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Volumn 125, Issue 17, 2015, Pages 2712-2719

Arterial thrombosis is accelerated in mice deficient in histidine-rich glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; BLOOD CLOTTING FACTOR 12A; DEOXYRIBONUCLEASE; DNA; GLYCOPROTEIN; HISTIDINE RICH GLYCOPROTEIN; RIBONUCLEASE; RNA; THROMBIN; UNCLASSIFIED DRUG; BLOOD CLOTTING FACTOR 12; CHLORIDE; FERRIC CHLORIDE; FERRIC ION; HISTIDINE-RICH PROTEINS; PROTEIN;

EID: 84928485155     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2014-11-611319     Document Type: Article
Times cited : (41)

References (48)
  • 1
    • 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. 1964;202:498-499.
    • (1964) Nature , vol.202 , pp. 498-499
    • MacFarlane, R.G.1
  • 2
    • 0029908545 scopus 로고    scopus 로고
    • Fatal embryonic bleeding events in mice lacking tissue factor, the cell-associated initiator of blood coagulation
    • Bugge TH, Xiao Q, Kombrinck KW, et al. Fatal embryonic bleeding events in mice lacking tissue factor, the cell-associated initiator of blood coagulation. Proc Natl Acad Sci USA. 1996; 93(13):6258-6263.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.13 , pp. 6258-6263
    • Bugge, T.H.1    Xiao, Q.2    Kombrinck, K.W.3
  • 3
    • 0030775316 scopus 로고    scopus 로고
    • Mice lacking factor VII develop normally but suffer fatal perinatal bleeding
    • Rosen ED, Chan JC, Idusogie E, et al. Mice lacking factor VII develop normally but suffer fatal perinatal bleeding. Nature. 1997;390(6657):290-294.
    • (1997) Nature , vol.390 , Issue.6657 , pp. 290-294
    • Rosen, E.D.1    Chan, J.C.2    Idusogie, E.3
  • 4
    • 34547630092 scopus 로고    scopus 로고
    • Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis
    • Mackman N, Tilley RE, Key NS. Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis. Arterioscler Thromb Vasc Biol. 2007;27(8):1687-1693.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , Issue.8 , pp. 1687-1693
    • Mackman, N.1    Tilley, R.E.2    Key, N.S.3
  • 5
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes
    • Colman RW, Schmaier AH. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood. 1997;90(10):3819-3843.
    • (1997) Blood , vol.90 , Issue.10 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 6
    • 36349012420 scopus 로고    scopus 로고
    • Intrinsic pathway of coagulation and arterial thrombosis
    • Gailani D, Renné T. Intrinsic pathway of coagulation and arterial thrombosis. Arterioscler Thromb Vasc Biol. 2007;27(12):2507-2513.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , Issue.12 , pp. 2507-2513
    • Gailani, D.1    Renné, T.2
  • 7
    • 22944462705 scopus 로고    scopus 로고
    • Defective thrombus formation in mice lacking coagulation factor XII
    • Renné T, Pozgajová M,Grüner S, et al. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med. 2005;202(2):271-281.
    • (2005) J Exp Med , vol.202 , Issue.2 , pp. 271-281
    • Renné, T.1    Pozgajová, M.2    Grüner, S.3
  • 8
    • 33645066112 scopus 로고    scopus 로고
    • Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis
    • Kleinschnitz C, Stoll G, Bendszus M, et al. Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis. J Exp Med. 2006;203(3):513-518.
    • (2006) J Exp Med , vol.203 , Issue.3 , pp. 513-518
    • Kleinschnitz, C.1    Stoll, G.2    Bendszus, M.3
  • 9
    • 33747200433 scopus 로고    scopus 로고
    • Effects of factor XI deficiency on ferric chloride-induced vena cava thrombosis in mice
    • Wang X, Smith PL, Hsu MY, et al. Effects of factor XI deficiency on ferric chloride-induced vena cava thrombosis in mice. J Thromb Haemost. 2006; 4(9):1982-1988.
