메뉴 건너뛰기




Volumn 18, Issue 5, 2011, Pages 349-355

Factor XI and XII as antithrombotic targets

Author keywords

factor XI; factor XII; hemostasis; intrinsic pathway of coagulation; polyphosphate; thrombosis

Indexed keywords

3 CARBOXAMIDE COUMARIN INHIBITOR; ANTISENSE OLIGONUCLEOTIDE; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 12; BLOOD CLOTTING FACTOR 12A; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING INHIBITOR; BMS 262084; CLAVATADINE A; CLAVATADINE B; COMPOUND 32; CONTACT PHASE INHIBITOR; DABIGATRAN ETEXILATE; DEXTRO PHENYLALANYLPROLYLARGINYL CHLOROMETHYL KETONE; FONDAPARINUX; HEPARIN; HUMAN ALBUMIN; INFESTIN 4; LOW MOLECULAR WEIGHT HEPARIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 14E11; MONOCLONAL ANTIBODY O1A6; NEUTRALIZING ANTIBODY; PROTEIN INHIBITOR; RIVAROXABAN; THROMBOPLASTIN; UNCLASSIFIED DRUG; WARFARIN;

EID: 80051794851     PISSN: 10656251     EISSN: 15317048     Source Type: Journal    
DOI: 10.1097/MOH.0b013e3283497e61     Document Type: Review
Times cited : (107)

References (71)
  • 1
    • 39749109478 scopus 로고    scopus 로고
    • Triggers, targets and treatments for thrombosis
    • DOI 10.1038/nature06797, PII NATURE06797
    • Mackman N. Triggers, targets and treatments for thrombosis. Nature 2008;451:914-918. (Pubitemid 351301746)
    • (2008) Nature , vol.451 , Issue.7181 , pp. 914-918
    • Mackman, N.1
  • 2
    • 50449098285 scopus 로고    scopus 로고
    • Mechanisms of thrombus formation
    • Furie B, Furie BC. Mechanisms of thrombus formation. N Engl J Med 2008;359:938-949.
    • (2008) N Engl J Med , vol.359 , pp. 938-949
    • Furie, B.1    Furie, B.C.2
  • 3
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie EW, Ratnoff OD. Waterfall sequence for intrinsic blood clotting. Science 1964;145:1310-1312.
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 4
    • 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
  • 5
    • 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 2009;108:1447-1452.
    • (2009) Anesth Analg , vol.108 , pp. 1447-1452
    • Mackman, N.1
  • 6
    • 35848964833 scopus 로고    scopus 로고
    • Contact activation (kallikrein-kinin) pathway: Multiple physiologic and pathophysiologic activities
    • Colman RW, Mader VJ, Clowes AW, et al. editors, 5th ed. Philadelphia: Lippincott Williams & Wilkins
    • Colman RW. Contact activation (kallikrein-kinin) pathway: multiple physiologic and pathophysiologic activities. In Colman RW, Mader VJ, Clowes AW, et al. editors. Hemostasis and thrombosis: basic principles and clinical practice. 5th ed. Philadelphia: Lippincott Williams & Wilkins; 2006. pp. 107-130.
    • (2006) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 107-130
    • Colman, R.W.1
  • 7
    • 71149116751 scopus 로고    scopus 로고
    • Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo
    • study identifies polyphosphate an inorganic polymer as the activator of the FXII-driven intrinsic pathway of coagulation on procoagulant platelets. Polyphosphates initiate thrombosis in animal models and patients and provide procoagulant activity to propagate arterial thrombi in a FXII-dependent manner
    • Muller F, Mutch NJ, Schenk WA, et al. Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo. Cell 2009;139:1143-1156. The study identifies polyphosphate (an inorganic polymer) as the activator of the FXII-driven intrinsic pathway of coagulation on procoagulant platelets. Polyphosphates initiate thrombosis in animal models and patients and provide procoagulant activity to propagate arterial thrombi in a FXII-dependent manner.
