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Volumn 38, Issue 4, 2015, Pages 1707-1726

Viscoelasticity and Ultrastructure in Coagulation and Inflammation: Two Diverse Techniques, One Conclusion

Author keywords

coagulation; fibrinogen fibrin; inflammation; morphology; platelets

Indexed keywords

BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 13; BLOOD CLOTTING FACTOR 13A; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9A; CALCIUM; FIBRIN; FIBRIN MONOMER; FIBRINOGEN; THROMBIN; THROMBOPLASTIN;

EID: 84937253753     PISSN: 03603997     EISSN: 15732576     Source Type: Journal    
DOI: 10.1007/s10753-015-0148-7     Document Type: Article
Times cited : (17)

References (198)
  • 1
    • 83555166113 scopus 로고    scopus 로고
    • Writing a narrative biomedical review: Considerations for authors, peer reviewers, and editors
    • PID: 21800117
    • Gasparyan, A.Y., L. Ayvazyan, H. Blackmore, and G.D. Kitas. 2011. Writing a narrative biomedical review: Considerations for authors, peer reviewers, and editors. Rheumatology International 31(11): 1409–1417.
    • (2011) Rheumatology International , vol.31 , Issue.11 , pp. 1409-1417
    • Gasparyan, A.Y.1    Ayvazyan, L.2    Blackmore, H.3    Kitas, G.D.4
  • 2
    • 0037813859 scopus 로고    scopus 로고
    • A history of blood coagulation
    • Mayo Foundation for Medical Education and Research, Rochester
    • Owen, C.A. (2001) A history of blood coagulation. In: W.L. Nichols & E.J.W. Bowie (eds) Mayo Foundation for Medical Education and Research, Rochester, pp 169–180.
    • (2001) W.L , pp. 169-180
    • Owen, C.A.1
  • 3
    • 84979859827 scopus 로고
    • The chemistry of blood coagulation
    • Connor, W.E. 1958. The chemistry of blood coagulation. A.M.A. Archives of Internal Medicine 102(4): 681–682.
    • (1958) A.M.A. Archives of Internal Medicine , vol.102 , Issue.4 , pp. 681-682
    • Connor, W.E.1
  • 4
    • 33645450196 scopus 로고    scopus 로고
    • Max Schultze (1865), G. Bizzozero (1882) and the discovery of the platelet
    • PID: 16643426
    • Brewer, D.B. 2006. Max Schultze (1865), G. Bizzozero (1882) and the discovery of the platelet. British Journal of Haematology 133(3): 251–258.
    • (2006) British Journal of Haematology , vol.133 , Issue.3 , pp. 251-258
    • Brewer, D.B.1
  • 5
    • 34547821918 scopus 로고    scopus 로고
    • Giulio Bizzozero and the discovery of platelets
    • COI: 1:CAS:528:DC%2BD2sXovFKnt7s%3D, PID: 17383722
    • Ribatti, D., and E. Crivellato. 2007. Giulio Bizzozero and the discovery of platelets. Leukemia Research 31(10): 1339–1341.
    • (2007) Leukemia Research , vol.31 , Issue.10 , pp. 1339-1341
    • Ribatti, D.1    Crivellato, E.2
  • 6
    • 0242585716 scopus 로고    scopus 로고
    • Blood coagulation
    • PID: 10821379
    • Dahlbäck, B. 2000. Blood coagulation. Lancet 355(9215): 1627–1632.
    • (2000) Lancet , vol.355 , Issue.9215 , pp. 1627-1632
    • Dahlbäck, B.1
  • 8
    • 0029086642 scopus 로고
    • Biochemical and molecular aspects of the coagulation cascade
    • COI: 1:CAS:528:DyaK2MXnvVSrt7g%3D, PID: 8578439
    • Davie, E.W. 1995. Biochemical and molecular aspects of the coagulation cascade. Thrombosis and Haemostasis 74(1): 1–6.
    • (1995) Thrombosis and Haemostasis , vol.74 , Issue.1
    • Davie, E.W.1
  • 9
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • COI: 1:CAS:528:DyaF2cXktFensrY%3D, PID: 14167839
    • Macfarlane, R.G. 1964. An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202(4931): 498–499.
    • (1964) Nature , vol.202 , Issue.4931 , pp. 498-499
    • Macfarlane, R.G.1
  • 10
    • 0028151281 scopus 로고
    • Platelet procoagulant complex assembly in a tissue factor-initiated system
    • COI: 1:CAS:528:DyaK2MXhvFyjtb0%3D, PID: 7803283
    • Monroe, D.M., H.R. Roberts, and M. Hoffman. 1994. Platelet procoagulant complex assembly in a tissue factor-initiated system. British Journal of Haematology 88(2): 364–371.
    • (1994) British Journal of Haematology , vol.88 , Issue.2 , pp. 364-371
    • Monroe, D.M.1    Roberts, H.R.2    Hoffman, M.3
  • 11
    • 0029144243 scopus 로고
    • Factors IXa and Xa play distinct roles in tissue factor-dependent initiation of coagulation
    • COI: 1:CAS:528:DyaK2MXnslKrtbc%3D, PID: 7655009
    • Hoffman, M., D.M. Monroe, J.A. Oliver, and H.R. Roberts. 1995. Factors IXa and Xa play distinct roles in tissue factor-dependent initiation of coagulation. Blood 86(5): 1794–1801.
    • (1995) Blood , vol.86 , Issue.5 , pp. 1794-1801
    • Hoffman, M.1    Monroe, D.M.2    Oliver, J.A.3    Roberts, H.R.4
  • 12
    • 0029744067 scopus 로고    scopus 로고
    • Transmission of a procoagulant signal from tissue factor-bearing cells to platelets
    • COI: 1:STN:280:DyaK28vjslWqsg%3D%3D, PID: 8839998
    • Monroe, D.M., M. Hoffman, and H.R. Roberts. 1996. Transmission of a procoagulant signal from tissue factor-bearing cells to platelets. Blood Coagulation and Fibrinolysis 7(4): 459–464.
    • (1996) Blood Coagulation and Fibrinolysis , vol.7 , Issue.4 , pp. 459-464
    • Monroe, D.M.1    Hoffman, M.2    Roberts, H.R.3
  • 13
    • 37349131729 scopus 로고    scopus 로고
    • The new coagulation cascade and its possible influence on the delicate balance between thrombosis and hemorrhage. La nueva cascada de la coagulación y su posible influencia en el difícil equilibrio entre trombosis y hemorragia
    • PID: 18082084
    • Pérez-Gómez, F., and R. Bover. 2007. The new coagulation cascade and its possible influence on the delicate balance between thrombosis and hemorrhage. La nueva cascada de la coagulación y su posible influencia en el difícil equilibrio entre trombosis y hemorragia. Revista Espanola de Cardiologia 60(12): 1217–1219.
    • (2007) Revista Espanola de Cardiologia , vol.60 , Issue.12 , pp. 1217-1219
    • Pérez-Gómez, F.1    Bover, R.2
  • 15
    • 61449101394 scopus 로고    scopus 로고
    • The cell-based model of coagulation: State-of-the-art review
    • PID: 19691581
    • Smith, S.A. 2009. The cell-based model of coagulation: State-of-the-art review. Journal of Veterinary Emergency and Critical Care 19(1): 3–10.
    • (2009) Journal of Veterinary Emergency and Critical Care , vol.19 , Issue.1 , pp. 3-10
    • Smith, S.A.1
  • 16
    • 0025819769 scopus 로고
    • Role of calcium ion in the generation of factor XIII activity
    • COI: 1:CAS:528:DyaK3MXktVGkt7o%3D, PID: 2059625
    • Hornyak, T.J., and J.A. Shafer. 1991. Role of calcium ion in the generation of factor XIII activity. Biochemistry 30(25): 6175–6182.
    • (1991) Biochemistry , vol.30 , Issue.25 , pp. 6175-6182
    • Hornyak, T.J.1    Shafer, J.A.2
  • 17
    • 0037710318 scopus 로고    scopus 로고
    • Factor XIII subunit A as an intracellular transglutaminase
    • COI: 1:CAS:528:DC%2BD3sXls1Wru7g%3D, PID: 12861374
    • Adany, R., and H. Bardos. 2003. Factor XIII subunit A as an intracellular transglutaminase. Cellular and Molecular Life Sciences CMLS 60(6): 1049–1060.
    • (2003) Cellular and Molecular Life Sciences CMLS , vol.60 , Issue.6 , pp. 1049-1060
    • Adany, R.1    Bardos, H.2
  • 18
    • 0021080275 scopus 로고
    • Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen
    • COI: 1:CAS:528:DyaL2cXktVer, PID: 6661434
    • Janus, T.J., S.D. Lewis, L. Lorand, and J.A. Shafer. 1983. Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen. Biochemistry 22(26): 6269–6272.
    • (1983) Biochemistry , vol.22 , Issue.26 , pp. 6269-6272
    • Janus, T.J.1    Lewis, S.D.2    Lorand, L.3    Shafer, J.A.4
  • 19
    • 1842678190 scopus 로고    scopus 로고
    • Remodeling the blood coagulation cascade
    • COI: 1:CAS:528:DC%2BD2cXovVGjsA%3D%3D, PID: 14760207
    • Hoffman, M. 2003. Remodeling the blood coagulation cascade. Journal of Thrombosis and Thrombolysis 16(1–2): 17–20.
    • (2003) Journal of Thrombosis and Thrombolysis , vol.16 , Issue.1-2 , pp. 17-20
    • Hoffman, M.1
  • 20
    • 0034971291 scopus 로고    scopus 로고
    • A cell-based model of hemostasis
    • COI: 1:CAS:528:DC%2BD3MXlt1GhtLo%3D, PID: 11434702
    • Hoffman, M., and D.M. Monroe Iii. 2001. A cell-based model of hemostasis. Thrombosis and Haemostasis 85(6): 958–965.
    • (2001) Thrombosis and Haemostasis , vol.85 , Issue.6 , pp. 958-965
    • Hoffman, M.1    Monroe Iii, D.M.2
  • 21
    • 74049100937 scopus 로고    scopus 로고
    • Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability
    • COI: 1:CAS:528:DC%2BD1MXhsFGqsb3O, PID: 19797520
    • Campbell, R.A., K.A. Overmyer, C.H. Selzman, B.C. Sheridan, and A.S. Wolberg. 2009. Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability. Blood 114(23): 4886–4896.
    • (2009) Blood , vol.114 , Issue.23 , pp. 4886-4896
    • Campbell, R.A.1    Overmyer, K.A.2    Selzman, C.H.3    Sheridan, B.C.4    Wolberg, A.S.5
  • 22
    • 0027367669 scopus 로고
    • Introduction: Blood coagulation
    • COI: 1:CAS:528:DyaK2cXltVOiug%3D%3D, PID: 8412787
    • Mann, K.G. 1993. Introduction: Blood coagulation. Methods in Enzymology 222: 1–10.
    • (1993) Methods in Enzymology , vol.222
    • Mann, K.G.1
  • 23
    • 0027123107 scopus 로고
    • Molecular and cellular biology of blood coagulation
    • COI: 1:CAS:528:DyaK38XitFWms7s%3D, PID: 1538724
    • Furie, B., and B.C. Furie. 1992. Molecular and cellular biology of blood coagulation. New England Journal of Medicine 326(12): 800–806.
    • (1992) New England Journal of Medicine , vol.326 , Issue.12 , pp. 800-806
    • Furie, B.1    Furie, B.C.2
  • 24
    • 0030221068 scopus 로고    scopus 로고
    • Initiation of blood coagulation: the tissue factor/factor VIIa complex
    • COI: 1:CAS:528:DyaK28XkvVKrtro%3D, PID: 8768895
    • Kirchhofer, D., and Y. Nemerson. 1996. Initiation of blood coagulation: the tissue factor/factor VIIa complex. Current Opinion in Biotechnology 7(4): 386–391.