    • (2006) J Thromb Haemost , vol.4 , Issue.9 , pp. 1982-1988
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3
  • 10
    • 78649471947 scopus 로고    scopus 로고
    • Inhibition of the intrinsic coagulation pathway factor XI by antisense oligonucleotides: A novel antithrombotic strategy with lowered bleeding risk
    • Zhang H, Löwenberg EC, Crosby JR, et al. Inhibition of the intrinsic coagulation pathway factor XI by antisense oligonucleotides: a novel antithrombotic strategy with lowered bleeding risk. Blood. 2010;116(22):4684-4692.
    • (2010) Blood , vol.116 , Issue.22 , pp. 4684-4692
    • Zhang, H.1    Löwenberg, E.C.2    Crosby, J.R.3
  • 11
    • 81155133305 scopus 로고    scopus 로고
    • Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding
    • Revenko AS, Gao D, Crosby JR, et al. Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding. Blood. 2011;118(19): 5302-5311.
    • (2011) Blood , vol.118 , Issue.19 , pp. 5302-5311
    • Revenko, A.S.1    Gao, D.2    Crosby, J.R.3
  • 12
    • 84863229481 scopus 로고    scopus 로고
    • Antisense inhibition of coagulation factor XI prolongs APTT without increased bleeding risk in cynomolgus monkeys
    • Younis HS, Crosby J, Huh JI, et al. Antisense inhibition of coagulation factor XI prolongs APTT without increased bleeding risk in cynomolgus monkeys. Blood. 2012;119(10):2401-2408.
    • (2012) Blood , vol.119 , Issue.10 , pp. 2401-2408
    • Younis, H.S.1    Crosby, J.2    Huh, J.I.3
  • 13
    • 84879076198 scopus 로고    scopus 로고
    • Antithrombotic effect of antisense factor XI oligonucleotide treatment in primates
    • Crosby JR, Marzec U, Revenko AS, et al. Antithrombotic effect of antisense factor XI oligonucleotide treatment in primates. Arterioscler Thromb Vasc Biol. 2013;33(7):1670-1678.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , Issue.7 , pp. 1670-1678
    • Crosby, J.R.1    Marzec, U.2    Revenko, A.S.3
  • 14
    • 84893834884 scopus 로고    scopus 로고
    • A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk
    • Larsson M, Rayzman V, Nolte MW, et al. A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk. Sci Transl Med. 2014;6(22 2):222ra17.
    • (2014) Sci Transl Med , vol.6 , Issue.222 , pp. 222ra17
    • Larsson, M.1    Rayzman, V.2    Nolte, M.W.3
  • 15
    • 80051794851 scopus 로고    scopus 로고
    • Factor XI and XII as antithrombotic targets
    • Müller F, Gailani D, Renné T. Factor XI and XII as antithrombotic targets. Curr Opin Hematol. 2011; 18(5):349-355.
    • (2011) Curr Opin Hematol , vol.18 , Issue.5 , pp. 349-355
    • Müller, F.1    Gailani, D.2    Renné, T.3
  • 16
    • 84862729665 scopus 로고    scopus 로고
    • Polyphosphate: An ancient molecule that links platelets, coagulation, and inflammation
    • Morrissey JH, Choi SH, Smith SA. Polyphosphate: an ancient molecule that links platelets, coagulation, and inflammation. Blood. 2012;119(25):5972-5979.
    • (2012) Blood , vol.119 , Issue.25 , pp. 5972-5979
    • Morrissey, J.H.1    Choi, S.H.2    Smith, S.A.3
  • 17
    • 52249111403 scopus 로고    scopus 로고
    • Circulating DNA. Its origin and fluctuation
    • van der Vaart M, Pretorius PJ. Circulating DNA. Its origin and fluctuation. Ann N Y Acad Sci. 2008; 1137:18-26.
    • (2008) Ann N y Acad Sci , vol.1137 , pp. 18-26
    • Van Der Vaart, M.1    Pretorius, P.J.2
  • 18
    • 84891505072 scopus 로고    scopus 로고
    • NETosis: How vital is it?
    • Yipp BG, Kubes P. NETosis: how vital is it? Blood. 2013;122(16):2784-2794.
