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Volumn 1, Issue 2, 2003, Pages 257-269

Inhibition of von Willebrand factor-GPIb/IX/V interactions as a strategy to prevent arterial thrombosis

Author keywords

animal model; antiplatelet therapy; gain of function mutation; GPIb ; platelet receptor; thrombosis; von Willebrand disease; von Willebrand factor

Indexed keywords

ANTITHROMBOCYTIC AGENT; THROMBIN RECEPTOR; VON WILLEBRAND FACTOR;

EID: 2142718259     PISSN: 14779072     EISSN: 17448344     Source Type: Journal    
DOI: 10.1586/14779072.1.2.257     Document Type: Review
Times cited : (21)

References (95)
  • 1
    • 0030983708 scopus 로고    scopus 로고
    • Mortality by cause for eight regions of the world: Global Burden of Disease Study
    • Murray CJ, Lopez AD. Mortality by cause for eight regions of the world: Global Burden of Disease Study. Lancet 349, 1269 – 1276 (1997).
    • (1997) Lancet , vol.349 , pp. 1269-1276
    • Murray, C.J.1    Lopez, A.D.2
  • 2
    • 0031786309 scopus 로고    scopus 로고
    • Current issues in reperfusion therapy. Am
    • Gersh BJ. Current issues in reperfusion therapy. Am. j Canliol. 82,3P-11P (1998).
    • (1998) j Canliol , vol.82 , pp. 3P-11P
    • Gersh, B.J.1
  • 3
    • 0033573790 scopus 로고    scopus 로고
    • Platelet GPIIb-IIIa blockers
    • Topol EJ, Byzova TV, Plow EE Platelet GPIIb-IIIa blockers. Lancet 353 (9148), 227 – 231 (1999).
    • (1999) Lancet , vol.353 , Issue.9148 , pp. 227-231
    • Topol, E.J.1    Byzova, T.V.2    Plow, E.E.3
  • 4
    • 85018878242 scopus 로고    scopus 로고
    • Antiplatelet therapy in cardiology
    • Thrombotic and Non-thrombotic Disonlers, Gresele P, Page C, Fuster V, Vermylen J (Eds). Cambridge University Press, Cambridge, UK
    • Aronow HD, Topol EJ. Antiplatelet therapy in cardiology. In: Platelets in Thrombotic and Non-thrombotic Disonlers: Gresele P, Page C, Fuster V, Vermylen J (Eds). Cambridge University Press, Cambridge, UK (2002).
    • (2002) In: Platelets in
    • Aronow, H.D.1    Topol, E.J.2
  • 5
    • 0026680643 scopus 로고
    • Tumor necrosis factor-a modulation of glycoprotein Iba expression in human endothelial and erythroleukemia cells
    • Rajagopalan V, Essex DW, Shapiro SS, Konlde BA. Tumor necrosis factor-a modulation of glycoprotein Iba expression in human endothelial and erythroleukemia cells. B/ooc/ 80, 153 – 161 (1992).
    • (1992) B/ooc/ , vol.80 , pp. 153-161
    • Rajagopalan, V.1    Essex, D.W.2    Shapiro, S.S.3    Konlde, B.A.4
  • 6
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Iba and its complex with von Willebrand factor Al domain
    • Huizinga EG, Tsuji S, Romijn RA et al Structures of glycoprotein Iba and its complex with von Willebrand factor Al domain. Science 297, 1176 – 1179 (2002).
    • (2002) Science , vol.297 , pp. 1176-1179
    • Huizinga, E.G.1    Tsuji, S.2    Romijn, R.A.3
  • 7
    • 12944317287 scopus 로고    scopus 로고
    • Requirement of leucine-rich repeats of glycoprotein (GP) Iba for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex
    • Shen Y, Romo GM, Dong JF et al Requirement of leucine-rich repeats of glycoprotein (GP) Iba for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex. B/ooc/ 95, 903 – 910 (2000).
    • (2000) B/ooc/ , vol.95 , pp. 903-910
    • Shen, Y.1    Romo, G.M.2    Dong, J.F.3
  • 8
    • 0037127313 scopus 로고    scopus 로고
    • Interaction between platelet glycoprotein Iba and filamin-1 is essential for glycoprotein Ib/IX receptor anchorage at high shear
    • Williamson D, Pikovski I, Cranmer SL et al Interaction between platelet glycoprotein Iba and filamin-1 is essential for glycoprotein Ib/IX receptor anchorage at high shear. j Biol. Chem. 277, 2151 – 2159 (2002).
    • (2002) j Biol. Chem , vol.277 , pp. 2151-2159
    • Williamson, D.1    Pikovski, I.2    Cranmer, S.L.3
  • 9
    • 0034731480 scopus 로고    scopus 로고
    • Synergistic adhesive interactions and signaling mechanisms operating between platelet glycoprotein Ib/IX and integrin allb13 3. Studies in human platelets and transfected Chinese hamster ovary cells
    • Yap CL, Hughan SC, Cranmer SL et al Synergistic adhesive interactions and signaling mechanisms operating between platelet glycoprotein Ib/IX and integrin allb13 3. Studies in human platelets and transfected Chinese hamster ovary cells.1. Biol. Chem. 275,41377-41388 (2000).
    • (2000) 1. Biol. Chem. , vol.275 , pp. 41377-41388
    • Yap, C.L.1    Hughan, S.C.2    Cranmer, S.L.3
  • 10
    • 0035437184 scopus 로고    scopus 로고
    • Interaction of calmodulin with the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews RK, Munday AD, Mitchell CA, Berndt MC. Interaction of calmodulin with the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. B/ooc/ 98, 681 – 687 (2001).
    • (2001) B/ooc/ , vol.98 , pp. 681-687
    • Andrews, R.K.1    Munday, A.D.2    Mitchell, C.A.3    Berndt, M.C.4
  • 11
    • 0038542920 scopus 로고    scopus 로고
    • Interaction between von Willebrand factor and glycoprotein Ib activates Src kinase in human platelets: role of phosphoinositide 3-kinase
    • Wu Y, Asazuma N, Satoh K et al Interaction between von Willebrand factor and glycoprotein Ib activates Src kinase in human platelets: role of phosphoinositide 3-kinase. Blood 101,3469-3476 (2003).