    • (1996) Current Opinion in Biotechnology , vol.7 , Issue.4 , pp. 386-391
    • Kirchhofer, D.1    Nemerson, Y.2
  • 25
    • 0031759213 scopus 로고    scopus 로고
    • The role of the tissue factor pathway in initiation of coagulation
    • COI: 1:CAS:528:DyaK1cXnsVCisL4%3D, PID: 9819022
    • Mann, K.G., C. Van’t Veer, K. Cawthern, and S. Butenas. 1998. The role of the tissue factor pathway in initiation of coagulation. Blood Coagulation and Fibrinolysis 9(SUPPL. 1): S3–S7.
    • (1998) Blood Coagulation and Fibrinolysis , vol.9 , pp. S3-S7
    • Mann, K.G.1    Van’t Veer, C.2    Cawthern, K.3    Butenas, S.4
  • 26
    • 0029916926 scopus 로고    scopus 로고
    • Cellular interactions in hemostasis
    • COI: 1:CAS:528:DyaK28XitlKktbY%3D, PID: 8904166
    • Hoffman, M., D.M. Monroe, and H.R. Roberts. 1996. Cellular interactions in hemostasis. Haemostasis 26(SUPPL. 1): 12–16.
    • (1996) Haemostasis , vol.26 , pp. 12-16
    • Hoffman, M.1    Monroe, D.M.2    Roberts, H.R.3
  • 28
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • COI: 1:CAS:528:DyaK1cXlsFOmsLY%3D, PID: 9759493
    • Sadler, J.E. 1998. Biochemistry and genetics of von Willebrand factor. Annual Review of Biochemistry 67: 395–424.
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 29
    • 0025874052 scopus 로고
    • Factor XI activation in a revised model of blood coagulation
    • COI: 1:CAS:528:DyaK3MXlvVShtr8%3D, PID: 1652157
    • Gailani, D., and G.J. Broze Jr. 1991. Factor XI activation in a revised model of blood coagulation. Science 253(5022): 909–912.
    • (1991) Science , vol.253 , Issue.5022 , pp. 909-912
    • Gailani, D.1    Broze, G.J.2
  • 30
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency—A study on 74 subjects from 14 Swiss families
    • COI: 1:STN:280:DyaK3M3nt1aitg%3D%3D, PID: 1905067
    • Lammle, B., W.A. Wuillemin, I. Huber, M. Krauskopf, C. Zurcher, R. Pflugshaupt, and M. Furlan. 1991. Thromboembolism and bleeding tendency in congenital factor XII deficiency—A study on 74 subjects from 14 Swiss families. Thrombosis and Haemostasis 65(2): 117–121.
    • (1991) Thrombosis and Haemostasis , vol.65 , Issue.2 , pp. 117-121
    • Lammle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zurcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 32
    • 0030070996 scopus 로고    scopus 로고
    • Cell biology of tissue factor, the principal initiator of blood coagulation
    • Camerer, E., A.B.. Kolstø, and H. Prydz. 1996. Cell biology of tissue factor, the principal initiator of blood coagulation. Thrombosis Research 81(1): 1–41.
    • (1996) Thrombosis Research , vol.81 , Issue.1
    • Camerer, E.1    Kolstø, A.B.2    Prydz, H.3
  • 33
    • 0034917278 scopus 로고    scopus 로고
    • Tissue factor: An enzyme cofactor and a true receptor
    • COI: 1:CAS:528:DC%2BD3MXlsVeks7s%3D, PID: 11487043
    • Morrissey, J.H. 2001. Tissue factor: An enzyme cofactor and a true receptor. Thrombosis and Haemostasis 86(1): 66–74.
    • (2001) Thrombosis and Haemostasis , vol.86 , Issue.1 , pp. 66-74
    • Morrissey, J.H.1
  • 34
    • 0027977907 scopus 로고
    • Erratum: Fibrinogen and factor VII in the prediction of coronary risk: Results from the PROCAM study in healthy men (Arteriosclerosis and Thrombosis (1994) 14 (54-59))
    • Heinrich, J., L. Balleisen, H. Schulte, G. Assmann, and J. Van de Loo. 1994. Erratum: Fibrinogen and factor VII in the prediction of coronary risk: Results from the PROCAM study in healthy men (Arteriosclerosis and Thrombosis (1994) 14 (54-59)). Arteriosclerosis and Thrombosis 14(8): 1392.
    • (1994) Arteriosclerosis and Thrombosis , vol.14 , Issue.8 , pp. 1392
    • Heinrich, J.1    Balleisen, L.2    Schulte, H.3    Assmann, G.4    Van de Loo, J.5
  • 36
    • 0022244862 scopus 로고
    • Cleavage of human high molecular weight kininogen by factor XIa in vitro: Effect on structure and function
    • COI: 1:CAS:528:DyaL2MXlsFKgs74%3D, PID: 3875612
    • Scott, C.F., L.D. Silver, A.D. Purdon, and R.W. Colman. 1985. Cleavage of human high molecular weight kininogen by factor XIa in vitro: Effect on structure and function. Journal of Biological Chemistry 260(19): 10856–10863.
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.19 , pp. 10856-10863
    • Scott, C.F.1    Silver, L.D.2    Purdon, A.D.3    Colman, R.W.4
  • 37
    • 0025815673 scopus 로고
    • Factor XI deficiency in Ashkenazi Jews in Israel
    • COI: 1:STN:280:DyaK3M3ntVehtQ%3D%3D, PID: 2052060
    • Asakai, R., D.W. Chung, E.W. Davie, and U. Seligsohn. 1991. Factor XI deficiency in Ashkenazi Jews in Israel. New England Journal of Medicine 325(3): 153–158.
    • (1991) New England Journal of Medicine , vol.325 , Issue.3 , pp. 153-158
    • Asakai, R.1    Chung, D.W.2    Davie, E.W.3    Seligsohn, U.4
  • 39
    • 0032744352 scopus 로고    scopus 로고
    • Biologic activities of the contact factors in vivo. Potentiation of hypotension, inflammation, and fibrinolysis, and inhibition of cell adhesion, angiogenesis and thrombosis
    • COI: 1:CAS:528:DyaK1MXotVehsbw%3D, PID: 10613636
    • Colman, R.W. 1999. Biologic activities of the contact factors in vivo. Potentiation of hypotension, inflammation, and fibrinolysis, and inhibition of cell adhesion, angiogenesis and thrombosis. Thrombosis and Haemostasis 82(6): 1568–1577.
    • (1999) Thrombosis and Haemostasis , vol.82 , Issue.6 , pp. 1568-1577
    • Colman, R.W.1
  • 40
    • 0025991461 scopus 로고
    • The effect of plasma von Willebrand factor on the binding of human factor VIII to thrombin-activated human platelets
    • COI: 1:CAS:528:DyaK3MXmtVCgsbg%3D, PID: 1917924
    • Nesheim, M., D.D. Pittman, A.R. Giles, D.N. Fass, J.H. Wang, D. Slonosky, and R.J. Kaufman. 1991. The effect of plasma von Willebrand factor on the binding of human factor VIII to thrombin-activated human platelets. Journal of Biological Chemistry 266(27): 17815–17820.
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 17815-17820
    • Nesheim, M.1    Pittman, D.D.2    Giles, A.R.3    Fass, D.N.4    Wang, J.H.5    Slonosky, D.6    Kaufman, R.J.7
  • 41
    • 0023274887 scopus 로고
    • The effect of thrombin on the complex between factor VIII and von Willebrand factor
    • COI: 1:CAS:528:DyaL2sXlsFWru7g%3D, PID: 3113951
    • Hamer, R.J., J.A. Koedam, N.H. Beeser-Visser, and J.J. Sixma. 1987. The effect of thrombin on the complex between factor VIII and von Willebrand factor. European Journal of Biochemistry 167(2): 253–259.
    • (1987) European Journal of Biochemistry , vol.167 , Issue.2 , pp. 253-259
    • Hamer, R.J.1    Koedam, J.A.2    Beeser-Visser, N.H.3    Sixma, J.J.4
  • 43
    • 0018622772 scopus 로고
    • The contribution of bovine factor V and factor Va to the activity of prothrombinase
    • COI: 1:CAS:528:DyaE1MXlvVyksL0%3D, PID: 500617
    • Nesheim, M.E., J.B. Taswell, and K.G. Mann. 1979. The contribution of bovine factor V and factor Va to the activity of prothrombinase. Journal of Biological Chemistry 254(21): 10952–10962.
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.21 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 44
    • 0027435759 scopus 로고
    • Meizothrombin: active intermediate formed during prothrombinase-catalyzed activation of Prothrombin
    • COI: 1:CAS:528:DyaK2cXhtVSjurw%3D, PID: 8412800
    • Doyle, M.F., and P.E. Haley. 1993. Meizothrombin: active intermediate formed during prothrombinase-catalyzed activation of Prothrombin. Methods in Enzymology 222: 299–312.
    • (1993) Methods in Enzymology , vol.222 , pp. 299-312
    • Doyle, M.F.1    Haley, P.E.2
  • 46
    • 0029850530 scopus 로고    scopus 로고
    • A common genetic variation in the 3′-untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increase in venous thrombosis
    • COI: 1:CAS:528:DyaK28XntVahsLg%3D, PID: 8916933
    • Poort, S.R., F.R. Rosendaal, P.H. Reitsma, and R.M. Bertina. 1996. A common genetic variation in the 3′-untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increase in venous thrombosis. Blood 88(10): 3698–3703.
    • (1996) Blood , vol.88 , Issue.10 , pp. 3698-3703
    • Poort, S.R.1    Rosendaal, F.R.2    Reitsma, P.H.3    Bertina, R.M.4
  • 47
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • COI: 1:CAS:528:DC%2BD38XltF2rsLk%3D, PID: 12070020
    • Brummel, K.E., S.G. Paradis, S. Butenas, and K.G. Mann. 2002. Thrombin functions during tissue factor-induced blood coagulation. Blood 100(1): 148–152.
    • (2002) Blood , vol.100 , Issue.1 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3    Mann, K.G.4
  • 48
    • 0030013427 scopus 로고    scopus 로고
    • Molecular interactions of thrombin
    • COI: 1:STN:280:DyaK28vgtFegsw%3D%3D, PID: 8807707
    • Tulinsky, A. 1996. Molecular interactions of thrombin. Seminars in Thrombosis and Hemostasis 22(2): 117–124.
    • (1996) Seminars in Thrombosis and Hemostasis , vol.22 , Issue.2 , pp. 117-124
    • Tulinsky, A.1
  • 49
    • 0022967224 scopus 로고
    • Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
    • COI: 1:CAS:528:DyaL2sXot1Wnug%3D%3D, PID: 3801570
    • Weisel, J.W. 1986. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophysical Journal 50(6): 1079–1093.
    • (1986) Biophysical Journal , vol.50 , Issue.6 , pp. 1079-1093
    • Weisel, J.W.1
  • 50
    • 0034770081 scopus 로고    scopus 로고
    • The hemostatic system and angiogenesis in malignancy
    • COI: 1:STN:280:DC%2BD3MnjvVCjtQ%3D%3D, PID: 11687948
    • Wojtukiewicz, M.Z., E. Sierko, P. Klement, and J. Rak. 2001. The hemostatic system and angiogenesis in malignancy. Neoplasia 3(5): 371–384.
    • (2001) Neoplasia , vol.3 , Issue.5 , pp. 371-384
    • Wojtukiewicz, M.Z.1    Sierko, E.2    Klement, P.3    Rak, J.4
  • 51
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • COI: 1:CAS:528:DyaK38XhtVejur8%3D, PID: 1931959
    • Davie, E.W., K. Fujikawa, and W. Kisiel. 1991. The coagulation cascade: Initiation, maintenance, and regulation. Biochemistry 30(43): 10363–10370.
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 54
    • 0032697618 scopus 로고    scopus 로고
    • Biochemistry and physiology of blood coagulation
    • COI: 1:CAS:528:DyaK1MXnsVWnur8%3D, PID: 10605701
    • Mann, K.G. 1999. Biochemistry and physiology of blood coagulation. Thrombosis and Haemostasis 82(2): 165–174.