    • (2009) Cell , vol.139 , pp. 1143-1156
    • Muller, F.1    Mutch, N.J.2    Schenk, W.A.3
  • 8
    • 36349012420 scopus 로고    scopus 로고
    • Intrinsic pathway of coagulation and arterial thrombosis
    • DOI 10.1161/ATVBAHA.107.155952
    • Gailani D, Renne T. Intrinsic pathway of coagulation and arterial thrombosis. Arterioscler Thromb Vasc Biol 2007;27:2507-2513. (Pubitemid 350158899)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.12 , pp. 2507-2513
    • Gailani, D.1    Renne, T.2
  • 9
    • 0025874052 scopus 로고
    • Factor XI activation in a revised model of blood coagulation
    • Gailani D, Broze GJ Jr. Factor XI activation in a revised model of blood coagulation. Science 1991;253:909-912. (Pubitemid 21917236)
    • (1991) Science , vol.253 , Issue.5022 , pp. 909-912
    • Gailani, D.1    Broze Jr., G.J.2
  • 10
    • 77956519082 scopus 로고    scopus 로고
    • Evidence against a protein in plasma that is a product of a factor XI mRNA splice variant missing exons 6 and 7
    • author reply 1186-1187
    • Gailani D, Sun MF, Cheng Q, et al. Evidence against a protein in plasma that is a product of a factor XI mRNA splice variant missing exons 6 and 7. Blood 2010;116:1185-1186; author reply 1186-1187.
    • (2010) Blood , vol.116 , pp. 1185-1186
    • Gailani, D.1    Sun, M.F.2    Cheng, Q.3
  • 11
    • 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 1955;34:602-613.
    • (1955) J Clin Invest , vol.34 , pp. 602-613
    • Ratnoff, O.D.1    Colopy, J.E.2
  • 13
    • 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 U S A 1996;93:6258-6263.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6258-6263
    • Bugge, T.H.1    Xiao, Q.2    Kombrinck, K.W.3
  • 14
    • 70350464419 scopus 로고    scopus 로고
    • Structural analysis of eight novel and 112 previously reported missense mutations in the interactive FXI mutation database reveals new insight on FXI deficiency
    • Saunders RE, Shiltagh N, Gomez K, et al. Structural analysis of eight novel and 112 previously reported missense mutations in the interactive FXI mutation database reveals new insight on FXI deficiency. Thromb Haemost 2009;102:287-301.
    • (2009) Thromb Haemost , vol.102 , pp. 287-301
    • Saunders, R.E.1    Shiltagh, N.2    Gomez, K.3
  • 15
    • 67651124966 scopus 로고    scopus 로고
    • Factor XI contributes to thrombin generation in the absence of factor XII
    • Kravtsov DV, Matafonov A, Tucker EI, et al. Factor XI contributes to thrombin generation in the absence of factor XII. Blood 2009;114:452-458.
    • (2009) Blood , vol.114 , pp. 452-458
    • Kravtsov, D.V.1    Matafonov, A.2    Tucker, E.I.3
  • 16
    • 2342478700 scopus 로고    scopus 로고
    • Tissue factor: In at the start... and the finish?
    • Morrissey JH. Tissue factor: in at the start...and the finish? J Thromb Haemost 2003;1:878-880.
    • (2003) J Thromb Haemost , vol.1 , pp. 878-880
    • Morrissey, J.H.1
  • 17
    • 0028843737 scopus 로고
    • Feedback activation of factorXI by thrombin in plasma results in additional formation of thrombin that protects fibrin clots from fibrinolysis
    • von dem Borne PA, Meijers JC, Bouma BN. Feedback activation of factorXI by thrombin in plasma results in additional formation of thrombin that protects fibrin clots from fibrinolysis. Blood 1995;86:3035-3042.
    • (1995) Blood , vol.86 , pp. 3035-3042
    • Von Dem Borne, P.A.1    Meijers, J.C.2    Bouma, B.N.3
  • 21
    • 0036212988 scopus 로고    scopus 로고
    • 3-induced injury of the carotid artery in the mouse
    • Rosen ED, Gailani D, Castellino FJ. FXI is essential for thrombus formation following FeCl3-induced injury of the carotid artery in the mouse. Thromb Haemost 2002;87:774-776. (Pubitemid 34302972)
    • (2002) Thrombosis and Haemostasis , vol.87 , Issue.4 , pp. 774-776
    • Rosen, E.D.1    Gailani, D.2    Castellino, F.J.3
  • 24
    • 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;203:513-518.