    • (2003) Blood , vol.101 , pp. 3469-3476
    • Wu, Y.1    Asazuma, N.2    Satoh, K.3
  • 12
    • 0034051457 scopus 로고    scopus 로고
    • Molecular pathogenesis of Bernard–Soulier syndrome
    • Hayashi T, Suzuki K. Molecular pathogenesis of Bernard–Soulier syndrome. Semin. Thromb. Hemost. 26, 53 – 59 (2000).
    • (2000) Semin. Thromb. Hemost , vol.26 , pp. 53-59
    • Hayashi, T.1    Suzuki, K.2
  • 13
    • 0035885959 scopus 로고    scopus 로고
    • Phenotype changes resulting in high-affinity binding of von Willebrand factor to recombinant glycoprotein Ib—IX: analysis of the platelet-type von Willebrand disease mutations
    • Tait AS, Cranmer SL, Jackson SP, Dawes IW, Chong BH. Phenotype changes resulting in high-affinity binding of von Willebrand factor to recombinant glycoprotein Ib—IX: analysis of the platelet-type von Willebrand disease mutations. B/ooc/ 98, 1812 – 1818 (2001).
    • (2001) B/ooc/ , vol.98 , pp. 1812-1818
    • Tait, A.S.1    Cranmer, S.L.2    Jackson, S.P.3    Dawes, I.W.4    Chong, B.H.5
  • 14
    • 0017658776 scopus 로고
    • Synthesis of Factor VIII antigen by cultured guinea-pig megakaryocytes
    • Nachman R, Levine R, Jaffe EA. Synthesis of Factor VIII antigen by cultured guinea-pig megakaryocytes. j Clin. Invest. 60, 914 – 9921 (1977).
    • (1977) j Clin. Invest , vol.60 , pp. 914-9921
    • Nachman, R.1    Levine, R.2    Jaffe, E.A.3
  • 15
    • 0011694667 scopus 로고
    • Hoyer LW Nachman RL. Synthesis of von Willebrand factor by cultured human endothelial cells
    • Jaffe EA, Hoyer LW Nachman RL. Synthesis of von Willebrand factor by cultured human endothelial cells. Pmc. Nat! Acad. Sci. USA 71, 1906 – 1909 (1974).
    • (1974) Pmc. Nat! Acad. Sci. USA , vol.71 , pp. 1906-1909
    • Jaffe, E.A.1
  • 16
    • 0022532391 scopus 로고
    • cDNA sequences for human von Willebrand factor reveal five types of repeated domains and five possible protein sequence polymorphisms
    • Shelton-Inloes BB, Titani K, Sadler JE. cDNA sequences for human von Willebrand factor reveal five types of repeated domains and five possible protein sequence polymorphisms. Biochemistry 25, 3164 – 3171 (1986).
    • (1986) Biochemistry , vol.25 , pp. 3164-3171
    • Shelton-Inloes, B.B.1    Titani, K.2    Sadler, J.E.3
  • 17
    • 0037674992 scopus 로고    scopus 로고
    • Mapping the collagen-binding site in the von Willebrand factor A3-domain
    • Romijn RA, Westein E, Bouma B et al Mapping the collagen-binding site in the von Willebrand factor A3-domain. j Biol. Chem. 278, 15035 – 15039 (2003).
    • (2003) j Biol. Chem , vol.278 , pp. 15035-15039
    • Romijn, R.A.1    Westein, E.2    Bouma, B.3
  • 18
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand Factor Al domain and implications for the binding of platelet glycoprotein Ib
    • Emsley J, Cruz M, Handin R, Liddington R. Crystal structure of the von Willebrand Factor Al domain and implications for the binding of platelet glycoprotein Ib. j Biol. Chem. 273, 10396 – 10401 (1998).
    • (1998) j Biol. Chem , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Handin, R.3    Liddington, R.4
  • 19
    • 0032521230 scopus 로고    scopus 로고
    • Molecular modeling of ligand and mutation sites of the type A domains of human von Willebrand factor and their relevance to von Willebrand's disease
    • Jenkins PV, Pasi KJ, Perkins SJ. Molecular modeling of ligand and mutation sites of the type A domains of human von Willebrand factor and their relevance to von Willebrand's disease. B/ooc/91, 2032 -2044 (1998).
    • (1998) B/ooc/91 , pp. 2032-2044
    • Jenkins, P.V.1    Pasi, K.J.2    Perkins, S.J.3
  • 20
    • 0028360720 scopus 로고
    • The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions
    • Perkins SJ, Smith KF, Williams SC, Hans PI, Chapman D, Sim RB. The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions. j Mal Biol. 238, 104 – 119 (1994).
    • (1994) j Mal Biol , vol.238 , pp. 104-119
    • Perkins, S.J.1    Smith, K.F.2    Williams, S.C.3    Hans, P.I.4    Chapman, D.5    Sim, R.B.6
  • 21
    • 0025951858 scopus 로고
    • Identification of discontinuous von Willebrand factor sequences involved in complex formation with botrocetin
    • Sugimoto M, Mohri H, McClintock RA, Ruggeri ZM. Identification of discontinuous von Willebrand factor sequences involved in complex formation with botrocetin. j Biol. Chem. 266, 18172 – 18178 (1991).
    • (1991) j Biol. Chem , vol.266 , pp. 18172-18178
    • Sugimoto, M.1    Mohri, H.2    McClintock, R.A.3    Ruggeri, Z.M.4
  • 22
    • 0031941354 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor Al domain in complex with the function blocking NMC-4 Fab
    • Celikel R, Varughese KT, Madhusudan, Yoshioka A, Ware J, Ruggeri ZM. Crystal structure of the von Willebrand factor Al domain in complex with the function blocking NMC-4 Fab. Nat. Struct. Biol. 5, 189 – 194 (1998).