    • (2013) Blood , vol.122 , Issue.16 , pp. 2784-2794
    • Yipp, B.G.1    Kubes, P.2
  • 19
    • 34447322451 scopus 로고    scopus 로고
    • Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation
    • Kannemeier C, Shibamiya A, Nakazawa F, et al. Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation. Proc Natl Acad Sci USA. 2007;104(15):6388-6393.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.15 , pp. 6388-6393
    • Kannemeier, C.1    Shibamiya, A.2    Nakazawa, F.3
  • 20
    • 78149439563 scopus 로고    scopus 로고
    • Polyphosphate exerts differential effects on blood clotting, depending on polymer size
    • Smith SA, Choi SH, Davis-Harrison R, et al. Polyphosphate exerts differential effects on blood clotting, depending on polymer size. Blood. 2010; 116(20):4353-4359.
    • (2010) Blood , vol.116 , Issue.20 , pp. 4353-4359
    • Smith, S.A.1    Choi, S.H.2    Davis-Harrison, R.3
  • 21
    • 84855414173 scopus 로고    scopus 로고
    • Neutrophil extracellular traps promote deep vein thrombosis in mice
    • Brill A, Fuchs TA, Savchenko AS, et al. Neutrophil extracellular traps promote deep vein thrombosis in mice. J Thromb Haemost. 2012;10(1):136-144.
    • (2012) J Thromb Haemost , vol.10 , Issue.1 , pp. 136-144
    • Brill, A.1    Fuchs, T.A.2    Savchenko, A.S.3
  • 23
    • 34948826463 scopus 로고    scopus 로고
    • Extracellular RNA mediates endothelial-cell permeability via vascular endothelial growth factor
    • Fischer S, Gerriets T, Wessels C, et al. Extracellular RNA mediates endothelial-cell permeability via vascular endothelial growth factor. Blood. 2007;110(7):2457-2465.
    • (2007) Blood , vol.110 , Issue.7 , pp. 2457-2465
    • Fischer, S.1    Gerriets, T.2    Wessels, C.3
  • 24
    • 0019174107 scopus 로고
    • Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein
    • Lijnen HR, Hoylaerts M, Collen D. Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein. J Biol Chem. 1980;255(21):10214-10222.
    • (1980) J Biol Chem , vol.255 , Issue.21 , pp. 10214-10222
    • Lijnen, H.R.1    Hoylaerts, M.2    Collen, D.3
  • 25
    • 79951846927 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein: The Swiss Army knife of mammalian plasma
    • Poon IK, Patel KK, Davis DS, Parish CR, Hulett MD. Histidine-rich glycoprotein: the Swiss Army knife of mammalian plasma. Blood. 2011;117(7):2093-2101.
    • (2011) Blood , vol.117 , Issue.7 , pp. 2093-2101
    • Poon, I.K.1    Patel, K.K.2    Davis, D.S.3    Parish, C.R.4    Hulett, M.D.5
  • 26
    • 16344375246 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein: A novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems
    • Jones AL, Hulett MD, Parish CR. Histidine-rich glycoprotein: A novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems. Immunol Cell Biol. 2005; 83(2):106-118.
    • (2005) Immunol Cell Biol , vol.83 , Issue.2 , pp. 106-118
    • Jones, A.L.1    Hulett, M.D.2    Parish, C.R.3
  • 27
    • 79954617276 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein binds factor XIIa with high affinity and inhibits contact-initiated coagulation
    • MacQuarrie JL, Stafford AR, Yau JW, et al. Histidine-rich glycoprotein binds factor XIIa with high affinity and inhibits contact-initiated coagulation. Blood. 2011;117(15):4134-4141.
    • (2011) Blood , vol.117 , Issue.15 , pp. 4134-4141
    • MacQuarrie, J.L.1    Stafford, A.R.2    Yau, J.W.3
  • 28
    • 80052217355 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein binds fibrin(ogen) with high affinity and competes with thrombin for binding to the gamma'-chain
    • Vu TT, Stafford AR, Leslie BA, Kim PY, Fredenburgh JC, Weitz JI. Histidine-rich glycoprotein binds fibrin(ogen) with high affinity and competes with thrombin for binding to the gamma'-chain. J BiolChem.2011;286(35):30314-30323.