    • (2006) J Exp Med , vol.203 , pp. 513-518
    • Kleinschnitz, C.1    Stoll, G.2    Bendszus, M.3
  • 25
    • 74149092410 scopus 로고    scopus 로고
    • Enhanced cortical reperfusion protects coagulation factor XII-deficient mice from ischemic stroke as revealed by high-field MRI
    • Pham M, Kleinschnitz C, Helluy X, et al. Enhanced cortical reperfusion protects coagulation factor XII-deficient mice from ischemic stroke as revealed by high-field MRI. Neuroimage 2010;49:2907-2914.
    • (2010) Neuroimage , vol.49 , pp. 2907-2914
    • Pham, M.1    Kleinschnitz, C.2    Helluy, X.3
  • 26
    • 78149428887 scopus 로고    scopus 로고
    • A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo
    • Cheng Q, Tucker EI, Pine MS, et al. A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo. Blood 2010;116:3981-3989.
    • (2010) Blood , vol.116 , pp. 3981-3989
    • Cheng, Q.1    Tucker, E.I.2    Pine, M.S.3
  • 27
    • 34447344048 scopus 로고    scopus 로고
    • Role of factor XII in hemostasis and thrombosis: Clinical implications
    • DOI 10.1586/14779072.5.4.733
    • Renne T, Gailani D. Role of factor XII in hemostasis and thrombosis: clinical implications. Expert Rev Cardiovasc Ther 2007;5:733-741. (Pubitemid 47050183)
    • (2007) Expert Review of Cardiovascular Therapy , vol.5 , Issue.4 , pp. 733-741
    • Renne, T.1    Gailani, D.2
  • 28
    • 78650517652 scopus 로고    scopus 로고
    • Coagulation in vertebrates with a focus on evolution and inflammation
    • Doolittle RF. Coagulation in vertebrates with a focus on evolution and inflammation. J Innate Immun 2011;3:9-16.
    • (2011) J Innate Immun , vol.3 , pp. 9-16
    • Doolittle, R.F.1
  • 30
    • 0015288960 scopus 로고
    • The role of platelets in the contact phase of blood coagulation
    • Walsh PN. The role of platelets in the contact phase of blood coagulation. Br J Haematol 1972;22:237-254.
    • (1972) Br J Haematol , vol.22 , pp. 237-254
    • Walsh, P.N.1
  • 31
    • 79952384703 scopus 로고    scopus 로고
    • Platelet polyphosphates: The nexus of primary and secondary hemostasis
    • Muller F, Renne T. Platelet polyphosphates: the nexus of primary and secondary hemostasis. Scand J Clin Lab Invest 2011;71:82-86.
    • (2011) Scand J Clin Lab Invest , vol.71 , pp. 82-86
    • Muller, F.1    Renne, T.2
  • 32
    • 51349160073 scopus 로고    scopus 로고
    • Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation
    • Maas C, Govers-Riemslag JW, Bouma B, et al. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. J Clin Invest 2008;118:3208-3218.
    • (2008) J Clin Invest , vol.118 , pp. 3208-3218
    • Maas, C.1    Govers-Riemslag, J.W.2    Bouma, B.3
  • 33
    • 79951741353 scopus 로고    scopus 로고
    • Mast cells increase vascular permeability by heparin-initiated bradykinin formation in vivo
    • Oschatz C, Maas C, Lecher B, et al. Mast cells increase vascular permeability by heparin-initiated bradykinin formation in vivo. Immunity 2011;34:258-268.
    • (2011) Immunity , vol.34 , pp. 258-268
    • Oschatz, C.1    Maas, C.2    Lecher, B.3
  • 34
    • 23844555133 scopus 로고    scopus 로고
    • Local bradykinin formation is controlled by glycosaminoglycans
    • Renne T, Schuh K, Muller-Esterl W. Local bradykinin formation is controlled by glycosaminoglycans. J Immunol 2005;175:3377-3385. (Pubitemid 41170560)
    • (2005) Journal of Immunology , vol.175 , Issue.5 , pp. 3377-3385
    • Renne, T.1    Schuh, K.2    Muller-Esterl, W.3
  • 35
    • 0034721787 scopus 로고    scopus 로고
    • High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells
    • Renne T, Dedio J, David G, Muller-Esterl W. High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells. J Biol Chem 2000;275:33688-33696.
