메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Thrombomodulin: A bifunctional modulator of inflammation and coagulation in sepsis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84866253982     PISSN: 20901305     EISSN: 20901313     Source Type: Journal    
DOI: 10.1155/2012/614545     Document Type: Review
Times cited : (78)

References (95)
  • 1
    • 33750047495 scopus 로고    scopus 로고
    • Management of sepsis
    • DOI 10.1056/NEJMra043632
    • Russell J. A., Management of sepsis. The New England Journal of Medicine 2006 355 16 1699 1713 2-s2.0-33750047495 10.1056/NEJMra043632 (Pubitemid 44583960)
    • (2006) New England Journal of Medicine , vol.355 , Issue.16 , pp. 1699-1713
    • Russell, J.A.1
  • 2
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • DOI 10.1056/NEJMoa022139
    • Martin G. S., Mannino D. M., Eaton S., Moss M., The epidemiology of sepsis in the United States from 1979 through 2000. The New England Journal of Medicine 2003 348 16 1546 1554 2-s2.0-0037451929 10.1056/NEJMoa022139 (Pubitemid 36437931)
    • (2003) New England Journal of Medicine , vol.348 , Issue.16 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 3
    • 14544299688 scopus 로고    scopus 로고
    • Therapeutic intervention and targets for sepsis
    • DOI 10.1146/annurev.med.56.082103.104356
    • Rice T. W., Bernard G. R., Therapeutic intervention and targets for sepsis. Annual Review of Medicine 2005 56 225 248 2-s2.0-14544299688 10.1146/annurev.med.56.082103.104356 (Pubitemid 40299782)
    • (2005) Annual Review of Medicine , vol.56 , pp. 225-248
    • Rice, T.W.1    Bernard, G.R.2
  • 4
    • 77956258291 scopus 로고    scopus 로고
    • The endothelium: Physiological functions and role in microcirculatory failure during severe sepsis
    • 2-s2.0-77956258291 10.1007/s00134-010-1893-6
    • Ait-Oufella H., Maury E., Lehoux S., Guidet B., Offenstadt G., The endothelium: physiological functions and role in microcirculatory failure during severe sepsis. Intensive Care Medicine 2010 36 8 1286 1298 2-s2.0-77956258291 10.1007/s00134-010-1893-6
    • (2010) Intensive Care Medicine , vol.36 , Issue.8 , pp. 1286-1298
    • Ait-Oufella, H.1    Maury, E.2    Lehoux, S.3    Guidet, B.4    Offenstadt, G.5
  • 5
    • 27144451165 scopus 로고    scopus 로고
    • Disseminated intravascular coagulation in sepsis
    • DOI 10.1378/chest.128.4.2864
    • Zeerleder S., Hack C. E., Wuillemin W. A., Disseminated intravascular coagulation in sepsis. Chest 2005 128 4 2864 2875 2-s2.0-27144451165 10.1378/chest.128.4.2864 (Pubitemid 41507648)
    • (2005) Chest , vol.128 , Issue.4 , pp. 2864-2875
    • Zeerleder, S.1    Hack, C.E.2    Wuillemin, W.A.3
  • 7
    • 79961081848 scopus 로고    scopus 로고
    • Thrombomodulin alfa in the treatment of infectious patients complicated by disseminated intravascular coagulation: Sub-analysis from the phase III trial
    • 2-s2.0-78149305222 10.1097/SHK.0b013e318204c019
    • Aikawa N., Shimazaki S., Yamamoto Y., Saito H., Maruyama I., Ohno R., Hirayama A., Aoki Y., Aoki N., Thrombomodulin alfa in the treatment of infectious patients complicated by disseminated intravascular coagulation: sub-analysis from the phase III trial. Shock 2011 35 4 349 354 2-s2.0-78149305222 10.1097/SHK.0b013e318204c019
    • (2011) Shock , vol.35 , Issue.4 , pp. 349-354
    • Aikawa, N.1    Shimazaki, S.2    Yamamoto, Y.3    Saito, H.4    Maruyama, I.5    Ohno, R.6    Hirayama, A.7    Aoki, Y.8    Aoki, N.9
  • 8
    • 79955786719 scopus 로고    scopus 로고
    • Treatment effects of recombinant human soluble thrombomodulin in patients with severe sepsis: A historical control study
    • Yamakawa K., Fujimi S., Mohri T., Treatment effects of recombinant human soluble thrombomodulin in patients with severe sepsis: a historical control study. Critical Care 2011 15 3 R123
    • (2011) Critical Care , vol.15 , Issue.3
    • Yamakawa, K.1    Fujimi, S.2    Mohri, T.3
  • 9
    • 33845513582 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: Results of a phase III, randomized, double-blind clinical trial
    • DOI 10.1111/j.1538-7836.2006.02267.x
    • Saito H., Maruyama I., Shimazaki S., Yamamoto Y., Aikawa N., Ohno R., Hirayama A., Matsuda T., Asakura H., Nakashima M., Aoki N., Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: results of a phase III, randomized, double-blind clinical trial. Journal of Thrombosis and Haemostasis 2007 5 1 31 41 2-s2.0-33845513582 10.1111/j.1538-7836.2006.02267.x (Pubitemid 44921064)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.1 , pp. 31-41
    • Saito, H.1    Maruyama, I.2    Shimazaki, S.3    Yamamoto, Y.4    Aikawa, N.5    Ohno, R.6    Hirayama, A.7    Matsuda, T.8    Asakura, H.9    Nakashima, M.10    Aoki, N.11
  • 11
    • 23844438376 scopus 로고    scopus 로고
    • Dose-response study of recombinant human soluble thrombomodulin (ART-123) in the prevention of venous thromboembolism after total hip replacement
    • DOI 10.1111/j.1538-7836.2005.01251.x
    • Kearon C., Comp P., Douketis J., Royds R., Yamada K., Gent M., Dose-response study of recombinant human soluble thrombomodulin (ART-123) in the prevention of venous thromboembolism after total hip replacement. Journal of Thrombosis and Haemostasis 2005 3 5 962 968 2-s2.0-23844438376 10.1111/j.1538-7836.2005.01251.x (Pubitemid 41632827)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.5 , pp. 962-968