    • (2011) J BiolChem , vol.286 , Issue.35 , pp. 30314-30323
    • Vu, T.T.1    Stafford, A.R.2    Leslie, B.A.3    Kim, P.Y.4    Fredenburgh, J.C.5    Weitz, J.I.6
  • 29
    • 74249120395 scopus 로고    scopus 로고
    • HD1, a thrombin- and prothrombin-binding DNA aptamer, inhibits thrombin generation by attenuating prothrombin activation and thrombin feedback reactions
    • Kretz CA, Cuddy KK, Stafford AR, Fredenburgh JC, Roberts R, Weitz JI. HD1, a thrombin- and prothrombin-binding DNA aptamer, inhibits thrombin generation by attenuating prothrombin activation and thrombin feedback reactions. Thromb Haemost. 2010;103(1):83-93.
    • (2010) Thromb Haemost , vol.103 , Issue.1 , pp. 83-93
    • Kretz, C.A.1    Cuddy, K.K.2    Stafford, A.R.3    Fredenburgh, J.C.4    Roberts, R.5    Weitz, J.I.6
  • 30
    • 77957726744 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein promotes bacterial entrapment in clots and decreases mortality in a mouse model of sepsis
    • Shannon O, Rydengård V, Schmidtchen A, et al. Histidine-rich glycoprotein promotes bacterial entrapment in clots and decreases mortality in a mouse model of sepsis. Blood. 2010;116(13): 2365-2372.
    • (2010) Blood , vol.116 , Issue.13 , pp. 2365-2372
    • Shannon, O.1    Rydengård, V.2    Schmidtchen, A.3
  • 31
    • 23844519751 scopus 로고    scopus 로고
    • Enhanced blood coagulation and fibrinolysis in mice lacking histidine-rich glycoprotein (HRG)
    • Tsuchida-Straeten N, Ensslen S, Schäfer C, et al. Enhanced blood coagulation and fibrinolysis in mice lacking histidine-rich glycoprotein (HRG). J Thromb Haemost. 2005;3(5):865-872.
    • (2005) J Thromb Haemost , vol.3 , Issue.5 , pp. 865-872
    • Tsuchida-Straeten, N.1    Ensslen, S.2    Schäfer, C.3
  • 32
    • 80055105836 scopus 로고    scopus 로고
    • Breast cancer chemotherapy induces the release of cell-free DNA, a novel procoagulant stimulus
    • Swystun LL, Mukherjee S, Liaw PC. Breast cancer chemotherapy induces the release of cell-free DNA, a novel procoagulant stimulus. J Thromb Haemost. 2011;9(11):2313-2321.
    • (2011) J Thromb Haemost , vol.9 , Issue.11 , pp. 2313-2321
    • Swystun, L.L.1    Mukherjee, S.2    Liaw, P.C.3
  • 33
    • 23044453832 scopus 로고    scopus 로고
    • Effects of factor IX or factor XI deficiency on ferric chloride-induced carotid artery occlusion in mice
    • Wang X, Cheng Q, Xu L, et al. Effects of factor IX or factor XI deficiency on ferric chloride-induced carotid artery occlusion in mice. J Thromb Haemost. 2005;3(4):695-702.
    • (2005) J Thromb Haemost , vol.3 , Issue.4 , pp. 695-702
    • Wang, X.1    Cheng, Q.2    Xu, L.3
  • 34
    • 80052421895 scopus 로고    scopus 로고
    • Towards a standardization of the murine ferric chloride-induced carotid arterial thrombosis model
    • Owens AP 3rd, Lu Y, Whinna HC, Gachet C, Fay WP, Mackman N. Towards a standardization of the murine ferric chloride-induced carotid arterial thrombosis model. J Thromb Haemost. 2011;9(9): 1862-1863.