    • (1999) Thrombosis and Haemostasis , vol.82 , Issue.2 , pp. 165-174
    • Mann, K.G.1
  • 55
    • 0018816742 scopus 로고
    • Blood coagulation
    • COI: 1:CAS:528:DyaL3cXkvFahur8%3D, PID: 6996572
    • Jackson, C.M., and Y. Nemerson. 1980. Blood coagulation. Annual Review of Biochemistry 49(1): 765–811.
    • (1980) Annual Review of Biochemistry , vol.49 , Issue.1 , pp. 765-811
    • Jackson, C.M.1    Nemerson, Y.2
  • 56
    • 33947282669 scopus 로고    scopus 로고
    • Platelet-neutrophil-interactions: linking hemostasis and inflammation
    • COI: 1:CAS:528:DC%2BD2sXlsFGlu7Y%3D, PID: 16987572
    • Zarbock, A., R.K. Polanowska-Grabowska, and K. Ley. 2007. Platelet-neutrophil-interactions: linking hemostasis and inflammation. Blood Reviews 21(2): 99–111.
    • (2007) Blood Reviews , vol.21 , Issue.2 , pp. 99-111
    • Zarbock, A.1    Polanowska-Grabowska, R.K.2    Ley, K.3
  • 58
    • 0038454527 scopus 로고    scopus 로고
    • Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets
    • COI: 1:CAS:528:DC%2BD3sXkslCjs7s%3D, PID: 12595308
    • Mosnier, L.O., P. Buijtenhuijs, P.F. Marx, J.C. Meijers, and B.N. Bouma. 2003. Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets. Blood 101(12): 4844–4846.
    • (2003) Blood , vol.101 , Issue.12 , pp. 4844-4846
    • Mosnier, L.O.1    Buijtenhuijs, P.2    Marx, P.F.3    Meijers, J.C.4    Bouma, B.N.5
  • 59
    • 0029119149 scopus 로고
    • Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin
    • COI: 1:CAS:528:DyaK2MXntlKmurg%3D
    • Frenette, P.S., R.C. Johnson, R.O. Hynes, and D.D. Wagner. 1995. Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin. Proceedings of the National Academy of Sciences 92(16): 7450–7454.
    • (1995) Proceedings of the National Academy of Sciences , vol.92 , Issue.16 , pp. 7450-7454
    • Frenette, P.S.1    Johnson, R.C.2    Hynes, R.O.3    Wagner, D.D.4
  • 60
    • 0032519765 scopus 로고    scopus 로고
    • Platelet–endothelial interactions in inflamed mesenteric venules
    • COI: 1:CAS:528:DyaK1cXhtVGks7k%3D, PID: 9454762
    • Frenette, P.S., C. Moyna, D.W. Hartwell, J.B. Lowe, R.O. Hynes, and D.D. Wagner. 1998. Platelet–endothelial interactions in inflamed mesenteric venules. Blood 91(4): 1318–1324.
    • (1998) Blood , vol.91 , Issue.4 , pp. 1318-1324
    • Frenette, P.S.1    Moyna, C.2    Hartwell, D.W.3    Lowe, J.B.4    Hynes, R.O.5    Wagner, D.D.6
  • 61
    • 84937254117 scopus 로고
    • Platelets
    • Stamatoyannopoulos G, Nienhuis AW, Leder P, Majerus P, (eds), W.B. Saunders Co, Philadelphia
    • Majerus, P. 1987. Platelets. In The molecular basis of blood diseases, ed. G. Stamatoyannopoulos, A.W. Nienhuis, P. Leder, and P. Majerus. Philadelphia: W.B. Saunders Co.
    • (1987) The molecular basis of blood diseases
    • Majerus, P.1
  • 62
    • 0023603317 scopus 로고
    • Structure–function relationship of human von Willebrand factor
    • COI: 1:CAS:528:DyaL2sXlslaqu7c%3D, PID: 3304456
    • Girma, J.P., D. Meyer, C.L. Verweij, H. Pannekoek, and J.J. Sixma. 1987. Structure–function relationship of human von Willebrand factor. Blood 70(3): 605–611.
    • (1987) Blood , vol.70 , Issue.3 , pp. 605-611
    • Girma, J.P.1    Meyer, D.2    Verweij, C.L.3    Pannekoek, H.4    Sixma, J.J.5
  • 63
    • 0023612519 scopus 로고
    • Von Willebrand factor and von Willebrand disease
    • COI: 1:CAS:528:DyaL2sXmtlCjsro%3D, PID: 3307951
    • Ruggeri, Z.M., and T.S. Zimmerman. 1987. Von Willebrand factor and von Willebrand disease. Blood 70(4): 895–904.
    • (1987) Blood , vol.70 , Issue.4 , pp. 895-904
    • Ruggeri, Z.M.1    Zimmerman, T.S.2
  • 65
    • 0020450843 scopus 로고
    • Identification of the fibrinogen receptor on human platelets by photoaffinity labeling
    • COI: 1:CAS:528:DyaL38XkvV2ltL8%3D, PID: 6282870
    • Bennett, J.S., G. Vilaire, and D.B. Cines. 1982. Identification of the fibrinogen receptor on human platelets by photoaffinity labeling. Journal of Biological Chemistry 257(14): 8049–8054.
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.14 , pp. 8049-8054
    • Bennett, J.S.1    Vilaire, G.2    Cines, D.B.3
  • 66
    • 0025910094 scopus 로고
    • Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein IIb–IIIa on nonactivated platelets
    • COI: 1:CAS:528:DyaK3MXks12iu7o%3D, PID: 2040630
    • Savage, B., and Z.M. Ruggeri. 1991. Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein IIb–IIIa on nonactivated platelets. Journal of Biological Chemistry 266(17): 11227–11233.
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 11227-11233
    • Savage, B.1    Ruggeri, Z.M.2
  • 68
    • 67849116915 scopus 로고    scopus 로고
    • Novel molecules in calcium signaling in platelets
    • COI: 1:CAS:528:DC%2BD1MXpvV2is78%3D, PID: 19630797
    • Bergmeier, W., and L. Stefanini. 2009. Novel molecules in calcium signaling in platelets. Journal of Thrombosis and Haemostasis 7(SUPPL. 1): 187–190.
    • (2009) Journal of Thrombosis and Haemostasis , vol.7 , pp. 187-190
    • Bergmeier, W.1    Stefanini, L.2
  • 69
    • 0025267690 scopus 로고
    • Calcium signaling in human platelets
    • COI: 1:CAS:528:DyaK3cXlvVymt78%3D, PID: 2158766
    • Rink, T., and S. Sage. 1990. Calcium signaling in human platelets. Annual Review of Physiology 52(1): 431–449.
    • (1990) Annual Review of Physiology , vol.52 , Issue.1 , pp. 431-449
    • Rink, T.1    Sage, S.2
  • 70
    • 77950635369 scopus 로고    scopus 로고
    • Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow
    • COI: 1:CAS:528:DC%2BC3cXntlKnsLo%3D, PID: 20371335
    • Neeves, K., D. Illing, and S. Diamond. 2010. Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow. Biophysical Journal 98(7): 1344–1352.
    • (2010) Biophysical Journal , vol.98 , Issue.7 , pp. 1344-1352
    • Neeves, K.1    Illing, D.2    Diamond, S.3
  • 71
    • 0034491170 scopus 로고    scopus 로고
    • On the determination of the average molecular weight, radius of gyration, and mass/length ratio of polydisperse solutions of polymerizing rod-like macromolecular monomers by multi-angle static lightscattering
    • Ferri, F., M. Greco, and M. Rocco. 2001. On the determination of the average molecular weight, radius of gyration, and mass/length ratio of polydisperse solutions of polymerizing rod-like macromolecular monomers by multi-angle static lightscattering. Macromolecular Symposia 162(1): 23–44.
    • (2001) Macromolecular Symposia , vol.162 , Issue.1 , pp. 23-44
    • Ferri, F.1    Greco, M.2    Rocco, M.3
  • 72
    • 77958474678 scopus 로고    scopus 로고
    • Nanostructure of the fibrin clot
    • COI: 1:CAS:528:DC%2BC3cXht1ClsbfN, PID: 20923635
    • Yeromonahos, C., B. Polack, and F. Caton. 2010. Nanostructure of the fibrin clot. Biophysical Journal 99(7): 2018–2027.
    • (2010) Biophysical Journal , vol.99 , Issue.7 , pp. 2018-2027
    • Yeromonahos, C.1    Polack, B.2    Caton, F.3
  • 73
    • 0035940439 scopus 로고    scopus 로고
    • Crystal structure of native chicken fibrinogen at 2.7 Å resolution
    • COI: 1:CAS:528:DC%2BD3MXntVynsbg%3D, PID: 11601975
    • Yang, Z., J.M. Kollman, L. Pandi, and R.F. Doolittle. 2001. Crystal structure of native chicken fibrinogen at 2.7 Å resolution. Biochemistry 40(42): 12515–12523.
    • (2001) Biochemistry , vol.40 , Issue.42 , pp. 12515-12523
    • Yang, Z.1    Kollman, J.M.2    Pandi, L.3    Doolittle, R.F.4
  • 74
    • 0001454124 scopus 로고
    • Preparation and properties of serum and plasma proteins. IX. Human fibrin in the form of an elastic film
    • COI: 1:CAS:528:DyaH2sXhsFeksg%3D%3D, PID: 20292444
    • Ferry, J.D., and P.R. Morrison. 1947. Preparation and properties of serum and plasma proteins. IX. Human fibrin in the form of an elastic film. Journal of the American Chemical Society 69(2): 400–409.
    • (1947) Journal of the American Chemical Society , vol.69 , Issue.2 , pp. 400-409
    • Ferry, J.D.1    Morrison, P.R.2
  • 78
    • 9644260704 scopus 로고    scopus 로고
    • The mechanical properties of fibrin for basic scientists and clinicians
    • COI: 1:CAS:528:DC%2BD2cXhtVamu7vK, PID: 15572258
    • Weisel, J.W. 2004. The mechanical properties of fibrin for basic scientists and clinicians. Biophysical Chemistry 112(2-3 SPEC. ISS): 267–276.
    • (2004) Biophysical Chemistry , vol.112 , Issue.2-3 SPEC. ISS , pp. 267-276
    • Weisel, J.W.1
  • 80
    • 68449088259 scopus 로고    scopus 로고
    • Multiscale mechanics of fibrin polymer: Gel stretching with protein unfolding and loss of water
    • COI: 1:CAS:528:DC%2BD1MXptl2gurY%3D, PID: 19661428
    • Brown, A.E.X., R.I. Litvinov, D.E. Discher, P.K. Purohit, and J.W. Weisel. 2009. Multiscale mechanics of fibrin polymer: Gel stretching with protein unfolding and loss of water. Science 325(5941): 741–744.
    • (2009) Science , vol.325 , Issue.5941 , pp. 741-744
    • Brown, A.E.X.1    Litvinov, R.I.2    Discher, D.E.3    Purohit, P.K.4    Weisel, J.W.5
  • 81
    • 0001577585 scopus 로고    scopus 로고
    • Strain hardening of fibrin gels and plasma clots
    • COI: 1:CAS:528:DyaK2sXlt1agtrk%3D
    • Shah, J.V., and P.A. Janmey. 1997. Strain hardening of fibrin gels and plasma clots. Rheologica Acta 36(3): 262–268.
    • (1997) Rheologica Acta , vol.36 , Issue.3 , pp. 262-268
    • Shah, J.V.1    Janmey, P.A.2
  • 82
    • 36949027299 scopus 로고    scopus 로고
    • Local and global deformations in a strain-stiffening fibrin gel
    • Wen, Q., A. Basu, J.P. Winer, A. Yodh, and P.A. Janmey. 2007. Local and global deformations in a strain-stiffening fibrin gel. New Journal of Physics 9(11): 428.