    • (1998) Nat. Struct. Biol , vol.5 , pp. 189-194
    • Celikel, R.1    Varughese, K.T.2    Madhusudan, Y.A.3    Ware, J.4    Ruggeri, Z.M.5
  • 23
    • 0034724673 scopus 로고    scopus 로고
    • Modeling and functional analysis of the interaction between von Willebrand factor Al domain and glycoprotein Iba
    • Vasudevan S, Roberts JR, McClintock RA et al Modeling and functional analysis of the interaction between von Willebrand factor Al domain and glycoprotein Iba.1. Biol. Chem. 275,12763-12768 (2000).
    • (2000) 1. Biol. Chem. , vol.275 , pp. 12763-12768
    • Vasudevan, S.1    Roberts, J.R.2    McClintock, R.A.3
  • 24
    • 0034646604 scopus 로고    scopus 로고
    • Localization of von Willebrand factor-binding sites for platelet glycoprotein Ib and botrocetin by charged-to-alanine scanning mutagenesis
    • Matsushita T, Meyer D, Sadler JE. Localization of von Willebrand factor-binding sites for platelet glycoprotein Ib and botrocetin by charged-to-alanine scanning mutagenesis. j Biol. Chem. 275, 11044 – 11049 (2000).
    • (2000) j Biol. Chem , vol.275 , pp. 11044-11049
    • Matsushita, T.1    Meyer, D.2    Sadler, J.E.3
  • 25
    • 0034705544 scopus 로고    scopus 로고
    • Mapping the glycoprotein Ib-binding site in the von Willebrand factor Al domain
    • Cruz MA, Diacovo TG, Emsley J, Liddington R, Handin RI. Mapping the glycoprotein Ib-binding site in the von Willebrand factor Al domain. j Biol. Chem. 275, 19098 – 19105 (2000).
    • (2000) j Biol. Chem , vol.275 , pp. 19098-19105
    • Cruz, M.A.1    Diacovo, T.G.2    Emsley, J.3    Liddington, R.4    Handin, R.I.5
  • 26
    • 0037441595 scopus 로고    scopus 로고
    • Shielding the front-strand 133 of the von Willebrand factor Al domain inhibits its binding to platelet glycoprotein Iba
    • Bonnefoy A, Yamamoto H, Thys C, Kito M, Vermylen J, Hoylaerts ME. Shielding the front-strand 133 of the von Willebrand factor Al domain inhibits its binding to platelet glycoprotein Iba. Blood 101, 1375 – 1383 (2003).
    • (2003) Blood , vol.101 , pp. 1375-1383
    • Bonnefoy, A.1    Yamamoto, H.2    Thys, C.3    Kito, M.4    Vermylen, J.5    Hoylaerts, M.E.6
  • 28
    • 0026630044 scopus 로고
    • Impaired intracellular transport produced by a subset of Type IIA von Willebrand disease mutations
    • Lyons SE, Bruck ME, Bowie EJ, Ginsburg D. Impaired intracellular transport produced by a subset of Type IIA von Willebrand disease mutations. j Biol. Chem. 267, 4424 – 4430 (1992).
    • (1992) j Biol. Chem , vol.267 , pp. 4424-4430
    • Lyons, S.E.1    Bruck, M.E.2    Bowie, E.J.3    Ginsburg, D.4
  • 29
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler JE. Biochemistry and genetics of von Willebrand factor. Ann. Rev Biochem. 67, 395 – 424 (1998).
    • (1998) Ann. Rev Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 30
    • 0026661585 scopus 로고
    • Modulation of platelet function through adhesion receptors. A dual role for glycoprotein IIb—IIIa (integrin a11,133) mediated by fibrinogen and glycoprotein Ib-von Willebrand factor
    • Savage B, Shattil SJ, Ruggeri ZM. Modulation of platelet function through adhesion receptors. A dual role for glycoprotein IIb—IIIa (integrin a11,133) mediated by fibrinogen and glycoprotein Ib-von Willebrand factor. j Biol. Chem. 267, 11300 – 11306 (1992).
    • (1992) j Biol. Chem , vol.267 , pp. 11300-11306
    • Savage, B.1    Shattil, S.J.2    Ruggeri, Z.M.3
  • 31
    • 0033838314 scopus 로고    scopus 로고
    • Persistence of platelet thrombus formation in arterioles of mice lacking both von Willebrand factor and fibrinogen
    • Ni H, Denis CV, Subbarao S et al Persistence of platelet thrombus formation in arterioles of mice lacking both von Willebrand factor and fibrinogen. j Clin. Invest 106, 385 – 392 (2000).
    • (2000) j Clin. Invest , vol.106 , pp. 385-392
    • Ni, H.1    Denis, C.V.2    Subbarao, S.3
  • 32
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage B, Saldivar E, Ruggeri ZM. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Ce1184, 289 – 297 (1996).
    • (1996) Ce1184 , pp. 289-297
    • Savage, B.1    Saldivar, E.2    Ruggeri, Z.M.3
  • 34
    • 0033548494 scopus 로고    scopus 로고
    • Single-polymer dynamics in steady shear flow
    • Smith DE, Babcock HP, Chu S. Single-polymer dynamics in steady shear flow. Science 283 (5408), 1724 – 1727 (1999).
    • (1999) Science , vol.283 , Issue.5408 , pp. 1724-1727
    • Smith, D.E.1    Babcock, H.P.2    Chu, S.3
  • 35
    • 0029907370 scopus 로고    scopus 로고
    • Von Willebrand factor: molecular size and functional activity
    • Furlan M. Von Willebrand factor: molecular size and functional activity. Ann. Hematol 72, 341 – 348 (1996).
    • (1996) Ann. Hematol , vol.72 , pp. 341-348
    • Furlan, M.1
  • 36
    • 0038446690 scopus 로고    scopus 로고
    • Aspects of hydrodynamic shear regulating shear-induced platelet activation and self-association of von Willebrand factor in suspension
    • Shankaran H, Alexandridis P, Neelamegham S. Aspects of hydrodynamic shear regulating shear-induced platelet activation and self-association of von Willebrand factor in suspension. Blood 101, 2637 – 2645 (2003).