    • (2011) J Thromb Haemost , vol.9 , Issue.9 , pp. 1862-1863
    • Owens, A.P.1    Lu, Y.2    Whinna, H.C.3    Gachet, C.4    Fay, W.P.5    Mackman, N.6
  • 35
    • 84905174491 scopus 로고    scopus 로고
    • Comparison of the effect of coagulation and platelet function impairments on various mouse bleeding models
    • Vaezzadeh N, Ni R, Kim PY, Weitz JI, Gross PL. Comparison of the effect of coagulation and platelet function impairments on various mouse bleeding models. Thromb Haemost. 2014;112(2):412-418.
    • (2014) Thromb Haemost , vol.112 , Issue.2 , pp. 412-418
    • Vaezzadeh, N.1    Ni, R.2    Kim, P.Y.3    Weitz, J.I.4    Gross, P.L.5
  • 36
    • 84861659305 scopus 로고    scopus 로고
    • Diannexin, an annexin A5 homodimer, binds phosphatidylserine with high affinity and is a potent inhibitor of platelet-mediated events during thrombus formation
    • Rand ML, Wang H, Pluthero FG, et al. Diannexin, an annexin A5 homodimer, binds phosphatidylserine with high affinity and is a potent inhibitor of platelet-mediated events during thrombus formation. J Thromb Haemost. 2012;10(6):1109-1119.
    • (2012) J Thromb Haemost , vol.10 , Issue.6 , pp. 1109-1119
    • Rand, M.L.1    Wang, H.2    Pluthero, F.G.3
  • 37
    • 77955410626 scopus 로고    scopus 로고
    • Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases
    • Massberg S, Grahl L, von Bruehl ML, et al. Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases. Nat Med. 2010;16(8):887-896.
    • (2010) Nat Med , vol.16 , Issue.8 , pp. 887-896
    • Massberg, S.1    Grahl, L.2    Von Bruehl, M.L.3
  • 38
    • 60249092962 scopus 로고    scopus 로고
    • Vascular smooth muscle-derived tissue factor is critical for arterial thrombosis after ferric chloride-induced injury
    • Wang L, Miller C, Swarthout RF, Rao M, Mackman N, Taubman MB. Vascular smooth muscle-derived tissue factor is critical for arterial thrombosis after ferric chloride-induced injury. Blood. 2009;113(3):705-713.
    • (2009) Blood , vol.113 , Issue.3 , pp. 705-713
    • Wang, L.1    Miller, C.2    Swarthout, R.F.3    Rao, M.4    Mackman, N.5    Taubman, M.B.6
  • 39
    • 0021031042 scopus 로고
    • Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation
    • Leung LL, Harpel PC, Nachman RL, Rabellino EM. Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation. Blood. 1983;62(5):1016-1021.
    • (1983) Blood , vol.62 , Issue.5 , pp. 1016-1021
    • Leung, L.L.1    Harpel, P.C.2    Nachman, R.L.3    Rabellino, E.M.4
  • 40
    • 0036839329 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein binds to DNA and Fc gamma RI and potentiates the ingestion of apoptotic cells by macrophages
    • Gorgani NN, Smith BA, Kono DH, Theofilopoulos AN. Histidine-rich glycoprotein binds to DNA and Fc gamma RI and potentiates the ingestion of apoptotic cells by macrophages. J Immunol. 2002; 169(9):4745-4751.
    • (2002) J Immunol , vol.169 , Issue.9 , pp. 4745-4751
    • Gorgani, N.N.1    Smith, B.A.2    Kono, D.H.3    Theofilopoulos, A.N.4
  • 41
    • 79953314017 scopus 로고    scopus 로고
    • Mechanisms underlying FeCl3-induced arterial thrombosis
    • Eckly A, Hechler B, Freund M, et al. Mechanisms underlying FeCl3-induced arterial thrombosis. J Thromb Haemost. 2011;9(4):779-789.
