메뉴 건너뛰기




Volumn 124, Issue 25, 2014, Pages 3799-3807

Exploiting the kinetic interplay between GPIbα-VWF binding interfaces to regulate hemostasis and thrombosis

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN IB ALPHA; VON WILLEBRAND FACTOR; PROTEIN BINDING; THROMBIN RECEPTOR;

EID: 84919635656     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2014-04-569392     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 33748704252 scopus 로고    scopus 로고
    • Activation-independent platelet adhesion and aggregation under elevated shear stress
    • Ruggeri ZM, Orje JN, Habermann R, Federici AB, Reininger AJ. Activation-independent platelet adhesion and aggregation under elevated shear stress. Blood. 2006;108(6):1903-1910.
    • (2006) Blood , vol.108 , Issue.6 , pp. 1903-1910
    • Ruggeri, Z.M.1    Orje, J.N.2    Habermann, R.3    Federici, A.B.4    Reininger, A.J.5
  • 2
    • 0018770590 scopus 로고
    • Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-Von Willebrand factor bound to the subendothelium
    • Sakariassen KS, Bolhuis PA, Sixma JJ. Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-Von Willebrand factor bound to the subendothelium. Nature. 1979;279(5714):636-638.
    • (1979) Nature , vol.279 , Issue.5714 , pp. 636-638
    • Sakariassen, K.S.1    Bolhuis, P.A.2    Sixma, J.J.3
  • 4
    • 14544302314 scopus 로고    scopus 로고
    • New concepts in von Willebrand disease
    • Sadler JE. New concepts in von Willebrand disease. Annu Rev Med. 2005;56:173-191.
    • (2005) Annu Rev Med , vol.56 , pp. 173-191
    • Sadler, J.E.1
  • 5
    • 0034705544 scopus 로고    scopus 로고
    • Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain
    • Cruz MA, Diacovo TG, Emsley J, Liddington R, Handin RI. Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain. J Biol Chem. 2000;275(25):19098-19105.
    • (2000) J Biol Chem , vol.275 , Issue.25 , pp. 19098-19105
    • Cruz, M.A.1    Diacovo, T.G.2    Emsley, J.3    Liddington, R.4    Handin, R.I.5
  • 6
    • 0024426748 scopus 로고
    • Production in escherichia coli of a biologically active subfragment of von Willebrand factor corresponding to the platelet glycoprotein Ib, collagen and heparin binding domains
    • Piétu G, Meulien P, Cherel G, et al. Production in escherichia coli of a biologically active subfragment of von Willebrand factor corresponding to the platelet glycoprotein Ib, collagen and heparin binding domains. Biochem Biophys Res Commun. 1989;164(3):1339-1347.
    • (1989) Biochem Biophys Res Commun , vol.164 , Issue.3 , pp. 1339-1347
    • Piétu, G.1    Meulien, P.2    Cherel, G.3
  • 7
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage B, Saldívar E, Ruggeri ZM. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell. 1996;84(2):289-297.
    • (1996) Cell , vol.84 , Issue.2 , pp. 289-297
    • Savage, B.1    Saldívar, E.2    Ruggeri, Z.M.3
  • 8
    • 0025880446 scopus 로고
    • Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli
    • Sugimoto M, Ricca G, Hrinda ME, et al. Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli. Biochemistry. 1991;30(21):5202-5209.
    • (1991) Biochemistry , vol.30 , Issue.21 , pp. 5202-5209
    • Sugimoto, M.1    Ricca, G.2    Hrinda, M.E.3
  • 9
    • 2542480051 scopus 로고    scopus 로고
    • Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations
    • Dumas JJ, Kumar R, McDonagh T, et al. Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations. J Biol Chem. 2004;279(22):23327-23334.
    • (2004) J Biol Chem , vol.279 , Issue.22 , pp. 23327-23334
    • Dumas, J.J.1    Kumar, R.2    McDonagh, T.3
  • 10
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain
    • Huizinga EG, Tsuji S, Romijn RA, et al. Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain. Science. 2002;297(5584):1176-1179.
