메뉴 건너뛰기




Volumn 93, Issue 1, 2013, Pages 327-358

New Fundamentals in hemostasis

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; IMMUNOGLOBULIN RECEPTOR; INTEGRIN; PROTEIN C; PROTEIN S; PROTEINASE; PROTEINASE ACTIVATED RECEPTOR; THROMBIN;

EID: 84872288751     PISSN: 00319333     EISSN: 15221210     Source Type: Journal    
DOI: 10.1152/physrev.00016.2011     Document Type: Review
Times cited : (813)

References (332)
  • 1
    • 2442647329 scopus 로고    scopus 로고
    • Protease-activated receptor 2-dependent phosphorylation of the tissue factor cytoplasmic domain
    • Ahamed J, Ruf W. Protease-activated receptor 2-dependent phosphorylation of the tissue factor cytoplasmic domain. J Biol Chem 279: 23038-23044, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 23038-23044
    • Ahamed, J.1    Ruf, W.2
  • 3
    • 0023676384 scopus 로고
    • Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cells
    • Akagi S, Yamamoto A, Yoshimori T, Masaki R, Ogawa R, Tashiro Y. Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cells. J Histochem Cytochem 36: 1069-1074, 1988.
    • (1988) J Histochem Cytochem , vol.36 , pp. 1069-1074
    • Akagi, S.1    Yamamoto, A.2    Yoshimori, T.3    Masaki, R.4    Ogawa, R.5    Tashiro, Y.6
  • 5
    • 0033613269 scopus 로고    scopus 로고
    • Proteaseactivated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity
    • Andersen H, Greenberg DL, Fujikawa K, Xu W, Chung DW, Davie EW. Proteaseactivated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity. Proc Natl Acad Sci USA 96: 11189-11193, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11189-11193
    • Andersen, H.1    Greenberg, D.L.2    Fujikawa, K.3    Xu, W.4    Chung, D.W.5    Davie, E.W.6
  • 6
    • 84884800657 scopus 로고    scopus 로고
    • The glycoprotein Ib-IX-V complex
    • Burlington: Academic
    • Andrews RK, Berndt MC, Lopez JA. The glycoprotein Ib-IX-V complex. In: Platelets. Burlington: Academic, 2007, p. 145-163.
    • (2007) Platelets , pp. 145-163
    • Andrews, R.K.1    Berndt, M.C.2    Lopez, J.A.3
  • 8
    • 0036682920 scopus 로고    scopus 로고
    • Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms
    • Ariens RA, Lai TS, Weisel JW, Greenberg CS, Grant PJ. Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms. Blood 100: 743-754, 2002.
    • (2002) Blood , vol.100 , pp. 743-754
    • Ariens, R.A.1    Lai, T.S.2    Weisel, J.W.3    Greenberg, C.S.4    Grant, P.J.5
  • 9
    • 0036624844 scopus 로고    scopus 로고
    • Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: Studies using optical tweezers
    • Arya M, Anvari B, Romo GM, Cruz MA, Dong JF, McIntire LV, Moake JL, Lopez JA. Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers. Blood 99: 3971-3977, 2002.
    • (2002) Blood , vol.99 , pp. 3971-3977
    • Arya, M.1    Anvari, B.2    Romo, G.M.3    Cruz, M.A.4    Dong, J.F.5    McIntire, L.V.6    Moake, J.L.7    Lopez, J.A.8
  • 10
    • 18144381003 scopus 로고    scopus 로고
    • Adhesion of human and mouse platelets to collagen under shear: A unifying model
    • Auger JM, Kuijpers MJ, Senis YA, Watson SP, Heemskerk JW. Adhesion of human and mouse platelets to collagen under shear: a unifying model. FASEB J 19: 825-827, 2005.
    • (2005) FASEB J , vol.19 , pp. 825-827
    • Auger, J.M.1    Kuijpers, M.J.2    Senis, Y.A.3    Watson, S.P.4    Heemskerk, J.W.5
  • 11
    • 52449117487 scopus 로고    scopus 로고
    • Dynamic tyrosine kinase-regulated signaling and actin polymerisation mediate aggregate stability under shear
    • Auger JM, Watson SP. Dynamic tyrosine kinase-regulated signaling and actin polymerisation mediate aggregate stability under shear. Arterioscler Thromb Vasc Biol 28: 1499-1504, 2008.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 1499-1504
    • Auger, J.M.1    Watson, S.P.2
  • 12
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium
    • Bach R, Rifkin DB. Expression of tissue factor procoagulant activity: regulation by cytosolic calcium. Proc Natl Acad Sci USA 87: 6995-6999, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6995-6999
    • Bach, R.1    Rifkin, D.B.2
  • 14
    • 0031005422 scopus 로고    scopus 로고
    • Mechanism of tissue factor activation on HL-60 cells
    • Bach RR, Moldow CF. Mechanism of tissue factor activation on HL-60 cells. Blood 89: 3270-3276, 1997.
    • (1997) Blood , vol.89 , pp. 3270-3276
    • Bach, R.R.1    Moldow, C.F.2
  • 15
    • 37049012509 scopus 로고    scopus 로고
    • The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
    • Bae JS, Yang L, Manithody C, Rezaie AR. The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells. Blood 110: 3909-3916, 2007.
    • (2007) Blood , vol.110 , pp. 3909-3916
    • Bae, J.S.1    Yang, L.2    Manithody, C.3    Rezaie, A.R.4
  • 16
    • 43749120051 scopus 로고    scopus 로고
    • Lipid raft localization regulates the cleavage specificity of protease activated receptor 1 in endothelial cells
    • Bae JS, Yang L, Rezaie AR. Lipid raft localization regulates the cleavage specificity of protease activated receptor 1 in endothelial cells. J Thromb Haemost 6: 954-961, 2008.
    • (2008) J Thromb Haemost , vol.6 , pp. 954-961
    • Bae, J.S.1    Yang, L.2    Rezaie, A.R.3
  • 18
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 271: 16603-16608, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 20
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan JF. Structural design and molecular evolution of a cytokine receptor superfamily. Proc Natl Acad Sci USA 87: 6934-6938, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 22
    • 0344389051 scopus 로고    scopus 로고
    • Fibrin-dependent platelet procoagulant activity requires GPIb receptors and von Willebrand factor
    • Beguin S, Kumar R, Keularts I, Seligsohn U, Coller BS, Hemker HC. Fibrin-dependent platelet procoagulant activity requires GPIb receptors and von Willebrand factor. Blood 93: 564-570, 1999.
    • (1999) Blood , vol.93 , pp. 564-570
    • Beguin, S.1    Kumar, R.2    Keularts, I.3    Seligsohn, U.4    Coller, B.S.5    Hemker, H.C.6
  • 25
    • 84859111545 scopus 로고    scopus 로고
    • Effect of shear stress, statins and TNF-alpha on hemostatic genes in human endothelial cells
    • Bergh N, Larsson P, Ulfhammer E, Jern S. Effect of shear stress, statins and TNF-alpha on hemostatic genes in human endothelial cells. Biochem Biophys Res Commun 420: 166-171, 2012.
    • (2012) Biochem Biophys Res Commun , vol.420 , pp. 166-171
    • Bergh, N.1    Larsson, P.2    Ulfhammer, E.3    Jern, S.4
  • 30
    • 0000105161 scopus 로고
    • Su di un nuovo elemento morfologico del sangue dei mammiferi e della sua importanza nella trombosi e nella coagulazione
    • Bizzozero G. Su di un nuovo elemento morfologico del sangue dei mammiferi e della sua importanza nella trombosi e nella coagulazione. L'Osservatore 17: 3, 1881.
    • (1881) L'Osservatore , vol.17 , pp. 3
    • Bizzozero, G.1
  • 31
    • 0037391809 scopus 로고    scopus 로고
    • Alternatively spliced human tissue factor: A circulating, soluble, thrombogenic protein
    • Bogdanov VY, Balasubramanian V, Hathcock J, Vele O, Lieb M, Nemerson Y. Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein. Nat Med 9: 458-462, 2003.
    • (2003) Nat Med , vol.9 , pp. 458-462
    • Bogdanov, V.Y.1    Balasubramanian, V.2    Hathcock, J.3    Vele, O.4    Lieb, M.5    Nemerson, Y.6
  • 32
    • 67949121949 scopus 로고    scopus 로고
    • Human alternatively spliced tissue factor is not secreted and does not trigger coagulation
    • Boing AN, Hau CM, Sturk A, Nieuwland R. Human alternatively spliced tissue factor is not secreted and does not trigger coagulation. J Thromb Haemost 7: 1423-1426, 2009.
    • (2009) J Thromb Haemost , vol.7 , pp. 1423-1426
    • Boing, A.N.1    Hau, C.M.2    Sturk, A.3    Nieuwland, R.4
  • 33
    • 13544255506 scopus 로고    scopus 로고
    • PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells
    • Boire A, Covic L, Agarwal A, Jacques S, Sherifi S, Kuliopulos A. PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells. Cell 120: 303-313, 2005.
    • (2005) Cell , vol.120 , pp. 303-313
    • Boire, A.1    Covic, L.2    Agarwal, A.3    Jacques, S.4    Sherifi, S.5    Kuliopulos, A.6
  • 34
    • 40449094486 scopus 로고    scopus 로고
    • The evolving role of thrombospondin-1 in hemostasis and vascular biology
    • Bonnefoy A, Moura R, Hoylaerts MF. The evolving role of thrombospondin-1 in hemostasis and vascular biology. Cell Mol Life Sci 65: 713-727, 2008.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 713-727
    • Bonnefoy, A.1    Moura, R.2    Hoylaerts, M.F.3
  • 35
    • 84884808691 scopus 로고    scopus 로고
    • Signal transduction during platelet plug formation
    • edited by Michelson AD. Burlington: Academic
    • Brass LF, Stalker TJ, Zhu L, Woulfe DS. Signal transduction during platelet plug formation. In: Platelets, edited by Michelson AD. Burlington: Academic, 2001, p. 319-346.
    • (2001) Platelets , pp. 319-346
    • Brass, L.F.1    Stalker, T.J.2    Zhu, L.3    Woulfe, D.S.4
  • 36
    • 79960638351 scopus 로고    scopus 로고
    • Regulating thrombus growth and stability to achieve an optimal response to injury
    • Brass LF, Wannemacher KM, Ma P, Stalker TJ. Regulating thrombus growth and stability to achieve an optimal response to injury. J Thromb Haemost 9 Suppl 1: 66-75, 2011.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 SUPPL. , pp. 66-75
    • Brass, L.F.1    Wannemacher, K.M.2    Ma, P.3    Stalker, T.J.4
  • 37
    • 0142029006 scopus 로고    scopus 로고
    • Evidence for functionally active protease-activated receptor-3 (PAR-3) in human vascular smooth muscle cells
    • Bretschneider E, Spanbroek R, Lotzer K, Habenicht AJ, Schror K. Evidence for functionally active protease-activated receptor-3 (PAR-3) in human vascular smooth muscle cells. Thromb Haemost 90: 704-709, 2003.
    • (2003) Thromb Haemost , vol.90 , pp. 704-709
    • Bretschneider, E.1    Spanbroek, R.2    Lotzer, K.3    Habenicht, A.J.4    Schror, K.5
  • 38
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68: 533-544, 1992.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 39
    • 84860303349 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: Structure-function
    • Broze GJ Jr, Girard TJ. Tissue factor pathway inhibitor: structure-function. Front Biosci 17: 262-280, 2012.