    • (2000) J Biol Chem , vol.275 , pp. 33688-33696
    • Renne, T.1    Dedio, J.2    David, G.3    Muller-Esterl, W.4
  • 36
    • 0001486918 scopus 로고
    • The demise of John Hageman
    • Ratnoff OD. The demise of John Hageman. N Engl J Med 1968;279:760-761.
    • (1968) N Engl J Med , vol.279 , pp. 760-761
    • Ratnoff, O.D.1
  • 37
    • 4344609673 scopus 로고    scopus 로고
    • The occasional venous thromboses seen in patients with severe (Homozygous) FXII deficiency are probably due to associated risk factors: A study of prevalence in 21 patients and review of the literature
    • DOI 10.1023/B:THRO.0000037670.42776.cd
    • Girolami A, Randi ML, Gavasso S, et al. The occasional venous thromboses seen in patients with severe (homozygous) FXII deficiency are probably due to associated risk factors: a study of prevalence in 21 patients and review of the literature. J Thromb Thrombolysis 2004;17:139-143. (Pubitemid 39157964)
    • (2004) Journal of Thrombosis and Thrombolysis , vol.17 , Issue.2 , pp. 139-143
    • Girolami, A.1    Randi, M.L.2    Gavasso, S.3    Lombardi, A.M.4    Spiezia, F.5
  • 38
    • 38349171226 scopus 로고    scopus 로고
    • Coagulation factor XII (FXII) activity, activated FXII, distribution of FXII C46T gene polymorphism and coronary risk
    • Bach J, Endler G, Winkelmann BR, et al. Coagulation factor XII (FXII) activity, activated FXII, distribution of FXII C46T gene polymorphism and coronary risk. J Thromb Haemost 2008;6:291-296.
    • (2008) J Thromb Haemost , vol.6 , pp. 291-296
    • Bach, J.1    Endler, G.2    Winkelmann, B.R.3
  • 39
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer WM, Mannhalter C, Feichtinger C, et al. The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost 1992;68:285-290.
    • (1992) Thromb Haemost , vol.68 , pp. 285-290
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3
  • 40
    • 13244284702 scopus 로고    scopus 로고
    • Myocardial infarction and arterial thrombosis in severe (homozygous) FXII deficiency: No apparent causative relation
    • DOI 10.1177/107602960501100105
    • Girolami A, Morello M, Girolami B, et al. Myocardial infarction and arterial thrombosis in severe (homozygous) FXII deficiency: no apparent causative relation. Clin Appl Thromb Hemost 2005;11:49-53. (Pubitemid 40194197)
    • (2005) Clinical and Applied Thrombosis/Hemostasis , vol.11 , Issue.1 , pp. 49-53
    • Girolami, A.1    Morello, M.2    Girolami, B.3    Lombardi, A.M.4    Bertolo, C.5
  • 42
    • 0032825571 scopus 로고    scopus 로고
    • Reevaluation of the incidence of thromboembolic complications in congenital factor XII deficiency. A study on 73 subjects from 14 Swiss families
    • Zeerleder S, Schloesser M, Redondo M, et al. Reevaluation of the incidence of thromboembolic complications in congenital factor XII deficiency: a study on 73 subjects from 14 Swiss families. Thromb Haemost 1999;82:1240-1246. (Pubitemid 29473785)
    • (1999) Thrombosis and Haemostasis , vol.82 , Issue.4 , pp. 1240-1246
    • Zeerleder, S.1    Schloesser, M.2    Redondo, M.3    Wuillemin, W.A.4    Engel, W.5    Furlan, M.6    Lammle, B.7
  • 43
    • 67849119604 scopus 로고    scopus 로고
    • Factor XI deficiency in animal models
    • Renne T, Oschatz C, Seifert S, et al. Factor XI deficiency in animal models. J Thromb Haemost 2009;7(Suppl 1):79-83.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 SUPPL. , pp. 79-83
    • Renne, T.1    Oschatz, C.2    Seifert, S.3
  • 44
    • 43249088304 scopus 로고    scopus 로고
    • Reduced incidence of ischemic stroke in patients with severe factor XI deficiency
    • Salomon O, Steinberg DM, Koren-Morag N, et al. Reduced incidence of ischemic stroke in patients with severe factor XI deficiency. Blood 2008;111:4113-4117.