    • (2007) New Journal of Physics , vol.9 , Issue.11 , pp. 428
    • Wen, Q.1    Basu, A.2    Winer, J.P.3    Yodh, A.4    Janmey, P.A.5
  • 83
    • 65249122033 scopus 로고    scopus 로고
    • Nonlinear elasticity of stiff filament networks: Strain stiffening, negative normal stress, and filament alignment in fibrin gels
    • COI: 1:CAS:528:DC%2BD1MXitlGhs78%3D
    • Kang, H., Q. Wen, P.A. Janmey, J.X. Tang, E. Conti, and F.C. MacKintosh. 2009. Nonlinear elasticity of stiff filament networks: Strain stiffening, negative normal stress, and filament alignment in fibrin gels. Journal of Physical Chemistry B 113(12): 3799–3805.
    • (2009) Journal of Physical Chemistry B , vol.113 , Issue.12 , pp. 3799-3805
    • Kang, H.1    Wen, Q.2    Janmey, P.A.3    Tang, J.X.4    Conti, E.5    MacKintosh, F.C.6
  • 84
    • 0015594187 scopus 로고
    • Viscoelastic properties of fibrin clots
    • COI: 1:STN:280:DyaE3s3jsVWnsQ%3D%3D, PID: 4724175
    • Roberts, W.W., L. Lorand, and L.F. Mockros. 1973. Viscoelastic properties of fibrin clots. Biorheology 10(1): 29–42.
    • (1973) Biorheology , vol.10 , Issue.1 , pp. 29-42
    • Roberts, W.W.1    Lorand, L.2    Mockros, L.F.3
  • 85
    • 46049117087 scopus 로고    scopus 로고
    • Probing nonlinear rheology with inertio-elastic oscillations
    • COI: 1:CAS:528:DC%2BD1cXnsFOnur4%3D
    • Yao, N.Y., R.J. Larsen, and D.A. Weitz. 2008. Probing nonlinear rheology with inertio-elastic oscillations. Journal of Rheology 52(4): 1013–1025.
    • (2008) Journal of Rheology , vol.52 , Issue.4 , pp. 1013-1025
    • Yao, N.Y.1    Larsen, R.J.2    Weitz, D.A.3
  • 86
    • 0020734317 scopus 로고
    • Rheology of fibrin clots—6. Stress relaxation, creep, and differential dynamic modulus of fine clots in large shearing deformations
    • Janmey, P.A., E.J. Amis, and J.D. Ferry. 1983. Rheology of fibrin clots—6. Stress relaxation, creep, and differential dynamic modulus of fine clots in large shearing deformations. Journal of Rheology 27(2): 135–153.
    • (1983) Journal of Rheology , vol.27 , Issue.2 , pp. 135-153
    • Janmey, P.A.1    Amis, E.J.2    Ferry, J.D.3
  • 87
    • 0024241291 scopus 로고
    • Strain enhancement of elastic modulus in fine fibrin clots
    • COI: 1:STN:280:DyaL1M7mt1eiug%3D%3D, PID: 3232126
    • Bale, M.D., and J.D. Ferry. 1988. Strain enhancement of elastic modulus in fine fibrin clots. Thrombosis Research 52(6): 565–572.
    • (1988) Thrombosis Research , vol.52 , Issue.6 , pp. 565-572
    • Bale, M.D.1    Ferry, J.D.2
  • 88
    • 2542627629 scopus 로고    scopus 로고
    • Elastic behavior of cross-linked and bundled actin networks
    • COI: 1:CAS:528:DC%2BD2cXkt1Ggu78%3D, PID: 15166374
    • Gardel, M.L., J.H. Shin, F.C. MacKintosh, L. Mahadevan, P. Matsudaira, and D.A. Weitz. 2004. Elastic behavior of cross-linked and bundled actin networks. Science 304(5675): 1301–1305.
    • (2004) Science , vol.304 , Issue.5675 , pp. 1301-1305
    • Gardel, M.L.1    Shin, J.H.2    MacKintosh, F.C.3    Mahadevan, L.4    Matsudaira, P.5    Weitz, D.A.6
  • 89
    • 0032729622 scopus 로고    scopus 로고
    • Structural origins of fibrin clot rheology
    • COI: 1:CAS:528:DyaK1MXnt1Wku7s%3D, PID: 10545379
    • Ryan, E.A., L.F. Mockros, J.W. Weisel, and L. Lorand. 1999. Structural origins of fibrin clot rheology. Biophysical Journal 77(5): 2813–2826.
    • (1999) Biophysical Journal , vol.77 , Issue.5 , pp. 2813-2826
    • Ryan, E.A.1    Mockros, L.F.2    Weisel, J.W.3    Lorand, L.4
  • 90
    • 0034680846 scopus 로고    scopus 로고
    • Strain hardening of actin filament networks: regulation by the dynamic cross-linking protein α-actinin
    • COI: 1:CAS:528:DC%2BD3cXosVSkt7Y%3D, PID: 10954703
    • Xu, J., Y. Tseng, and D. Wirtz. 2000. Strain hardening of actin filament networks: regulation by the dynamic cross-linking protein α-actinin. Journal of Biological Chemistry 275(46): 35886–35892.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.46 , pp. 35886-35892
    • Xu, J.1    Tseng, Y.2    Wirtz, D.3
  • 92
    • 77951637514 scopus 로고    scopus 로고
    • Stiffening of individual fibrin fibers equitably distributes strain and strengthens networks
    • COI: 1:CAS:528:DC%2BC3cXht1WnsrvK, PID: 20409484
    • Hudson, N.E., J.R. Houser, E.T. O’Brien Iii, R.M. Taylor Ii, R. Superfine, S.T. Lord, and M.R. Falvo. 2010. Stiffening of individual fibrin fibers equitably distributes strain and strengthens networks. Biophysical Journal 98(8): 1632–1640.
    • (2010) Biophysical Journal , vol.98 , Issue.8 , pp. 1632-1640
    • Hudson, N.E.1    Houser, J.R.2    O’Brien Iii, E.T.3    Taylor Ii, R.M.4    Superfine, R.5    Lord, S.T.6    Falvo, M.R.7
  • 93
    • 54149115887 scopus 로고    scopus 로고
    • Length of tandem repeats in fibrin’s αC region correlates with fiber extensibility
    • COI: 1:CAS:528:DC%2BD1cXhsVyqs7rP, PID: 18761721
    • Falvo, M.R., D. Millard, E.T. O’Brien Iii, R. Superfine, and S.T. Lord. 2008. Length of tandem repeats in fibrin’s αC region correlates with fiber extensibility. Journal of Thrombosis and Haemostasis 6(11): 1991–1993.
    • (2008) Journal of Thrombosis and Haemostasis , vol.6 , Issue.11 , pp. 1991-1993
    • Falvo, M.R.1    Millard, D.2    O’Brien Iii, E.T.3    Superfine, R.4    Lord, S.T.5
  • 95
  • 96
    • 18744376043 scopus 로고    scopus 로고
    • Nonlinear elasticity in biological gels
    • COI: 1:CAS:528:DC%2BD2MXktVWhtLs%3D, PID: 15889088
    • Storm, C., J.J. Pastore, F.C. MacKintosh, T.C. Lubensky, and P.A. Janmey. 2005. Nonlinear elasticity in biological gels. Nature 435(7039): 191–194.
    • (2005) Nature , vol.435 , Issue.7039 , pp. 191-194
    • Storm, C.1    Pastore, J.J.2    MacKintosh, F.C.3    Lubensky, T.C.4    Janmey, P.A.5
  • 97
    • 34047229067 scopus 로고    scopus 로고
    • Thrombin generation and fibrin clot structure
    • COI: 1:CAS:528:DC%2BD2sXmt1egsL8%3D, PID: 17208341
    • Wolberg, A.S. 2007. Thrombin generation and fibrin clot structure. Blood Reviews 21(3): 131–142.
    • (2007) Blood Reviews , vol.21 , Issue.3 , pp. 131-142
    • Wolberg, A.S.1
  • 98
    • 40849126406 scopus 로고    scopus 로고
    • Thrombin generation, fibrin clot formation and hemostasis
    • PID: 18282807
    • Wolberg, A.S., and R.A. Campbell. 2008. Thrombin generation, fibrin clot formation and hemostasis. Transfusion and Apheresis Science 38(1): 15–23.
    • (2008) Transfusion and Apheresis Science , vol.38 , Issue.1 , pp. 15-23
    • Wolberg, A.S.1    Campbell, R.A.2
  • 100
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • COI: 1:CAS:528:DyaK28XhsFeisL4%3D, PID: 8598903
    • Banner, D.W., A. D’Arcy, C. Chene, F.K. Winkler, A. Guha, W.H. Konigsberg, Y. Nemerson, and D. Kirchhofer. 1996. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380(6569): 41–46.
    • (1996) Nature , vol.380 , Issue.6569 , pp. 41-46
    • Banner, D.W.1    D’Arcy, A.2    Chene, C.3    Winkler, F.K.4    Guha, A.5    Konigsberg, W.H.6    Nemerson, Y.7    Kirchhofer, D.8
  • 101
    • 0025280666 scopus 로고
    • Glycoprotein Ib, von Willebrand factor, and glycoprotein IIb: IIIa are all involved in platelet adhesion to fibrin in flowing whole blood
    • COI: 1:CAS:528:DyaK3cXlsV2ntLw%3D, PID: 2369638
    • Hantgan, R.R., G. Hindriks, R.G. Taylor, J.J. Sixma, and P.G. de Groot. 1990. Glycoprotein Ib, von Willebrand factor, and glycoprotein IIb: IIIa are all involved in platelet adhesion to fibrin in flowing whole blood. Blood 76(2): 345–353.
    • (1990) Blood , vol.76 , Issue.2 , pp. 345-353
    • Hantgan, R.R.1    Hindriks, G.2    Taylor, R.G.3    Sixma, J.J.4    de Groot, P.G.5
  • 102
    • 0028269598 scopus 로고
    • Evidence for a role of glycoprotein IIb–IIIa, distinct from its ability to support aggregation, in platelet activation by ionophores in the presence of extracellular divalent cations
    • COI: 1:CAS:528:DyaK2cXksl2gs74%3D, PID: 8167340
    • Lages, B., and H.J. Weiss. 1994. Evidence for a role of glycoprotein IIb–IIIa, distinct from its ability to support aggregation, in platelet activation by ionophores in the presence of extracellular divalent cations. Blood 83(9): 2549–2559.
    • (1994) Blood , vol.83 , Issue.9 , pp. 2549-2559
    • Lages, B.1    Weiss, H.J.2
  • 103
    • 33751158321 scopus 로고
    • Characterization of cation-binding sequences in the platelet integrin GPIIb-IIIa (. alpha. IIb. beta. 3) by terbium luminescence
    • COI: 1:CAS:528:DyaK2cXmslCksrg%3D, PID: 7522557
    • Cierniewski, C.S., J.W. Smith, E.F. Plow, and T. Haas. 1994. Characterization of cation-binding sequences in the platelet integrin GPIIb-IIIa (. alpha. IIb. beta. 3) by terbium luminescence. Biochemistry 33(40): 12238–12246.
    • (1994) Biochemistry , vol.33 , Issue.40 , pp. 12238-12246
    • Cierniewski, C.S.1    Smith, J.W.2    Plow, E.F.3    Haas, T.4
  • 104
    • 0025908304 scopus 로고
    • Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins. Effects of lipids and temperature
    • COI: 1:CAS:528:DyaK3MXktVems7g%3D, PID: 2039481
    • Rivas, G., and J. Gonzalez-Rodriguez. 1991. Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins. Effects of lipids and temperature. The Biochemical Journal 276: 35–40.
    • (1991) The Biochemical Journal , vol.276 , pp. 35-40
    • Rivas, G.1    Gonzalez-Rodriguez, J.2
  • 106
    • 0016267498 scopus 로고
    • Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor
    • COI: 1:CAS:528:DyaE2cXlsV2gsL4%3D, PID: 4859234
    • Curtis, C., K. Brown, R. Credo, R. Domanik, A. Gray, P. Stenberg, and L. Lorand. 1974. Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor. Biochemistry 13(18): 3774–3780.