    • (2012) Front Biosci , vol.17 , pp. 262-280
    • Broze Jr., G.J.1    Girard, T.J.2
  • 40
    • 0023851665 scopus 로고
    • The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: Insight into its possible mechanism of action
    • Broze GJ Jr, Warren LA, Novotny WF, Higuchi DA, Girard JJ, Miletich JP. The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action. Blood 71: 335-343, 1988.
    • (1988) Blood , vol.71 , pp. 335-343
    • Broze Jr., G.J.1    Warren, L.A.2    Novotny, W.F.3    Higuchi, D.A.4    Girard, J.J.5    Miletich, J.P.6
  • 42
    • 0034010134 scopus 로고    scopus 로고
    • Binding of factor VIIa to tissue factor on keratinocytes induces gene expression
    • Camerer E, Gjernes E, Wiiger M, Pringle S, Prydz H. Binding of factor VIIa to tissue factor on keratinocytes induces gene expression. J Biol Chem 275: 6580-6585, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 6580-6585
    • Camerer, E.1    Gjernes, E.2    Wiiger, M.3    Pringle, S.4    Prydz, H.5
  • 43
    • 0032522957 scopus 로고    scopus 로고
    • Platelet-derived factor Va/Va Leiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C
    • Camire RM, Kalafatis M, Simioni P, Girolami A, Tracy PB. Platelet-derived factor Va/Va Leiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C. Blood 91: 2818-2829, 1998.
    • (1998) Blood , vol.91 , pp. 2818-2829
    • Camire, R.M.1    Kalafatis, M.2    Simioni, P.3    Girolami, A.4    Tracy, P.B.5
  • 44
    • 4644368365 scopus 로고    scopus 로고
    • Signalling through the platelet glycoprotein Ib-V-IX complex
    • Canobbio I, Balduini C, Torti M. Signalling through the platelet glycoprotein Ib-V-IX complex. Cell Signal 16: 1329-1344, 2004.
    • (2004) Cell Signal , vol.16 , pp. 1329-1344
    • Canobbio, I.1    Balduini, C.2    Torti, M.3
  • 45
    • 74749084650 scopus 로고    scopus 로고
    • Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma
    • Castoldi E, Simioni P, Tormene D, Rosing J, Hackeng TM. Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma. J Thromb Haemost 8: 294-300, 2010.
    • (2010) J Thromb Haemost , vol.8 , pp. 294-300
    • Castoldi, E.1    Simioni, P.2    Tormene, D.3    Rosing, J.4    Hackeng, T.M.5
  • 46
    • 79960978263 scopus 로고    scopus 로고
    • Bleeding manifestations of congenital and drug-induced defects of the platelet P2Y12 receptor for adenosine diphosphate
    • Cattaneo M. Bleeding manifestations of congenital and drug-induced defects of the platelet P2Y12 receptor for adenosine diphosphate. Thromb Haemost 105 Suppl 1: S67-74, 2011.
    • (2011) Thromb Haemost , vol.105 , Issue.1 SUPPL.
    • Cattaneo, M.1
  • 47
  • 48
    • 0038112077 scopus 로고    scopus 로고
    • Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets
    • Chen H, Kahn ML. Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets. Mol Cell Biol 23: 4764-4777, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 4764-4777
    • Chen, H.1    Kahn, M.L.2
  • 49
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J, Furie BC, Coughlin SR, Furie B. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J Clin Invest 118: 1123-1131, 2008.
    • (2008) J Clin Invest , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 50
    • 84255201932 scopus 로고    scopus 로고
    • Polyphosphate is a cofactor for the activation of factor XI by thrombin
    • Choi SH, Smith SA, Morrissey JH. Polyphosphate is a cofactor for the activation of factor XI by thrombin. Blood 118: 6963-6970, 2011.
    • (2011) Blood , vol.118 , pp. 6963-6970
    • Choi, S.H.1    Smith, S.A.2    Morrissey, J.H.3
  • 51
    • 0036090191 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule-1 signaling inhibits the activation of human platelets
    • Cicmil M, Thomas JM, Leduc M, Bon C, Gibbins JM. Platelet endothelial cell adhesion molecule-1 signaling inhibits the activation of human platelets. Blood 99: 137-144, 2002.
    • (2002) Blood , vol.99 , pp. 137-144
    • Cicmil, M.1    Thomas, J.M.2    Leduc, M.3    Bon, C.4    Gibbins, J.M.5
  • 52
    • 0032828086 scopus 로고    scopus 로고
    • The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors
    • Clemetson JM, Polgar J, Magnenat E, Wells TN, Clemetson KJ. The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors. J Biol Chem 274: 29019-29024, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 29019-29024
    • Clemetson, J.M.1    Polgar, J.2    Magnenat, E.3    Wells, T.N.4    Clemetson, K.J.5
  • 53
    • 84884789064 scopus 로고    scopus 로고
    • Platelet receptors
    • Burlington: Academic
    • Clemetson KJ, Clemetson CJ. Platelet receptors. In: Platelets. Burlington: Academic, 2007, p. 117-143.
    • (2007) Platelets , pp. 117-143
    • Clemetson, K.J.1    Clemetson, C.J.2
  • 58
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • Coughlin SR. Protease-activated receptors in hemostasis, thrombosis and vascular biology. J Thromb Haemost 3: 1800-1814, 2005.
    • (2005) J Thromb Haemost , vol.3 , pp. 1800-1814
    • Coughlin, S.R.1
  • 59
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin SR. Thrombin signalling and protease-activated receptors. Nature 407: 258-264, 2000.
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 61
    • 20444427991 scopus 로고    scopus 로고
    • The anticoagulant protein C pathway
    • Dahlback B, Villoutreix BO. The anticoagulant protein C pathway. FEBS Lett 579: 3310-3316, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 3310-3316
    • Dahlback, B.1    Villoutreix, B.O.2
  • 62
    • 21544447526 scopus 로고    scopus 로고
    • Regulation of blood coagulation by the protein C anticoagulant pathway: Novel insights into structure-function relationships and molecular recognition
    • Dahlback B, Villoutreix BO. Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition. Arterioscler Thromb Vasc Biol 25: 1311-1320, 2005.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 1311-1320
    • Dahlback, B.1    Villoutreix, B.O.2
  • 63
    • 28444436585 scopus 로고    scopus 로고
    • Coated-platelets: An emerging component of the procoagulant response
    • Dale GL. Coated-platelets: an emerging component of the procoagulant response. J Thromb Haemost 3: 2185-2192, 2005.
    • (2005) J Thromb Haemost , vol.3 , pp. 2185-2192
    • Dale, G.L.1
  • 64
    • 0142218366 scopus 로고    scopus 로고
    • Regulation of transbilayer plasma membrane phospholipid asymmetry
    • Daleke DL. Regulation of transbilayer plasma membrane phospholipid asymmetry. J Lipid Res 44: 233-242, 2003.
    • (2003) J Lipid Res , vol.44 , pp. 233-242
    • Daleke, D.L.1
  • 67
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie EW, Ratnoff OD. Waterfall sequence for intrinsic blood clotting. Science 145: 1310-1312, 1964.
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 68
    • 0035895962 scopus 로고    scopus 로고
    • Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets
    • De Candia E, Hall SW, Rutella S, Landolfi R, Andrews RK, De Cristofaro R. Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets. J Biol Chem 276: 4692-4698, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4692-4698
    • de Candia, E.1    Hall, S.W.2    Rutella, S.3    Landolfi, R.4    Andrews, R.K.5    de Cristofaro, R.6
  • 70
    • 23944509766 scopus 로고    scopus 로고
    • Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation
    • Del Conde I, Shrimpton CN, Thiagarajan P, Lopez JA. Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation. Blood 106: 1604-1611, 2005.
    • (2005) Blood , vol.106 , pp. 1604-1611
    • Del Conde, I.1    Shrimpton, C.N.2    Thiagarajan, P.3    Lopez, J.A.4
  • 71
    • 0027076617 scopus 로고
    • Thrombosis in antithrombin-III-deficient persons. Report of a large kindred and literature review
    • Demers C, Ginsberg JS, Hirsh J, Henderson P, Blajchman MA. Thrombosis in antithrombin-III-deficient persons. Report of a large kindred and literature review. Ann Intern Med 116: 754-761, 1992.
    • (1992) Ann Intern Med , vol.116 , pp. 754-761
    • Demers, C.1    Ginsberg, J.S.2    Hirsh, J.3    Henderson, P.4    Blajchman, M.A.5
  • 72
    • 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 Sci USA 87: 6306-6310, 1990.
    • (1990) Proc Natl Acad Sci 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
  • 73
    • 1842547895 scopus 로고    scopus 로고
    • Treatment effects of drotrecogin alfa (activated) in patients with severe sepsis with or without overt disseminated intravascular coagulation
    • Dhainaut JF, Yan SB, Joyce DE, Pettila V, Basson B, Brandt JT, Sundin DP, Levi M. Treatment effects of drotrecogin alfa (activated) in patients with severe sepsis with or without overt disseminated intravascular coagulation. J Thromb Haemost 2: 1924-1933, 2004.
    • (2004) J Thromb Haemost , vol.2 , pp. 1924-1933
    • Dhainaut, J.F.1    Yan, S.B.2    Joyce, D.E.3    Pettila, V.4    Basson, B.5    Brandt, J.T.6    Sundin, D.P.7    Levi, M.8
  • 74
    • 79953155300 scopus 로고    scopus 로고
    • The endothelial protein C receptor supports tissue factor ternary coagulation initiation complex signaling through protease-activated receptors
    • Disse J, Petersen HH, Larsen KS, Persson E, Esmon N, Esmon CT, Teyton L, Petersen LC, Ruf W. The endothelial protein C receptor supports tissue factor ternary coagulation initiation complex signaling through protease-activated receptors. J Biol Chem 286: 5756-5767, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 5756-5767
    • Disse, J.1    Petersen, H.H.2    Larsen, K.S.3    Persson, E.4    Esmon, N.5    Esmon, C.T.6    Teyton, L.7    Petersen, L.C.8    Ruf, W.9
  • 75
    • 4644312977 scopus 로고    scopus 로고
    • Cross-talk of integrin alpha3beta1 and tissue factor in cell migration
    • Dorfleutner A, Hintermann E, Tarui T, Takada Y, Ruf W. Cross-talk of integrin alpha3beta1 and tissue factor in cell migration. Mol Biol Cell 15: 4416-4425, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 4416-4425
    • Dorfleutner, A.1    Hintermann, E.2    Tarui, T.3    Takada, Y.4    Ruf, W.5
  • 76
    • 0344826105 scopus 로고    scopus 로고
    • Regulation of tissue factor cytoplasmic domain phosphorylation by palmitoylation
    • Dorfleutner A, Ruf W. Regulation of tissue factor cytoplasmic domain phosphorylation by palmitoylation. Blood 102: 3998-4005, 2003.
    • (2003) Blood , vol.102 , pp. 3998-4005
    • Dorfleutner, A.1    Ruf, W.2
  • 77
    • 0027725139 scopus 로고
    • Expression of tissue factor, thrombomodulin, and E-selectin in baboons with lethal E. Coli Sepsis
    • Drake TA, Cheng J, Chang A, Taylor FB Jr. Expression of tissue factor, thrombomodulin, and E-selectin in baboons with lethal E. coli sepsis. Am J Pathol 142: 1458-1470, 1993.
    • (1993) Am J Pathol , vol.142 , pp. 1458-1470
    • Drake, T.A.1    Cheng, J.2    Chang, A.3    Taylor Jr., F.B.4
  • 78
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues
    • Drake TA, Morrissey JH, Edgington TS. Selective cellular expression of tissue factor in human tissues. Am J Pathol 134: 1087-1097, 1989.