    • Kearon, C.1    Comp, P.2    Douketis, J.3    Royds, R.4    Yamada, K.5    Gent, M.6
  • 12
    • 74949117097 scopus 로고    scopus 로고
    • Inflammation and coagulation
    • 2-s2.0-74949117097 10.1097/CCM.0b013e3181c98d21
    • Levi M., van der Poll T., Inflammation and coagulation. Critical Care Medicine 2010 38 2 S26 S34 2-s2.0-74949117097 10.1097/CCM.0b013e3181c98d21
    • (2010) Critical Care Medicine , vol.38 , Issue.2
    • Levi, M.1    Van Der Poll, T.2
  • 13
    • 33644801469 scopus 로고    scopus 로고
    • The interactions between inflammation and coagulation
    • DOI 10.1111/j.1365-2141.2005.05753.x
    • Esmon C. T., The interactions between inflammation and coagulation. British Journal of Haematology 2005 131 4 417 430 2-s2.0-33644801469 10.1111/j.1365-2141.2005.05753.x (Pubitemid 43899639)
    • (2005) British Journal of Haematology , vol.131 , Issue.4 , pp. 417-430
    • Esmon, C.T.1
  • 14
    • 67849130574 scopus 로고    scopus 로고
    • The many faces of tissue factor
    • nmackman@med.unc.edu supplement 1 10.1111/j.1538-7836.2009.03368.x
    • Mackman N., nmackman@med.unc.edu The many faces of tissue factor. Journal of Thrombosis and Haemostasis 2009 7 supplement 1 136 139 10.1111/j.1538-7836. 2009.03368.x
    • (2009) Journal of Thrombosis and Haemostasis , vol.7 , pp. 136-139
    • MacKman, N.1
  • 16
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • DOI 10.1111/j.1538-7836.2005.01377.x
    • Coughlin S. R., Protease-activated receptors in hemostasis, thrombosis and vascular biology. Journal of Thrombosis and Haemostasis 2005 3 8 1800 1814 2-s2.0-28344436780 10.1111/j.1538-7836.2005.01377.x (Pubitemid 41716567)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.8 , pp. 1800-1814
    • Coughlin, S.R.1
  • 17
    • 0022470963 scopus 로고
    • Thrombin-induced chemotaxis and aggregation of neutrophils
    • Bizios R., Lai L., Fenton J. W., Malik A. B., Thrombin-induced chemotaxis and aggregation of neutrophils. Journal of Cellular Physiology 1986 128 3 485 490 2-s2.0-0022470963 (Pubitemid 16015533)
    • (1986) Journal of Cellular Physiology , vol.128 , Issue.3 , pp. 485-490
    • Bizios, R.1    Lai, L.2    Fenton II, J.W.3    Malik, A.B.4
  • 18
    • 0026938894 scopus 로고
    • Leukocyte-endothelial cell interactions
    • 2-s2.0-0026938894
    • McEver R. P., Leukocyte-endothelial cell interactions. Current Opinion in Cell Biology 1992 4 5 840 849 2-s2.0-0026938894
    • (1992) Current Opinion in Cell Biology , vol.4 , Issue.5 , pp. 840-849
    • McEver, R.P.1
  • 19
    • 0032525041 scopus 로고    scopus 로고
    • Potential mechanisms for a proinflammatory vascular cytokine response to coagulation activation
    • Johnson K., Choi Y., DeGroot E., Samuels I., Creasey A., Aarden L., Potential mechanisms for a proinflammatory vascular cytokine response to coagulation activation. Journal of Immunology 1998 160 10 5130 5135 2-s2.0-0032525041 (Pubitemid 28215352)
    • (1998) Journal of Immunology , vol.160 , Issue.10 , pp. 5130-5135
    • Johnson, K.1    Choi, Y.2    DeGroot, E.3    Samuels, I.4    Creasey, A.5    Aarden, L.6
  • 20
    • 0027511564 scopus 로고
    • Thrombin enhances T cell proliferative responses and cytokine production
    • DOI 10.1006/cimm.1993.1076
    • Naldini A., Carney D. H., Bocci V., Klimpel K. D., Asuncion M., Soares L. E., Klimpel G. R., Thrombin enhances T cell proliferative responses and cytokine production. Cellular Immunology 1993 147 2 367 377 2-s2.0-0027511564 10.1006/cimm.1993.1076 (Pubitemid 23113934)
    • (1993) Cellular Immunology , vol.147 , Issue.2 , pp. 367-377
    • Naldini, A.1    Carney, D.H.2    Bocci, V.3    Klimpel, K.D.4    Asuncion, M.5    Soares, L.E.6    Klimpel, G.R.7
  • 22
    • 84857860942 scopus 로고    scopus 로고
    • Thrombomodulin and its role in inflammation
    • 10.1007/s00281-011-0282-8
    • Conway E. M., Thrombomodulin and its role in inflammation. Seminars in Immunopathology 2012 34 1 107 125 10.1007/s00281-011-0282-8
    • (2012) Seminars in Immunopathology , vol.34 , Issue.1 , pp. 107-125
    • Conway, E.M.1
  • 23
    • 33746859068 scopus 로고    scopus 로고
    • Thrombin-cofactor interactions: Structural insights into regulatory mechanisms
    • DOI 10.1161/01.ATV.0000228844.65168.d1, PII 0004360520060800000010
    • Adams T. E., Huntington J. A., Thrombin-cofactor interactions: structural insights into regulatory mechanisms. Arteriosclerosis, Thrombosis, and Vascular Biology 2006 26 8 1738 1745 2-s2.0-33746859068 10.1161/01.ATV.0000228844.65168. d1 (Pubitemid 44305326)
    • (2006) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.26 , Issue.8 , pp. 1738-1745
    • Adams, T.E.1    Huntington, J.A.2
  • 25
    • 0036339949 scopus 로고    scopus 로고
    • Activated protein C inhibits lipopolysaccharide-induced tumor necrosis factor-α production by inhibiting activation of both nuclear factor-κB and activator protein-1 in human monocytes
    • Yuksel M., Okajima K., Uchiba M., Horiuchi S., Okabe H., Activated protein C inhibits lipopolysaccharide-induced tumor necrosis factor- α production by inhibiting activation of both nuclear factor- κ B and activator protein-1 in human monocytes. Thrombosis and Haemostasis 2002 88 2 267 273 2-s2.0-0036339949 (Pubitemid 34873708)