    • (2003) Blood , vol.101 , pp. 2637-2645
    • Shankaran, H.1    Alexandridis, P.2    Neelamegham, S.3
  • 37
    • 0030816261 scopus 로고    scopus 로고
    • Prospective study of hemostatic factors and incidence of coronary heart disease: the Atherosclerosis Risk in Communities (ARIC) Study
    • Folsom AR, Wu KK, Rosamond WD, Sharrett AR, Chambless LE. Prospective study of hemostatic factors and incidence of coronary heart disease: the Atherosclerosis Risk in Communities (ARIC) Study. Circulation 96, 1102 – 1108 (1997).
    • (1997) Circulation , vol.96 , pp. 1102-1108
    • Folsom, A.R.1    Wu, K.K.2    Rosamond, W.D.3    Sharrett, A.R.4    Chambless, L.E.5
  • 38
    • 0033537485 scopus 로고    scopus 로고
    • Enhanced shear-induced platelet aggregation in acute myocardial infarction
    • Goto S, Sakai H, Goto M et al Enhanced shear-induced platelet aggregation in acute myocardial infarction. Circulation 99, 608 – 613 (1999).
    • (1999) Circulation , vol.99 , pp. 608-613
    • Goto, S.1    Sakai, H.2    Goto, M.3
  • 39
    • 0030972393 scopus 로고    scopus 로고
    • Fibrin(ogen) and von Willebrand factor deposition are associated with intimal thickening after balloon angioplasty of the rabbit carotid artery
    • Bosmans JM, Kockx MM, Vrints CJ, Bult H, De Meyer GR, Herman AG. Fibrin(ogen) and von Willebrand factor deposition are associated with intimal thickening after balloon angioplasty of the rabbit carotid artery. Arterioscler. Thromb. Vasc. Biol. 17, 634 – 645 (1997).
    • (1997) Arterioscler. Thromb. Vasc. Biol , vol.17 , pp. 634-645
    • Bosmans, J.M.1    Kockx, M.M.2    Vrints, C.J.3    Bult, H.4    De Meyer, G.R.5    Herman, A.G.6
  • 41
    • 0035490306 scopus 로고    scopus 로고
    • Remodeling and suppression of intimal hyperplasia of vascular grafts with a distal arteriovenous fistula in a rat model
    • Qin F, Dardik H, Pangilinan A, Robinson J, Chuy J, Wengerter K. Remodeling and suppression of intimal hyperplasia of vascular grafts with a distal arteriovenous fistula in a rat model. j Vasc. Surg. 34, 701 – 706 (2001).
    • (2001) j Vasc. Surg , vol.34 , pp. 701-706
    • Qin, F.1    Dardik, H.2    Pangilinan, A.3    Robinson, J.4    Chuy, J.5    Wengerter, K.6
  • 42
    • 0037097809 scopus 로고    scopus 로고
    • Endothelial von Willebrand factor recruits platelets to atherosclerosis-prone sites in response to hypercholesterolemia
    • Theilmeier G, Michiels C, Spaepen E et al Endothelial von Willebrand factor recruits platelets to atherosclerosis-prone sites in response to hypercholesterolemia. B/ooc/99, 4486 – 4493 (2002).
    • (2002) B/ooc/99 , pp. 4486-4493
    • Theilmeier, G.1    Michiels, C.2    Spaepen, E.3
  • 43
    • 0032857493 scopus 로고    scopus 로고
    • Circulating activated platelets assist THP-1 monocytoid/endothelial cell interaction under shear stress
    • Theilmeier G, Lenaerts T, Remade C, Collen D, Vermylen J, Hoylaerts ME. Circulating activated platelets assist THP-1 monocytoid/endothelial cell interaction under shear stress. Blood 94, 2725 – 2734 (1999).
    • (1999) Blood , vol.94 , pp. 2725-2734
    • Theilmeier, G.1    Lenaerts, T.2    Remade, C.3    Collen, D.4    Vermylen, J.5    Hoylaerts, M.E.6
  • 44
    • 0035469891 scopus 로고    scopus 로고
    • Localized reduction of atherosclerosis in von Willebrand factor-deficient mice
    • Methia N, Andre P, Denis CV, Economopoulos M, Wagner DD. Localized reduction of atherosclerosis in von Willebrand factor-deficient mice. Blood 98, 1424 – 1428 (2001).
    • (2001) Blood , vol.98 , pp. 1424-1428
    • Methia, N.1    Andre, P.2    Denis, C.V.3    Economopoulos, M.4    Wagner, D.D.5
  • 45
    • 0022852282 scopus 로고
    • Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation
    • Moake JL, Turner NA, Stathopoulos NA, Nolasco LH, Hellums JD. Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation. j Clin. Invest. 78, 1456 – 1461 (1986).
    • (1986) j Clin. Invest , vol.78 , pp. 1456-1461
    • Moake, J.L.1    Turner, N.A.2    Stathopoulos, N.A.3    Nolasco, L.H.4    Hellums, J.D.5
  • 47
    • 0029878123 scopus 로고    scopus 로고
    • Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion
    • Tsai HM. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. B/ooc/ 87, 4235 – 4244 (1996).
    • (1996) B/ooc/ , vol.87 , pp. 4235-4244
    • Tsai, H.M.1
  • 48
    • 0025044664 scopus 로고
    • Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in Type IIA von Willebrand factor
    • Dent JA, Berkowitz SD, Ware J, Kasper CK, Ruggeri ZM. Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in Type IIA von Willebrand factor. Proc. Natl Acad. Li. USA 87, 6306 – 6310 (1990).
    • (1990) Proc. Natl Acad. Li. USA , vol.87 , pp. 6306-6310
    • Dent, J.A.1    Berkowitz, S.D.2    Ware, J.3    Kasper, C.K.4    Ruggeri, Z.M.5
  • 49
    • 0028266474 scopus 로고
    • Shear stress enhances the proteolysis of von Willebrand factor in normal plasma
    • Tsai HM, Sussman II, Nagel RL. Shear stress enhances the proteolysis of von Willebrand factor in normal plasma. Blood 83, 2171 – 2179 (1994).
    • (1994) Blood , vol.83 , pp. 2171-2179
    • Tsai, H.M.1    Sussman, I.I.2    Nagel, R.L.3
  • 50
    • 0036893186 scopus 로고    scopus 로고
    • ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
    • Dong JF, Moake JL, Nolasco L et al ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood 100, 4033 – 4039 (2002).