    • (1989) Am J Pathol , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrissey, J.H.2    Edgington, T.S.3
  • 79
    • 34147187419 scopus 로고    scopus 로고
    • Real-time in vivo imaging of platelets during thrombus formation
    • Burlington: Academic
    • Dubois C, Atkinson B, Furie BA, Furie B. Real-time in vivo imaging of platelets during thrombus formation. In: Platelets. Burlington: Academic, 2007, p. 611-626.
    • (2007) Platelets , pp. 611-626
    • Dubois, C.1    Atkinson, B.2    Furie, B.A.3    Furie, B.4
  • 85
    • 0034912330 scopus 로고    scopus 로고
    • Role of coagulation inhibitors in inflammation
    • Esmon CT. Role of coagulation inhibitors in inflammation. Thromb Haemost 86: 51-56, 2001.
    • (2001) Thromb Haemost , vol.86 , pp. 51-56
    • Esmon, C.T.1
  • 86
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon CT. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J Biol Chem 264: 4743-4746, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 87
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, Swiatkowska M. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86: 2168-2173, 1995.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 88
    • 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
    • Falati S, Liu Q, Gross P, Merrill-Skoloff G, Chou J, Vandendries E, Celi A, Croce K, Furie BC, Furie B. 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: 1585-1598, 2003.
    • (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
  • 90
    • 34250730360 scopus 로고    scopus 로고
    • Platelet receptor recognition and cross-talk in collagen-induced activation of platelets
    • Farndale RW, Slatter DA, Siljander PR, Jarvis GE. Platelet receptor recognition and cross-talk in collagen-induced activation of platelets. J Thromb Haemost 5 Suppl 1: 220-229, 2007.
    • (2007) J Thromb Haemost , vol.5 , Issue.1 SUPPL. , pp. 220-229
    • Farndale, R.W.1    Slatter, D.A.2    Siljander, P.R.3    Jarvis, G.E.4
  • 92
    • 0027938728 scopus 로고
    • Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site
    • Fay PJ, Beattie T, Huggins CF, Regan LM. Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site. J Biol Chem 269: 20522-20527, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20522-20527
    • Fay, P.J.1    Beattie, T.2    Huggins, C.F.3    Regan, L.M.4
  • 93
    • 17044427680 scopus 로고    scopus 로고
    • Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation
    • Feistritzer C, Riewald M. Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation. Blood 105: 3178-3184, 2005.
    • (2005) Blood , vol.105 , pp. 3178-3184
    • Feistritzer, C.1    Riewald, M.2
  • 94
    • 20444443508 scopus 로고    scopus 로고
    • Activated protein C mediates novel lung endothelial barrier enhancement: Role of sphingosine 1-phosphate receptor transactivation
    • Finigan JH, Dudek SM, Singleton PA, Chiang ET, Jacobson JR, Camp SM, Ye SQ, Garcia JG. Activated protein C mediates novel lung endothelial barrier enhancement: role of sphingosine 1-phosphate receptor transactivation. J Biol Chem 280: 17286-17293, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 17286-17293
    • Finigan, J.H.1    Dudek, S.M.2    Singleton, P.A.3    Chiang, E.T.4    Jacobson, J.R.5    Camp, S.M.6    Ye, S.Q.7    Garcia, J.G.8
  • 95
    • 77949274538 scopus 로고    scopus 로고
    • Formation of procoagulant microparticles and properties
    • Freyssinet JM, Toti F. Formation of procoagulant microparticles and properties. Thromb Res 125 Suppl 1: S46-48, 2010.
    • (2010) Thromb Res , vol.125 , Issue.1 SUPPL.
    • Freyssinet, J.M.1    Toti, F.2
  • 96
    • 0027943163 scopus 로고
    • Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor
    • Fukudome K, Esmon CT. Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor. J Biol Chem 269: 26486-26491, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 26486-26491
    • Fukudome, K.1    Esmon, C.T.2
  • 98
    • 79960019927 scopus 로고    scopus 로고
    • P2X7 receptor signaling contributes to tissue factor-dependent thrombosis in mice
    • Furlan-Freguia C, Marchese P, Gruber A, Ruggeri ZM, Ruf W. P2X7 receptor signaling contributes to tissue factor-dependent thrombosis in mice. J Clin Invest 121: 2932-2944, 2011.
    • (2011) J Clin Invest , vol.121 , pp. 2932-2944
    • Furlan-Freguia, C.1    Marchese, P.2    Gruber, A.3    Ruggeri, Z.M.4    Ruf, W.5
  • 100
    • 34249722192 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor acts as a cellular receptor for factor VIIa on endothelium
    • Ghosh S, Pendurthi UR, Steinoe A, Esmon CT, Rao LV. Endothelial cell protein C receptor acts as a cellular receptor for factor VIIa on endothelium. J Biol Chem 282: 11849-11857, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 11849-11857
    • Ghosh, S.1    Pendurthi, U.R.2    Steinoe, A.3    Esmon, C.T.4    Rao, L.V.5
  • 101
    • 4444260266 scopus 로고    scopus 로고
    • Platelet adhesion signalling and the regulation of thrombus formation
    • Gibbins JM. Platelet adhesion signalling and the regulation of thrombus formation. J Cell Sci 117: 3415-3425, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 3415-3425
    • Gibbins, J.M.1
  • 104
    • 84856604115 scopus 로고    scopus 로고
    • TFPIbeta is the GPI-anchored TFPI isoform on human endothelial cells and placental microsomes
    • Girard TJ, Tuley E, Broze GJ Jr. TFPIbeta is the GPI-anchored TFPI isoform on human endothelial cells and placental microsomes. Blood 119: 1256-1262, 2012.
    • (2012) Blood , vol.119 , pp. 1256-1262
    • Girard, T.J.1    Tuley, E.2    Broze Jr., G.J.3
  • 105
  • 108
    • 0029767998 scopus 로고    scopus 로고
    • Apoptosis is associated with increased cell surface tissue factor procoagulant activity
    • Greeno EW, Bach RR, Moldow CF. Apoptosis is associated with increased cell surface tissue factor procoagulant activity. Lab Invest 75: 281-289, 1996.
    • (1996) Lab Invest , vol.75 , pp. 281-289
    • Greeno, E.W.1    Bach, R.R.2    Moldow, C.F.3
  • 109
    • 0345257356 scopus 로고    scopus 로고
    • Multiple integrin-ligand interactions synergize in shear-resistant platelet adhesion at sites of arterial injury in vivo
    • Gruner S, Prostredna M, Schulte V, Krieg T, Eckes B, Brakebusch C, Nieswandt B. Multiple integrin-ligand interactions synergize in shear-resistant platelet adhesion at sites of arterial injury in vivo. Blood 102: 4021-4027, 2003.
    • (2003) Blood , vol.102 , pp. 4021-4027
    • Gruner, S.1    Prostredna, M.2    Schulte, V.3    Krieg, T.4    Eckes, B.5    Brakebusch, C.6    Nieswandt, B.7
  • 110
    • 0037044806 scopus 로고    scopus 로고
    • Disruption of the endothelial cell protein C receptor gene in mice causes placental thrombosis and early embryonic lethality
    • Gu JM, Crawley JT, Ferrell G, Zhang F, Li W, Esmon NL, Esmon CT. Disruption of the endothelial cell protein C receptor gene in mice causes placental thrombosis and early embryonic lethality. J Biol Chem 277: 43335-43343, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 43335-43343
    • Gu, J.M.1    Crawley, J.T.2    Ferrell, G.3    Zhang, F.4    Li, W.5    Esmon, N.L.6    Esmon, C.T.7
  • 111
    • 33644772164 scopus 로고    scopus 로고
    • Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor
    • Hackeng TM, Sere KM, Tans G, Rosing J. Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor. Proc Natl Acad Sci USA 103: 3106-3111, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3106-3111
    • Hackeng, T.M.1    Sere, K.M.2    Tans, G.3    Rosing, J.4
  • 112
    • 77149165099 scopus 로고    scopus 로고
    • In vivo and in vitro effects of the anticoagulant, thrombomodulin, on the inflammatory response in rodent models
    • Hagiwara S, Iwasaka H, Matsumoto S, Hasegawa A, Yasuda N, Noguchi T. In vivo and in vitro effects of the anticoagulant, thrombomodulin, on the inflammatory response in rodent models. Shock 33: 282-288, 2010.
    • (2010) Shock , vol.33 , pp. 282-288
    • Hagiwara, S.1    Iwasaka, H.2    Matsumoto, S.3    Hasegawa, A.4    Yasuda, N.5    Noguchi, T.6
  • 113
    • 0027440076 scopus 로고
    • Granulocytes enhance LPS-induced tissue factor activity in monocytes via an interaction with platelets
    • Halvorsen J, Olsen JO, Osterud B. Granulocytes enhance LPS-induced tissue factor activity in monocytes via an interaction with platelets. J Leukoc Biol 54: 275-282, 1993.
    • (1993) J Leukoc Biol , vol.54 , pp. 275-282
    • Halvorsen, J.1    Olsen, J.O.2    Osterud, B.3
  • 114
    • 0028181696 scopus 로고
    • Tissue-factor pathway inhibitor and lipoproteins. Evidence for association with and regulation by LDL in human plasma
    • Hansen JB, Huseby NE, Sandset PM, Svensson B, Lyngmo V, Nordoy A. Tissue-factor pathway inhibitor and lipoproteins. Evidence for association with and regulation by LDL in human plasma. Arterioscler Thromb 14: 223-229, 1994.
    • (1994) Arterioscler Thromb , vol.14 , pp. 223-229
    • Hansen, J.B.1    Huseby, N.E.2    Sandset, P.M.3    Svensson, B.4    Lyngmo, V.5    Nordoy, A.6
  • 115
    • 77953748386 scopus 로고    scopus 로고
    • 2 entry and phosphatidylserine exposure downstream of glycoprotein VI in platelets
    • 2 entry and phosphatidylserine exposure downstream of glycoprotein VI in platelets. J Biol Chem 285: 19865-19873, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 19865-19873
    • Harper, M.T.1    Poole, A.W.2
  • 116
    • 3343011051 scopus 로고    scopus 로고
    • Adhesive interactions of blood cells and the vascular wall in hemostasis and thrombosis
    • edited by RW Colman JH, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins
    • Hawiger J. Adhesive interactions of blood cells and the vascular wall in hemostasis and thrombosis. In: Hemostasis and Thrombosis, Basic Principles and Clinical Practice, edited by RW Colman JH, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins, 2001, p. 639-660.
    • (2001) Hemostasis and Thrombosis, Basic Principles and Clinical Practice , pp. 639-660
    • Hawiger, J.1
  • 117
    • 80052377991 scopus 로고    scopus 로고
    • P2 receptors and platelet function
    • Hechler B, Gachet C. P2 receptors and platelet function. Purinergic Signal 7: 293-303, 2011.
    • (2011) Purinergic Signal , vol.7 , pp. 293-303
    • Hechler, B.1    Gachet, C.2
  • 119
    • 0027404562 scopus 로고
    • Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C
    • Heeb MJ, Mesters RM, Tans G, Rosing J, Griffin JH. Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C. J Biol Chem 268: 2872-2877, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 2872-2877
    • Heeb, M.J.1    Mesters, R.M.2    Tans, G.3    Rosing, J.4    Griffin, J.H.5
  • 122
    • 79958136353 scopus 로고    scopus 로고
    • Unravelling the different functions of protein kinase C isoforms in platelets
    • Heemskerk JW, Harper MT, Cosemans JM, Poole AW. Unravelling the different functions of protein kinase C isoforms in platelets. FEBS Lett 585: 1711-1716, 2011.