    • (2002) Thrombosis and Haemostasis , vol.88 , Issue.2 , pp. 267-273
    • Yuksel, M.1    Okajima, K.2    Uchiba, M.3    Horiuchi, S.4    Okabe, H.5
  • 26
    • 0030034186 scopus 로고    scopus 로고
    • Activated protein C attenuates endotoxin-induced pulmonary vascular injury by inhibiting activated leukocytes in rats
    • Murakami K., Okajima K., Uchiba M., Johno M., Nakagaki T., Okabe H., Takatsuki K., Activated protein C attenuates endotoxin-induced pulmonary vascular injury by inhibiting activated leukocytes in rats. Blood 1996 87 2 642 647 2-s2.0-0030034186 (Pubitemid 26030319)
    • (1996) Blood , vol.87 , Issue.2 , pp. 642-647
    • Murakami, K.1    Okajima, K.2    Uchiba, M.3    Johno, M.4    Nakagaki, T.5    Okabe, H.6    Takatsuki, K.7
  • 27
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • DOI 10.1074/jbc.271.28.16603
    • Bajzar L., Morser J., Nesheim M., TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. Journal of Biological Chemistry 1996 271 28 16603 16608 2-s2.0-0029895009 10.1074/jbc.271.28.16603 (Pubitemid 26239017)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.28 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 28
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell W. D., Lazoura E., Okada N., Okada H., Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiology and Immunology 2002 46 2 131 134 2-s2.0-0036191244 (Pubitemid 34194973)
    • (2002) Microbiology and Immunology , vol.46 , Issue.2 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 30
    • 0023374585 scopus 로고
    • Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation
    • 2-s2.0-0023374585
    • Suzuki K., Kusumoto H., Deyashiki Y., Nishioka J., Maruyama I., Zushi M., Kawahara S., Honda G., Yamamoto S., Horiguchi S., Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation. EMBO Journal 1987 6 7 1891 1897 2-s2.0-0023374585
    • (1987) EMBO Journal , vol.6 , Issue.7 , pp. 1891-1897
    • Suzuki, K.1    Kusumoto, H.2    Deyashiki, Y.3    Nishioka, J.4    Maruyama, I.5    Zushi, M.6    Kawahara, S.7    Honda, G.8    Yamamoto, S.9    Horiguchi, S.10
  • 31
    • 0030843884 scopus 로고    scopus 로고
    • Thrombomodulin structure and function
    • Sadler J. E., Thrombomodulin structure and function. Thrombosis and Haemostasis 1997 78 1 392 395 2-s2.0-0030843884 (Pubitemid 27289273)
    • (1997) Thrombosis and Haemostasis , vol.78 , Issue.1 , pp. 392-395
    • Sadler, J.E.1
  • 32
    • 0031023957 scopus 로고    scopus 로고
    • The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis
    • Conway E. M., Pollefeyt S., Collen D., Steiner-Mosonyi M., The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis. Blood 1997 89 2 652 661 2-s2.0-0031023957 (Pubitemid 27051702)
    • (1997) Blood , vol.89 , Issue.2 , pp. 652-661
    • Conway, E.M.1    Pollefeyt, S.2    Collen, D.3    Steiner-Mosonyi, M.4
  • 33
    • 0036719075 scopus 로고    scopus 로고
    • The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor κB and mitogen-activated protein kinase pathways
    • DOI 10.1084/jem.20020077
    • Conway E. M., Van de Wouwer M., Pollefeyt S., Jurk K., Van Aken H., De Vriese A., Weitz J. I., Weiler H., Hellings P. W., Schaeffer P., Herbert J. M., Collen D., Theilmeier G., The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor κ B and mitogen-activated protein kinase pathways. Journal of Experimental Medicine 2002 196 5 565 577 2-s2.0-0036719075 10.1084/jem.20020077 (Pubitemid 35024436)
    • (2002) Journal of Experimental Medicine , vol.196 , Issue.5 , pp. 565-577
    • Conway, E.M.1    Van De Wouwer, M.2    Pollefeyt, S.3    Jurk, K.4    Van Aken, H.5    De Vriese, A.6    Weitz, J.I.7    Weiler, H.8    Hellings, P.W.9    Schaeffer, P.10    Herbert, J.-M.11    Collen, D.12    Theilmeier, G.13
  • 34
    • 0029050715 scopus 로고
    • The epidermal growth factor-like domain of recombinant human thrombomodulin exhibits mitogenic activity for Swiss 3T3 cells
    • 2-s2.0-0029050715
    • Hamada H., Ishii H., Sakyo K., Horie S., Nishiki K., Kazama M., The epidermal growth factor-like domain of recombinant human thrombomodulin exhibits mitogenic activity for Swiss 3T3 cells. Blood 1995 86 1 225 233 2-s2.0-0029050715
    • (1995) Blood , vol.86 , Issue.1 , pp. 225-233
    • Hamada, H.1    Ishii, H.2    Sakyo, K.3    Horie, S.4    Nishiki, K.5    Kazama, M.6
  • 35
    • 0031674015 scopus 로고    scopus 로고
    • Expression of thrombomodulin in atherosclerotic lesions and mitogenic activity of recombinant thrombomodulin in vascular smooth muscle cells
    • Tohda G., Oida K., Okada Y., Kosaka S., Okada E., Takahashi S., Ishii H., Miyamori I., Expression of thrombomodulin in atherosclerotic lesions and mitogenic activity of recombinant thrombomodulin in vascular smooth muscle cells. Arteriosclerosis, Thrombosis, and Vascular Biology 1998 18 12 1861 1869 2-s2.0-0031674015 (Pubitemid 28565747)
    • (1998) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.18 , Issue.12 , pp. 1861-1869
    • Tohda, G.1    Oida, K.2    Okada, Y.3    Kosaka, S.4    Okada, E.5    Takahashi, S.6    Ishii, H.7    Miyamori, I.8