    • (2002) Blood , vol.100 , pp. 4033-4039
    • Dong, J.F.1    Moake, J.L.2    Nolasco, L.3
  • 51
    • 0020428664 scopus 로고
    • Unusually large plasma Factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura
    • Moake JL, Rudy CK, Troll JH et al Unusually large plasma Factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura. N. Engl. Med. 307, 1432 – 1435 (1982).
    • (1982) N. Engl. Med , vol.307 , pp. 1432-1435
    • Moake, J.L.1    Rudy, C.K.2    Troll, J.H.3
  • 52
    • 0030980679 scopus 로고    scopus 로고
    • Proteolytic cleavage of recombinant Type 2A von Willebrand factor mutants R834W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-1
    • Tsai HM, Sussman II, Ginsburg D, Lankhof H, Sixrna JJ, Nagel RL. Proteolytic cleavage of recombinant Type 2A von Willebrand factor mutants R834W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-1. Blooc189, 1954 -1962 (1997).
    • (1997) Blooc189 , pp. 1954-1962
    • Tsai, H.M.1    Sussman, I.I.2    Ginsburg, D.3    Lankhof, H.4    Sixrna, J.J.5    Nagel, R.L.6
  • 53
    • 0037039439 scopus 로고    scopus 로고
    • Functional self-association of von Willebrand factor during platelet adhesion under flow
    • Savage B, Sixrna JJ, Ruggeri ZM. Functional self-association of von Willebrand factor during platelet adhesion under flow. Proc. Natl Acad. Li. USA 99, 425 – 430 (2002).
    • (2002) Proc. Natl Acad. Li. USA , vol.99 , pp. 425-430
    • Savage, B.1    Sixrna, J.J.2    Ruggeri, Z.M.3
  • 54
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1. I
    • Xie L, Chesterman CN, Hogg PJ. Control of von Willebrand factor multimer size by thrombospondin-1. I Exp. Med 193, 1341 – 1349 (2001).
    • (2001) Exp. Med , vol.193 , pp. 1341-1349
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 55
    • 85018906918 scopus 로고    scopus 로고
    • Proteolysis of ultra-large von Willebrand Factor multimers on the endothelial surface requires protease docking and is inhibited by thrombospondin-1
    • Annual American Society for Hematology Philidelphia, PA, USA (Abstract 457).
    • Dong JF, Bernardo A, Nolasco L, Padilla A, Moake J, Lopez J. Proteolysis of ultra-large von Willebrand Factor multimers on the endothelial surface requires protease docking and is inhibited by thrombospondin-1. Annual American Society for Hematology Philidelphia, PA, USA (2002) (Abstract 457).
    • (2002)
    • Dong, J.F.1    Bernardo, A.2    Nolasco, L.3    Padilla, A.4    Moake, J.5    Lopez, J.6
  • 56
    • 0026730092 scopus 로고
    • A monomeric von Willebrand factor fragment, Leu-504—Lys-728, inhibits von Willebrand factor interaction with glycoprotein lb-TX [coryeeted]
    • Erratum in: Proc. Natl. Acad. Sci. USA 90, 3118 (1993).
    • Gralnick HR, Williams S, McKeown L et al A monomeric von Willebrand factor fragment, Leu-504—Lys-728, inhibits von Willebrand factor interaction with glycoprotein lb-TX [coryeeted]. f3vc Nat! Acad. Li USA 89,7880-7884 (1992). Erratum in: Proc. Natl. Acad. Sci. USA 90, 3118 (1993).
    • (1992) f3vc Nat! Acad. Li USA , vol.89 , pp. 7880-7884
    • Gralnick, H.R.1    Williams, S.2    McKeown, L.3
  • 57
    • 0030586152 scopus 로고    scopus 로고
    • Guinea-pig blood: a model for the pharmacologic modulation of the GPIb/IX-vWF axis
    • Andre P, Hamaud P, Bal dit Sollier C et al Guinea-pig blood: a model for the pharmacologic modulation of the GPIb/IX-vWF axis. Thromb. Res. 83, 127 – 136 (1996).
    • (1996) Thromb. Res , vol.83 , pp. 127-136
    • Andre, P.1    Hamaud, P.2    Bal dit Sollier, C.3
  • 58
    • 0028240844 scopus 로고
    • Blockade of platelet membrane glycoprotein lb receptors delays intracoronary thrombogenesis, enhances thrombolysis and delays coronary artery reocdusion in dogs
    • Yao SK, Ober JC, Garfinkel LI et al Blockade of platelet membrane glycoprotein lb receptors delays intracoronary thrombogenesis, enhances thrombolysis and delays coronary artery reocdusion in dogs. Ciaulation 89, 2822 – 2828 (1994).
    • (1994) Ciaulation , vol.89 , pp. 2822-2828
    • Yao, S.K.1    Ober, J.C.2    Garfinkel, L.I.3
  • 59
    • 0028641293 scopus 로고
    • Abolition of cyclic flow variations in stenosed, endothelium-injured coronary arteries in nonhuman primates with a peptide fragment (VCL) derived from human plasma von Willebrand factor-glycoprotein lb binding domain
    • McGhie AI, McNatt J, Ezov N et al Abolition of cyclic flow variations in stenosed, endothelium-injured coronary arteries in nonhuman primates with a peptide fragment (VCL) derived from human plasma von Willebrand factor-glycoprotein lb binding domain. Circulation 90, 2976 – 2981 (1994).
    • (1994) Circulation , vol.90 , pp. 2976-2981
    • McGhie, A.I.1    McNatt, J.2    Ezov, N.3
  • 60
    • 0029077090 scopus 로고
    • VCL, an antagonist of the platelet GPlb receptor, markedly inhibits platelet adhesion and intimal thickening after balloon injury in the rat
    • Zahger D, Fishbein MC, Garfinkel LI et al VCL, an antagonist of the platelet GPlb receptor, markedly inhibits platelet adhesion and intimal thickening after balloon injury in the rat. Ciaulation 92, 1269 – 1273 (1995).