    • (2011) FEBS Lett , vol.585 , pp. 1711-1716
    • Heemskerk, J.W.1    Harper, M.T.2    Cosemans, J.M.3    Poole, A.W.4
  • 123
    • 0026606856 scopus 로고
    • Spiking in cytosolic calcium concentration in single fibrinogen-bound fura-2-loaded human platelets
    • Heemskerk JW, Hoyland J, Mason WT, Sage SO. Spiking in cytosolic calcium concentration in single fibrinogen-bound fura-2-loaded human platelets. Biochem J 283: 379-383, 1992.
    • (1992) Biochem J , vol.283 , pp. 379-383
    • Heemskerk, J.W.1    Hoyland, J.2    Mason, W.T.3    Sage, S.O.4
  • 124
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler ME. VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu Rev Immunol 8: 365-400, 1990.
    • (1990) Annu Rev Immunol , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 125
    • 8944220715 scopus 로고    scopus 로고
    • Macrophages and neutrophils infiltrating into the liver are responsible for tissue factor expression in a rabbit model of acute obstructive cholangitis
    • Higure A, Okamoto K, Hirata K, Todoroki H, Nagafuchi Y, Takeda S, Katoh H, Itoh H, Ohsato K, Nakamura S. Macrophages and neutrophils infiltrating into the liver are responsible for tissue factor expression in a rabbit model of acute obstructive cholangitis. Thromb Haemost 75: 791-795, 1996.
    • (1996) Thromb Haemost , vol.75 , pp. 791-795
    • Higure, A.1    Okamoto, K.2    Hirata, K.3    Todoroki, H.4    Nagafuchi, Y.5    Takeda, S.6    Katoh, H.7    Itoh, H.8    Ohsato, K.9    Nakamura, S.10
  • 126
    • 84869483085 scopus 로고    scopus 로고
    • The multiple roles of tissue factor in wound healing
    • Hoffman M, Monroe DM. The multiple roles of tissue factor in wound healing. Front Biosci 4: 713-721, 2012.
    • (2012) Front Biosci , vol.4 , pp. 713-721
    • Hoffman, M.1    Monroe, D.M.2
  • 129
    • 79960638185 scopus 로고    scopus 로고
    • Serpin structure, function and dysfunction
    • Huntington JA. Serpin structure, function and dysfunction. J Thromb Haemost 9 Suppl 1: 26-34, 2011.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 SUPPL. , pp. 26-34
    • Huntington, J.A.1
  • 130
    • 47749110988 scopus 로고    scopus 로고
    • Redundant mechanism of platelet adhesion to laminin and collagen under flow: Involvement of von Willebrand factor and glycoprotein Ib-IX-V
    • Inoue O, Suzuki-Inoue K, Ozaki Y. Redundant mechanism of platelet adhesion to laminin and collagen under flow: involvement of von Willebrand factor and glycoprotein Ib-IX-V. J Biol Chem 283: 16279-16282, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 16279-16282
    • Inoue, O.1    Suzuki-Inoue, K.2    Ozaki, Y.3
  • 132
    • 0034468568 scopus 로고    scopus 로고
    • Platelets and the injured vessel wall "rolling into action": Focus on glycoprotein Ib/V/IX and the platelet cytoskeleton
    • Jackson SP, Mistry N, Yuan Y. Platelets and the injured vessel wall "rolling into action": focus on glycoprotein Ib/V/IX and the platelet cytoskeleton. Trends Cardiovasc Med 10: 192-197, 2000.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 192-197
    • Jackson, S.P.1    Mistry, N.2    Yuan, Y.3
  • 135
    • 0017842254 scopus 로고
    • The inhibition of activated bovine coagulation factors X and VII by antithrombin III
    • Jesty J. The inhibition of activated bovine coagulation factors X and VII by antithrombin III. Arch Biochem Biophys 185: 165-173, 1978.
    • (1978) Arch Biochem Biophys , vol.185 , pp. 165-173
    • Jesty, J.1
  • 136
    • 70449508204 scopus 로고    scopus 로고
    • Tissue factor activity of blood mononuclear cells is increased after total knee arthroplasty
    • Johnson GJ, Leis LA, Bach RR. Tissue factor activity of blood mononuclear cells is increased after total knee arthroplasty. Thromb Haemost 102: 728-734, 2009.
    • (2009) Thromb Haemost , vol.102 , pp. 728-734
    • Johnson, G.J.1    Leis, L.A.2    Bach, R.R.3
  • 138
    • 0037159218 scopus 로고    scopus 로고
    • Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va. Amino acid residues 323-331 of factor V represent an interactive site for activated factor X
    • Kalafatis M, Beck DO. Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va. Amino acid residues 323-331 of factor V represent an interactive site for activated factor X. Biochemistry 41: 12715-12728, 2002.
    • (2002) Biochemistry , vol.41 , pp. 12715-12728
    • Kalafatis, M.1    Beck, D.O.2
  • 139
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor V and human factor Va by activated protein C
    • Kalafatis M, Rand MD, Mann KG. The mechanism of inactivation of human factor V and human factor Va by activated protein C. J Biol Chem 269: 31869-31880, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 143
    • 0037458275 scopus 로고    scopus 로고
    • Differential actions of PAR2 and PAR1 in stimulating human endothelial cell exocytosis and permeability: The role of Rho-GTPases
    • Klarenbach SW, Chipiuk A, Nelson RC, Hollenberg MD, Murray AG. Differential actions of PAR2 and PAR1 in stimulating human endothelial cell exocytosis and permeability: the role of Rho-GTPases. Circ Res 92: 272-278, 2003.
    • (2003) Circ Res , vol.92 , pp. 272-278
    • Klarenbach, S.W.1    Chipiuk, A.2    Nelson, R.C.3    Hollenberg, M.D.4    Murray, A.G.5
  • 144
    • 0032524918 scopus 로고    scopus 로고
    • Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C
    • Kokame K, Zheng X, Sadler JE. Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C. J Biol Chem 273: 12135-12139, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12135-12139
    • Kokame, K.1    Zheng, X.2    Sadler, J.E.3
  • 149
    • 0033528761 scopus 로고    scopus 로고
    • Plasmin desensitization of the PAR1 thrombin receptor: Kinetics, sites of truncation, and implications for thrombolytic therapy
    • Kuliopulos A, Covic L, Seeley SK, Sheridan PJ, Helin J, Costello CE. Plasmin desensitization of the PAR1 thrombin receptor: kinetics, sites of truncation, and implications for thrombolytic therapy. Biochemistry 38: 4572-4585, 1999.
    • (1999) Biochemistry , vol.38 , pp. 4572-4585
    • Kuliopulos, A.1    Covic, L.2    Seeley, S.K.3    Sheridan, P.J.4    Helin, J.5    Costello, C.E.6
  • 150
    • 0033961491 scopus 로고    scopus 로고
    • The influence exerted by a restricted phospholipid microenvironment on the expression of tissue factor activity at the cell plasma membrane surface
    • Kunzelmann-Marche C, Satta N, Toti F, Zhang Y, Nawroth PP, Morrissey JH, Freyssinet JM. The influence exerted by a restricted phospholipid microenvironment on the expression of tissue factor activity at the cell plasma membrane surface. Thromb Haemost 83: 282-289, 2000.
    • (2000) Thromb Haemost , vol.83 , pp. 282-289
    • Kunzelmann-Marche, C.1    Satta, N.2    Toti, F.3    Zhang, Y.4    Nawroth, P.P.5    Morrissey, J.H.6    Freyssinet, J.M.7
  • 151
    • 0032943041 scopus 로고    scopus 로고
    • Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release
    • Langer F, Morys-Wortmann C, Küsters B, Storck J. Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release. Br J Haematol 105: 541-550, 1999.
    • (1999) Br J Haematol , vol.105 , pp. 541-550
    • Langer, F.1    Morys-Wortmann, C.2    Küsters, B.3    Storck, J.4
  • 152
    • 0030776168 scopus 로고    scopus 로고
    • Human protein C receptor is present primarily on endothelium of large blood vessels: Implications for the control of the protein C pathway
    • Laszik Z, Mitro A, Taylor FB Jr, Ferrell G, Esmon CT. Human protein C receptor is present primarily on endothelium of large blood vessels: implications for the control of the protein C pathway. Circulation 96: 3633-3640, 1997.
    • (1997) Circulation , vol.96 , pp. 3633-3640
    • Laszik, Z.1    Mitro, A.2    Taylor Jr., F.B.3    Ferrell, G.4    Esmon, C.T.5
  • 155
    • 0026650453 scopus 로고
    • Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces
    • Le DT, Rapaport SI, Rao LVM. Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces. J Biol Chem 267: 15447-15454, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 15447-15454
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.M.3
  • 158
    • 55049107958 scopus 로고    scopus 로고
    • The role of natural anticoagulants in the pathogenesis and management of systemic activation of coagulation and inflammation in critically ill patients
    • Levi M, van der Poll T. The role of natural anticoagulants in the pathogenesis and management of systemic activation of coagulation and inflammation in critically ill patients. Semin Thromb Hemost 34: 459-468, 2008.
    • (2008) Semin Thromb Hemost , vol.34 , pp. 459-468
    • Levi, M.1    van der Poll, T.2
  • 159
    • 80053397337 scopus 로고    scopus 로고
    • The Syk-kinase inhibitor R406 impairs platelet activation and monocyte tissue factor expression triggered by heparin-PF4 complex directed antibodies
    • Lhermusier T, van Rottem J, Garcia C, Xuereb JM, Ragab A, Martin V, Gratacap MP, Sie P, Payrastre B. The Syk-kinase inhibitor R406 impairs platelet activation and monocyte tissue factor expression triggered by heparin-PF4 complex directed antibodies. J Thromb Haemost 9: 2067-2076, 2011.
    • (2011) J Thromb Haemost , vol.9 , pp. 2067-2076
    • Lhermusier, T.1    van Rottem, J.2    Garcia, C.3    Xuereb, J.M.4    Ragab, A.5    Martin, V.6    Gratacap, M.P.7    Sie, P.8    Payrastre, B.9
  • 160
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombinheparin ternary complex reveals the antithrombotic mechanism of heparin
    • Li W, Johnson DJ, Esmon CT, Huntington JA. Structure of the antithrombin-thrombinheparin ternary complex reveals the antithrombotic mechanism of heparin. Nat Struct Mol Biol 11: 857-862, 2004.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3    Huntington, J.A.4
  • 162
    • 67849118814 scopus 로고    scopus 로고
    • Genotype/phenotype association in von Willebrand disease: Is the glass half full or empty?
    • Lillicrap D. Genotype/phenotype association in von Willebrand disease: is the glass half full or empty? J Thromb Haemost 7 Suppl 1: 65-70, 2009.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 SUPPL. , pp. 65-70
    • Lillicrap, D.1
  • 163
    • 0026003287 scopus 로고
    • The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity
    • Liu LW, Vu TKH, Esmon CT, Coughlin SR. The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity. J Biol Chem 266: 16977-16980, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 16977-16980
    • Liu, L.W.1    Vu, T.K.H.2    Esmon, C.T.3    Coughlin, S.R.4
  • 164
    • 1242288387 scopus 로고    scopus 로고
    • Diverse substrate recognition mechanisms for rhomboids: Thrombomodulin is cleaved by mammalian rhomboids
    • Lohi O, Urban S, Freeman M. Diverse substrate recognition mechanisms for rhomboids: thrombomodulin is cleaved by mammalian rhomboids. Curr Biol 14: 236-241, 2004.