    • (1974) Biochemistry , vol.13 , Issue.18 , pp. 3774-3780
    • Curtis, C.1    Brown, K.2    Credo, R.3    Domanik, R.4    Gray, A.5    Stenberg, P.6    Lorand, L.7
  • 108
    • 0018565072 scopus 로고
    • Factor XIII
    • COI: 1:STN:280:DyaL3c%2Fnslanug%3D%3D, PID: 514066
    • Kitchens, C.S., and T.F. Newcomb. 1979. Factor XIII. Medicine 58(6): 413–429.
    • (1979) Medicine , vol.58 , Issue.6 , pp. 413-429
    • Kitchens, C.S.1    Newcomb, T.F.2
  • 109
    • 0022351911 scopus 로고
    • Tissue factor accelerates the activation of coagulation factor VII: The role of a bifunctional coagulation cofactor
    • COI: 1:CAS:528:DyaL28Xjt1ensA%3D%3D, PID: 4082113
    • Nemerson, Y., and D. Repke. 1985. Tissue factor accelerates the activation of coagulation factor VII: The role of a bifunctional coagulation cofactor. Thrombosis Research 40(3): 351–358.
    • (1985) Thrombosis Research , vol.40 , Issue.3 , pp. 351-358
    • Nemerson, Y.1    Repke, D.2
  • 110
    • 0023688352 scopus 로고
    • The effect of platelets upon factor Xa-catalyzed activation of factor VII in vitro
    • COI: 1:CAS:528:DyaL1cXlt1Knurk%3D, PID: 3135857
    • Rao, L., and S.I. Rapaport. 1988. The effect of platelets upon factor Xa-catalyzed activation of factor VII in vitro. Blood 72(2): 396–401.
    • (1988) Blood , vol.72 , Issue.2 , pp. 396-401
    • Rao, L.1    Rapaport, S.I.2
  • 111
    • 0024345543 scopus 로고
    • Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation
    • COI: 1:CAS:528:DyaL1MXktlOhtro%3D, PID: 2785997
    • Sakai, T., T. Lund-Hansen, L. Paborsky, A. Pedersen, and W. Kisiel. 1989. Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation. Journal of Biological Chemistry 264(17): 9980–9988.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.17 , pp. 9980-9988
    • Sakai, T.1    Lund-Hansen, T.2    Paborsky, L.3    Pedersen, A.4    Kisiel, W.5
  • 112
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
    • COI: 1:CAS:528:DyaL28Xos1Sjsw%3D%3D, PID: 3082357
    • Eaton, D., H. Rodriguez, and G.A. Vehar. 1986. Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry 25(2): 505–512.
    • (1986) Biochemistry , vol.25 , Issue.2 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 114
    • 0002162129 scopus 로고
    • Activation of the fibrin stabilizing factor of plasma by thrombin
    • COI: 1:CAS:528:DyaF2cXktVKgt7w%3D, PID: 14165504
    • Lorand, L., and K. Konishi. 1964. Activation of the fibrin stabilizing factor of plasma by thrombin. Archives of Biochemistry and Biophysics 105(1): 58–67.
    • (1964) Archives of Biochemistry and Biophysics , vol.105 , Issue.1 , pp. 58-67
    • Lorand, L.1    Konishi, K.2
  • 115
    • 0026083164 scopus 로고
    • Characterization of the kinetic pathway for fibrin promotion of. alpha.-thrombin-catalyzed activation of plasma factor XIII
    • COI: 1:CAS:528:DyaK3MXhsVSntbc%3D, PID: 1989686
    • Naski, M.C., L. Lorand, and J.A. Shafer. 1991. Characterization of the kinetic pathway for fibrin promotion of. alpha.-thrombin-catalyzed activation of plasma factor XIII. Biochemistry 30(4): 934–941.
    • (1991) Biochemistry , vol.30 , Issue.4 , pp. 934-941
    • Naski, M.C.1    Lorand, L.2    Shafer, J.A.3
  • 116
    • 0017567792 scopus 로고
    • Anticoagulant properties of bovine plasma protein C following activation by thrombin
    • COI: 1:CAS:528:DyaE1cXhvFOmsg%3D%3D, PID: 588557
    • Kisiel, W., W.M. Canfield, L.H. Ericsson, and E.W. Davie. 1977. Anticoagulant properties of bovine plasma protein C following activation by thrombin. Biochemistry 16(26): 5824–5831.
    • (1977) Biochemistry , vol.16 , Issue.26 , pp. 5824-5831
    • Kisiel, W.1    Canfield, W.M.2    Ericsson, L.H.3    Davie, E.W.4
  • 117
    • 0020072618 scopus 로고
    • Mechanism of action of human activated protein C, a thrombin-dependent anticoagulant enzyme
    • COI: 1:CAS:528:DyaL38XktlKksb8%3D, PID: 6803853
    • Marlar, R.A., A.J. Kleiss, and J.H. Griffin. 1982. Mechanism of action of human activated protein C, a thrombin-dependent anticoagulant enzyme. Blood 59(5): 1067–1072.
    • (1982) Blood , vol.59 , Issue.5 , pp. 1067-1072
    • Marlar, R.A.1    Kleiss, A.J.2    Griffin, J.H.3
  • 118
    • 0018860405 scopus 로고
    • Preparation and properties of bovine factor VIII (antihemophilic factor)
    • COI: 1:CAS:528:DyaL3cXptVWrsw%3D%3D, PID: 7356933
    • Vehar, G.A., and E.W. Davie. 1980. Preparation and properties of bovine factor VIII (antihemophilic factor). Biochemistry 19(3): 401–410.
    • (1980) Biochemistry , vol.19 , Issue.3 , pp. 401-410
    • Vehar, G.A.1    Davie, E.W.2
  • 119
    • 0019332589 scopus 로고
    • Regulation of activated protein C by a new protein. A possible function for bovine protein S
    • COI: 1:CAS:528:DyaL3cXks1Ogu7Y%3D, PID: 6892911
    • Walker, F.J. 1980. Regulation of activated protein C by a new protein. A possible function for bovine protein S. Journal of Biological Chemistry 255(12): 5521–5524.
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.12 , pp. 5521-5524
    • Walker, F.J.1
  • 120
    • 50849101992 scopus 로고    scopus 로고
    • How Na+ activates thrombin—A review of the functional and structural data
    • COI: 1:CAS:528:DC%2BD1cXps1Ohur0%3D, PID: 18979627
    • Huntington, J.A. 2008. How Na+ activates thrombin—A review of the functional and structural data. Biological Chemistry 389(8): 1025–1035.
    • (2008) Biological Chemistry , vol.389 , Issue.8 , pp. 1025-1035
    • Huntington, J.A.1
  • 121
    • 84869443502 scopus 로고    scopus 로고
    • An ensemble view of thrombin allostery
    • COI: 1:CAS:528:DC%2BC38XhsVGiur3F, PID: 22944689
    • Lechtenberg, B.C., S.M.V. Freund, and J.A. Huntington. 2012. An ensemble view of thrombin allostery. Biological Chemistry 393(9): 889–898.
    • (2012) Biological Chemistry , vol.393 , Issue.9 , pp. 889-898
    • Lechtenberg, B.C.1    Freund, S.M.V.2    Huntington, J.A.3
  • 122
    • 84857783253 scopus 로고    scopus 로고
    • Mechanisms of platelet activation by thrombin: a short history
    • PID: 22137742
    • De Candia, E. 2012. Mechanisms of platelet activation by thrombin: a short history. Thrombosis Research 129(3): 250–256.
    • (2012) Thrombosis Research , vol.129 , Issue.3 , pp. 250-256
    • De Candia, E.1
  • 123
    • 47949133729 scopus 로고    scopus 로고
    • Inflammation
    • COI: 1:CAS:528:DC%2BD1cXovV2mt7w%3D, PID: 18650912
    • Weiss, U. 2008. Inflammation. Nature 454(7203): 427.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 427
    • Weiss, U.1
  • 124
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • COI: 1:CAS:528:DC%2BD1cXovV2mtbw%3D, PID: 18650913
    • Medzhitov, R. 2008. Origin and physiological roles of inflammation. Nature 454(7203): 428–435.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 428-435
    • Medzhitov, R.1
  • 126
    • 0032502978 scopus 로고    scopus 로고
    • Linkage between inflammation and coagulation: an update on the molecular basis of the crosstalk
    • COI: 1:CAS:528:DyaK1cXisFymsL4%3D, PID: 9600323
    • Cicala, C., and G. Cirino. 1998. Linkage between inflammation and coagulation: an update on the molecular basis of the crosstalk. Life Sciences 62(20): 1817–1824.
    • (1998) Life Sciences , vol.62 , Issue.20 , pp. 1817-1824
    • Cicala, C.1    Cirino, G.2
  • 127
    • 0035799341 scopus 로고    scopus 로고
    • Inflammation and thrombosis: The clot thickens
    • COI: 1:CAS:528:DC%2BD3MXjsFGgsLw%3D, PID: 11282900
    • Libby, P., and D.I. Simon. 2001. Inflammation and thrombosis: The clot thickens. Circulation 103(13): 1718–1720.
    • (2001) Circulation , vol.103 , Issue.13 , pp. 1718-1720
    • Libby, P.1    Simon, D.I.2
  • 128
    • 79751511868 scopus 로고    scopus 로고
    • Platelets in inflammation and thrombosis
    • COI: 1:CAS:528:DC%2BC3MXpvFQ%3D
    • Gasparyan, A. 2010. Platelets in inflammation and thrombosis. Inflammation & Allergy Drug Targets 9(5): 319.
    • (2010) Inflammation & Allergy Drug Targets , vol.9 , Issue.5 , pp. 319
    • Gasparyan, A.1
  • 129
    • 79953738262 scopus 로고    scopus 로고
    • Mean platelet volume: a link between thrombosis and inflammation?
    • COI: 1:CAS:528:DC%2BC3MXltVSmtrc%3D, PID: 21247392
    • Gasparyan, A.Y., L. Ayvazyan, D.P. Mikhailidis, and G.D. Kitas. 2011. Mean platelet volume: a link between thrombosis and inflammation? Current Pharmaceutical Design 17(1): 47–58.
    • (2011) Current Pharmaceutical Design , vol.17 , Issue.1 , pp. 47-58
    • Gasparyan, A.Y.1    Ayvazyan, L.2    Mikhailidis, D.P.3    Kitas, G.D.4
  • 130
    • 77954424901 scopus 로고    scopus 로고
    • Mean platelet volume in patients with rheumatoid arthritis: the effect of anti-TNF-alpha therapy
    • COI: 1:CAS:528:DC%2BC3cXmsFOqsrk%3D, PID: 20066426
    • Gasparyan, A., A. Sandoo, A. Stavropoulos-Kalinoglou, and G. Kitas. 2010. Mean platelet volume in patients with rheumatoid arthritis: the effect of anti-TNF-alpha therapy. Rheumatology International 30(8): 1125–1129.
    • (2010) Rheumatology International , vol.30 , Issue.8 , pp. 1125-1129
    • Gasparyan, A.1    Sandoo, A.2    Stavropoulos-Kalinoglou, A.3    Kitas, G.4
  • 132
    • 1142273373 scopus 로고    scopus 로고
    • Role of platelets in coronary thrombosis and reperfusion of ischemic myocardium
    • COI: 1:CAS:528:DC%2BD2cXhtFWmsLs%3D, PID: 14962480
    • Gawaz, M. 2004. Role of platelets in coronary thrombosis and reperfusion of ischemic myocardium. Cardiovascular Research 61(3): 498–511.