  • 36
    • 0020404408 scopus 로고
    • Complex formation between thrombin and thrombomodulin inhibits both thrombin-catalyzed fibrin formation and factor V activation
    • Esmon C. T., Esmon N. L., Harris K. W., Complex formation between thrombin and thrombomodulin inhibits both thrombin-catalyzed fibrin formation and factor V activation. Journal of Biological Chemistry 1982 257 14 7944 7947 2-s2.0-0020404408 (Pubitemid 13241217)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.14 , pp. 7944-7947
    • Esmon, C.T.1    Esmon, N.L.2    Harris, K.W.3
  • 37
    • 0021053984 scopus 로고
    • Thrombomodulin blocks the ability of thrombin to activate platelets
    • Esmon N. L., Carroll R. C., Esmon C. T., Thrombomodulin blocks the ability of thrombin to activate platelets. Journal of Biological Chemistry 1983 258 20 12238 12242 2-s2.0-0021053984 (Pubitemid 14230011)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.20 , pp. 12238-12242
    • Esmon, N.L.1    Carroll, R.C.2    Esmon, C.T.3
  • 38
    • 0022529127 scopus 로고
    • Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors
    • Hofsteenge J., Taguchi H., Stone S. R., Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors. Biochemical Journal 1986 237 1 243 251 2-s2.0-0022529127 (Pubitemid 16063113)
    • (1986) Biochemical Journal , vol.237 , Issue.1 , pp. 243-251
    • Hofsteenge, J.1    Taguchi, H.2    Stone, S.R.3
  • 39
    • 0026775230 scopus 로고
    • Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity
    • 2-s2.0-0026775230
    • Tsiang M., Lentz S. R., Sadler J. E., Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. Journal of Biological Chemistry 1992 267 9 6164 6170 2-s2.0-0026775230
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.9 , pp. 6164-6170
    • Tsiang, M.1    Lentz, S.R.2    Sadler, J.E.3
  • 40
    • 0034725622 scopus 로고    scopus 로고
    • Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation
    • DOI 10.1074/jbc.M001760200
    • Wang W., Nagashima M., Schneider M., Morser J., Nesheim M., Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation. Journal of Biological Chemistry 2000 275 30 22942 22947 2-s2.0-0034725622 10.1074/jbc.M001760200 (Pubitemid 30646181)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 22942-22947
    • Wang, W.1    Nagashima, M.2    Schneider, M.3    Morser, J.4    Nesheim, M.5
  • 41
    • 65449180750 scopus 로고    scopus 로고
    • The roles of selected arginine and lysine residues of TAFI (Pro-CPU) in its activation to TAFIa by the thrombin-thrombomodulin complex
    • 2-s2.0-65449180750 10.1074/jbc.M804745200
    • Wu C., Kim P. Y., Manuel R., Seto M., Whitlow M., Nagashima M., Morser J., Gils A., Declerck P., Nesheim M. E., The roles of selected arginine and lysine residues of TAFI (Pro-CPU) in its activation to TAFIa by the thrombin-thrombomodulin complex. Journal of Biological Chemistry 2009 284 11 7059 7067 2-s2.0-65449180750 10.1074/jbc.M804745200
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.11 , pp. 7059-7067
    • Wu, C.1    Kim, P.Y.2    Manuel, R.3    Seto, M.4    Whitlow, M.5    Nagashima, M.6    Morser, J.7    Gils, A.8    Declerck, P.9    Nesheim, M.E.10
  • 42
    • 0025763975 scopus 로고
    • Different glycoforms of human thrombomodulin. Their glycosaminoglycan- dependent modulatory effects on thrombin inactivation by heparin cofactor II and antithrombin III
    • 2-s2.0-0025763975
    • Koyama T., Parkinson J. F., Sie P., Bang N. U., Muller-Berghaus G., Preissner K. T., Different glycoforms of human thrombomodulin. Their glycosaminoglycan-dependent modulatory effects on thrombin inactivation by heparin cofactor II and antithrombin III. European Journal of Biochemistry 1991 198 3 563 570 2-s2.0-0025763975
    • (1991) European Journal of Biochemistry , vol.198 , Issue.3 , pp. 563-570
    • Koyama, T.1    Parkinson, J.F.2    Sie, P.3    Bang, N.U.4    Muller-Berghaus, G.5    Preissner, K.T.6
  • 43
    • 0032030653 scopus 로고    scopus 로고
    • Protein C inhibitor acts as a procoagulant by inhibiting the thrombomodulin-induced activation of protein C in human plasma
    • Elisen M. G., Von Dem Borne P. A., Bouma B. N., Meijers J. C., Protein C inhibitor acts as a procoagulant by inhibiting the thrombomodulin-induced activation of protein C in human plasma. Blood 1998 91 5 1542 1547 2-s2.0-0032030653 (Pubitemid 28110317)
    • (1998) Blood , vol.91 , Issue.5 , pp. 1542-1547
    • Elisen, M.G.L.M.1    Von Dem Borne, P.A.2    Bouma, B.N.3    Meijers, J.C.M.4
  • 44
    • 78650934956 scopus 로고    scopus 로고
    • Platelet factor 4 inhibits thrombomodulin-dependent activation of thrombin-activatable fibrinolysis inhibitor (TAFI) by thrombin
    • 2-s2.0-78650934956 10.1074/jbc.M110.147959
    • Mosnier L. O., Platelet factor 4 inhibits thrombomodulin-dependent activation of thrombin-activatable fibrinolysis inhibitor (TAFI) by thrombin. Journal of Biological Chemistry 2011 286 1 502 510 2-s2.0-78650934956 10.1074/jbc.M110.147959
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.1 , pp. 502-510
    • Mosnier, L.O.1
  • 45
    • 0032578548 scopus 로고    scopus 로고
    • Effect of high- and low-molecular-weight heparins on thrombin- thrombomodulin interaction and protein C activation