    • (2004) Curr Biol , vol.14 , pp. 236-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 165
    • 34548076281 scopus 로고    scopus 로고
    • Binding of factor VIIa to the endothelial cell protein C receptor reduces its coagulant activity
    • Lopez-Sagaseta J, Montes R, Puy C, Diez N, Fukudome K, Hermida J. Binding of factor VIIa to the endothelial cell protein C receptor reduces its coagulant activity. J Thromb Haemost 5: 1817-1824, 2007.
    • (2007) J Thromb Haemost , vol.5 , pp. 1817-1824
    • Lopez-Sagaseta, J.1    Montes, R.2    Puy, C.3    Diez, N.4    Fukudome, K.5    Hermida, J.6
  • 168
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • Macfarlane RG. An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202: 498-499, 1964.
    • (1964) Nature , vol.202 , pp. 498-499
    • Macfarlane, R.G.1
  • 169
    • 84863541709 scopus 로고    scopus 로고
    • New insights into the mechanisms of venous thrombosis
    • Mackman N. New insights into the mechanisms of venous thrombosis. J Clin Invest 122: 2331-2336, 2012.
    • (2012) J Clin Invest , vol.122 , pp. 2331-2336
    • Mackman, N.1
  • 170
    • 65349153112 scopus 로고    scopus 로고
    • The role of tissue factor and factor VIIa in hemostasis
    • Mackman N. The role of tissue factor and factor VIIa in hemostasis. Anesth Analg 108: 1447-1452, 2009.
    • (2009) Anesth Analg , vol.108 , pp. 1447-1452
    • Mackman, N.1
  • 171
    • 11144223766 scopus 로고    scopus 로고
    • Acute cholesterol depletion impairs functional expression of tissue factor in fibroblasts: Modulation of tissue factor activity by membrane cholesterol
    • Mandal SK, Iakhiaev A, Pendurthi UR, Rao LV. Acute cholesterol depletion impairs functional expression of tissue factor in fibroblasts: modulation of tissue factor activity by membrane cholesterol. Blood 105: 153-160, 2005.
    • (2005) Blood , vol.105 , pp. 153-160
    • Mandal, S.K.1    Iakhiaev, A.2    Pendurthi, U.R.3    Rao, L.V.4
  • 172
    • 0030843304 scopus 로고    scopus 로고
    • Activated protein C cleavage of factor Va leads to dissociation of the A2 domain
    • Mann KG, Hockin MF, Begin KJ, Kalafatis M. Activated protein C cleavage of factor Va leads to dissociation of the A2 domain. J Biol Chem 272: 20678-20683, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 20678-20683
    • Mann, K.G.1    Hockin, M.F.2    Begin, K.J.3    Kalafatis, M.4
  • 174
    • 42449084553 scopus 로고    scopus 로고
    • Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation
    • Maurissen LF, Thomassen MC, Nicolaes GA, Dahlback B, Tans G, Rosing J, Hackeng TM. Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation. Blood 111: 3034-3041, 2008.
    • (2008) Blood , vol.111 , pp. 3034-3041
    • Maurissen, L.F.1    Thomassen, M.C.2    Nicolaes, G.A.3    Dahlback, B.4    Tans, G.5    Rosing, J.6    Hackeng, T.M.7
  • 176
    • 0016606075 scopus 로고
    • Association of tissue factor activity with the surface of cultured cells
    • Maynard JR, Heckman CA, Pitlick FA, Nemerson Y. Association of tissue factor activity with the surface of cultured cells. J Clin Invest 55: 814-824, 1975.
    • (1975) J Clin Invest , vol.55 , pp. 814-824
    • Maynard, J.R.1    Heckman, C.A.2    Pitlick, F.A.3    Nemerson, Y.4
  • 177
    • 71749112406 scopus 로고    scopus 로고
    • Thrombotic thrombocytopenia purpura (TTP) and other thrombotic microangiopathies
    • Moake J. Thrombotic thrombocytopenia purpura (TTP) and other thrombotic microangiopathies. Best Pract Res Clin Haematol 22: 567-576, 2009.
    • (2009) Best Pract Res Clin Haematol , vol.22 , pp. 567-576
    • Moake, J.1
  • 180
    • 0002388354 scopus 로고    scopus 로고
    • Structure and function of von Willebrand factor
    • edited by RW Colman, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins
    • Montgomery RR. Structure and function of von Willebrand factor. In: Hemostasis and Thrombosis, Basic Principles and Clinical Practice, edited by RW Colman, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins, 2007, p. 249-274.
    • (2007) Hemostasis and Thrombosis, Basic Principles and Clinical Practice , pp. 249-274
    • Montgomery, R.R.1
  • 182
    • 0024426540 scopus 로고
    • A patient with platelets deficient in glycoprotein VI that lack both collagen-induced aggregation and adhesion
    • Moroi M, Jung SM, Okuma M, Shinmyozu K. A patient with platelets deficient in glycoprotein VI that lack both collagen-induced aggregation and adhesion. J Clin Invest 84: 1440-1445, 1989.
    • (1989) J Clin Invest , vol.84 , pp. 1440-1445
    • Moroi, M.1    Jung, S.M.2    Okuma, M.3    Shinmyozu, K.4
  • 183
    • 0034019174 scopus 로고    scopus 로고
    • Involvement of activated integrin alpha2beta1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions
    • Moroi M, Onitsuka I, Imaizumi T, Jung SM. Involvement of activated integrin alpha2beta1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions. Thromb Haemost 83: 769-776, 2000.
    • (2000) Thromb Haemost , vol.83 , pp. 769-776
    • Moroi, M.1    Onitsuka, I.2    Imaizumi, T.3    Jung, S.M.4
  • 190
    • 0027411150 scopus 로고
    • Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity
    • Nagashima M, Lundh E, Leonard JC, Morser J, Parkinson JF. Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity. J Biol Chem 268: 2888-2892, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 2888-2892
    • Nagashima, M.1    Lundh, E.2    Leonard, J.C.3    Morser, J.4    Parkinson, J.F.5
  • 192
    • 44949100143 scopus 로고    scopus 로고
    • Haplotypes of the EPCR gene, prothrombin levels, and the risk of venous thrombosis in carriers of the prothrombin G20210A mutation
    • Navarro S, Medina P, Mira Y, Estelles A, Villa P, Ferrando F, Vaya A, Bertina RM, Espana F. Haplotypes of the EPCR gene, prothrombin levels, and the risk of venous thrombosis in carriers of the prothrombin G20210A mutation. Haematologica 93: 885-891, 2008.
    • (2008) Haematologica , vol.93 , pp. 885-891
    • Navarro, S.1    Medina, P.2    Mira, Y.3    Estelles, A.4    Villa, P.5    Ferrando, F.6    Vaya, A.7    Bertina, R.M.8    Espana, F.9
  • 193
    • 0022601049 scopus 로고
    • Modulation of endothelial cell hemostatic properties by tumor necrosis factor
    • Nawroth PP, Stern DM. Modulation of endothelial cell hemostatic properties by tumor necrosis factor. J Exp Med 163: 740-745, 1986.
    • (1986) J Exp Med , vol.163 , pp. 740-745
    • Nawroth, P.P.1    Stern, D.M.2
  • 194
    • 43749120255 scopus 로고    scopus 로고
    • Protein S enhances the tissue factor pathway inhibitor inhibition of factor Xa but not its inhibition of factor VIIa-tissue factor
    • Ndonwi M, Broze G Jr. Protein S enhances the tissue factor pathway inhibitor inhibition of factor Xa but not its inhibition of factor VIIa-tissue factor. J Thromb Haemost 6: 1044-1046, 2008.
    • (2008) J Thromb Haemost , vol.6 , pp. 1044-1046
    • Ndonwi, M.1    Broze Jr., G.2
  • 195
    • 77956547096 scopus 로고    scopus 로고
    • The Kunitz-3 domain of TFPI-alpha is required for protein S-dependent enhancement of factor Xa inhibition
    • Ndonwi M, Tuley EA, Broze GJ Jr. The Kunitz-3 domain of TFPI-alpha is required for protein S-dependent enhancement of factor Xa inhibition. Blood 116: 1344-1351, 2010.
    • (2010) Blood , vol.116 , pp. 1344-1351
    • Ndonwi, M.1    Tuley, E.A.2    Broze Jr., G.J.3
  • 198
    • 0027494426 scopus 로고
    • Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism
    • Neuenschwander PF, Fiore MM, Morrissey JH. Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism. J Biol Chem 268: 21489-21492, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 21489-21492
    • Neuenschwander, P.F.1    Fiore, M.M.2    Morrissey, J.H.3
  • 199
    • 0242663326 scopus 로고    scopus 로고
    • Control of thrombus embolization and fibronectin internalization by integrin alpha IIb beta 3 engagement of the fibrinogen gamma chain
    • Ni H, Papalia JM, Degen JL, Wagner DD. Control of thrombus embolization and fibronectin internalization by integrin alpha IIb beta 3 engagement of the fibrinogen gamma chain. Blood 102: 3609-3614, 2003.
    • (2003) Blood , vol.102 , pp. 3609-3614
    • Ni, H.1    Papalia, J.M.2    Degen, J.L.3    Wagner, D.D.4
  • 200
    • 0036124011 scopus 로고    scopus 로고
    • Factor V and thrombotic disease: Description of a janusfaced protein
    • Nicolaes GA, Dahlback B. Factor V and thrombotic disease: description of a janusfaced protein. Arterioscler Thromb Vasc Biol 22: 530-538, 2002.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 530-538
    • Nicolaes, G.A.1    Dahlback, B.2
  • 202
    • 79960649902 scopus 로고    scopus 로고
    • Platelet adhesion and activation mechanisms in arterial thrombosis and ischaemic stroke
    • Nieswandt B, Pleines I, Bender M. Platelet adhesion and activation mechanisms in arterial thrombosis and ischaemic stroke. J Thromb Haemost 9 Suppl 1: 92-104, 2011.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 SUPPL. , pp. 92-104
    • Nieswandt, B.1    Pleines, I.2    Bender, M.3
  • 203
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • Nieswandt B, Watson SP. Platelet-collagen interaction: is GPVI the central receptor? Blood 102: 449-461, 2003.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 204
    • 3242676770 scopus 로고    scopus 로고
    • Binding of platelet glycoprotein Ibalpha to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS13
    • Nishio K, Anderson PJ, Zheng XL, Sadler JE. Binding of platelet glycoprotein Ibalpha to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS13. Proc Natl Acad Sci USA 101: 10578-10583, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10578-10583
    • Nishio, K.1    Anderson, P.J.2    Zheng, X.L.3    Sadler, J.E.4
  • 206
    • 0025851449 scopus 로고
    • Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples
    • Novotny WF, Brown SG, Miletich JP, Rader DJ, Broze GJ Jr. Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples. Blood 78: 387-393, 1991.
    • (1991) Blood , vol.78 , pp. 387-393
    • Novotny, W.F.1    Brown, S.G.2    Miletich, J.P.3    Rader, D.J.4    Broze Jr., G.J.5
  • 207
    • 0024231919 scopus 로고
    • Platelets secrete a coagulation inhibitor functionally and antigenically similar to the lipoprotein associated coagulation inhibitor
    • Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr. Platelets secrete a coagulation inhibitor functionally and antigenically similar to the lipoprotein associated coagulation inhibitor. Blood 72: 2020-2025, 1988.