    • (2002) Science , vol.297 , Issue.5584 , pp. 1176-1179
    • Huizinga, E.G.1    Tsuji, S.2    Romijn, R.A.3
  • 11
    • 15544366749 scopus 로고    scopus 로고
    • The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation
    • Fukuda K, Doggett T, Laurenzi IJ, Liddington RC, Diacovo TG. The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation. Nat Struct Mol Biol. 2005;12(2):152-159.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.2 , pp. 152-159
    • Fukuda, K.1    Doggett, T.2    Laurenzi, I.J.3    Liddington, R.C.4    Diacovo, T.G.5
  • 12
    • 84896868212 scopus 로고    scopus 로고
    • Structural basis of regulation of von Willebrand factor binding to glycoprotein Ib
    • Blenner MA, Dong X, Springer TA. Structural basis of regulation of von Willebrand factor binding to glycoprotein Ib. J Biol Chem. 2014;289(9):5565-5579.
    • (2014) J Biol Chem , vol.289 , Issue.9 , pp. 5565-5579
    • Blenner, M.A.1    Dong, X.2    Springer, T.A.3
  • 13
    • 42349105714 scopus 로고    scopus 로고
    • Identification of peptide antagonists to glycoprotein Ibalpha that selectively inhibit von Willebrand factor dependent platelet aggregation
    • Benard SA, Smith TM, Cunningham K, et al. Identification of peptide antagonists to glycoprotein Ibalpha that selectively inhibit von Willebrand factor dependent platelet aggregation. Biochemistry. 2008;47(16):4674-4682.
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4674-4682
    • Benard, S.A.1    Smith, T.M.2    Cunningham, K.3
  • 14
    • 74049134780 scopus 로고    scopus 로고
    • Glycoprotein Ibalpha inhibitor complex structure reveals a combined steric and allosteric mechanism of von Willebrand factor antagonism
    • McEwan PA, Andrews RK, Emsley J. Glycoprotein Ibalpha inhibitor complex structure reveals a combined steric and allosteric mechanism of von Willebrand factor antagonism. Blood. 2009;114(23):4883-4885.
    • (2009) Blood , vol.114 , Issue.23 , pp. 4883-4885
    • McEwan, P.A.1    Andrews, R.K.2    Emsley, J.3
  • 15
    • 77956628683 scopus 로고    scopus 로고
    • Regulation of von Willebrand factor-platelet interactions
    • Lenting PJ, Pegon JN, Groot E, de Groot PG. Regulation of von Willebrand factor-platelet interactions. Thromb Haemost. 2010;104(3):449-455.
    • (2010) Thromb Haemost , vol.104 , Issue.3 , pp. 449-455
    • Lenting, P.J.1    Pegon, J.N.2    Groot, E.3    De Groot, P.G.4
  • 16
    • 33646194222 scopus 로고    scopus 로고
    • Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V
    • Ulrichts H, Udvardy M, Lenting PJ, et al. Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V. J Biol Chem. 2006;281(8):4699-4707.
    • (2006) J Biol Chem , vol.281 , Issue.8 , pp. 4699-4707
    • Ulrichts, H.1    Udvardy, M.2    Lenting, P.J.3
  • 17
    • 34548816709 scopus 로고    scopus 로고
    • beta2-Glycoprotein I inhibits von Willebrand factor dependent platelet adhesion and aggregation
    • Hulstein JJ, Lenting PJ, de Laat B, Derksen RH, Fijnheer R, de Groot PG. beta2-Glycoprotein I inhibits von Willebrand factor dependent platelet adhesion and aggregation. Blood. 2007;110(5):1483-1491.
    • (2007) Blood , vol.110 , Issue.5 , pp. 1483-1491
    • Hulstein, J.J.1    Lenting, P.J.2    De Laat, B.3    Derksen, R.H.4    Fijnheer, R.5    De Groot, P.G.6
  • 18
    • 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
    • Dong JF, Berndt MC, Schade A, McIntire LV, Andrews RK, López JA. 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. 2001;97(1):162-168.
    • (2001) Blood , vol.97 , Issue.1 , pp. 162-168
    • Dong, J.F.1    Berndt, M.C.2    Schade, A.3    McIntire, L.V.4    Andrews, R.K.5    López, J.A.6
  • 19
    • 34249952122 scopus 로고    scopus 로고
    • Shear-induced unfolding triggers adhesion of von Willebrand factor fibers
    • Schneider SW, Nuschele S, Wixforth A, et al. Shear-induced unfolding triggers adhesion of von Willebrand factor fibers. Proc Natl Acad Sci USA. 2007;104(19):7899-7903.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.19 , pp. 7899-7903
    • Schneider, S.W.1    Nuschele, S.2    Wixforth, A.3
  • 20
    • 22244484056 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor
    • Arya M, Kolomeisky AB, Romo GM, Cruz MA, López JA, Anvari B. Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor. Biophys J. 2005;88(6):4391-4401.