    • De Cristofaro R., De Candia E., Landolfi R., Effect of high- and low-molecular-weight heparins on thrombin- thrombomodulin interaction and protein C activation. Circulation 1998 98 13 1297 1301 2-s2.0-0032578548 (Pubitemid 28443393)
    • (1998) Circulation , vol.98 , Issue.13 , pp. 1297-1301
    • De Cristofaro, R.1    De Candia, E.2    Landolfi, R.3
  • 46
    • 0028039927 scopus 로고
    • Thrombomodulin lacking the cytoplasmic domain efficiently internalizes thrombin via nonclathrin-coated, pit-mediated endocytosis
    • Conway E. M., Nowakowski B., Steiner-Mosonyi M., Thrombomodulin lacking the cytoplasmic domain efficiently internalizes thrombin via nonclathrin-coated, pit-mediated endocytosis. Journal of Cellular Physiology 1994 158 2 285 298 2-s2.0-0028039927 (Pubitemid 24063556)
    • (1994) Journal of Cellular Physiology , vol.158 , Issue.2 , pp. 285-298
    • Conway, E.M.1    Nowakowski, B.2    Steiner-Mosonyi, M.3
  • 48
    • 0028876697 scopus 로고
    • Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system
    • 2-s2.0-0028876697 10.1073/pnas.92.3.850
    • Healy A. M., Rayburn H. B., Rosenberg R. D., Weiler H., Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system. Proceedings of the National Academy of Sciences of the United States of America 1995 92 3 850 854 2-s2.0-0028876697 10.1073/pnas.92.3.850
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.3 , pp. 850-854
    • Healy, A.M.1    Rayburn, H.B.2    Rosenberg, R.D.3    Weiler, H.4
  • 49
    • 0035070573 scopus 로고    scopus 로고
    • Tissue-restricted expression of thrombomodulin in the placenta rescues thrombomodulin-deficient mice from early lethality and reveals a secondary developmental block
    • Isermann B., Hendrickson S. B., Hutley K., Wing M., Weiler H., Tissue-restricted expression of thrombomodulin in the placenta rescues thrombomodulin-deficient mice from early lethality and reveals a secondary developmental block. Development 2001 128 6 827 838 2-s2.0-0035070573 (Pubitemid 32288194)
    • (2001) Development , vol.128 , Issue.6 , pp. 827-838
    • Isermann, B.1    Hendrickson, S.B.2    Hutley, K.3    Wing, M.4    Weiler, H.5
  • 50
    • 0033562859 scopus 로고    scopus 로고
    • Structure-function analyses of thrombomodulin by gene-targeting in mice: The cytoplasmic domain is not required for normal fetal development
    • Conway E. M., Pollefeyt S., Cornelissen J., DeBaere I., Steiner-Mosonyi M., Weitz J. I., Weiler-Guettler H., Carmeliet P., Collen D., Structure-function analyses of thrombomodulin by gene-targeting in mice: the cytoplasmic domain is not required for normal fetal development. Blood 1999 93 10 3442 3450 2-s2.0-0033562859 (Pubitemid 29220911)
    • (1999) Blood , vol.93 , Issue.10 , pp. 3442-3450
    • Conway, E.M.1    Pollefeyt, S.2    Cornelissen, J.3    DeBaere, I.4    Steiner-Mosonyi, M.5    Weitz, J.I.6    Weiler-Guettler, H.7    Carmeliet, P.8    Collen, D.9
  • 51
    • 0024559613 scopus 로고
    • A domain composed of epidermal growth factor-like structures of human thrombomodulin is essential for thrombin binding and for protein C activation
    • Suzuki K., Hayashi T., Nishioka J., Kosaka Y., Zushi M., Honda G., Yamamoto S., A domain composed of epidermal growth factor-like structures of human thrombomodulin is essential for thrombin binding and for protein C activation. Journal of Biological Chemistry 1989 264 9 4872 4876 2-s2.0-0024559613 (Pubitemid 19092897)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.9 , pp. 4872-4876
    • Suzuki, K.1    Hayashi, T.2    Nishioka, J.3    Kosaka, Y.4    Zushi, M.5    Honda, G.6    Yamamoto, S.7
  • 52
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon C. T., Molecular events that control the protein C anticoagulant pathway. Thrombosis and Haemostasis 1993 70 1 29 35 2-s2.0-0027161205 (Pubitemid 23225446)
    • (1993) Thrombosis and Haemostasis , vol.70 , Issue.1 , pp. 29-35
    • Esmon, C.T.1
  • 53
    • 0028940777 scopus 로고
    • Human protein C and activated protein C: Components of the human anticoagulation system
    • 2-s2.0-0028940777 10.1016/1050-1738(94)00031-X
    • Castellino F. J., Human protein C and activated protein C: components of the human anticoagulation system. Trends in Cardiovascular Medicine 1995 5 2 55 62 2-s2.0-0028940777 10.1016/1050-1738(94)00031-X
    • (1995) Trends in Cardiovascular Medicine , vol.5 , Issue.2 , pp. 55-62
    • Castellino, F.J.1
  • 54
    • 0141509969 scopus 로고    scopus 로고
    • Thrombomodulin enhances the reactivity of thrombin with protein C inhibitor by providing both a binding site for the serpin and allosterically modulating the activity of thrombin
    • DOI 10.1074/jbc.M307243200
    • Yang L., Manithody C., Walston T. D., Cooper S. T., Rezaie A. R., Thrombomodulin enhances the reactivity of thrombin with protein C inhibitor by providing both a binding site for the serpin and allosterically modulating the activity of thrombin. Journal of Biological Chemistry 2003 278 39 37465 37470 2-s2.0-0141509969 10.1074/jbc.M307243200 (Pubitemid 37175267)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37465-37470
    • Yang, L.1    Manithody, C.2    Walston, T.D.3    Cooper, S.T.4    Rezaie, A.R.5
  • 55
    • 0023219464 scopus 로고