    • (1988) Blood , vol.72 , pp. 2020-2025
    • Novotny, W.F.1    Girard, T.J.2    Miletich, J.P.3    Broze Jr., G.J.4
  • 208
    • 79960636704 scopus 로고    scopus 로고
    • Advances in our understanding of the molecular basis of disorders of platelet function
    • Nurden A, Nurden P. Advances in our understanding of the molecular basis of disorders of platelet function. J Thromb Haemost 9 Suppl 1: 76-91, 2011.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 SUPPL. , pp. 76-91
    • Nurden, A.1    Nurden, P.2
  • 210
    • 0034608013 scopus 로고    scopus 로고
    • Thrombin responses in human endothelial cells. Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1
    • O'Brien PJ, Prevost N, Molino M, Hollinger MK, Woolkalis MJ, Woulfe DS, Brass LF. Thrombin responses in human endothelial cells. Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1. J Biol Chem 275: 13502-13509, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13502-13509
    • O'Brien, P.J.1    Prevost, N.2    Molino, M.3    Hollinger, M.K.4    Woolkalis, M.J.5    Woulfe, D.S.6    Brass, L.F.7
  • 211
    • 33845606632 scopus 로고    scopus 로고
    • Activation of platelet function through G protein-coupled receptors
    • Offermanns S. Activation of platelet function through G protein-coupled receptors. Circ Res 99: 1293-1304, 2006.
    • (2006) Circ Res , vol.99 , pp. 1293-1304
    • Offermanns, S.1
  • 212
    • 0035952734 scopus 로고    scopus 로고
    • In vivo functions of heterotrimeric G-proteins: Studies in G-deficient mice
    • Offermanns S. In vivo functions of heterotrimeric G-proteins: studies in G-deficient mice. Oncogene 20: 1635-1642, 2001.
    • (2001) Oncogene , vol.20 , pp. 1635-1642
    • Offermanns, S.1
  • 214
    • 0037100452 scopus 로고    scopus 로고
    • Activated protein C cleaves factor Va more efficiently on endothelium than on platelet surfaces
    • Oliver JA, Monroe DM, Church FC, Roberts HR, Hoffman M. Activated protein C cleaves factor Va more efficiently on endothelium than on platelet surfaces. Blood 100: 539-546, 2002.
    • (2002) Blood , vol.100 , pp. 539-546
    • Oliver, J.A.1    Monroe, D.M.2    Church, F.C.3    Roberts, H.R.4    Hoffman, M.5
  • 216
    • 0036872229 scopus 로고    scopus 로고
    • Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases
    • Olson ST, Chuang YJ. Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases. Trends Cardiovasc Med 12: 331-338, 2002.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 331-338
    • Olson, S.T.1    Chuang, Y.J.2
  • 217
    • 0025730441 scopus 로고
    • Quantitative characterization of the thrombinheparin interaction. Discrimination between specific and nonspecific binding models
    • Olson ST, Halvorson HR, Bjork I. Quantitative characterization of the thrombinheparin interaction. Discrimination between specific and nonspecific binding models. J Biol Chem 266: 6342-6352, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 6342-6352
    • Olson, S.T.1    Halvorson, H.R.2    Bjork, I.3
  • 218
    • 9144269020 scopus 로고    scopus 로고
    • Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin
    • Olson ST, Swanson R, Raub-Segall E, Bedsted T, Sadri M, Petitou M, Herault JP, Herbert JM, Bjork I. Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin. Thromb Haemost 92: 929-939, 2004.
    • (2004) Thromb Haemost , vol.92 , pp. 929-939
    • Olson, S.T.1    Swanson, R.2    Raub-Segall, E.3    Bedsted, T.4    Sadri, M.5    Petitou, M.6    Herault, J.P.7    Herbert, J.M.8    Bjork, I.9
  • 220
    • 0026709656 scopus 로고
    • Deletion analysis of recombinant human factor V. Evidence for a phosphatidylserine binding site in the second C-type domain
    • Ortel TL, vore-Carter D, Quinn-Allen M, Kane WH. Deletion analysis of recombinant human factor V. Evidence for a phosphatidylserine binding site in the second C-type domain. J Biol Chem 267: 4189-4198, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 4189-4198
    • Ortel, T.L.1    Vore-Carter, D.2    Quinn-Allen, M.3    Kane, W.H.4
  • 221
    • 0034125350 scopus 로고    scopus 로고
    • Induction of tissue factor expression in whole blood: Lack of evidence for the presence of tissue factor expression in granulocytes
    • Osterud B, Rao LV, Olsen JO. Induction of tissue factor expression in whole blood: lack of evidence for the presence of tissue factor expression in granulocytes. Thromb Haemost 83: 861-867, 2000.
    • (2000) Thromb Haemost , vol.83 , pp. 861-867
    • Osterud, B.1    Rao, L.V.2    Olsen, J.O.3
  • 222
    • 37549062234 scopus 로고    scopus 로고
    • Protease-activated receptor (PAR)-induced interleukin-8 production in airway epithelial cells requires activation of MAP kinases p44/42 and JNK
    • Ostrowska E, Reiser G. Protease-activated receptor (PAR)-induced interleukin-8 production in airway epithelial cells requires activation of MAP kinases p44/42 and JNK. Biochem Biophys Res Commun 366: 1030-1035, 2008.
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 1030-1035
    • Ostrowska, E.1    Reiser, G.2
  • 224
    • 79957493898 scopus 로고    scopus 로고
    • Microparticles in hemostasis and thrombosis
    • Owens AP 3rd, Mackman N. Microparticles in hemostasis and thrombosis. Circ Res 108: 1284-1297, 2011.
    • (2011) Circ Res , vol.108 , pp. 1284-1297
    • Owens III, A.P.1    Mackman, N.2
  • 227
    • 37049001668 scopus 로고    scopus 로고
    • Tissue factor activation: Is disulfide bond switching a regulatory mechanism?
    • Pendurthi UR, Ghosh S, Mandal SK, Rao LV. Tissue factor activation: is disulfide bond switching a regulatory mechanism? Blood 110: 3900-3908, 2007.
    • (2007) Blood , vol.110 , pp. 3900-3908
    • Pendurthi, U.R.1    Ghosh, S.2    Mandal, S.K.3    Rao, L.V.4
  • 228
    • 20844460991 scopus 로고    scopus 로고
    • Mutation of hydrophobic residues in the factor Va C1 and C2 domains blocks membrane-dependent prothrombin activation
    • Peng W, Quinn-Allen MA, Kane WH. Mutation of hydrophobic residues in the factor Va C1 and C2 domains blocks membrane-dependent prothrombin activation. J Thromb Haemost 3: 351-354, 2005.
    • (2005) J Thromb Haemost , vol.3 , pp. 351-354
    • Peng, W.1    Quinn-Allen, M.A.2    Kane, W.H.3
  • 229
    • 84859799365 scopus 로고    scopus 로고
    • TFPI-dependent activities of protein S
    • Peraramelli S, Rosing J, Hackeng TM. TFPI-dependent activities of protein S. Thromb Res 129 Suppl 2: S23-26, 2012.
    • (2012) Thromb Res , vol.129 , Issue.2 SUPPL.
    • Peraramelli, S.1    Rosing, J.2    Hackeng, T.M.3
  • 230
    • 0035794140 scopus 로고    scopus 로고
    • Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa
    • Petrovan RJ, Ruf W. Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa. J Biol Chem 276: 6616-6620, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 6616-6620
    • Petrovan, R.J.1    Ruf, W.2
  • 231
    • 73149093011 scopus 로고    scopus 로고
    • Integrin alpha IIb beta 3
    • edited by Michelson AD. Burlington: Academic
    • Plow EW, Pesho MM, Ma YQ. Integrin alpha IIb beta 3. In: Platelets, edited by Michelson AD. Burlington: Academic, 2007, p. 165-184.
    • (2007) Platelets , pp. 165-184
    • Plow, E.W.1    Pesho, M.M.2    Ma, Y.Q.3
  • 233
    • 77951082802 scopus 로고    scopus 로고
    • Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac
    • Pollitt AY, Grygielska B, Leblond B, Desire L, Eble JA, Watson SP. Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac. Blood 115: 2938-2946, 2010.
    • (2010) Blood , vol.115 , pp. 2938-2946
    • Pollitt, A.Y.1    Grygielska, B.2    Leblond, B.3    Desire, L.4    Eble, J.A.5    Watson, S.P.6
  • 234
    • 79961097221 scopus 로고    scopus 로고
    • Vitronectin in vascular context: Facets of a multitalented matricellular protein
    • Preissner KT, Reuning U. Vitronectin in vascular context: facets of a multitalented matricellular protein. Semin Thromb Hemost 37: 408-424, 2011.
    • (2011) Semin Thromb Hemost , vol.37 , pp. 408-424
    • Preissner, K.T.1    Reuning, U.2
  • 235
    • 77953922179 scopus 로고    scopus 로고
    • Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood
    • Pugh N, Simpson AM, Smethurst PA, de Groot PG, Raynal N, Farndale RW. Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood. Blood 115: 5069-5079, 2010.
    • (2010) Blood , vol.115 , pp. 5069-5079
    • Pugh, N.1    Simpson, A.M.2    Smethurst, P.A.3    de Groot, P.G.4    Raynal, N.5    Farndale, R.W.6
  • 236
    • 77949382071 scopus 로고    scopus 로고
    • The endothelial cells downregulate the generation of factor VIIa through EPCR binding
    • Puy C, Lopez-Sagaseta J, Hermida J, Montes R. The endothelial cells downregulate the generation of factor VIIa through EPCR binding. Br J Haematol 149: 111-117, 2010.
    • (2010) Br J Haematol , vol.149 , pp. 111-117
    • Puy, C.1    Lopez-Sagaseta, J.2    Hermida, J.3    Montes, R.4
  • 237
    • 0034672357 scopus 로고    scopus 로고
    • Fyn and Lyn phosphorylate the Fc receptor gamma chain downstream of glycoprotein VI in murine platelets, and Lyn regulates a novel feedback pathway
    • Quek LS, Pasquet JM, Hers I, Cornall R, Knight G, Barnes M, Hibbs ML, Dunn AR, Lowell CA, Watson SP. Fyn and Lyn phosphorylate the Fc receptor gamma chain downstream of glycoprotein VI in murine platelets, and Lyn regulates a novel feedback pathway. Blood 96: 4246-4253, 2000.
    • (2000) Blood , vol.96 , pp. 4246-4253
    • Quek, L.S.1    Pasquet, J.M.2    Hers, I.3    Cornall, R.4    Knight, G.5    Barnes, M.6    Hibbs, M.L.7    Dunn, A.R.8    Lowell, C.A.9    Watson, S.P.10
  • 240
    • 77049208954 scopus 로고
    • A familial hemorrhagic trait associated with a deficiency of a clot-promoting fraction of plasma
    • Ratnoff OD, Colopy JE. A familial hemorrhagic trait associated with a deficiency of a clot-promoting fraction of plasma. J Clin Invest 34: 602-613, 1955.
    • (1955) J Clin Invest , vol.34 , pp. 602-613
    • Ratnoff, O.D.1    Colopy, J.E.2
  • 241
    • 37549037907 scopus 로고    scopus 로고
    • SERCA2b and 3 play a regulatory role in store-operated calcium entry in human platelets
    • Redondo PC, Salido GM, Pariente JA, Sage SO, Rosado JA. SERCA2b and 3 play a regulatory role in store-operated calcium entry in human platelets. Cell Signal 20: 337-346, 2008.
    • (2008) Cell Signal , vol.20 , pp. 337-346
    • Redondo, P.C.1    Salido, G.M.2    Pariente, J.A.3    Sage, S.O.4    Rosado, J.A.5
  • 242
    • 0025821169 scopus 로고
    • The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII
    • Rehemtulla A, Ruf W, Edgington TS. The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII. J Biol Chem 266: 10294-10299, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 10294-10299
    • Rehemtulla, A.1    Ruf, W.2    Edgington, T.S.3
  • 245
    • 34447344048 scopus 로고    scopus 로고
    • Role of Factor XII in hemostasis and thrombosis: Clinical implications
    • Renne T, Gailani D. Role of Factor XII in hemostasis and thrombosis: clinical implications. Expert Rev Cardiovasc Ther 5: 733-741, 2007.
