, Y.7    Titani, K.8
  • 42
    • 0242381352 scopus 로고    scopus 로고
    • Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus
    • K. Horii, D. Okuda, T. Morita, and H. Mizuno Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus Biochemistry 42 2003 12497 124502
    • (2003) Biochemistry , vol.42 , pp. 12497-124502
    • Horii, K.1    Okuda, D.2    Morita, T.3    Mizuno, H.4
  • 44
    • 1642338019 scopus 로고    scopus 로고
    • Crystal structure of a platelet agglutinating factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)
    • Huang, K.F., Ko, T.P., Hung, C.C., Chu, J., Wang, A.H., Chiou, S.H., 2004. Crystal structure of a platelet agglutinating factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus). Biochem. J. 378, 399-407.
    • (2004) Biochem. J. , vol.378 , pp. 399-407
    • Huang, K.F.1    Ko, T.P.2    Hung, C.C.3    Chu, J.4    Wang, A.H.5    Chiou, S.H.6
  • 45
  • 47
    • 0345118115 scopus 로고    scopus 로고
    • Crystal structure of echicetin from Echis carinatus (Indian saw-scaled viper) at 2.4 Å resolution
    • J. Jasti, M. Paramasivam, A. Srinivasan, and T.P. Singh Crystal structure of echicetin from Echis carinatus (Indian saw-scaled viper) at 2.4 Å resolution J. Mol. Biol. 335 2004 167 176
    • (2004) J. Mol. Biol. , vol.335 , pp. 167-176
    • Jasti, J.1    Paramasivam, M.2    Srinivasan, A.3    Singh, T.P.4
  • 48
    • 0242321217 scopus 로고    scopus 로고
    • PO41, a snake venom metalloproteinase inhibitor isolated from Philander opossum serum
    • P.B. Jurgilas, A.G. Neves-Ferreira, G.B. Domont, and J. Perales PO41, a snake venom metalloproteinase inhibitor isolated from Philander opossum serum Toxicon 42 2003 621 628
    • (2003) Toxicon , vol.42 , pp. 621-628
    • Jurgilas, P.B.1    Neves-Ferreira, A.G.2    Domont, G.B.3    Perales, J.4
  • 49
    • 0029949611 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation as the result of cleavage of α2β1-integrin by the snake venom metalloproteinase jararhagin
    • A.S. Kamiguti, C.R. Hay, and M. Zuzel Inhibition of collagen-induced platelet aggregation as the result of cleavage of α2β1-integrin by the snake venom metalloproteinase jararhagin Biochem. J. 320 1996 635 641
    • (1996) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.2    Zuzel, M.3
  • 50
    • 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
    • A.S. Kamiguti, P. Gallagher, C. Marcinkiewicz, R.D. Theakston, M. Zuzel, and J.W. Fox Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function Fed. Eur. Biol. Soc. Lett. 549 2003 129 134
    • (2003) Fed. Eur. Biol. Soc. Lett. , vol.549 , pp. 129-134
    • Kamiguti, A.S.1    Gallagher, P.2    Marcinkiewicz, C.3    Theakston, R.D.4    Zuzel, M.5    Fox, J.W.6
  • 52
    • 0037023778 scopus 로고    scopus 로고
    • Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin αIIbβ3
    • A. Kasirer-Friede, J. Ware, L. Leng, P. Marchese, Z.M. Ruggeri, and S.J. Shattil Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin αIIbβ3 J. Biol. Chem. 277 2002 11949 11956
    • (2002) J. Biol. Chem. , vol.277 , pp. 11949-11956
    • Kasirer-Friede, A.1    Ware, J.2    Leng, L.3    Marchese, P.4    Ruggeri, Z.M.5    Shattil, S.J.6
  • 54
    • 0942276833 scopus 로고    scopus 로고
    • VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13
    • K. Kokame, M. Matsumoto, Y. Fujimura, and T. Miyata VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13 Blood 103 2004 607 612
    • (2004) Blood , vol.103 , pp. 607-612
    • Kokame, K.1    Matsumoto, M.2    Fujimura, Y.3    Miyata, T.4
  • 57
    • 0037682088 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a platelet glycoprotein Ib-binding protein from the venom of Trimeresurus stejnegeri