    • (1995) Ciaulation , vol.92 , pp. 1269-1273
    • Zahger, D.1    Fishbein, M.C.2    Garfinkel, L.I.3
  • 61
    • 0035437196 scopus 로고    scopus 로고
    • Epitope mapping of inhibitory antibodies against platelet glycoprotein Iba reveals interaction between the leucine-rich repeat N-terminal and C-terminal flanking domains of glycoprotein Iba
    • Cauwenberghs N, Vanhoorelbeke K, Vauterin SN et al Epitope mapping of inhibitory antibodies against platelet glycoprotein Iba reveals interaction between the leucine-rich repeat N-terminal and C-terminal flanking domains of glycoprotein Iba. B/ooc/98, 652 – 660 (2001).
    • (2001) B/ooc/98 , pp. 652-660
    • Cauwenberghs, N.1    Vanhoorelbeke, K.2    Vauterin, S.N.3
  • 62
    • 0029951698 scopus 로고    scopus 로고
    • Platelet-type von Willebrand disease
    • Miller JL. Platelet-type von Willebrand disease. Thmmh I-Lemost. 75, 865 – 869 (1996).
    • (1996) Thmmh I-Lemost , vol.75 , pp. 865-869
    • Miller, J.L.1
  • 63
    • 0037093219 scopus 로고    scopus 로고
    • Inhibition of the von Willebrand (vWF) -collagen interaction by an antihuman vWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons
    • Wu D, Vanhoorelbeke K, Cauwenberghs N et al Inhibition of the von Willebrand (vWF) -collagen interaction by an antihuman vWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons. B/ooc/ 99, 3623 – 3628 (2002).
    • (2002) B/ooc/ , vol.99 , pp. 3623-3628
    • Wu, D.1    Vanhoorelbeke, K.2    Cauwenberghs, N.3
  • 64
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Iba. Identification of the sulfated tyrosine/anionic sequence Tyr-276—Glu-282 of glycoprotein Iba as a binding site for von Willebrand factor and a-thrombin
    • Ward CM, Andrews RK, Smith AI, Berndt MC. Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Iba. Identification of the sulfated tyrosine/anionic sequence Tyr-276—Glu-282 of glycoprotein Iba as a binding site for von Willebrand factor and a-thrombin. Biochemistry 35, 4929 – 4938 (1996).
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1    Andrews, R.K.2    Smith, A.I.3    Berndt, M.C.4
  • 65
    • 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
    • De Luca M, Dunlop LC, Andrews RK et al 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, 26734 – 26737 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 26734-26737
    • De Luca, M.1    Dunlop, L.C.2    Andrews, R.K.3
  • 66
    • 0032429437 scopus 로고    scopus 로고
    • Effects of a metalloproteinase that truncates P-selectin glycoprotein ligand on neutrophil-induced cardiac dysfunction in ischaemia/reperfusion
    • Lefer AM, Campbell B, Shin YK. Effects of a metalloproteinase that truncates P-selectin glycoprotein ligand on neutrophil-induced cardiac dysfunction in ischaemia/reperfusion. j Mal Cell Can:hal 30, 2561 – 2566 (1998).
    • (1998) j Mal Cell Can:hal , vol.30 , pp. 2561-2566
    • Lefer, A.M.1    Campbell, B.2    Shin, Y.K.3
  • 67
    • 0032031490 scopus 로고    scopus 로고
    • Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib antagonist from venom of Gratalus atrox
    • Chang MC, Lin HK, Peng HC, Huang TE Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib antagonist from venom of Gratalus atrox. BloocI 91, 1582 – 1589 (1998).
    • (1998) BloocI , vol.91 , pp. 1582-1589
    • Chang, M.C.1    Lin, H.K.2    Peng, H.C.3    Huang, T.E.4
  • 68
    • 0035657710 scopus 로고    scopus 로고
    • Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of
    • Wu WB, Peng HC, Huang TE Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Gratalus atrox. Thromb. kkemost. 86, 1501 – 1511 (2001).
    • (2001) Gratalus atrox. Thromb. kkemost , vol.86 , pp. 1501-1511
    • Wu, W.B.1    Peng, H.C.2    Huang, T.E.3
  • 69
    • 0030800626 scopus 로고    scopus 로고
    • Antithrombotic effects and bleeding risk of AJvW-2, a monoclonal antibody against human von Willebrand factor
    • Kageyama S, Yamamoto H, Nagano M, Arisaka H, Kayahara T, Yoshimoto R. Antithrombotic effects and bleeding risk of AJvW-2, a monoclonal antibody against human von Willebrand factor. BE J. Pharmacol 122, 165 – 171 (1997).
    • (1997) BE J. Pharmacol , vol.122 , pp. 165-171
    • Kageyama, S.1    Yamamoto, H.2    Nagano, M.3    Arisaka, H.4    Kayahara, T.5    Yoshimoto, R.6
  • 70
    • 0032918204 scopus 로고    scopus 로고
    • AJvW-2, an antivWF monoclonal antibody, inhibits enhanced platelet aggregation induced by high shear stress in platelet-rich plasma from patients with acute coronary syndromes
    • Eto K, Isshiki T, Yamamoto H et al AJvW-2, an antivWF monoclonal antibody, inhibits enhanced platelet aggregation induced by high shear stress in platelet-rich plasma from patients with acute coronary syndromes. Arterioscler. Thromb. Vasc. Biol. 19, 877 – 882 (1999).
    • (1999) Arterioscler. Thromb. Vasc. Biol , vol.19 , pp. 877-882
    • Eto, K.1    Isshiki, T.2    Yamamoto, H.3
  • 71
    • 0030955366 scopus 로고    scopus 로고
    • Prevention of arterial thrombosis using a novel heparin with enhanced antiplatelet activity and reduced anticoagulant activity
    • Poletti LF, Bird K, Harris RB, Marques D, Sobel M. Prevention of arterial thrombosis using a novel heparin with enhanced antiplatelet activity and reduced anticoagulant activity. J. Vasc. Surg. 26, 366 – 372 (1997).