    • (2007) Expert Rev Cardiovasc Ther , vol.5 , pp. 733-741
    • Renne, T.1    Gailani, D.2
  • 248
    • 0141446361 scopus 로고    scopus 로고
    • Activated protein C signals through the thrombin receptor PAR1 in endothelial cells
    • Riewald M, Petrovan RJ, Donner A, Ruf W. Activated protein C signals through the thrombin receptor PAR1 in endothelial cells. J Endotoxin Res 9: 317-321, 2003.
    • (2003) J Endotoxin Res , vol.9 , pp. 317-321
    • Riewald, M.1    Petrovan, R.J.2    Donner, A.3    Ruf, W.4
  • 249
    • 0034933683 scopus 로고    scopus 로고
    • Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor
    • Riewald M, Ruf W. Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor. Proc Natl Acad Sci USA 98: 7742-7747, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7742-7747
    • Riewald, M.1    Ruf, W.2
  • 250
    • 78549246810 scopus 로고    scopus 로고
    • Thrombospondin-1 induces platelet activation through CD36-dependent inhibition of the cAMP/protein kinase A signaling cascade
    • Roberts W, Magwenzi S, Aburima A, Naseem KM. Thrombospondin-1 induces platelet activation through CD36-dependent inhibition of the cAMP/protein kinase A signaling cascade. Blood 116: 4297-4306, 2010.
    • (2010) Blood , vol.116 , pp. 4297-4306
    • Roberts, W.1    Magwenzi, S.2    Aburima, A.3    Naseem, K.M.4
  • 253
    • 67849104652 scopus 로고    scopus 로고
    • Genetics of venous thrombosis
    • Rosendaal FR, Reitsma PH. Genetics of venous thrombosis. J Thromb Haemost 7 Suppl 1: 301-304, 2009.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 SUPPL. , pp. 301-304
    • Rosendaal, F.R.1    Reitsma, P.H.2
  • 254
    • 0025756188 scopus 로고
    • Self-association of tissue factor as revealed by chemical cross-linking
    • Roy S, Paborsky LR, Vehar GA. Self-association of tissue factor as revealed by chemical cross-linking. J Biol Chem 266: 4665-4668, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 4665-4668
    • Roy, S.1    Paborsky, L.R.2    Vehar, G.A.3
  • 255
    • 0036851876 scopus 로고    scopus 로고
    • Platelets in atherothrombosis
    • Ruggeri ZM. Platelets in atherothrombosis. Nat Med 8: 1227-1234, 2002.
    • (2002) Nat Med , vol.8 , pp. 1227-1234
    • Ruggeri, Z.M.1
  • 256
    • 0141498240 scopus 로고    scopus 로고
    • Von Willebrand factor, platelets and endothelial cell interactions
    • Ruggeri ZM. Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost 1: 1335-1342, 2003.
    • (2003) J Thromb Haemost , vol.1 , pp. 1335-1342
    • Ruggeri, Z.M.1
  • 257
    • 33845513582 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: Results of a phase III, randomized, double-blind clinical trial
    • Saito H, Maruyama I, Shimazaki S, Yamamoto Y, Aikawa N, Ohno R, Hirayama A, Matsuda T, Asakura H, Nakashima M, Aoki N. Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: results of a phase III, randomized, double-blind clinical trial. J Thromb Haemost 5: 31-41, 2007.
    • (2007) J Thromb Haemost , vol.5 , pp. 31-41
    • Saito, H.1    Maruyama, I.2    Shimazaki, S.3    Yamamoto, Y.4    Aikawa, N.5    Ohno, R.6    Hirayama, A.7    Matsuda, T.8    Asakura, H.9    Nakashima, M.10    Aoki, N.11
  • 258
    • 0030920922 scopus 로고    scopus 로고
    • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
    • Sakharov DV, Plow EF, Rijken DC. On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. J Biol Chem 272: 14477-14482, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 14477-14482
    • Sakharov, D.V.1    Plow, E.F.2    Rijken, D.C.3
  • 260
    • 0842307339 scopus 로고    scopus 로고
    • A haplotype of the EPCR gene is associated with increased plasma levels of sEPCR and is a candidate risk factor for thrombosis
    • Saposnik B, Reny JL, Gaussem P, Emmerich J, Aiach M, Gandrille S. A haplotype of the EPCR gene is associated with increased plasma levels of sEPCR and is a candidate risk factor for thrombosis. Blood 103: 1311-1318, 2004.
    • (2004) Blood , vol.103 , pp. 1311-1318
    • Saposnik, B.1    Reny, J.L.2    Gaussem, P.3    Emmerich, J.4    Aiach, M.5    Gandrille, S.6
  • 261
    • 44849114893 scopus 로고    scopus 로고
    • Platelet thrombus formation in flowing blood
    • Burlington: Academic
    • Savage B, Ruggeri ZM. Platelet thrombus formation in flowing blood. In: Platelets. Burlington: Academic, 2007, p. 359-367.
    • (2007) Platelets , pp. 359-367
    • Savage, B.1    Ruggeri, Z.M.2
  • 263
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric disulfide bonds
    • Schmidt B, Ho L, Hogg PJ. Allosteric disulfide bonds. Biochemistry 45: 7429-7433, 2006.
    • (2006) Biochemistry , vol.45 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 264
    • 0032510949 scopus 로고    scopus 로고
    • The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a PAR gene cluster and characterization in vascular endothelial cells and platelets
    • Schmidt VA, Nierman WC, Maglott DR, Cupit LD, Moskowitz KA, Wainer JA, Bahou WF. The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a PAR gene cluster and characterization in vascular endothelial cells and platelets. J Biol Chem 273: 15061-15068, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 15061-15068
    • Schmidt, V.A.1    Nierman, W.C.2    Maglott, D.R.3    Cupit, L.D.4    Moskowitz, K.A.5    Wainer, J.A.6    Bahou, W.F.7
  • 265
    • 1842728323 scopus 로고    scopus 로고
    • Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin
    • Schneider M, Brufatto N, Neill E, Nesheim M. Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin. J Biol Chem 279: 13340-13345, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 13340-13345
    • Schneider, M.1    Brufatto, N.2    Neill, E.3    Nesheim, M.4
  • 266
    • 41949096728 scopus 로고    scopus 로고
    • Activated protein C-cleaved protease activated receptor-1 is retained on the endothelial cell surface even in the presence of thrombin
    • Schuepbach RA, Feistritzer C, Brass LF, Riewald M. Activated protein C-cleaved protease activated receptor-1 is retained on the endothelial cell surface even in the presence of thrombin. Blood 111: 2667-2673, 2008.
    • (2008) Blood , vol.111 , pp. 2667-2673
    • Schuepbach, R.A.1    Feistritzer, C.2    Brass, L.F.3    Riewald, M.4
  • 269
    • 15844369922 scopus 로고    scopus 로고
    • Ligand-induced protease receptor translocation into caveolae: A mechanism for regulating cell surface proteolysis of the tissue factordependent coagulation pathway
    • Sevinsky JR, Rao LV, Ruf W. Ligand-induced protease receptor translocation into caveolae: a mechanism for regulating cell surface proteolysis of the tissue factordependent coagulation pathway. J Cell Biol 133: 293-304, 1996.
    • (1996) J Cell Biol , vol.133 , pp. 293-304
    • Sevinsky, J.R.1    Rao, L.V.2    Ruf, W.3
  • 270
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: The end game
    • Shattil SJ, Kim C, Ginsberg MH. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 11: 288-300, 2010.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.H.3
  • 271
    • 0028290275 scopus 로고
    • Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa
    • Shen L, Dahlback B. Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa. J Biol Chem 269: 18735-18738, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 18735-18738
    • Shen, L.1    Dahlback, B.2
  • 272
    • 0024532116 scopus 로고
    • Molecular mechanisms of platelet activation
    • Siess W. Molecular mechanisms of platelet activation. Physiol Rev 69: 58-178, 1989.
    • (1989) Physiol Rev , vol.69 , pp. 58-178
    • Siess, W.1
  • 277
    • 0029790055 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex
    • Stearns-Kurosawa DJ, Kurosawa S, Mollica JS, Ferrell GL, Esmon CT. The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex. Proc Natl Acad Sci USA 93: 10212-10216, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10212-10216
    • Stearns-Kurosawa, D.J.1    Kurosawa, S.2    Mollica, J.S.3    Ferrell, G.L.4    Esmon, C.T.5
  • 279
    • 79951669903 scopus 로고    scopus 로고
    • Platelet receptor signaling in thrombus formation
    • Stegner D, Nieswandt B. Platelet receptor signaling in thrombus formation. J Mol Med 89: 109-121, 2011.
    • (2011) J Mol Med , vol.89 , pp. 109-121
    • Stegner, D.1    Nieswandt, B.2
  • 280
    • 0028873577 scopus 로고
    • The tethered ligand receptor is the responsible receptor for the thrombin induced release of von Willebrand factor from endothelial cells (HUVEC)
    • Storck J, Kusters B, Zimmermann ER. The tethered ligand receptor is the responsible receptor for the thrombin induced release of von Willebrand factor from endothelial cells (HUVEC). Thromb Res 77: 249-258, 1995.
    • (1995) Thromb Res , vol.77 , pp. 249-258
    • Storck, J.1    Kusters, B.2    Zimmermann, E.R.3
  • 281
    • 79960645812 scopus 로고    scopus 로고
    • Novel platelet activation receptor CLEC-2: From discovery to prospects
    • Suzuki-Inoue K, Inoue O, Ozaki Y. Novel platelet activation receptor CLEC-2: from discovery to prospects. J Thromb Haemost 9 Suppl 1: 44-55, 2011.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 SUPPL. , pp. 44-55
    • Suzuki-Inoue, K.1    Inoue, O.2    Ozaki, Y.3
  • 282
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki J, Umeda M, Sims PJ, Nagata S. Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468: 834-838, 2010.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 284
    • 0001812985 scopus 로고    scopus 로고
    • Thrombin
    • edited by RW Colman, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins
    • Swords N, Mann KG. Thrombin. In: Hemostasis and Thrombosis, Basic Principles and Clinical Practice, edited by RW Colman, VJ Marder, AW Clowes, JN George. Philadelphia, PA: Lippincott Williams & Wilkins, 2001, p. 171-189.
    • (2001) Hemostasis and Thrombosis, Basic Principles and Clinical Practice , pp. 171-189
    • Swords, N.1    Mann, K.G.2
  • 285
    • 21844455249 scopus 로고    scopus 로고
    • Procoagulant soluble tissue factor is released from endothelial cells in response to inflammatory cytokines
    • Szotowski B, Antoniak S, Poller W, Schultheiss HP, Rauch U. Procoagulant soluble tissue factor is released from endothelial cells in response to inflammatory cytokines. Circ Res 96: 1233-1239, 2005.