    • W.H. Lee, and Y. Zhang Molecular cloning and characterization of a platelet glycoprotein Ib-binding protein from the venom of Trimeresurus stejnegeri Toxicon 41 2003 885 892
    • (2003) Toxicon , vol.41 , pp. 885-892
    • Lee, W.H.1    Zhang, Y.2
  • 58
    • 0142124285 scopus 로고    scopus 로고
    • Stejnulxin, a novel snake C-type lectin-like protein from Trimeresurus stejnegeri venom is a potent platelet agonist acting specifically via GPVI
    • W.H. Lee, X.Y. Du, Q.M. Lu, K.J. Clemetson, and Y. Zhang Stejnulxin, a novel snake C-type lectin-like protein from Trimeresurus stejnegeri venom is a potent platelet agonist acting specifically via GPVI Thromb. Haemost. 90 2003 662 671
    • (2003) Thromb. Haemost. , vol.90 , pp. 662-671
    • Lee, W.H.1    Du, X.Y.2    Lu, Q.M.3    Clemetson, K.J.4    Zhang, Y.5
  • 59
    • 0031568217 scopus 로고    scopus 로고
    • Crovidisin, a collagen-binding protein isolated from snake venom of Crotalus viridis, prevents platelet-collagen interaction
    • C.Z. Liu, and T.F. Huang Crovidisin, a collagen-binding protein isolated from snake venom of Crotalus viridis, prevents platelet-collagen interaction Arch. Biochem. Biophys. 337 1997 291 299
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 291-299
    • Liu, C.Z.1    Huang, T.F.2
  • 60
    • 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
    • N. Maita, K. Nishio, E. Nishimoto, T. Matsui, Y. Shikamoto, T. Morita, J.E. Sadler, and H. Mizuno 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. 278 2003 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
  • 61
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • F.S. Markland Snake venoms and the hemostatic system Toxicon 36 1998 1749 1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 63
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • T. Matsui, Y. Fujimura, and K. Titani Snake venom proteases affecting hemostasis and thrombosis Biochim. Biophys. Acta 1477 2000 146 156
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 64
    • 0037172802 scopus 로고    scopus 로고
    • Binding site on human von willebrand factor of bitiscetin, a snake venom-derived platelet aggregation inducer
    • T. Matsui, J. Hamako, T. Matsushita, T. Nakayama, Y. Fujimura, and K. Titani Binding site on human von willebrand factor of bitiscetin, a snake venom-derived platelet aggregation inducer Biochemistry 41 2002 7939 7946
    • (2002) Biochemistry , vol.41 , pp. 7939-7946
    • Matsui, T.1    Hamako, J.2    Matsushita, T.3    Nakayama, T.4    Fujimura, Y.5    Titani, K.6
  • 66
    • 0141458943 scopus 로고    scopus 로고
    • Crystal structure of the platelet activator convulxin, a disulfide-linked α4β4 cyclic tetramer from the venom of Crotalus durissus terrificus
    • M.T. Murakami, S.P. Zela, L.M. Gava, S. Michelan-Duarte, A.C. Cintra, and R.K. Arni Crystal structure of the platelet activator convulxin, a disulfide-linked α4β4 cyclic tetramer from the venom of Crotalus durissus terrificus Biochem. Biophys. Res. Commun. 310 2003 478 482
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 478-482
    • Murakami, M.T.1    Zela, S.P.2    Gava, L.M.3    Michelan-Duarte, S.4    Cintra, A.C.5    Arni, R.K.6
  • 67
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion
    • D.G. Myles, L.H. Kimmel, C.P. Blobel, J.M. White, and P. Primakoff Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion Proc. Natl Acad. Sci. USA 91 1994 4195 4198
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4195-4198
    • Myles, D.G.1    Kimmel, L.H.2    Blobel, C.P.3    White, J.M.4    Primakoff, P.5
  • 68
    • 0035871849 scopus 로고    scopus 로고
    • Echicetin, a GPIb-binding snake C-type lectin from Echis carinatus, also contains a binding site for IgMκ responsible for platelet agglutination in plasma and inducing signal transduction