    • (2008) Blood , vol.111 , pp. 4113-4117
    • Salomon, O.1    Steinberg, D.M.2    Koren-Morag, N.3
  • 45
    • 0142197166 scopus 로고    scopus 로고
    • Inherited factor XI deficiency confers no protection against acute myocardial infarction
    • Salomon O, Steinberg DM, Dardik R, et al. Inherited factor XI deficiency confers no protection against acute myocardial infarction. J Thromb Haemost 2003;1:658-661.
    • (2003) J Thromb Haemost , vol.1 , pp. 658-661
    • Salomon, O.1    Steinberg, D.M.2    Dardik, R.3
  • 46
    • 67849097372 scopus 로고    scopus 로고
    • Factor XI deficiency in humans
    • Recent and comprehensive review about clinics and therapy of hereditary FXI defiency in patients
    • Seligsohn U. Factor XI deficiency in humans. J Thromb Haemost 2009;7(Suppl 1):84-87. Recent and comprehensive review about clinics and therapy of hereditary FXI defiency in patients.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 SUPPL. , pp. 84-87
    • Seligsohn, U.1
  • 47
    • 79851476826 scopus 로고    scopus 로고
    • Patients with severe factor XI deficiency have a reduced incidence of deep-vein thrombosis
    • Salomon O, Steinberg DM, Zucker M, et al. Patients with severe factor XI deficiency have a reduced incidence of deep-vein thrombosis. Thromb Haemost 2011;105:269-273.
    • (2011) Thromb Haemost , vol.105 , pp. 269-273
    • Salomon, O.1    Steinberg, D.M.2    Zucker, M.3
  • 48
    • 78650792758 scopus 로고    scopus 로고
    • Factor Xa and thrombin as targets for new oral anticoagulants
    • Weitz JI. Factor Xa and thrombin as targets for new oral anticoagulants. Thromb Res 2011;127(Suppl 2):S5-S12.
    • (2011) Thromb Res , vol.127 , Issue.2 SUPPL.
    • Weitz, J.I.1
  • 50
    • 77950899732 scopus 로고    scopus 로고
    • Factor XIIa inhibitor recombinant human albumin Infestin-4 abolishes occlusive arterial thrombus formation without affecting bleeding
    • Hagedorn I, Schmidbauer S, Pleines I, et al. Factor XIIa inhibitor recombinant human albumin Infestin-4 abolishes occlusive arterial thrombus formation without affecting bleeding. Circulation 2010;121:1510-1517.
    • (2010) Circulation , vol.121 , pp. 1510-1517
    • Hagedorn, I.1    Schmidbauer, S.2    Pleines, I.3
  • 51
    • 70449698361 scopus 로고    scopus 로고
    • Ir-CPI, a coagulation contact phase inhibitor from the tick Ixodes ricinus, inhibits thrombus formation without impairing hemostasis
    • Decrem Y, Rath G, Blasioli V, et al. Ir-CPI, a coagulation contact phase inhibitor from the tick Ixodes ricinus, inhibits thrombus formation without impairing hemostasis. J Exp Med 2009;206:2381-2395.
    • (2009) J Exp Med , vol.206 , pp. 2381-2395
    • Decrem, Y.1    Rath, G.2    Blasioli, V.3
  • 53
    • 77953219775 scopus 로고    scopus 로고
    • COU254, a specific 3-carboxamidecoumarin inhibitor of coagulation factor XII, does not protect mice from acute ischemic stroke
    • Kraft P, Schwarz T, Pochet L, et al. COU254, a specific 3-carboxamidecoumarin inhibitor of coagulation factor XII, does not protect mice from acute ischemic stroke. Exp Transl Stroke Med 2010;2:5.