    • (2004) Cardiovascular Research , vol.61 , Issue.3 , pp. 498-511
    • Gawaz, M.1
  • 133
    • 84868699503 scopus 로고    scopus 로고
    • The inflammatory chemokine CXC motif ligand 16 triggers platelet activation and adhesion via CXC motif receptor 6-dependent phosphatidylinositide 3-kinase/akt signaling
    • COI: 1:CAS:528:DC%2BC38XhsFGqtrzN, PID: 22927331
    • Borst, O., P. Münzer, S. Gatidis, E.M. Schmidt, T. Schönberger, E. Schmid, S.T. Towhid, K. Stellos, P. Seizer, A.E. May, et al. 2012. The inflammatory chemokine CXC motif ligand 16 triggers platelet activation and adhesion via CXC motif receptor 6-dependent phosphatidylinositide 3-kinase/akt signaling. Circulation Research 111(10): 1297–1307.
    • (2012) Circulation Research , vol.111 , Issue.10 , pp. 1297-1307
    • Borst, O.1    Münzer, P.2    Gatidis, S.3    Schmidt, E.M.4    Schönberger, T.5    Schmid, E.6    Towhid, S.T.7    Stellos, K.8    Seizer, P.9    May, A.E.10
  • 134
    • 79954436381 scopus 로고    scopus 로고
    • Platelet function in rheumatoid arthritis: arthritic and cardiovascular implications
    • COI: 1:CAS:528:DC%2BC3MXpvFSjsw%3D%3D, PID: 20390282
    • Gasparyan, A., A. Stavropoulos-Kalinoglou, D. Mikhailidis, K.J. Douglas, and G. Kitas. 2011. Platelet function in rheumatoid arthritis: arthritic and cardiovascular implications. Rheumatology International 31(2): 153–164.
    • (2011) Rheumatology International , vol.31 , Issue.2 , pp. 153-164
    • Gasparyan, A.1    Stavropoulos-Kalinoglou, A.2    Mikhailidis, D.3    Douglas, K.J.4    Kitas, G.5
  • 135
    • 0030760353 scopus 로고    scopus 로고
    • Cytokines, platelet production and hemostasis
    • COI: 1:CAS:528:DyaK2sXks1yrsb4%3D, PID: 20297930
    • Burstein, S. 1997. Cytokines, platelet production and hemostasis. Platelets 8(2–3): 93–104.
    • (1997) Platelets , vol.8 , Issue.2-3 , pp. 93-104
    • Burstein, S.1
  • 136
    • 0030729723 scopus 로고    scopus 로고
    • Binding of factor VIIa to tissue factor induces alterations in gene expression in human fibroblast cells: up-regulation of poly(A) polymerase
    • COI: 1:CAS:528:DyaK2sXns1yltL8%3D, PID: 9356495
    • Pendurthi, U.R., D. Alok, and L.V.M. Rao. 1997. Binding of factor VIIa to tissue factor induces alterations in gene expression in human fibroblast cells: up-regulation of poly(A) polymerase. Proceedings of the National Academy of Sciences of the United States of America 94(23): 12598–12603.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.23 , pp. 12598-12603
    • Pendurthi, U.R.1    Alok, D.2    Rao, L.V.M.3
  • 137
    • 0031907778 scopus 로고    scopus 로고
    • CD40L–CD40 interactions regulate endothelial cell surface tissue factor and thrombomodulin expression
    • COI: 1:CAS:528:DyaK1cXhs1OqtLY%3D, PID: 9500526
    • Miller, D.L., R. Yaron, and M.J. Yellin. 1998. CD40L–CD40 interactions regulate endothelial cell surface tissue factor and thrombomodulin expression. Journal of Leukocyte Biology 63(3): 373–379.
    • (1998) Journal of Leukocyte Biology , vol.63 , Issue.3 , pp. 373-379
    • Miller, D.L.1    Yaron, R.2    Yellin, M.J.3
  • 139
    • 0032484987 scopus 로고    scopus 로고
    • CD40 ligand on activated platelets triggers an inflammatory reaction of endothelial cells
    • COI: 1:CAS:528:DyaK1cXhtVSlsb8%3D, PID: 9468137
    • Henn, V., J.R. Slupsky, M. Gräfe, I. Anagnostopoulos, R. Förster, G. Müller-Berghaus, and R.A. Kroczek. 1998. CD40 ligand on activated platelets triggers an inflammatory reaction of endothelial cells. Nature 391(6667): 591–594.
    • (1998) Nature , vol.391 , Issue.6667 , pp. 591-594
    • Henn, V.1    Slupsky, J.R.2    Gräfe, M.3    Anagnostopoulos, I.4    Förster, R.5    Müller-Berghaus, G.6    Kroczek, R.A.7
  • 140
    • 0031975236 scopus 로고    scopus 로고
    • Platelet-derived interleukin-1 induces cytokine production, but not proliferation of human vascular smooth muscle cells
    • COI: 1:CAS:528:DyaK1cXms1ah, PID: 9414277
    • Loppnow, H., R. Bil, S. Hirt, U. Schönbeck, M. Herzberg, K. Werdan, E.T. Rietschel, E. Brandt, and H.D. Flad. 1998. Platelet-derived interleukin-1 induces cytokine production, but not proliferation of human vascular smooth muscle cells. Blood 91(1): 134–141.
    • (1998) Blood , vol.91 , Issue.1 , pp. 134-141
    • Loppnow, H.1    Bil, R.2    Hirt, S.3    Schönbeck, U.4    Herzberg, M.5    Werdan, K.6    Rietschel, E.T.7    Brandt, E.8    Flad, H.D.9
  • 141
    • 0037318946 scopus 로고    scopus 로고
    • Bench-to-bedside review: Functional relationships between coagulation and the innate immune response and their respective roles in the pathogenesis of sepsis
    • PID: 12617738
    • Opal, S.M., and C.T. Esmon. 2003. Bench-to-bedside review: Functional relationships between coagulation and the innate immune response and their respective roles in the pathogenesis of sepsis. Critical Care 7(1): 23–38.
    • (2003) Critical Care , vol.7 , Issue.1 , pp. 23-38
    • Opal, S.M.1    Esmon, C.T.2
  • 142
    • 0029926254 scopus 로고    scopus 로고
    • Platelet-dependent primary hemostasis promotes selectin- and integrin-mediated neutrophil adhesion to damaged endothelium under flow conditions
    • COI: 1:CAS:528:DyaK28Xit1Krs74%3D, PID: 8605343
    • Kuijper, P.H.M., H.I. Gallardo Torres, J.A.M. Van Der Linden, J.W.J. Lammers, J.J. Sixma, L. Koenderman, and J.J. Zwaginga. 1996. Platelet-dependent primary hemostasis promotes selectin- and integrin-mediated neutrophil adhesion to damaged endothelium under flow conditions. Blood 87(8): 3271–3281.
    • (1996) Blood , vol.87 , Issue.8 , pp. 3271-3281
    • Kuijper, P.H.M.1    Gallardo Torres, H.I.2    Van Der Linden, J.A.M.3    Lammers, J.W.J.4    Sixma, J.J.5    Koenderman, L.6    Zwaginga, J.J.7
  • 144
    • 78650767604 scopus 로고    scopus 로고
    • Inflammation and coagulation. An overview
    • PID: 21193113
    • Petäjä, J. 2011. Inflammation and coagulation. An overview. Thrombosis Research 127(SUPPL. 2): S34–S37.
    • (2011) Thrombosis Research , vol.127 , pp. S34-S37
    • Petäjä, J.1
  • 146
    • 0034234462 scopus 로고    scopus 로고
    • Transfer of tissue factor from leukocytes to platelets is mediated by CD15 and tissue factor
    • COI: 1:CAS:528:DC%2BD3cXksVKjsbY%3D, PID: 10891447
    • Rauch, U., D. Bonderman, B. Bohrmann, J.J. Badimon, J. Himber, M.A. Riederer, and Y. Nemerson. 2000. Transfer of tissue factor from leukocytes to platelets is mediated by CD15 and tissue factor. Blood 96(1): 170–175.
    • (2000) Blood , vol.96 , Issue.1 , pp. 170-175
    • Rauch, U.1    Bonderman, D.2    Bohrmann, B.3    Badimon, J.J.4    Himber, J.5    Riederer, M.A.6    Nemerson, Y.7
  • 147
    • 74949117097 scopus 로고    scopus 로고
    • Inflammation and coagulation
    • COI: 1:CAS:528:DC%2BC3cXptlKnsA%3D%3D, PID: 20083910
    • Levi, M., and T. Van Der Poll. 2010. Inflammation and coagulation. Critical Care Medicine 38(SUPPL. 2): S26–S34.
    • (2010) Critical Care Medicine , vol.38 , pp. S26-S34
    • Levi, M.1    Van Der Poll, T.2
  • 148
    • 33644801469 scopus 로고    scopus 로고
    • The interactions between inflammation and coagulation
    • COI: 1:CAS:528:DC%2BD2MXhtlCisbnN, PID: 16281932
    • Esmon, C.T. 2005. The interactions between inflammation and coagulation. British Journal of Haematology 131(4): 417–430.
    • (2005) British Journal of Haematology , vol.131 , Issue.4 , pp. 417-430
    • Esmon, C.T.1
  • 149
    • 0031711701 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution in blood cells: Control mechanisms and pathophysiological significance
    • COI: 1:CAS:528:DyaK1cXmtFyqsLc%3D, PID: 9792430
    • Bevers, E.M., P. Comfurius, D.W.C. Dekkers, M. Harmsma, and R.F.A. Zwaal. 1998. Transmembrane phospholipid distribution in blood cells: Control mechanisms and pathophysiological significance. Biological Chemistry 379(8–9): 973–986.
    • (1998) Biological Chemistry , vol.379 , Issue.8-9 , pp. 973-986
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.C.3    Harmsma, M.4    Zwaal, R.F.A.5
  • 150
    • 0024325249 scopus 로고
    • Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: An isolated defect in platelet procoagulant activity
    • COI: 1:CAS:528:DyaK3cXhtlKku78%3D, PID: 2793843
    • Sims, P.J., T. Wiedmer, C.T. Esmon, H.J. Weiss, and S.J. Shattil. 1989. Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: An isolated defect in platelet procoagulant activity. Journal of Biological Chemistry 264(29): 17049–17057.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.29 , pp. 17049-17057
    • Sims, P.J.1    Wiedmer, T.2    Esmon, C.T.3    Weiss, H.J.4    Shattil, S.J.5
  • 151
    • 0023755932 scopus 로고
    • Tumor necrosis factor suppresses transcription of the thrombomodulin gene in endothelial cells
    • COI: 1:CAS:528:DyaL1MXjslGmsA%3D%3D, PID: 2854203
    • Conway, E.M., and R.D. Rosenberg. 1988. Tumor necrosis factor suppresses transcription of the thrombomodulin gene in endothelial cells. Molecular and Cellular Biology 8(12): 5588–5592.
    • (1988) Molecular and Cellular Biology , vol.8 , Issue.12 , pp. 5588-5592
    • Conway, E.M.1    Rosenberg, R.D.2
  • 152
    • 0027943163 scopus 로고
    • Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor
    • COI: 1:CAS:528:DyaK2cXmslensLk%3D, PID: 7929370
    • Fukudome, K., and C.T. Esmon. 1994. Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor. Journal of Biological Chemistry 269(42): 26486–26491.
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.42 , pp. 26486-26491
    • Fukudome, K.1    Esmon, C.T.2
  • 153
    • 0025241217 scopus 로고
    • Plasma thrombomodulin in health and diseases
    • COI: 1:STN:280:DyaK3M%2FlsFWjsA%3D%3D, PID: 2173634
    • Takano, S., S. Kimura, S. Ohdama, and N. Aoki. 1990. Plasma thrombomodulin in health and diseases. Blood 76(10): 2024–2029.
    • (1990) Blood , vol.76 , Issue.10 , pp. 2024-2029
    • Takano, S.1    Kimura, S.2    Ohdama, S.3    Aoki, N.4
  • 154
    • 0031756985 scopus 로고    scopus 로고
    • Tissue factor expression by monocytes: Regulation and pathophysiological roles
    • PID: 9819023
    • Østerud, B. 1998. Tissue factor expression by monocytes: Regulation and pathophysiological roles. Blood Coagulation and Fibrinolysis 9(SUPPL. 1): S9–S14.