    • A. Navdaev, D. Dormann, J.M. Clemetson, and K.J. Clemetson Echicetin, a GPIb-binding snake C-type lectin from Echis carinatus, also contains a binding site for IgMκ responsible for platelet agglutination in plasma and inducing signal transduction Blood 97 2001 2333 2341
    • (2001) Blood , vol.97 , pp. 2333-2341
    • Navdaev, A.1    Dormann, D.2    Clemetson, J.M.3    Clemetson, K.J.4
  • 69
    • 0035877664 scopus 로고    scopus 로고
    • Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma (Malayan pit viper), stimulates platelets by binding to α2β1 integrin and glycoprotein Ib, activating Syk and phospholipase Cγ2, but does not involve the glycoprotein VI/Fc receptor γ chain collagen receptor
    • A. Navdaev, J.M. Clemetson, J. Polgar, B.E. Kehrel, M. Glauner, E. Magnenat, T.N. Wells, and K.J. Clemetson Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma (Malayan pit viper), stimulates platelets by binding to α2β1 integrin and glycoprotein Ib, activating Syk and phospholipase Cγ2, but does not involve the glycoprotein VI/Fc receptor γ chain collagen receptor J. Biol. Chem. 276 2001 20882 20889
    • (2001) J. Biol. Chem. , vol.276 , pp. 20882-20889
    • Navdaev, A.1    Clemetson, J.M.2    Polgar, J.3    Kehrel, B.E.4    Glauner, M.5    Magnenat, E.6    Wells, T.N.7    Clemetson, K.J.8
  • 70
    • 0037066708 scopus 로고    scopus 로고
    • Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum
    • A.G. Neves-Ferreira, J. Perales, J.W. Fox, J.D. Shannon, D.L. Makino, R.C. Garratt, and G.B. Domont Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum J. Biol. Chem. 277 2002 13129 13137
    • (2002) J. Biol. Chem. , vol.277 , pp. 13129-13137
    • Neves-Ferreira, A.G.1    Perales, J.2    Fox, J.W.3    Shannon, J.D.4    Makino, D.L.5    Garratt, R.C.6    Domont, G.B.7
  • 71
    • 0033838314 scopus 로고    scopus 로고
    • Persistence of platelet thrombus formation in arterioles of mice lacking both von Willebrand factor and fibrinogen
    • H. Ni, C.V. Denis, S. Subbarao, J.L. Degen, T.N. Sato, R.O. Hynes, and D.D. Wagner Persistence of platelet thrombus formation in arterioles of mice lacking both von Willebrand factor and fibrinogen J. Clin. Invest. 106 2000 385 392
    • (2000) J. Clin. Invest. , vol.106 , pp. 385-392
    • Ni, H.1    Denis, C.V.2    Subbarao, S.3    Degen, J.L.4    Sato, T.N.5    Hynes, R.O.6    Wagner, D.D.7
  • 72
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • B. Nieswandt, and S.P. Watson Platelet-collagen interaction: is GPVI the central receptor? Blood 102 2003 449 461
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 74
    • 0033559304 scopus 로고    scopus 로고
    • Conformational changes in the A3 domain of von Willebrand factor modulate the interaction of the A1 domain with platelet glycoprotein Ib
    • B. Obert, A. Houllier, D. Meyer, and J.P. Girma Conformational changes in the A3 domain of von Willebrand factor modulate the interaction of the A1 domain with platelet glycoprotein Ib Blood 93 1999 1959 1968
    • (1999) Blood , vol.93 , pp. 1959-1968
    • Obert, B.1    Houllier, A.2    Meyer, D.3    Girma, J.P.4
  • 76
    • 0026723481 scopus 로고
    • Characterization of three alboaggregins purified from Trimeresurus albolabris venom
    • M. Peng, W. Lu, and E.P. Kirby Characterization of three alboaggregins purified from Trimeresurus albolabris venom Thromb. Haemost. 67 1992 702 707
    • (1992) Thromb. Haemost. , vol.67 , pp. 702-707
    • Peng, M.1    Lu, W.2    Kirby, E.P.3
  • 77
    • 0028006809 scopus 로고
    • Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: Characterization of the cleavage sites within the glycoprotein Ibα subunit