    • (2005) Biophys J , vol.88 , Issue.6 , pp. 4391-4401
    • Arya, M.1    Kolomeisky, A.B.2    Romo, G.M.3    Cruz, M.A.4    López, J.A.5    Anvari, B.6
  • 21
    • 0036286198 scopus 로고    scopus 로고
    • Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: The GPIb(a)-vWF tether bond
    • Doggett TA, Girdhar G, Lawshé A, et al. Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(a)-vWF tether bond. Biophys J. 2002;83(1):194-205.
    • (2002) Biophys J , vol.83 , Issue.1 , pp. 194-205
    • Doggett, T.A.1    Girdhar, G.2    Lawshé, A.3
  • 22
    • 0038644632 scopus 로고    scopus 로고
    • Alterations in the intrinsic properties of the GPIbalpha-VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val
    • Doggett TA, Girdhar G, Lawshe A, et al. Alterations in the intrinsic properties of the GPIbalpha-VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val. Blood. 2003;102(1):152-160.
    • (2003) Blood , vol.102 , Issue.1 , pp. 152-160
    • Doggett, T.A.1    Girdhar, G.2    Lawshe, A.3
  • 23
    • 0345412698 scopus 로고    scopus 로고
    • Kinetics of GPIbalpha-vWF-A1 tether bond under flow: Effect of GPIbalpha mutations on the association and dissociation rates
    • Kumar RA, Dong JF, Thaggard JA, Cruz MA, López JA, McIntire LV. Kinetics of GPIbalpha-vWF-A1 tether bond under flow: effect of GPIbalpha mutations on the association and dissociation rates. Biophys J. 2003;85(6):4099-4109.
    • (2003) Biophys J , vol.85 , Issue.6 , pp. 4099-4109
    • Kumar, R.A.1    Dong, J.F.2    Thaggard, J.A.3    Cruz, M.A.4    López, J.A.5    McIntire, L.V.6
  • 24
    • 84887430287 scopus 로고    scopus 로고
    • The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Iba
    • Ju L, Dong JF, Cruz MA, Zhu C. The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Iba. J Biol Chem. 2013;288(45):32289-32301.
    • (2013) J Biol Chem , vol.288 , Issue.45 , pp. 32289-32301
    • Ju, L.1    Dong, J.F.2    Cruz, M.A.3    Zhu, C.4
  • 25
    • 79551525710 scopus 로고    scopus 로고
    • Five challenges to bringing single-molecule force spectroscopy into living cells
    • Dufrêne YF, Evans E, Engel A, Helenius J, Gaub HE, Müller DJ. Five challenges to bringing single-molecule force spectroscopy into living cells. Nat Methods. 2011;8(2):123-127.
    • (2011) Nat Methods , vol.8 , Issue.2 , pp. 123-127
    • Dufrêne, Y.F.1    Evans, E.2    Engel, A.3    Helenius, J.4    Gaub, H.E.5    Müller, D.J.6
  • 26
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman KC, Nagy A. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat Methods. 2008;5(6):491-505.
    • (2008) Nat Methods , vol.5 , Issue.6 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 27
    • 0242585007 scopus 로고    scopus 로고
    • Protein-protein unbinding induced by force: Single-molecule studies
    • Weisel JW, Shuman H, Litvinov RI. Protein-protein unbinding induced by force: single-molecule studies. Curr Opin Struct Biol. 2003;13(2):227-235.
    • (2003) Curr Opin Struct Biol , vol.13 , Issue.2 , pp. 227-235
    • Weisel, J.W.1    Shuman, H.2    Litvinov, R.I.3
  • 28
    • 38049036483 scopus 로고    scopus 로고
    • Modifying murine von Willebrand factor A1 domain for in vivo assessment of human platelet therapies
    • Chen J, Tan K, Zhou H, et al. Modifying murine von Willebrand factor A1 domain for in vivo assessment of human platelet therapies. Nat Biotechnol. 2008;26(1):114-119.