    • (1997) J. Vasc. Surg , vol.26 , pp. 366-372
    • Poletti, L.F.1    Bird, K.2    Harris, R.B.3    Marques, D.4    Sobel, M.5
  • 73
    • 0035279906 scopus 로고    scopus 로고
    • Antihuman vWF monoclonal antibody, AJvW-2 Fab, inhibits repetitive coronary artery thrombosis without bleeding time prolongation in dogs
    • Kageyama S, Yamamoto H, Nakazawa H, Yoshimoto R. Antihuman vWF monoclonal antibody, AJvW-2 Fab, inhibits repetitive coronary artery thrombosis without bleeding time prolongation in dogs. Thromb. Res. 101, 395 – 404 (2001).
    • (2001) Thromb. Res , vol.101 , pp. 395-404
    • Kageyama, S.1    Yamamoto, H.2    Nakazawa, H.3    Yoshimoto, R.4
  • 74
    • 0033793186 scopus 로고    scopus 로고
    • Antihuman von Willebrand factor monoclonal antibody AJvW-2 prevents thrombus deposition and neointima formation after balloon injury in guinea-pigs
    • Kageyama S, Yamamoto H, Yoshimoto R. Antihuman von Willebrand factor monoclonal antibody AJvW-2 prevents thrombus deposition and neointima formation after balloon injury in guinea-pigs. Arterioscler. Thromb. Vasc. Biol. 20, 2303 – 2308 (2000).
    • (2000) Arterioscler. Thromb. Vasc. Biol , vol.20 , pp. 2303-2308
    • Kageyama, S.1    Yamamoto, H.2    Yoshimoto, R.3
  • 75
    • 0023449853 scopus 로고
    • Prevention of occlusive coronary artery thrombosis by a murine monoclonal antibody to porcine von Willebrand factor
    • Bellinger DA, Nichols TC, Read MS et al Prevention of occlusive coronary artery thrombosis by a murine monoclonal antibody to porcine von Willebrand factor. Proc. Natl Acad. Sci. USA 84, 8100 – 8104 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8100-8104
    • Bellinger, D.A.1    Nichols, T.C.2    Read, M.S.3
  • 76
    • 0026045619 scopus 로고
    • Isolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers
    • Weinstein M, Vosburgh E, Phillips M, Turner N, Chute-Rose L, Moake J. Isolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers. B/ooc/ 78, 2291 – 2298 (1991)
    • (1991) B/ooc/ , vol.78 , pp. 2291-2298
    • Weinstein, M.1    Vosburgh, E.2    Phillips, M.3    Turner, N.4    Chute-Rose, L.5    Moake, J.6
  • 77
    • 0025270361 scopus 로고
    • Aurintricarboxylic acid in a canine model of coronary artery thrombosis
    • Strony J, Phillips M, Brands D, Moake J, Adelman B. Aurintricarboxylic acid in a canine model of coronary artery thrombosis. Circulation 81, 1106 – 1114 (1990).
    • (1990) Circulation , vol.81 , pp. 1106-1114
    • Strony, J.1    Phillips, M.2    Brands, D.3    Moake, J.4    Adelman, B.5
  • 78
    • 0028919848 scopus 로고
    • Aurintricarboxylic acid prevents acute rethrombosis in a canine model of arterial thrombosis
    • Strony J, Song A, Rusterholtz L, Adelman B. Aurintricarboxylic acid prevents acute rethrombosis in a canine model of arterial thrombosis. Arterioscler. Thromb. Vasc. Biol. 15, 359 – 366 (1995).
    • (1995) Arterioscler. Thromb. Vasc. Biol , vol.15 , pp. 359-366
    • Strony, J.1    Song, A.2    Rusterholtz, L.3    Adelman, B.4
  • 79
    • 0030044552 scopus 로고    scopus 로고
    • The antithrombotic effect of aurin tricarboxylic acid in the guinea-pig is not solely due to its interaction with the von Willebrand factor-GPIb axis
    • Azzam K, Cisse-Thiam M, Drouet L. The antithrombotic effect of aurin tricarboxylic acid in the guinea-pig is not solely due to its interaction with the von Willebrand factor-GPIb axis. Thromb.themost. 75, 203 – 210 (1996).
    • (1996) Thromb.themost , vol.75 , pp. 203-210
    • Azzam, K.1    Cisse-Thiam, M.2    Drouet, L.3
  • 80
    • 0029123084 scopus 로고
    • Aurintricarboxylic acid reduces platelet deposition in stenosed and endothelially injured rabbit carotid arteries more effectively than other antiplatelet interventions
    • Golino P, Ragni M, Cirillo P et al Aurintricarboxylic acid reduces platelet deposition in stenosed and endothelially injured rabbit carotid arteries more effectively than other antiplatelet interventions. Thromb.themost. 74, 974 – 979 (1995).
    • (1995) Thromb.themost , vol.74 , pp. 974-979
    • Golino, P.1    Ragni, M.2    Cirillo, P.3
  • 81
    • 0026639850 scopus 로고
    • Unexpected effects of aurin tricarboxylic acid on human platelets
    • Kinlough-Rathbone RL, Packham MA. Unexpected effects of aurin tricarboxylic acid on human platelets. Thromb. Haemost. 68, 189 – 193 (1992).
    • (1992) Thromb. Haemost , vol.68 , pp. 189-193
    • Kinlough-Rathbone, R.L.1    Packham, M.A.2
  • 82
    • 0030761798 scopus 로고    scopus 로고
    • Inhibition of von Willebrand factor binding to platelet GP Ib by a fractionated aurintricarboxylic acid prevents restenosis after vascular injury in hamster carotid artery
    • Matsuno H, Kozawa 0, Niwa M, Uematsu T Inhibition of von Willebrand factor binding to platelet GP Ib by a fractionated aurintricarboxylic acid prevents restenosis after vascular injury in hamster carotid artery. Circulation 96, 1299 – 1304 (1997).
    • (1997) Circulation , vol.96 , pp. 1299-1304
    • Matsuno, H.1    Kozawa, O.2    Niwa, M.3    Uematsu, T.4
  • 83
    • 0028939740 scopus 로고
    • Promotion of binding of von Willebrand factor to platelet glycoprotein Ib by dimers of ristocetin
    • Hoylaerts ME, Nuyts K, Peerlinck K, Deckmyn H, Vermylen J. Promotion of binding of von Willebrand factor to platelet glycoprotein Ib by dimers of ristocetin. Biochem.j 306, 453 – 463 (1995).