    • (2010) Exp Transl Stroke Med , vol.2 , pp. 5
    • Kraft, P.1    Schwarz, T.2    Pochet, L.3
  • 54
    • 0025057006 scopus 로고
    • Cabbage seed protease inhibitor: A slow, tight-binding inhibitor of trypsin with activity toward thrombin, activated Stuart factor (factor Xa), activated Hageman factor (factor XIIa), and plasmin
    • Carter TH, Everson BA, Ratnoff OD. Cabbage seed protease inhibitor: a slow, tight-binding inhibitor of trypsin with activity toward thrombin, activated Stuart factor (factor Xa), activated Hageman factor (factor XIIa), and plasmin. Blood 1990;75:108-115. (Pubitemid 20031497)
    • (1990) Blood , vol.75 , Issue.1 , pp. 108-115
    • Carter, T.H.1    Everson, B.A.2    Ratnoff, O.D.3
  • 55
    • 0020402436 scopus 로고
    • Pumpkin seed inhibitor of human factor XII(a) (activated Hageman factor) and bovine trypsin
    • DOI 10.1021/bi00259a003
    • Hojima Y, Pierce JV, Pisano JJ. Pumpkin seed inhibitor of human factor XIIa (activated Hageman factor) and bovine trypsin. Biochemistry 1982;21:3741-3746. (Pubitemid 13230943)
    • (1982) Biochemistry , vol.21 , Issue.16 , pp. 3741-3746
    • Hojima, Y.1    Pierce, J.V.2    Pisano, J.J.3
  • 56
    • 0025084616 scopus 로고
    • A new protein inhibitor of trypsin and activated Hageman factor from pumpkin (Cucurbita maxima) seeds
    • DOI 10.1016/0014-5793(90)81075-Y
    • Krishnamoorthi R, Gong YX, Richardson M. A new protein inhibitor of trypsin and activated Hageman factor from pumpkin (Cucurbita maxima) seeds. FEBS Lett 1990;273:163-167. (Pubitemid 20362457)
    • (1990) FEBS Letters , vol.273 , Issue.1-2 , pp. 163-167
    • Krishnamoorthi, R.1    Gong, Y.2    Richardson, M.3
  • 57
    • 0021267818 scopus 로고
    • Amino acid sequence and secondary structural analysis of the corn inhibitor of trypsin and activated Hageman factor
    • Mahoney WC, Hermodson MA, Jones B, et al. Amino acid sequence and secondary structural analysis of the corn inhibitor of trypsin and activated Hageman Factor. J Biol Chem 1984;259:8412-8416. (Pubitemid 14090598)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.13 , pp. 8412-8416
    • Mahoney, W.C.1    Hermodson, M.A.2    Jones, B.3
  • 58
    • 8844236924 scopus 로고    scopus 로고
    • Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae)
    • DOI 10.1016/j.febslet.2004.10.052, PII S0014579304013031
    • Campos IT, Tanaka-Azevedo AM, Tanaka AS. Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae). FEBS Lett 2004;577:512-516. (Pubitemid 39535340)
    • (2004) FEBS Letters , vol.577 , Issue.3 , pp. 512-516
    • Campos, I.T.N.1    Tanaka-Azevedo, A.M.2    Tanaka, A.S.3
  • 59
    • 0029025751 scopus 로고
    • Ecotin is a potent inhibitor of the contact system proteases factor XIIa and plasma kallikrein
    • Ulmer JS, Lindquist RN, Dennis MS, Lazarus RA. Ecotin is a potent inhibitor of the contact system proteases factor XIIa and plasma kallikrein. FEBS Lett 1995;365:159-163.
    • (1995) FEBS Lett , vol.365 , pp. 159-163
    • Ulmer, J.S.1    Lindquist, R.N.2    Dennis, M.S.3    Lazarus, R.A.4
  • 60
    • 77649141885 scopus 로고    scopus 로고
    • Inhibition of factor XIa as a new approach to anticoagulation
    • comprehensive review gives an overview about coagulation factor XI and its inhibitors and summarizes current strategies to target this protease as an anticoagulant therapy
    • Schumacher WA, Luettgen JM, Quan ML, Seiffert DA. Inhibition of factor XIa as a new approach to anticoagulation. Arterioscler Thromb Vasc Biol 2010;30:388-392. The comprehensive review gives an overview about coagulation factor XI and its inhibitors and summarizes current strategies to target this protease as an anticoagulant therapy.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 388-392
    • Schumacher, W.A.1    Luettgen, J.M.2    Quan, M.L.3    Seiffert, D.A.4
  • 61
    • 77951667939 scopus 로고    scopus 로고
    • Inhibition of factor XI reduces thrombus formation in rabbit jugular vein under endothelial denudation and/or blood stasis
    • Takahashi M, Yamashita A, Moriguchi-Goto S, et al. Inhibition of factor XI reduces thrombus formation in rabbit jugular vein under endothelial denudation and/or blood stasis. Thromb Res 2010;125:464-470.