    • (2008) Nat Biotechnol , vol.26 , Issue.1 , pp. 114-119
    • Chen, J.1    Tan, K.2    Zhou, H.3
  • 29
    • 44949086574 scopus 로고    scopus 로고
    • Factor VIII accelerates proteolytic cleavage of von Willebrand factor by ADAMTS13
    • Cao W, Krishnaswamy S, Camire RM, Lenting PJ, Zheng XL. Factor VIII accelerates proteolytic cleavage of von Willebrand factor by ADAMTS13. Proc Natl Acad Sci USA. 2008;105(21):7416-7421.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.21 , pp. 7416-7421
    • Cao, W.1    Krishnaswamy, S.2    Camire, R.M.3    Lenting, P.J.4    Zheng, X.L.5
  • 30
    • 64049108912 scopus 로고    scopus 로고
    • Correction of murine ADAMTS13 deficiency by hematopoietic progenitor cell-mediated gene therapy
    • Laje P, Shang D, Cao W, et al. Correction of murine ADAMTS13 deficiency by hematopoietic progenitor cell-mediated gene therapy. Blood. 2009;113(10):2172-2180.
    • (2009) Blood , vol.113 , Issue.10 , pp. 2172-2180
    • Laje, P.1    Shang, D.2    Cao, W.3
  • 31
    • 58149267411 scopus 로고    scopus 로고
    • Correction of ADAMTS13 deficiency by in utero gene transfer of lentiviral vector encoding ADAMTS13 genes
    • Niiya M, Endo M, Shang D, et al. Correction of ADAMTS13 deficiency by in utero gene transfer of lentiviral vector encoding ADAMTS13 genes. Mol Ther. 2009;17(1):34-41.
    • (2009) Mol Ther , vol.17 , Issue.1 , pp. 34-41
    • Niiya, M.1    Endo, M.2    Shang, D.3
  • 32
    • 79251563498 scopus 로고    scopus 로고
    • Humanized mouse model of thrombosis is predictive of the clinical efficacy of antiplatelet agents
    • Magallon J, Chen J, Rabbani L, et al. Humanized mouse model of thrombosis is predictive of the clinical efficacy of antiplatelet agents. Circulation. 2011;123(3):319-326.
    • (2011) Circulation , vol.123 , Issue.3 , pp. 319-326
    • Magallon, J.1    Chen, J.2    Rabbani, L.3
  • 33
    • 0030850434 scopus 로고    scopus 로고
    • A type 2b von Willebrand disease mutation (Ile546->Val) associated with an unusual phenotype
    • Federici AB, Mannucci PM, Stabile F, et al. A type 2b von Willebrand disease mutation (Ile546->Val) associated with an unusual phenotype. Thromb Haemost. 1997;78(3):1132-1137.
    • (1997) Thromb Haemost , vol.78 , Issue.3 , pp. 1132-1137
    • Federici, A.B.1    Mannucci, P.M.2    Stabile, F.3
  • 34
    • 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. Blood. 1998;91(6):2032-2044.
    • (1998) Blood , vol.91 , Issue.6 , pp. 2032-2044
    • Jenkins, P.V.1    Pasi, K.J.2    Perkins, S.J.3
  • 36
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell GI. Models for the specific adhesion of cells to cells. Science. 1978;200(4342):618-627.
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 37
    • 70450246994 scopus 로고    scopus 로고
    • Maximum likelihood estimation of the kinetics of receptor-mediated adhesion
    • Uz B, Arslan E, Laurenzi IJ. Maximum likelihood estimation of the kinetics of receptor-mediated adhesion. J Theor Biol. 2010;262(3):478-487.
    • (2010) J Theor Biol , vol.262 , Issue.3 , pp. 478-487
    • Uz, B.1    Arslan, E.2    Laurenzi, I.J.3
  • 38
    • 84866847587 scopus 로고    scopus 로고
    • A murine model to characterize the antithrombotic effect of molecules targeting human von Willebrand factor
    • Navarrete AM, Casari C, Legendre P, et al. A murine model to characterize the antithrombotic effect of molecules targeting human von Willebrand factor. Blood. 2012;120(13):2723-2732.
    • (2012) Blood , vol.120 , Issue.13 , pp. 2723-2732
    • Navarrete, A.M.1    Casari, C.2    Legendre, P.3
  • 39
    • 0018913581 scopus 로고
    • Platelet production after administration of antiplatelet serum and 5-fluorouracil
    • Radley JM, Hodgson GS, Levin J. Platelet production after administration of antiplatelet serum and 5-fluorouracil. Blood. 1980;55(1):164-166.
    • (1980) Blood , vol.55 , Issue.1 , pp. 164-166
    • Radley, J.M.1    Hodgson, G.S.2    Levin, J.3
  • 40
    • 77955499972 scopus 로고    scopus 로고
    • Common VWF exon 28 polymorphisms in African Americans affecting the VWF activity assay by ristocetin cofactor
    • Flood VH, Gill JC, Morateck PA, et al. Common VWF exon 28 polymorphisms in African Americans affecting the VWF activity assay by ristocetin cofactor. Blood. 2010;116(2):280-286.