    • (1998) Blood Coagulation and Fibrinolysis , vol.9 , pp. S9-S14
    • Østerud, B.1
  • 155
    • 0030985937 scopus 로고    scopus 로고
    • Induction of cytokine expression in leukocytes by binding of thrombin-stimulated platelets
    • COI: 1:CAS:528:DyaK2sXjslKhtrw%3D, PID: 9170401
    • Neumann, F.J., N. Marx, M. Gawaz, K. Brand, I. Ott, C. Rokitta, C. Sticherling, C. Meinl, A. May, and A. Schömig. 1997. Induction of cytokine expression in leukocytes by binding of thrombin-stimulated platelets. Circulation 95(10): 2387–2394.
    • (1997) Circulation , vol.95 , Issue.10 , pp. 2387-2394
    • Neumann, F.J.1    Marx, N.2    Gawaz, M.3    Brand, K.4    Ott, I.5    Rokitta, C.6    Sticherling, C.7    Meinl, C.8    May, A.9    Schömig, A.10
  • 156
    • 0035144440 scopus 로고    scopus 로고
    • Antithrombin inhibits lipopolysaccharide-induced tissue factor and interleukin-6 production by mononuclear cells, human umbilical vein endothelial cells, and whole blood
    • COI: 1:CAS:528:DC%2BD3MXjslemu78%3D, PID: 11176173
    • Souter, P.J., S. Thomas, A.R. Hubbard, S. Poole, J. Römisch, and E. Gray. 2001. Antithrombin inhibits lipopolysaccharide-induced tissue factor and interleukin-6 production by mononuclear cells, human umbilical vein endothelial cells, and whole blood. Critical Care Medicine 29(1): 134–139.
    • (2001) Critical Care Medicine , vol.29 , Issue.1 , pp. 134-139
    • Souter, P.J.1    Thomas, S.2    Hubbard, A.R.3    Poole, S.4    Römisch, J.5    Gray, E.6
  • 157
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • COI: 1:CAS:528:DyaK2sXhtFWrsrg%3D, PID: 9028933
    • Zwaal, R.F.A., and A.J. Schroit. 1997. Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89(4): 1121–1132.
    • (1997) Blood , vol.89 , Issue.4 , pp. 1121-1132
    • Zwaal, R.F.A.1    Schroit, A.J.2
  • 158
    • 2942545798 scopus 로고    scopus 로고
    • Bidirectional relation between inflammation and coagulation
    • PID: 15184294
    • Levi, M., T. Van Der Poll, and H.R. Büller. 2004. Bidirectional relation between inflammation and coagulation. Circulation 109(22): 2698–2704.
    • (2004) Circulation , vol.109 , Issue.22 , pp. 2698-2704
    • Levi, M.1    Van Der Poll, T.2    Büller, H.R.3
  • 159
    • 0043240071 scopus 로고    scopus 로고
    • Expression and function of the endothelial protein C receptor in human neutrophils
    • COI: 1:CAS:528:DC%2BD3sXmsFWktLg%3D, PID: 12714492
    • Sturn, D.H., N.C. Kaneider, C. Feistritzer, A. Djanani, K. Fukudome, and C.J. Wiedermann. 2003. Expression and function of the endothelial protein C receptor in human neutrophils. Blood 102(4): 1499–1505.
    • (2003) Blood , vol.102 , Issue.4 , pp. 1499-1505
    • Sturn, D.H.1    Kaneider, N.C.2    Feistritzer, C.3    Djanani, A.4    Fukudome, K.5    Wiedermann, C.J.6
  • 160
    • 0035806897 scopus 로고    scopus 로고
    • Activated protein C prevents endotoxin-induced hypotension in rats by inhibiting excessive production of nitric oxide
    • COI: 1:CAS:528:DC%2BD3MXotlWnt78%3D, PID: 11535575
    • Isobe, H., K. Okajima, M. Uchiba, A. Mizutani, N. Harada, A. Nagasaki, and K. Okabe. 2001. Activated protein C prevents endotoxin-induced hypotension in rats by inhibiting excessive production of nitric oxide. Circulation 104(10): 1171–1175.
    • (2001) Circulation , vol.104 , Issue.10 , pp. 1171-1175
    • Isobe, H.1    Okajima, K.2    Uchiba, M.3    Mizutani, A.4    Harada, N.5    Nagasaki, A.6    Okabe, K.7
  • 161
    • 0037352279 scopus 로고    scopus 로고
    • Activated protein C blocks p53-mediated apoptosis in ischemic human brain endothelium and is neuroprotective
    • COI: 1:CAS:528:DC%2BD3sXhsFGgs7g%3D, PID: 12563316
    • Cheng, T., D. Liu, J.H. Griffin, J.A. Fernández, F. Castellino, E.D. Rosen, K. Fukudome, and B.V. Zlokovic. 2003. Activated protein C blocks p53-mediated apoptosis in ischemic human brain endothelium and is neuroprotective. Nature Medicine 9(3): 338–342.
    • (2003) Nature Medicine , vol.9 , Issue.3 , pp. 338-342
    • Cheng, T.1    Liu, D.2    Griffin, J.H.3    Fernández, J.A.4    Castellino, F.5    Rosen, E.D.6    Fukudome, K.7    Zlokovic, B.V.8
  • 162
    • 0035815747 scopus 로고    scopus 로고
    • Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis
    • COI: 1:CAS:528:DC%2BD3MXjvFGjsL0%3D, PID: 11278252
    • Joyce, D.E., L. Gelbert, A. Ciaccia, B. DeHoff, and B.W. Grinnell. 2001. Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis. Journal of Biological Chemistry 276(14): 11199–11203.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11199-11203
    • Joyce, D.E.1    Gelbert, L.2    Ciaccia, A.3    DeHoff, B.4    Grinnell, B.W.5
  • 163
    • 0036625064 scopus 로고    scopus 로고
    • Antithrombin III inhibits nuclear factor κB activation in human monocytes and vascular endothelial cells
    • PID: 12010802
    • Oelschläger, C., J. Römisch, A. Staubitz, H. Stauss, B. Leithäuser, H. Tillmanns, and H. Hölschermann. 2002. Antithrombin III inhibits nuclear factor κB activation in human monocytes and vascular endothelial cells. Blood 99(11): 4015–4020.
    • (2002) Blood , vol.99 , Issue.11 , pp. 4015-4020
    • Oelschläger, C.1    Römisch, J.2    Staubitz, A.3    Stauss, H.4    Leithäuser, B.5    Tillmanns, H.6    Hölschermann, H.7
  • 165
    • 0035707639 scopus 로고    scopus 로고
    • Regulation of inflammatory responses by natural anticoagulants
    • COI: 1:CAS:528:DC%2BD38XitVSgsL0%3D, PID: 11918684
    • Okajima, K. 2001. Regulation of inflammatory responses by natural anticoagulants. Immunological Reviews 184: 258–274.
    • (2001) Immunological Reviews , vol.184 , pp. 258-274
    • Okajima, K.1
  • 166
    • 0035851276 scopus 로고    scopus 로고
    • Hypercoagulability syndromes
    • COI: 1:STN:280:DC%2BD3MnotFWksw%3D%3D, PID: 11700155
    • Thomas, R.H. 2001. Hypercoagulability syndromes. Archives of Internal Medicine 161(20): 2433–2439.
    • (2001) Archives of Internal Medicine , vol.161 , Issue.20 , pp. 2433-2439
    • Thomas, R.H.1
  • 167
    • 23744503066 scopus 로고    scopus 로고
    • Tissue factor mediates inflammation
    • COI: 1:CAS:528:DC%2BD2MXns1WmsLk%3D, PID: 16036212
    • Chu, A.J. 2005. Tissue factor mediates inflammation. Archives of Biochemistry and Biophysics 440(2): 123–132.
    • (2005) Archives of Biochemistry and Biophysics , vol.440 , Issue.2 , pp. 123-132
    • Chu, A.J.1
  • 168
    • 0016938806 scopus 로고
    • Experimental inflammation induced by naturally occurring microcrystalline calcium salts
    • COI: 1:STN:280:DyaE287ptlKjsw%3D%3D, PID: 1271389
    • Denko, C.W., and M.W. Whitehouse. 1976. Experimental inflammation induced by naturally occurring microcrystalline calcium salts. The Journal of Rheumatology 3(1): 54–62.
    • (1976) The Journal of Rheumatology , vol.3 , Issue.1 , pp. 54-62
    • Denko, C.W.1    Whitehouse, M.W.2
  • 169
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium
    • COI: 1:CAS:528:DyaK3cXlvVykt7Y%3D
    • Bach, R., and D.B. Rifkin. 1990. Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium. Proceedings of the National Academy of Sciences 87(18): 6995–6999.
    • (1990) Proceedings of the National Academy of Sciences , vol.87 , Issue.18 , pp. 6995-6999
    • Bach, R.1    Rifkin, D.B.2
  • 170
    • 0026495238 scopus 로고
    • Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets
    • COI: 1:CAS:528:DyaK3sXkvFel, PID: 1279433
    • Palabrica, T., R. Lobb, B.C. Furie, M. Aronovitz, C. Benjamin, Y.-M. Hsu, S.A. Sajer, and B. Furie. 1992. Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets. Nature 359: 848–851.
    • (1992) Nature , vol.359 , pp. 848-851
    • Palabrica, T.1    Lobb, R.2    Furie, B.C.3    Aronovitz, M.4    Benjamin, C.5    Hsu, Y.-M.6    Sajer, S.A.7    Furie, B.8
  • 172
    • 0026004729 scopus 로고
    • Coexpression of GMP-140 and PAF by endothelium stimulated by histamine or thrombin: A juxtacrine system for adhesion and activation of neutrophils
    • COI: 1:CAS:528:DyaK3MXmtVGru7s%3D, PID: 1717478
    • Lorant, D.E., K.D. Patel, T.M. McIntyre, R.P. McEver, S.M. Prescott, and G.A. Zimmerman. 1991. Coexpression of GMP-140 and PAF by endothelium stimulated by histamine or thrombin: A juxtacrine system for adhesion and activation of neutrophils. The Journal of Cell Biology 115(1): 223–234.
    • (1991) The Journal of Cell Biology , vol.115 , Issue.1 , pp. 223-234
    • Lorant, D.E.1    Patel, K.D.2    McIntyre, T.M.3    McEver, R.P.4    Prescott, S.M.5    Zimmerman, G.A.6
  • 173
    • 84945200320 scopus 로고
    • The role of calcium in coagulation and anticoagulation. In Coagulation and blood transfusion, eds. Sibinga, C.T.S., Das, P.C., Mannucci, P.M., 26: 29–37
    • New York: Springer
    • Mikaelsson, M.E. (1991) The role of calcium in coagulation and anticoagulation. In Coagulation and blood transfusion, eds. Sibinga, C.T.S., Das, P.C., Mannucci, P.M., 26: 29–37. Developments in hematology and immunology. New York: Springer.
    • (1991) Developments in hematology and immunology
    • Mikaelsson, M.E.1
  • 174
    • 77449092811 scopus 로고    scopus 로고
    • The role of platelet and fibrin ultrastructure in identifying disease patterns
    • COI: 1:CAS:528:DC%2BD1MXhsFaqtrvM
    • Pretorius, E. 2007. The role of platelet and fibrin ultrastructure in identifying disease patterns. Pathophysiology of Haemostasis and Thrombosis 36(5): 251–258.
    • (2007) Pathophysiology of Haemostasis and Thrombosis , vol.36 , Issue.5 , pp. 251-258
    • Pretorius, E.1
  • 175
    • 84904470952 scopus 로고    scopus 로고
    • Estrogen causes ultrastructural changes of fibrin networks during the menstrual cycle: A qualitative investigation
    • Swanepoel, A.C., Lindeque, B.G., Swart, P.J., Abdool, Z., Pretorius, E. (2014) Estrogen causes ultrastructural changes of fibrin networks during the menstrual cycle: A qualitative investigation. Microscopy Research and Technique 77: 594–601.