    • D. Pidard, P. Renesto, M.C. Berndt, S. Rabhi, K.J. Clemetson, and M. Chignard Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ibα subunit Biochem. J. 303 1994 489 498
    • (1994) Biochem. J. , vol.303 , pp. 489-498
    • Pidard, D.1    Renesto, P.2    Berndt, M.C.3    Rabhi, S.4    Clemetson, K.J.5    Chignard, M.6
  • 80
    • 0032483550 scopus 로고    scopus 로고
    • Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • B. Savage, F. Almus-Jacobs, and Z.M. Ruggeri Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow Cell 94 1998 657 666
    • (1998) Cell , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 81
    • 0031195282 scopus 로고    scopus 로고
    • Sequence and biological activity of catrocollastatin-C: A disintegrin-like/cysteine-rich two-domain protein from Crotalus atrox venom
    • K. Shimokawa, J.D. Shannon, L.G. Jia, and J.W. Fox Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two-domain protein from Crotalus atrox venom Arch. Biochem. Biophys. 343 1997 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
  • 82
    • 0348111219 scopus 로고    scopus 로고
    • Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom
    • J. Shin, S.Y. Hong, K. Chung, I. Kang, Y. Jang, D.S. Kim, and W. Lee Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom Biochemistry 42 2003 14408 14415
    • (2003) Biochemistry , vol.42 , pp. 14408-14415
    • Shin, J.1    Hong, S.Y.2    Chung, K.3    Kang, I.4    Jang, Y.5    Kim, D.S.6    Lee, W.7
  • 84
    • 0035847108 scopus 로고    scopus 로고
    • Rhodocytin induces platelet aggregation by interacting with glycoprotein Ia/IIa (GPIa/IIa, integrin α2β1). Involvement of GPIa/IIa-associated src and protein tyrosinephosphorylation
    • K. Suzuki-Inoue, Y. Ozaki, M. Kainoh, Y. Shin, Y. Wu, Y. Yatomi, T. Ohmori, T. Tanaka, K. Satoh, and T. Morita Rhodocytin induces platelet aggregation by interacting with glycoprotein Ia/IIa (GPIa/IIa, integrin α2β1). Involvement of GPIa/IIa-associated src and protein tyrosinephosphorylation J. Biol. Chem. 276 2001 1643 1652
    • (2001) J. Biol. Chem. , vol.276 , pp. 1643-1652
    • Suzuki-Inoue, K.1    Ozaki, Y.2    Kainoh, M.3    Shin, Y.4    Wu, Y.5    Yatomi, Y.6    Ohmori, T.7    Tanaka, T.8    Satoh, K.9    Morita, T.10
  • 85
    • 0141763740 scopus 로고    scopus 로고
    • A tetrameric glycoprotein Ib-binding protein, agglucetin, from Formosan pit viper: Structure and interaction with human platelets
    • W.J. Wang, Q.D. Ling, M.Y. Liau, and T.F. Huang A tetrameric glycoprotein Ib-binding protein, agglucetin, from Formosan pit viper: structure and interaction with human platelets Thromb. Haemost. 90 2003 465 475
    • (2003) Thromb. Haemost. , vol.90 , pp. 465-475
    • Wang, W.J.1    Ling, Q.D.2    Liau, M.Y.3    Huang, T.F.4
  • 86
    • 0037423718 scopus 로고    scopus 로고
    • cDNA cloning and characterization of agkistin, a new metalloproteinase from Agkistrodon halys
    • S.H. Wang, X.C. Shen, G.Z. Yang, and X.F. Wu cDNA cloning and characterization of agkistin, a new metalloproteinase from Agkistrodon halys Biochem. Biophys. Res. Commun. 301 2003 298 303
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 298-303
    • Wang, S.H.1    Shen, X.C.2    Yang, G.Z.3    Wu, X.F.4
  • 87
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα. Identification of the sulfated tyrosine/anionic sequence Tyr276-Glu282 of glycoprotein Ibα as a binding site for von Willebrand factor and α-thrombin
    • C.M. Ward, R.K. Andrews, A.I. Smith, and M.C. Berndt Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα. Identification of the sulfated tyrosine/anionic sequence Tyr276-Glu282 of glycoprotein Ibα as a binding site for von Willebrand factor and α-thrombin Biochemistry 35 1996 4929 4938