    • (2011) J Thromb Haemost , vol.9 , Issue.4 , pp. 779-789
    • Eckly, A.1    Hechler, B.2    Freund, M.3
  • 42
    • 84879701801 scopus 로고    scopus 로고
    • Red blood cells mediate the onset of thrombosis in the ferric chloride murine model
    • Barr JD, Chauhan AK, Schaeffer GV, Hansen JK, Motto DG. Red blood cells mediate the onset of thrombosis in the ferric chloride murine model. Blood. 2013;121(18):3733-3741.
    • (2013) Blood , vol.121 , Issue.18 , pp. 3733-3741
    • Barr, J.D.1    Chauhan, A.K.2    Schaeffer, G.V.3    Hansen, J.K.4    Motto, D.G.5
  • 43
    • 84868526330 scopus 로고    scopus 로고
    • Prothrombin activation in blood coagulation: The erythrocyte contribution to thrombin generation
    • Whelihan MF, Zachary V, Orfeo T, Mann KG. Prothrombin activation in blood coagulation: the erythrocyte contribution to thrombin generation. Blood. 2012;120(18):3837-3845.
    • (2012) Blood , vol.120 , Issue.18 , pp. 3837-3845
    • Whelihan, M.F.1    Zachary, V.2    Orfeo, T.3    Mann, K.G.4
  • 44
    • 80051884192 scopus 로고    scopus 로고
    • Extracellular histones promote thrombin generation through platelet-dependent mechanisms: Involvement of platelet TLR2 and TLR4
    • Semeraro F, Ammollo CT, Morrissey JH, et al. Extracellular histones promote thrombin generation through platelet-dependent mechanisms: involvement of platelet TLR2 and TLR4. Blood. 2011;118(7):1952-1961.
    • (2011) Blood , vol.118 , Issue.7 , pp. 1952-1961
    • Semeraro, F.1    Ammollo, C.T.2    Morrissey, J.H.3
  • 45
    • 77957652949 scopus 로고    scopus 로고
    • Extracellular DNA traps promote thrombosis
    • Fuchs TA, Brill A, Duerschmied D, et al. Extracellular DNA traps promote thrombosis. Proc Natl Acad Sci USA. 2010;107(36):15880-15885.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.36 , pp. 15880-15885
    • Fuchs, T.A.1    Brill, A.2    Duerschmied, D.3
  • 46
    • 0027250293 scopus 로고
    • Packaging zinc, fibrinogen, and factor XIII in platelet alpha-granules
    • Marx G, Korner G, Mou X, Gorodetsky R. Packaging zinc, fibrinogen, and factor XIII in platelet alpha-granules. J Cell Physiol. 1993; 156(3):437-442.
    • (1993) J Cell Physiol , vol.156 , Issue.3 , pp. 437-442
    • Marx, G.1    Korner, G.2    Mou, X.3    Gorodetsky, R.4
  • 47
    • 0023212415 scopus 로고
    • Effect of negatively charged activating compounds on inactivation of factor XIIa by Cl inhibitor
    • Pixley RA, Schmaier A, Colman RW. Effect of negatively charged activating compounds on inactivation of factor XIIa by Cl inhibitor. Arch Biochem Biophys. 1987;256(2):490-498.
    • (1987) Arch Biochem Biophys , vol.256 , Issue.2 , pp. 490-498
    • Pixley, R.A.1    Schmaier, A.2    Colman, R.W.3
  • 48
    • 84928490957 scopus 로고    scopus 로고
    • Histidine rich glycoprotein binds to DNA, RNA and FXIIa with high affinity and attenuates contact-mediated coagulation in a mouse model of arterial thrombosis
    • Vu TT, Zhou J, Leslie BA, Stafford AR, Fredenburgh JC, Weitz JI. Histidine rich glycoprotein binds to DNA, RNA and FXIIa with high affinity and attenuates contact-mediated coagulation in a mouse model of arterial thrombosis. J Thromb Haemost. 2013; 11(Supp 2):Abstract AS13.1.
    • (2013) J Thromb Haemost , vol.11
    • Vu, T.T.1    Zhou, J.2    Leslie, B.A.3    Stafford, A.R.4    Fredenburgh, J.C.5    Weitz, J.I.6


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