    • Binding of thrombin to thrombomodulin accelerates inhibition of the enzyme by antithrombin III. Evidence for a heparin-independent mechanism
    • DOI 10.1021/bi00383a018
    • Preissner K. T., Delvos U., Muller-Bergbaus G., Binding of thrombin to thrombomodulin accelerates inhibition of the enzyme by antithrombin III. Evidence for a heparin-independent mechanism. Biochemistry 1987 26 9 2521 2528 2-s2.0-0023219464 (Pubitemid 17081481)
    • (1987) Biochemistry , vol.26 , Issue.9 , pp. 2521-2528
    • Preissner, K.T.1    Delvos, U.2    Muller-Berghaus, G.3
  • 56
    • 0022371596 scopus 로고
    • The turnover of thrombin-thrombomodulin complex in cultured human umbilical vein endothelial cells and A549 lung cancer cells. Endocytosis and degradation of thrombin
    • Maruyama I., Majerus P. W., The turnover of thrombin-thrombomodulin complex in cultured human umbilical vein endothelial cells and A549 lung cancer cells. Endocytosis and degradation of thrombin. Journal of Biological Chemistry 1985 260 29 15432 15438 2-s2.0-0022371596 (Pubitemid 16170074)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.29 , pp. 15432-15438
    • Maruyama, I.1    Majerus, P.W.2
  • 57
    • 0024589205 scopus 로고
    • Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelium cells in culture
    • Moore K. L., Esmon C. T., Esmon N. L., Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelium cells in culture. Blood 1989 73 1 159 165 2-s2.0-0024589205 (Pubitemid 19040970)
    • (1989) Blood , vol.73 , Issue.1 , pp. 159-165
    • Moore, K.L.1    Esmon, C.T.2    Esmon, N.L.3
  • 58
    • 0034892611 scopus 로고    scopus 로고
    • Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis
    • DOI 10.1172/JCI200113077
    • Isermann B., Hendrickson S. B., Zogg M., Wing M., Cummiskey M., Kisanuki Y. Y., Yanagisawa M., Weiler H., Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis. Journal of Clinical Investigation 2001 108 4 537 546 2-s2.0-0034892611 10.1172/JCI200113077 (Pubitemid 32777733)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.4 , pp. 537-546
    • Isermann, B.1    Hendrickson, S.B.2    Zogg, M.3    Wing, M.4    Cummiskey, M.5    Kisanuki, Y.Y.6    Yanagisawa, M.7    Weiler, H.8
  • 59
    • 0033880884 scopus 로고    scopus 로고
    • Activated protein C inhibits lipopolysaccharide-induced nuclear translocation of nuclear factor κB (NF-κB) and tumour necrosis factor α (TNF-α) production in the THP-1 monocytic cell line
    • DOI 10.1046/j.1365-2141.2000.02128.x
    • White B., Schmidt M., Murphy C., Activated protein C inhibits lipopolysaccharide-induced nuclear translocation of nuclear factor kappaB (NF-kappaB) and tumour necrosis factor alpha (TNF-alpha) production in the THP-1 monocytic cell line. British Journal of Haematology 2000 110 1 130 134 (Pubitemid 30625601)
    • (2000) British Journal of Haematology , vol.110 , Issue.1 , pp. 130-134
    • White, B.1    Schmidt, M.2    Murphy, C.3    Livingstone, W.4    O'Toole, D.5    Lawler, M.6    O'Neill, L.7    Kelleher, D.8    Schwarz, H.P.9    Smith, O.P.10
  • 60
    • 0036250817 scopus 로고    scopus 로고
    • Recombinant human activated protein C attenuates the inflammatory response in endothelium and monocytes by modulating nuclear factor-κB
    • Joyce D. E., Grinnell B. W., Recombinant human activated protein C attenuates the inflammatory response in endothelium and monocytes by modulating nuclear factor- κ B. Critical Care Medicine 2002 30 supplement 5 S288 S293 2-s2.0-0036250817 (Pubitemid 34508005)
    • (2002) Critical Care Medicine , vol.30 , Issue.5 SUPPL.
    • Joyce, D.E.1    Grinnell, B.W.2
  • 61
    • 0035815747 scopus 로고    scopus 로고
    • Gene Expression Profile of Antithrombotic Protein C Defines New Mechanisms Modulating Inflammation and Apoptosis
    • DOI 10.1074/jbc.C100017200
    • Joyce D. E., Gelbert L., Ciaccia A., DeHoff B., Grinnell B. W., Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis. Journal of Biological Chemistry 2001 276 14 11199 11203 2-s2.0-0035815747 10.1074/jbc.C100017200 (Pubitemid 38089304)
    • (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
  • 62
    • 84859718853 scopus 로고    scopus 로고
    • Protein C anticoagulant system-anti-inflammatory effects
    • esmonc@omrf.org 10.1007/s00281-011-0284-6
    • Esmon C. T., esmonc@omrf.org Protein C anticoagulant system-anti- inflammatory effects. Seminars in Immunopathology 2012 34 1 127 132 10.1007/s00281-011-0284-6
    • (2012) Seminars in Immunopathology , vol.34 , Issue.1 , pp. 127-132
    • Esmon, C.T.1
  • 63
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • DOI 10.1126/science.1071699
    • Riewald M., Petrovan R. J., Donner A., Mueller B. M., Ruf W., Activation of endothelial cell protease activated receptor 1 by the protein C pathway. Science 2002 296 5574 1880 1882 2-s2.0-0037036069 10.1126/science.1071699 (Pubitemid 34596276)
    • (2002) Science , vol.296 , Issue.5574 , pp. 1880-1882
    • Riewald, M.1    Petrovan, R.J.2    Donner, A.3    Mueller, B.M.4    Ruf, W.5
  • 65
    • 62549145323 scopus 로고    scopus 로고
    • Thrombin inhibits nuclear factor kappaB and RhoA pathways in cytokine-stimulated vascular endothelial cells when EPCR is occupied by protein C