    • (2010) Blood , vol.116 , Issue.2 , pp. 280-286
    • Flood, V.H.1    Gill, J.C.2    Morateck, P.A.3
  • 41
    • 38349065134 scopus 로고    scopus 로고
    • Monitoring receptor-ligand interactions between surfaces by thermal fluctuations
    • Chen W, Evans EA, McEver RP, Zhu C. Monitoring receptor-ligand interactions between surfaces by thermal fluctuations. Biophys J. 2008;94(2):694-701.
    • (2008) Biophys J , vol.94 , Issue.2 , pp. 694-701
    • Chen, W.1    Evans, E.A.2    McEver, R.P.3    Zhu, C.4
  • 42
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans EA, Calderwood DA. Forces and bond dynamics in cell adhesion. Science. 2007;316(5828):1148-1153.
    • (2007) Science , vol.316 , Issue.5828 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 43
    • 60349087842 scopus 로고    scopus 로고
    • Mechanochemistry of receptorligand bonds
    • Thomas WE. Mechanochemistry of receptorligand bonds. Curr Opin Struct Biol. 2009;19(1):50-55.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.1 , pp. 50-55
    • Thomas, W.E.1
  • 44
    • 51349154185 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF
    • Yago T, Lou J, Wu T, et al. Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF. J Clin Invest. 2008;118(9):3195-3207.
    • (2008) J Clin Invest , vol.118 , Issue.9 , pp. 3195-3207
    • Yago, T.1    Lou, J.2    Wu, T.3
  • 45
    • 78751685657 scopus 로고    scopus 로고
    • GPIba-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease
    • Coburn LA, Damaraju VS, Dozic S, Eskin SG, Cruz MA, McIntire LV. GPIba-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease. Biophys J. 2011;100(2):304-312.
    • (2011) Biophys J , vol.100 , Issue.2 , pp. 304-312
    • Coburn, L.A.1    Damaraju, V.S.2    Dozic, S.3    Eskin, S.G.4    Cruz, M.A.5    McIntire, L.V.6
  • 46
    • 0023697355 scopus 로고
    • Thrombotic thrombocytopenia with von Willebrand factor deficiency induced by botrocetin. An animal model
    • Sanders WE, Read MS, Reddick RL, Garris JB, Brinkhous KM. Thrombotic thrombocytopenia with von Willebrand factor deficiency induced by botrocetin. An animal model. Lab Invest. 1988;59(4):443-452.
    • (1988) Lab Invest , vol.59 , Issue.4 , pp. 443-452
    • Sanders, W.E.1    Read, M.S.2    Reddick, R.L.3    Garris, J.B.4    Brinkhous, K.M.5
  • 47
    • 0037119606 scopus 로고    scopus 로고
    • Biomedicine. Contact - How platelets touch von Willebrand factor
    • Sadler JE. Biomedicine. Contact - how platelets touch von Willebrand factor. Science. 2002;297(5584):1128-1129.
    • (2002) Science , vol.297 , Issue.5584 , pp. 1128-1129
    • Sadler, J.E.1
  • 48
    • 34547862097 scopus 로고    scopus 로고
    • The von Willebrand factor antagonist (GPG-290) prevents coronary thrombosis without prolongation of bleeding time
    • Wadanoli M, Sako D, Shaw GD, et al. The von Willebrand factor antagonist (GPG-290) prevents coronary thrombosis without prolongation of bleeding time. Thromb Haemost. 2007;98(2):397-405.
    • (2007) Thromb Haemost , vol.98 , Issue.2 , pp. 397-405
    • Wadanoli, M.1    Sako, D.2    Shaw, G.D.3
  • 49
    • 68649126744 scopus 로고    scopus 로고
    • Anti-von Willebrand factor aptamer ARC1779 for refractory thrombotic thrombocytopenic purpura
    • Knöbl P, Jilma B, Gilbert JC, Hutabarat RM, Wagner PG, Jilma-Stohlawetz P. Anti-von Willebrand factor aptamer ARC1779 for refractory thrombotic thrombocytopenic purpura. Transfusion. 2009;49(10):2181-2185.
    • (2009) Transfusion , vol.49 , Issue.10 , pp. 2181-2185
    • Knöbl, P.1    Jilma, B.2    Gilbert, J.C.3    Hutabarat, R.M.4    Wagner, P.G.5    Jilma-Stohlawetz, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.