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1    Andrews, R.K.2    Smith, A.I.3    Berndt, M.C.4
  • 88
    • 0010229714 scopus 로고    scopus 로고
    • Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other Elapidae venoms
    • C.M. Ward, D.V. Vinogradov, R.K. Andrews, and M.C. Berndt Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other Elapidae venoms Toxicon 34 1996 1203 1206
    • (1996) Toxicon , vol.34 , pp. 1203-1206
    • Ward, C.M.1    Vinogradov, D.V.2    Andrews, R.K.3    Berndt, M.C.4
  • 89
    • 0036709266 scopus 로고    scopus 로고
    • Purification and cloning of a novel C-type lectin-like protein with platelet aggregation activity from Trimeresurus mucrosquamatus venom
    • Q. Wei, Q.M. Lu, Y. Jin, R. Li, J.F. Wei, W.Y. Wang, and Y.L. Xiong Purification and cloning of a novel C-type lectin-like protein with platelet aggregation activity from Trimeresurus mucrosquamatus venom Toxicon 40 2002 1331 1338
    • (2002) Toxicon , vol.40 , pp. 1331-1338
    • Wei, Q.1    Lu, Q.M.2    Jin, Y.3    Li, R.4    Wei, J.F.5    Wang, W.Y.6    Xiong, Y.L.7
  • 90
    • 0035657710 scopus 로고    scopus 로고
    • Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox
    • W.B. Wu, H.C. Peng, and T.F. Huang Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox Thromb. Haemost. 86 2001 1501 1511
    • (2001) Thromb. Haemost. , vol.86 , pp. 1501-1511
    • Wu, W.B.1    Peng, H.C.2    Huang, T.F.3
  • 91
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • J.-P. Xiong, T. Stehle, S.L. Goodman, and M.A. Arnaout New insights into the structural basis of integrin activation Blood 102 2003 1155 1159
    • (2003) Blood , vol.102 , pp. 1155-1159
    • Xiong, J.-P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 92
    • 0347993780 scopus 로고    scopus 로고
    • A novel metalloprotease from gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains
    • W.K. You, H.J. Seo, K.H. Chung, and D.S. Kim A novel metalloprotease from gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains J. Biochem. (Tokyo) 134 2003 739 749
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 739-749
    • You, W.K.1    Seo, H.J.2    Chung, K.H.3    Kim, D.S.4
  • 93
    • 0029917707 scopus 로고    scopus 로고
    • The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain
    • Q. Zhou, C. Dangelmaier, and J.B. Smith The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain Biochem. Biophys. Res. Commun. 219 1996 720 726
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 720-726
    • Zhou, Q.1    Dangelmaier, C.2    Smith, J.B.3
  • 94
    • 0034653988 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of contortrostatin, a homodimeric disintegrin from southern copperhead snake venom
    • Q. Zhou, P. Hu, M.R. Ritter, S.D. Swenson, S. Argounova, A.L. Epstein, and F.S. Markland Molecular cloning and functional expression of contortrostatin, a homodimeric disintegrin from southern copperhead snake venom Arch. Biochem. Biophys. 375 2000 278 288
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 278-288
    • Zhou, Q.1    Hu, P.2    Ritter, M.R.3    Swenson, S.D.4    Argounova, S.5    Epstein, A.L.6    Markland, F.S.7
  • 95
    • 0037174925 scopus 로고    scopus 로고
    • The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast adhesion and signaling
    • P. Zigrino, A.S. Kamiguti, J. Eble, C. Drescher, R. Nischt, J.W. Fox, and C. Mauch The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast adhesion and signaling J. Biol. Chem. 277 2002 40528 40535
    • (2002) J. Biol. Chem. , vol.277 , pp. 40528-40535
    • Zigrino, P.1    Kamiguti, A.S.2    Eble, J.3    Drescher, C.4    Nischt, R.5    Fox, J.W.6    Mauch, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.