    • (2010) Thromb Res , vol.125 , pp. 464-470
    • Takahashi, M.1    Yamashita, A.2    Moriguchi-Goto, S.3
  • 62
    • 33745280932 scopus 로고    scopus 로고
    • Factor XI contributes to thrombus propagation on injured neointima of the rabbit iliac artery
    • Yamashita A, Nishihira K, Kitazawa T, et al. Factor XI contributes to thrombus propagation on injured neointima of the rabbit iliac artery. J Thromb Haemost 2006;4:1496-1501.
    • (2006) J Thromb Haemost , vol.4 , pp. 1496-1501
    • Yamashita, A.1    Nishihira, K.2    Kitazawa, T.3
  • 63
    • 0042243616 scopus 로고    scopus 로고
    • Factor XI-dependence of surface- and tissue factor-initiated thrombus propagation in primates
    • DOI 10.1182/blood-2003-01-0324
    • Gruber A, Hanson SR. Factor XI-dependence of surface-and tissue factorinitiated thrombus propagation in primates. Blood 2003;102:953-955. (Pubitemid 36917789)
    • (2003) Blood , vol.102 , Issue.3 , pp. 953-955
    • Gruber, A.1    Hanson, S.R.2
  • 64
    • 59649103257 scopus 로고    scopus 로고
    • Prevention of vascular graft occlusion and thrombus-associated thrombin generation by inhibition of factor XI
    • Tucker EI, Marzec UM, White TC, et al. Prevention of vascular graft occlusion and thrombus-associated thrombin generation by inhibition of factor XI. Blood 2009;113:936-944.
    • (2009) Blood , vol.113 , pp. 936-944
    • Tucker, E.I.1    Marzec, U.M.2    White, T.C.3
  • 68
    • 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 et al. described a new approach targeting FXI by RNA interference for prevention of arterial and venous thrombosis without increasing the risk of bleeding. FXI antisense oligonucleotide may be a potential strategy to interfere with thrombosis in humans
    • Zhang H, Lowenberg 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;116:4684-4692. Zhang et al. described a new approach targeting FXI by RNA interference for prevention of arterial and venous thrombosis without increasing the risk of bleeding. FXI antisense oligonucleotide may be a potential strategy to interfere with thrombosis in humans.
    • (2010) Blood , vol.116 , pp. 4684-4692
    • Zhang, H.1    Lowenberg, E.C.2    Crosby, J.R.3
  • 69
    • 3242719541 scopus 로고    scopus 로고
    • Antisense strategies
    • DOI 10.2174/1566524043360375
    • Crooke ST. Antisense strategies. Curr Mol Med 2004;4:465-487. (Pubitemid 38961192)
    • (2004) Current Molecular Medicine , vol.4 , Issue.5 , pp. 465-487
    • Crooke, S.T.1
  • 70
    • 33750207033 scopus 로고    scopus 로고
    • Potent reduction of apolipoprotein B and low-density lipoprotein cholesterol by short-term administration of an antisense inhibitor of apolipoprotein B
    • DOI 10.1161/CIRCULATIONAHA.105.606442, PII 0000301720061017000012
    • Kastelein JJ, Wedel MK, Baker BF, et al. Potent reduction of apolipoprotein B and low-density lipoprotein cholesterol by short-term administration of an antisense inhibitor of apolipoprotein B. Circulation 2006;114:1729-1735. (Pubitemid 44607121)
    • (2006) Circulation , vol.114 , Issue.16 , pp. 1729-1735
    • Kastelein, J.J.P.1    Wedel, M.K.2    Baker, B.F.3    Su, J.4    Bradley, J.D.5    Yu, R.Z.6    Chuang, E.7    Graham, M.J.8    Crooke, R.M.9
  • 71
    • 80051797372 scopus 로고    scopus 로고
    • Pharmacological characterization and structure activity relationship of FXI antisense oligonucleotides in cynomolgus monkeys
    • Mac Leod R, Crosby J, Zhao C. Pharmacological characterization and structure activity relationship of FXI antisense oligonucleotides in cynomolgus monkeys. Blood (ASH Annual Meeting Abstracts) 2009;114.
    • (2009) Blood (ASH Annual Meeting Abstracts) , pp. 114
    • Leod, R.M.1    Crosby, J.2    Zhao, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.