    • (1995) Biochem.j , vol.306 , pp. 453-463
    • Hoylaerts, M.E.1    Nuyts, K.2    Peerlinck, K.3    Deckmyn, H.4    Vermylen, J.5
  • 85
    • 0034877518 scopus 로고    scopus 로고
    • Production and characterization of saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion to collagen
    • Barnes CS, Krafft B, Frech M et al Production and characterization of saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion to collagen. Semin. Thmmb. Hemost. 27, 337 – 348 (2001).
    • (2001) Semin. Thmmb. Hemost , vol.27 , pp. 337-348
    • Barnes, C.S.1    Krafft, B.2    Frech, M.3
  • 86
    • 0035491108 scopus 로고    scopus 로고
    • Saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion, decreases platelet aggregation and intimal hyperplasia in a rat carotid endarterectomy model
    • Cruz CP, Eidt J, Drouilhet J et al Saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion, decreases platelet aggregation and intimal hyperplasia in a rat carotid endarterectomy model. Vasc. Surg. 34, 724 – 729 (2001).
    • (2001) Vasc. Surg , vol.34 , pp. 724-729
    • Cruz, C.P.1    Eidt, J.2    Drouilhet, J.3
  • 87
    • 0037047083 scopus 로고    scopus 로고
    • Involvement of glycoprotein VI in platelet thrombus formation on both collagen and von Willebrand factor surfaces under flow conditions
    • Goto S, Tamura N, Handa S, Arai M, Kodama K, Takayama H. Involvement of glycoprotein VI in platelet thrombus formation on both collagen and von Willebrand factor surfaces under flow conditions. Circulation 106, 266 – 272 (2002).
    • (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
  • 88
    • 0028931844 scopus 로고
    • Calmn from Ifirudo medicinalis, an inhibitor of platelet adhesion to collagen, prevents platelet-rich thrombosis in hamsters
    • Deckmyn H, Stassen JM, Vreys I, Van Houtte E, Sawyer RT, Vermylen J. Calmn from Ifirudo medicinalis, an inhibitor of platelet adhesion to collagen, prevents platelet-rich thrombosis in hamsters. Blood 85, 712 – 719 (1995).
    • (1995) Blood , vol.85 , pp. 712-719
    • Deckmyn, H.1    Stassen, J.M.2    Vreys, I.3    Van Houtte, E.4    Sawyer, R.T.5    Vermylen, J.6
  • 89
    • 0037160539 scopus 로고    scopus 로고
    • Cloning, expression analysis and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains
    • Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada V, Lopez-Otin C. Cloning, expression analysis and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene 283, 49 – 62 (2002).
    • (2002) Gene , vol.283 , pp. 49-62
    • Cal, S.1    Obaya, A.J.2    Llamazares, M.3    Garabaya, C.4    Quesada, V.5    Lopez-Otin, C.6
  • 90
    • 0033566876 scopus 로고    scopus 로고
    • Cytosolic calcium changes in a process of platelet adhesion and cohesion on a von Willebrand factor-coated surface under flow conditions
    • Kuwahara M, Sugimoto M, Tsuji S, Miyata S, Yoshioka A. Cytosolic calcium changes in a process of platelet adhesion and cohesion on a von Willebrand factor-coated surface under flow conditions. Blood 94, 1149 – 1155 (1999).
    • (1999) Blood , vol.94 , pp. 1149-1155
    • Kuwahara, M.1    Sugimoto, M.2    Tsuji, S.3    Miyata, S.4    Yoshioka, A.5
  • 91
    • 0037169514 scopus 로고    scopus 로고
    • Distinct glycoprotein IbN/IX and integrin a11b133-dependent calcium signals co-operatively regulate platelet adhesion under flow
    • Nesbitt WS, Kulkarni S, Giuliano S et al Distinct glycoprotein IbN/IX and integrin a11b133-dependent calcium signals co-operatively regulate platelet adhesion under flow. Bio/. Chem. 277, 2965 – 2972 (2002).
    • (2002) Bio/. Chem , vol.277 , pp. 2965-2972
    • Nesbitt, W.S.1    Kulkarni, S.2    Giuliano, S.3
  • 92
    • 0037108442 scopus 로고    scopus 로고
    • Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Iba mechanoreceptor
    • Mazzucato M, Pradella P, Cozzi MR, De Marco L, Ruggeri ZM. Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Iba mechanoreceptor. Blood 100, 2793 – 2800 (2002).
    • (2002) Blood , vol.100 , pp. 2793-2800
    • Mazzucato, M.1    Pradella, P.2    Cozzi, M.R.3    De Marco, L.4    Ruggeri, Z.M.5
  • 94
    • 0037097741 scopus 로고    scopus 로고
    • Site-directed mutagenesis of platelet glycoprotein Iba demonstrating residues involved in the sulfation of tyrosines 276,278 and 279
    • Tait AS, Dong JF, Lopez JA, Dawes IW, Chong BH. Site-directed mutagenesis of platelet glycoprotein Iba demonstrating residues involved in the sulfation of tyrosines 276,278 and 279. B/ooc/99, 4422 – 4427 (2002).
    • (2002) B/ooc/99 , pp. 4422-4427
    • Tait, A.S.1    Dong, J.F.2    Lopez, J.A.3    Dawes, I.W.4    Chong, B.H.5
  • 95
    • 0034724172 scopus 로고    scopus 로고
    • Necessity of conserved asparagine residues in the leucine-rich repeats of platelet glycoprotein Iba for the proper conformation and function of the ligand-binding region
    • Afshar-Kharghan V, Gineys G, Schade AJ et al Necessity of conserved asparagine residues in the leucine-rich repeats of platelet glycoprotein Iba for the proper conformation and function of the ligand-binding region. Biochemistry 39, 3384 – 3391 (2000).
    • (2000) Biochemistry , vol.39 , pp. 3384-3391
    • Afshar-Kharghan, V.1    Gineys, G.2    Schade, A.J.3


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