    • Bae J. S., Rezaie A. R., Thrombin inhibits nuclear factor kappaB and RhoA pathways in cytokine-stimulated vascular endothelial cells when EPCR is occupied by protein C. Journal of Thrombosis and Haemostasis 2009 101 3 513 520
    • (2009) Journal of Thrombosis and Haemostasis , vol.101 , Issue.3 , pp. 513-520
    • Bae, J.S.1    Rezaie, A.R.2
  • 66
    • 37049012509 scopus 로고    scopus 로고
    • The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
    • DOI 10.1182/blood-2007-06-096651
    • Bae J. S., Yang L., Manithody C., Rezaie A. R., The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells. Blood 2007 110 12 3909 3916 2-s2.0-37049012509 10.1182/blood-2007-06-096651 (Pubitemid 350248446)
    • (2007) Blood , vol.110 , Issue.12 , pp. 3909-3916
    • Bae, J.-S.1    Yang, L.2    Manithody, C.3    Rezaie, A.R.4
  • 67
    • 46749084607 scopus 로고    scopus 로고
    • Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand
    • DOI 10.1160/TH08-02-0127
    • Bae J. S., Rezaie A. R., Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand. Thrombosis and Haemostasis 2008 100 1 101 109 2-s2.0-46749084607 10.1160/TH08-02-0127 (Pubitemid 351948751)
    • (2008) Thrombosis and Haemostasis , vol.100 , Issue.1 , pp. 101-109
    • Bae, J.-S.1    Rezaie, A.R.2
  • 68
    • 77953504483 scopus 로고    scopus 로고
    • Regulation of the protein C anticoagulant and antiinflammatory pathways
    • 2-s2.0-77953504483 10.2174/092986710791233706
    • Rezaie A. R., Regulation of the protein C anticoagulant and antiinflammatory pathways. Current Medicinal Chemistry 2010 17 19 2059 2069 2-s2.0-77953504483 10.2174/092986710791233706
    • (2010) Current Medicinal Chemistry , vol.17 , Issue.19 , pp. 2059-2069
    • Rezaie, A.R.1
  • 69
    • 20444443508 scopus 로고    scopus 로고
    • Activated protein C mediates novel lung endothelial barrier enhancement: Role of sphingosine 1-phosphate receptor transactivation
    • DOI 10.1074/jbc.M412427200
    • Finigan J. H., Dudek S. M., Singleton P. A., Chiang E. T., Jacobson J. E., Camp S. M., Ye S. Q., Garcia J. G. N., Activated protein C mediates novel lung endothelial barrier enhancement: role of sphingosine 1-phosphate receptor transactivation. Journal of Biological Chemistry 2005 280 17 17286 17293 2-s2.0-20444443508 10.1074/jbc.M412427200 (Pubitemid 41389197)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17286-17293
    • Finigan, J.H.1    Dudek, S.M.2    Singleton, P.A.3    Chiang, E.T.4    Jacobson, J.E.5    Camp, S.M.6    Ye, S.Q.7    Garcia, J.G.N.8
  • 70
    • 17044427680 scopus 로고    scopus 로고
    • Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation
    • 2-s2.0-17044427680 10.1182/blood-2004-10-3985
    • Feistritzer C., Riewald M., Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation. Blood 2005 105 8 3178 3184 2-s2.0-17044427680 10.1182/blood-2004-10-3985
    • (2005) Blood , vol.105 , Issue.8 , pp. 3178-3184
    • Feistritzer, C.1    Riewald, M.2
  • 72
    • 77952296543 scopus 로고    scopus 로고
    • Activated protein C utilizes the angiopoietin/Tie2 axis to promote endothelial barrier function
    • 2-s2.0-77952296543 10.1096/fj.09-134445
    • Minhas N., Xue M., Fukudome K., Jackson C. J., Activated protein C utilizes the angiopoietin/Tie2 axis to promote endothelial barrier function. FASEB Journal 2010 24 3 873 881 2-s2.0-77952296543 10.1096/fj.09-134445
    • (2010) FASEB Journal , vol.24 , Issue.3 , pp. 873-881
    • Minhas, N.1    Xue, M.2    Fukudome, K.3    Jackson, C.J.4
  • 75
    • 0026534242 scopus 로고
    • Septic shock, multiple organ failure, and disseminated intravascular coagulation; Compared patterns of antithrombin III, protein C, and protein S deficiencies
    • 2-s2.0-0026534242
    • Fourrier F., Chopin C., Goudemand J., Hendrycx S., Caron C., Rime A., Marey A., Lestavel P., Septic shock, multiple organ failure, and disseminated intravascular coagulation; compared patterns of antithrombin III, protein C, and protein S deficiencies. Chest 1992 101 3 816 823 2-s2.0-0026534242
    • (1992) Chest , vol.101 , Issue.3 , pp. 816-823
    • Fourrier, F.1    Chopin, C.2    Goudemand, J.3    Hendrycx, S.4    Caron, C.5    Rime, A.6    Marey, A.7    Lestavel, P.8
  • 76
    • 0027214771 scopus 로고
    • Time course of hemostatic abnormalities in sepsis and its relation to outcome
    • Lorente J. A., Garcia-Frade L. J., Landin L., De Pablo R., Torrado C., Renes E., Garcia-Avello A., Time course of hemostatic abnormalities in sepsis and its relation to outcome. Chest 1993 103 5 1536 1542 2-s2.0-0027214771 (Pubitemid 23145617)
    • (1993) Chest , vol.103 , Issue.5 , pp. 1536-1542
    • Lorente, J.A.1    Garcia-Frade, L.J.2    Landin, L.3    De Pablo, R.4    Torrado, C.5    Renes, E.6    Garcia-Avello, A.7
  • 77
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • 2-s2.0-0029044322 10.1074/jbc.270.24.14477
    • Bajzar L., Manuel R., Nesheim M. E., Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. Journal of Biological Chemistry 1995 270 24 14477 14484 2-s2.0-0029044322 10.1074/jbc.270.24.14477
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.24 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 78
    • 77953779759 scopus 로고    scopus 로고
    • What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse?