    • (2014) Microscopy Research and Technique , vol.77 , pp. 594-601
    • Swanepoel, A.C.1    Lindeque, B.G.2    Swart, P.J.3    Abdool, Z.4    Pretorius, E.5
  • 176
    • 84921752328 scopus 로고    scopus 로고
    • Ultrastructural analysis of platelets during three phases of pregnancy: A qualitative and quantitative investigation
    • Swanepoel, A.C., Pretorius E. (2015) Ultrastructural analysis of platelets during three phases of pregnancy: A qualitative and quantitative investigation. Hematology 20: 39–47.
    • (2015) Hematology , vol.20 , pp. 39-47
    • Swanepoel, A.C.1    Pretorius, E.2
  • 177
    • 0016170040 scopus 로고
    • Calcium-induced dissociation of human plasma factor XIII and the appearance of catalytic activity
    • COI: 1:CAS:528:DyaE2MXotlOgsA%3D%3D, PID: 4463958
    • Cooke, R.D. 1974. Calcium-induced dissociation of human plasma factor XIII and the appearance of catalytic activity. The Biochemical Journal 141: 683–691.
    • (1974) The Biochemical Journal , vol.141 , pp. 683-691
    • Cooke, R.D.1
  • 178
    • 79953227683 scopus 로고    scopus 로고
    • Reversible activation of cellular factor XIII by calcium
    • COI: 1:CAS:528:DC%2BC3MXjtFOitbc%3D, PID: 21245142
    • Kristiansen, G.K., and M.D. Andersen. 2011. Reversible activation of cellular factor XIII by calcium. Journal of Biological Chemistry 286(11): 9833–9839.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.11 , pp. 9833-9839
    • Kristiansen, G.K.1    Andersen, M.D.2
  • 179
    • 3042662496 scopus 로고    scopus 로고
    • The impact of factor XIII on coagulation kinetics and clot strength determined by thrombelastography
    • COI: 1:CAS:528:DC%2BD2cXkvVGjsL8%3D, PID: 15281516
    • Nielsen, V.G., W.Q. Gurley Jr., and T.M. Burch. 2004. The impact of factor XIII on coagulation kinetics and clot strength determined by thrombelastography. Anesthesia and Analgesia 99(1): 120–123.
    • (2004) Anesthesia and Analgesia , vol.99 , Issue.1 , pp. 120-123
    • Nielsen, V.G.1    Gurley, W.Q.2    Burch, T.M.3
  • 180
    • 33846930612 scopus 로고    scopus 로고
    • Thrombelastographic method to quantify the contribution of factor XIII to coagulation kinetics
    • COI: 1:CAS:528:DC%2BD2sXhsVSisb0%3D
    • Nielsen, V.G., J.K. Kirklin, H. Hoogendoorn, T.C. Ellis, and W.L. Holman. 2007. Thrombelastographic method to quantify the contribution of factor XIII to coagulation kinetics. Blood Coagulation & Fibrinolysis 18(2): 145–150.
    • (2007) Blood Coagulation & Fibrinolysis , vol.18 , Issue.2 , pp. 145-150
    • Nielsen, V.G.1    Kirklin, J.K.2    Hoogendoorn, H.3    Ellis, T.C.4    Holman, W.L.5
  • 181
    • 80052097667 scopus 로고    scopus 로고
    • Qualitative scanning electron microscopy analysis of fibrin networks and platelet abnormalities in diabetes
    • COI: 1:CAS:528:DC%2BC3MXhtVaisb3F, PID: 21467917
    • Pretorius, E., H.M. Oberholzer, W.J. Van Der Spuy, A.C. Swanepoel, and P. Soma. 2011. Qualitative scanning electron microscopy analysis of fibrin networks and platelet abnormalities in diabetes. Blood Coagulation and Fibrinolysis 22(6): 463–467.
    • (2011) Blood Coagulation and Fibrinolysis , vol.22 , Issue.6 , pp. 463-467
    • Pretorius, E.1    Oberholzer, H.M.2    Van Der Spuy, W.J.3    Swanepoel, A.C.4    Soma, P.5
  • 184
    • 77952513645 scopus 로고    scopus 로고
    • Inflammatory mechanisms in ischemic stroke: role of inflammatory cells
    • COI: 1:CAS:528:DC%2BC3cXmvVCht74%3D, PID: 20130219
    • Jin, R., G. Yang, and G. Li. 2010. Inflammatory mechanisms in ischemic stroke: role of inflammatory cells. Journal of Leukocyte Biology 87(5): 779–789.
    • (2010) Journal of Leukocyte Biology , vol.87 , Issue.5 , pp. 779-789
    • Jin, R.1    Yang, G.2    Li, G.3
  • 185
    • 84863988965 scopus 로고    scopus 로고
    • Scanning electron microscopy of fibrin networks in rheumatoid arthritis: A qualitative analysis
    • COI: 1:CAS:528:DC%2BC38XnvF2ntrc%3D, PID: 21331577
    • Pretorius, E., H.M. Oberholzer, W.J. Van Der Spuy, A.C. Swanepoel, and P. Soma. 2012. Scanning electron microscopy of fibrin networks in rheumatoid arthritis: A qualitative analysis. Rheumatology International 32(6): 1611–1615.
    • (2012) Rheumatology International , vol.32 , Issue.6 , pp. 1611-1615
    • Pretorius, E.1    Oberholzer, H.M.2    Van Der Spuy, W.J.3    Swanepoel, A.C.4    Soma, P.5
  • 187
    • 0035932519 scopus 로고    scopus 로고
    • Cytokine pathways and joint inflammation in rheumatoid arthritis
    • Epstein, F.H., E.H. Choy, and G.S. Panayi. 2001. Cytokine pathways and joint inflammation in rheumatoid arthritis. New England Journal of Medicine 344(12): 907–916.
    • (2001) New England Journal of Medicine , vol.344 , Issue.12 , pp. 907-916
    • Epstein, F.H.1    Choy, E.H.2    Panayi, G.S.3
  • 188
    • 84897404263 scopus 로고    scopus 로고
    • Profound morphological changes in the erythrocytes and fibrin networks of patients with hemochromatosis or with hyperferritinemia, and their normalization by iron chelators and other agents
    • PID: 24416376
    • Pretorius, E., J. Bester, N. Vermeulen, B. Lipinski, G.S. Gericke, and D.B. Kell. 2014. Profound morphological changes in the erythrocytes and fibrin networks of patients with hemochromatosis or with hyperferritinemia, and their normalization by iron chelators and other agents. PLoS ONE 9(1): e85271.
    • (2014) PLoS ONE , vol.9 , Issue.1
    • Pretorius, E.1    Bester, J.2    Vermeulen, N.3    Lipinski, B.4    Gericke, G.S.5    Kell, D.B.6
  • 189
    • 53149123286 scopus 로고    scopus 로고
    • Attenuated inflammatory responses in hemochromatosis reveal a role for iron in the regulation of macrophage cytokine translation
    • COI: 1:CAS:528:DC%2BD1cXptlOjs7o%3D, PID: 18684963
    • Wang, L., E.E. Johnson, H.N. Shi, W.A. Walker, M. Wessling-Resnick, and B.J. Cherayil. 2008. Attenuated inflammatory responses in hemochromatosis reveal a role for iron in the regulation of macrophage cytokine translation. The Journal of Immunology 181(4): 2723–2731.
    • (2008) The Journal of Immunology , vol.181 , Issue.4 , pp. 2723-2731
    • Wang, L.1    Johnson, E.E.2    Shi, H.N.3    Walker, W.A.4    Wessling-Resnick, M.5    Cherayil, B.J.6
  • 190
    • 84864560482 scopus 로고    scopus 로고
    • Ultrastructural changes in platelet membranes due to cigarette smoking
    • PID: 22849525
    • Pretorius, E. 2012. Ultrastructural changes in platelet membranes due to cigarette smoking. Ultrastructural Pathology 36(4): 239–243.
    • (2012) Ultrastructural Pathology , vol.36 , Issue.4 , pp. 239-243
    • Pretorius, E.1
  • 192
    • 0036706191 scopus 로고    scopus 로고
    • The association between inflammation markers, coronary artery disease and smoking
    • PID: 12616981
    • De Maat, M.P.M., and C. Kluft. 2002. The association between inflammation markers, coronary artery disease and smoking. Vascular Pharmacology 39(3): 137–139.
    • (2002) Vascular Pharmacology , vol.39 , Issue.3 , pp. 137-139
    • De Maat, M.P.M.1    Kluft, C.2
  • 193
    • 84857606308 scopus 로고    scopus 로고
    • Non-invasive biomarkers of lung inflammation in smoking subjects
    • COI: 1:CAS:528:DC%2BC38Xhs1ygtbw%3D, PID: 22320297
    • Malerba, M., and P. Montuschi. 2012. Non-invasive biomarkers of lung inflammation in smoking subjects. Current Medicinal Chemistry 19(2): 187–196.
    • (2012) Current Medicinal Chemistry , vol.19 , Issue.2 , pp. 187-196
    • Malerba, M.1    Montuschi, P.2
  • 194
    • 4043062803 scopus 로고    scopus 로고
    • Acute effects of cigarette smoke on inflammation and oxidative stress: A review
    • PID: 15282395
    • Van Der Vaart, H., D.S. Postma, W. Timens, and N.H.T. Ten Hacken. 2004. Acute effects of cigarette smoke on inflammation and oxidative stress: A review. Thorax 59(8): 713–721.
    • (2004) Thorax , vol.59 , Issue.8 , pp. 713-721
    • Van Der Vaart, H.1    Postma, D.S.2    Timens, W.3    Ten Hacken, N.H.T.4
  • 195
    • 84903301627 scopus 로고    scopus 로고
    • An ultrastructural analysis of platelets, erythrocytes, white blood cells, and fibrin network in systemic lupus erythematosus
    • Pretorius, E., du Plooy, J., Soma, P., Gasparyan, AY. (2014) An ultrastructural analysis of platelets, erythrocytes, white blood cells, and fibrin network in systemic lupus erythematosus. Rheumatology International 34: 1005–1009.
    • (2014) Rheumatology International , vol.34 , pp. 1005-1009
    • Pretorius, E.1    du Plooy, J.2    Soma, P.3    Gasparyan, A.Y.4
  • 196
    • 0030032603 scopus 로고    scopus 로고
    • Pathology and pathogenesis of vascular injury in systemic lupus erythematosus Interactions of inflammatory cells and activated endothelium
    • COI: 1:STN:280:DyaK287jtlamtQ%3D%3D, PID: 8546744
    • Belmont, H.M., S.B. Abramson, and J.T. Lie. 1996. Pathology and pathogenesis of vascular injury in systemic lupus erythematosus Interactions of inflammatory cells and activated endothelium. Arthritis and Rheumatism 39(1): 9–22.
    • (1996) Arthritis and Rheumatism , vol.39 , Issue.1 , pp. 9-22
    • Belmont, H.M.1    Abramson, S.B.2    Lie, J.T.3
  • 197
    • 62349094301 scopus 로고    scopus 로고
    • Ultrastructural changes of platelets and fibrin networks in human asthma: A qualitative case study
    • PID: 19786943
    • Pretorius, E., and H.M. Oberholzer. 2009. Ultrastructural changes of platelets and fibrin networks in human asthma: A qualitative case study. Blood Coagulation and Fibrinolysis 20(2): 146–149.
    • (2009) Blood Coagulation and Fibrinolysis , vol.20 , Issue.2 , pp. 146-149
    • Pretorius, E.1    Oberholzer, H.M.2
  • 198
    • 0025900437 scopus 로고
    • Asthma and inflammation
    • COI: 1:STN:280:DyaK3M3isFemtg%3D%3D, PID: 2026843
    • Kay, A.B.. 1991. Asthma and inflammation. Journal of Allergy and Clinical Immunology 87(5): 893–910.
    • (1991) Journal of Allergy and Clinical Immunology , vol.87 , Issue.5 , pp. 893-910
    • Kay, A.B.1


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