    • (2005) Circ Res , vol.96 , pp. 1233-1239
    • Szotowski, B.1    Antoniak, S.2    Poller, W.3    Schultheiss, H.P.4    Rauch, U.5
  • 287
    • 0021330424 scopus 로고
    • Localization of the metal-induced conformational transition of bovine prothrombin
    • Tai MM, Furie BC, Furie B. Localization of the metal-induced conformational transition of bovine prothrombin. J Biol Chem 259: 4162-4168, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 4162-4168
    • Tai, M.M.1    Furie, B.C.2    Furie, B.3
  • 288
    • 0029156005 scopus 로고
    • Role of free protein S and C4b binding protein in regulating the coagulant response to Escherichia coli
    • Taylor FB Jr, Dahlback B, Chang AC, Lockhart MS, Hatanaka K, Peer G, Esmon CT. Role of free protein S and C4b binding protein in regulating the coagulant response to Escherichia coli. Blood 86: 2642-2652, 1995.
    • (1995) Blood , vol.86 , pp. 2642-2652
    • Taylor Jr., F.B.1    Dahlback, B.2    Chang, A.C.3    Lockhart, M.S.4    Hatanaka, K.5    Peer, G.6    Esmon, C.T.7
  • 289
    • 0035869411 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor plays an important role in protein C activation in vivo
    • Taylor FB Jr, Peer GT, Lockhart MS, Ferrell G, Esmon CT. Endothelial cell protein C receptor plays an important role in protein C activation in vivo. Blood 97: 1685-1688, 2001.
    • (2001) Blood , vol.97 , pp. 1685-1688
    • Taylor Jr., F.B.1    Peer, G.T.2    Lockhart, M.S.3    Ferrell, G.4    Esmon, C.T.5
  • 292
    • 80051894582 scopus 로고    scopus 로고
    • P-selectin ligation induces platelet activation and enhances microaggregate and thrombus formation
    • Theoret JF, Yacoub D, Hachem A, Gillis MA, Merhi Y. P-selectin ligation induces platelet activation and enhances microaggregate and thrombus formation. Thromb Res 128: 243-250, 2011.
    • (2011) Thromb Res , vol.128 , pp. 243-250
    • Theoret, J.F.1    Yacoub, D.2    Hachem, A.3    Gillis, M.A.4    Merhi, Y.5
  • 293
    • 0023830633 scopus 로고
    • Exposure of binding sites for vitronectin on platelets following stimulation
    • Thiagarajan P, Kelly KL. Exposure of binding sites for vitronectin on platelets following stimulation. J Biol Chem 263: 3035-3038, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 3035-3038
    • Thiagarajan, P.1    Kelly, K.L.2
  • 296
    • 84872899526 scopus 로고    scopus 로고
    • Autoimmune thrombotic microangiopathy: Advances in pathogenesis, diagnosis, and management
    • Tsai HM. Autoimmune thrombotic microangiopathy: advances in pathogenesis, diagnosis, and management. Semin Thromb Hemost 38: 469-482, 2012.
    • (2012) Semin Thromb Hemost , vol.38 , pp. 469-482
    • Tsai, H.M.1
  • 297
    • 0141832540 scopus 로고    scopus 로고
    • Is severe deficiency of ADAMTS-13 specific for thrombotic thrombocytopenic purpura? Yes
    • Tsai HM. Is severe deficiency of ADAMTS-13 specific for thrombotic thrombocytopenic purpura? Yes. J Thromb Haemost 1: 625-631, 2003.
    • (2003) J Thromb Haemost , vol.1 , pp. 625-631
    • Tsai, H.M.1
  • 298
    • 0026775230 scopus 로고
    • Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity
    • Tsiang M, Lentz SR, Sadler JE. Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. J Biol Chem 267: 6164-6170, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 6164-6170
    • Tsiang, M.1    Lentz, S.R.2    Sadler, J.E.3
  • 300
    • 84856283500 scopus 로고    scopus 로고
    • The relationship between tissue factor and cancer progression: Insights from bench and bedside
    • Van den Berg YW, Osanto S, Reitsma PH, Versteeg HH. The relationship between tissue factor and cancer progression: insights from bench and bedside. Blood 119: 924-932, 2012.
    • (2012) Blood , vol.119 , pp. 924-932
    • van den Berg, Y.W.1    Osanto, S.2    Reitsma, P.H.3    Versteeg, H.H.4
  • 301
    • 80053216002 scopus 로고    scopus 로고
    • Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue fagctor
    • Van den Hengel LG, Kocaturk B, Reitsma PH, Ruf W, Versteeg HH. Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue fagctor. Blood 118: 3446-3448, 2011.
    • (2011) Blood , vol.118 , pp. 3446-3448
    • van den Hengel, L.G.1    Kocaturk, B.2    Reitsma, P.H.3    Ruf, W.4    Versteeg, H.H.5
  • 303
    • 48249101329 scopus 로고    scopus 로고
    • Thrombin-induced endothelial barrier disruption in intact microvessels: Role of RhoA/ Rho kinase-myosin phosphatase axis
    • Van Nieuw Amerongen GP, Musters RJ, Eringa EC, Sipkema P, van Hinsbergh VW. Thrombin-induced endothelial barrier disruption in intact microvessels: role of RhoA/ Rho kinase-myosin phosphatase axis. Am J Physiol Cell Physiol 294: C1234-C1241, 2008.
    • (2008) Am J Physiol Cell Physiol , vol.294
    • van Nieuw, A.G.P.1    Musters, R.J.2    Eringa, E.C.3    Sipkema, P.4    van Hinsbergh, V.W.5
  • 305
    • 0026594345 scopus 로고
    • Regulation of hepatic protein synthesis in chronic inflammation and sepsis
    • Vary TC, Kimball SR. Regulation of hepatic protein synthesis in chronic inflammation and sepsis. Am J Physiol Cell Physiol 262: C445-C452, 1992.
    • (1992) Am J Physiol Cell Physiol , vol.262
    • Vary, T.C.1    Kimball, S.R.2
  • 307
    • 34548494139 scopus 로고    scopus 로고
    • Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
    • Versteeg HH, Ruf W. Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity. J Biol Chem 282: 25416-25424, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 25416-25424
    • Versteeg, H.H.1    Ruf, W.2
  • 309
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TKH, Hung DT, Wheaton VI, Coughlin SR. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64: 1057-1068, 1991.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 310
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • Wang W, Boffa MB, Bajzar L, Walker JB, Nesheim ME. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 273: 27176-27181, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 311
    • 0025213938 scopus 로고
    • Disseminated intravascular coagulation in rabbits induced by administration of endotoxin or tissue factor: Effect of anti-tissue factor antibodies and measurement of plasma extrinsic pathway inhibitor activity
    • Warr TA, Rao LVM, Rapaport SI. Disseminated intravascular coagulation in rabbits induced by administration of endotoxin or tissue factor: effect of anti-tissue factor antibodies and measurement of plasma extrinsic pathway inhibitor activity. Blood 75: 1481-1489, 1990.
    • (1990) Blood , vol.75 , pp. 1481-1489
    • Warr, T.A.1    Rao, L.V.M.2    Rapaport, S.I.3
  • 313
    • 77955047782 scopus 로고    scopus 로고
    • GPVI and CLEC-2 in hemostasis and vascular integrity
    • Watson SP, Herbert JM, Pollitt AY. GPVI and CLEC-2 in hemostasis and vascular integrity. J Thromb Haemost 8: 1456-1467, 2010.
    • (2010) J Thromb Haemost , vol.8 , pp. 1456-1467
    • Watson, S.P.1    Herbert, J.M.2    Pollitt, A.Y.3
  • 314
    • 54049130877 scopus 로고    scopus 로고
    • The glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface
    • Weeterings C, de Groot PG, Adelmeijer J, Lisman T. The glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface. Blood 112: 3227-3233, 2008.
    • (2008) Blood , vol.112 , pp. 3227-3233
    • Weeterings, C.1    de Groot, P.G.2    Adelmeijer, J.3    Lisman, T.4
  • 316
    • 69249235449 scopus 로고    scopus 로고
    • Impaired platelet procoagulant mechanisms in patients with bleeding disorders
    • Weiss HJ. Impaired platelet procoagulant mechanisms in patients with bleeding disorders. Semin Thromb Hemost 35: 233-241, 2009.
    • (2009) Semin Thromb Hemost , vol.35 , pp. 233-241
    • Weiss, H.J.1
  • 318
    • 0001495165 scopus 로고
    • Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque
    • Wilcox JN, Smith KM, Schwartz SM, Gordon D. Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque. Proc Natl Acad Sci USA 86: 2839-2843, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2839-2843
    • Wilcox, J.N.1    Smith, K.M.2    Schwartz, S.M.3    Gordon, D.4
  • 321
    • 0037189528 scopus 로고    scopus 로고
    • Activation of Rap1B by G(i) family members in platelets
    • Woulfe D, Jiang H, Mortensen R, Yang J, Brass LF. Activation of Rap1B by G(i) family members in platelets. J Biol Chem 277: 23382-23390, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 23382-23390
    • Woulfe, D.1    Jiang, H.2    Mortensen, R.3    Yang, J.4    Brass, L.F.5
  • 322
    • 0037426381 scopus 로고    scopus 로고
    • Interaction between soluble thrombomodulin and intercellular adhesion molecule-1 in predicting risk of coronary heart disease
    • Wu KK, Aleksic N, Ballantyne CM, Ahn C, Juneja H, Boerwinkle E. Interaction between soluble thrombomodulin and intercellular adhesion molecule-1 in predicting risk of coronary heart disease. Circulation 107: 1729-1732, 2003.
    • (2003) Circulation , vol.107 , pp. 1729-1732
    • Wu, K.K.1    Aleksic, N.2    Ballantyne, C.M.3    Ahn, C.4    Juneja, H.5    Boerwinkle, E.6
  • 323
    • 0034009976 scopus 로고    scopus 로고
    • Metalloproteolytic release of endothelial cell protein C receptor
    • Xu J, Qu D, Esmon NL, Esmon CT. Metalloproteolytic release of endothelial cell protein C receptor. J Biol Chem 275: 6038-6044, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 6038-6044
    • Xu, J.1    Qu, D.2    Esmon, N.L.3    Esmon, C.T.4
  • 327
    • 80051802621 scopus 로고    scopus 로고
    • Kindlin: Helper, co-activator, or booster of talin in integrin activation?
    • Ye F, Petrich BG. Kindlin: helper, co-activator, or booster of talin in integrin activation? Curr Opin Hematol 18: 356-360, 2011.
    • (2011) Curr Opin Hematol , vol.18 , pp. 356-360
    • Ye, F.1    Petrich, B.G.2
  • 328
    • 0025045118 scopus 로고
    • Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal
    • Yoshimori T, Semba T, Takemoto H, Akagi S, Yamamoto A, Tashiro Y. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem 265: 15984-15990, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 15984-15990
    • Yoshimori, T.1    Semba, T.2    Takemoto, H.3    Akagi, S.4    Yamamoto, A.5    Tashiro, Y.6
  • 329
    • 33846869746 scopus 로고    scopus 로고
    • Effects of membrane and soluble EPCR on the hemostatic balance and endotoxemia in mice
    • Zheng X, Li W, Gu JM, Qu D, Ferrell GL, Esmon NL, Esmon CT. Effects of membrane and soluble EPCR on the hemostatic balance and endotoxemia in mice. Blood 109: 1003-1009, 2007.
    • (2007) Blood , vol.109 , pp. 1003-1009
    • Zheng, X.1    Li, W.2    Gu, J.M.3    Qu, D.4    Ferrell, G.L.5    Esmon, N.L.6    Esmon, C.T.7
  • 331
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • Zwaal RF, Comfurius P, Bevers EM. Surface exposure of phosphatidylserine in pathological cells. Cell Mol Life Sci 62: 971-988, 2005.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 971-988
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 332
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • Zwaal RF, Schroit AJ. Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89: 1121-1132, 1997.
    • (1997) Blood , vol.89 , pp. 1121-1132
    • Zwaal, R.F.1    Schroit, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.