    • 2-s2.0-77953779759 10.1111/j.1538-7836.2010.03787.x
    • Morser J., Gabazza E. C., Myles T., Leung L. L., What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse? Journal of Thrombosis and Haemostasis 2010 8 5 868 876 2-s2.0-77953779759 10.1111/j.1538-7836.2010.03787.x
    • (2010) Journal of Thrombosis and Haemostasis , vol.8 , Issue.5 , pp. 868-876
    • Morser, J.1    Gabazza, E.C.2    Myles, T.3    Leung, L.L.4
  • 79
    • 33750222459 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by Thrombin Activatable Fibrinolysis Inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis
    • DOI 10.1161/01.ATV.0000244680.14653.9a, PII 0004360520061100000006
    • Mosnier L. O., Bouma B. N., Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis. Arteriosclerosis, Thrombosis, and Vascular Biology 2006 26 11 2445 2453 2-s2.0-33750222459 10.1161/01.ATV. 0000244680.14653.9a (Pubitemid 44607464)
    • (2006) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.26 , Issue.11 , pp. 2445-2453
    • Mosnier, L.O.1    Bouma, B.N.2
  • 80
    • 57149122316 scopus 로고    scopus 로고
    • Complexity of complement activation in sepsis: Crossroads in sepsis research review series
    • 2-s2.0-57149122316 10.1111/j.1582-4934.2008.00504.x
    • Markiewski M. M., Deangelis R. A., Lambris J. D., Complexity of complement activation in sepsis: crossroads in sepsis research review series. Journal of Cellular and Molecular Medicine A 2008 12 6 2245 2254 2-s2.0-57149122316 10.1111/j.1582-4934.2008.00504.x
    • (2008) Journal of Cellular and Molecular Medicine A , vol.12 , Issue.6 , pp. 2245-2254
    • Markiewski, M.M.1    Deangelis, R.A.2    Lambris, J.D.3
  • 81
    • 34548849117 scopus 로고    scopus 로고
    • The role of complement in inflammatory diseases from behind the scenes into the spotlight
    • DOI 10.2353/ajpath.2007.070166
    • Markiewski M. M., Lambris J. D., The role of complement in inflammatory diseases from behind the scenes into the spotlight. American Journal of Pathology 2007 171 3 715 727 2-s2.0-34548849117 10.2353/ajpath.2007.070166 (Pubitemid 47440971)
    • (2007) American Journal of Pathology , vol.171 , Issue.3 , pp. 715-727
    • Markiewski, M.M.1    Lambris, J.D.2
  • 82
    • 43349093340 scopus 로고    scopus 로고
    • Role of the complement in experimental sepsis
    • DOI 10.1189/jlb.0607376
    • Ward P. A., Role of the complement in experimental sepsis. Journal of Leukocyte Biology 2008 83 3 467 470 2-s2.0-43349093340 10.1189/jlb.0607376 (Pubitemid 351966852)
    • (2008) Journal of Leukocyte Biology , vol.83 , Issue.3 , pp. 467-470
    • Ward, P.A.1
  • 83
    • 18844435687 scopus 로고    scopus 로고
    • Do-all receptor takes on coagulation, inflammation
    • DOI 10.1038/nm0505-475
    • Esmon C., Do-all receptor takes on coagulation, inflammation. Nature Medicine 2005 11 5 475 477 2-s2.0-18844435687 10.1038/nm0505-475 (Pubitemid 40685966)
    • (2005) Nature Medicine , vol.11 , Issue.5 , pp. 475-477
    • Esmon, C.1
  • 84
    • 0035853404 scopus 로고    scopus 로고
    • Thrombomodulin prolongs thrombin-induced extracellular signal-regulated kinase phosphorylation and nuclear retention in endothelial cells
    • Olivot J. M., Estebanell E., Lafay M., Brohard B., Aiach M., Rendu F., Thrombomodulin prolongs thrombin-induced extracellular signal-regulated kinase phosphorylation and nuclear retention in endothelial cells. Circulation Research 2001 88 7 681 687 2-s2.0-0035853404 (Pubitemid 32378137)
    • (2001) Circulation Research , vol.88 , Issue.7 , pp. 681-687
    • Olivot, J.-M.1    Estebanell, E.2    Lafay, M.3    Brohard, B.4    Aiach, M.5    Rendu, F.6
  • 85
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal
    • DOI 10.1038/nri1594
    • Lotze M. T., Tracey K. J., High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nature Reviews Immunology 2005 5 4 331 342 2-s2.0-17144376810 10.1038/nri1594 (Pubitemid 40516158)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.4 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 88
    • 0025218438 scopus 로고
    • Antithrombotic effect of recombinant human thrombomodulin on thrombin-induced thromboembolism in mice
    • Gomi K., Zushi M., Honda G., Kawahara S., Matsuzaki O., Kanabayashi T., Yamamoto S., Maruyama I., Suzuki K., Antithrombotic effect of recombinant human thrombomodulin on thrombin-induced thromboembolism in mice. Blood 1990 75 7 1396 1399 2-s2.0-0025218438 (Pubitemid 20114874)
    • (1990) Blood , vol.75 , Issue.7 , pp. 1396-1399
    • Gomi, K.1    Zushi, M.2    Honda, G.3    Kawahara, S.4    Matsuzaki, O.5    Kanabayashi, T.6    Yamamoto, S.7    Maruyama, I.8    Suzuki, K.9
  • 89
    • 0028230847 scopus 로고
    • Intravenous extended infusion of recombinant human soluble thrombomodulin prevented tissue factor-induced disseminated intravascular coagulation in rats
    • Mohri M., Oka M., Aoki Y., Gonda Y., Hirata S., Gomi K., Kiyota T., Sugihara T., Yamamoto S., Ishida T., Maruyama I., Intravenous extended infusion of recombinant human soluble thrombomodulin prevented tissue factor-induced disseminated intravascular coagulation in rats. American Journal of Hematology 1994 45 4 298 303 2-s2.0-0028230847 (Pubitemid 24109905)
    • (1994) American Journal of Hematology , vol.45 , Issue.4 , pp. 298-303
    • Mohri, M.1    Oka, M.2    Aoki, Y.3    Gonda, Y.4    Hirata, S.5    Gomi, K.6    Kiyota, T.7    Sugihara, T.8    Yamamoto, S.9    Ishida, T.10    Maruyama, I.11
  • 90
    • 0027291336 scopus 로고
    • Antithrombotic effect of recombinant human soluble thrombomodulin on endotoxin-induced disseminated intravascular coagulation in rats
    • DOI 10.1016/0049-3848(93)90201-X
    • Gonda Y., Hirata S., Saitoh K., Aoki Y., Mohri M., Gomi K., Sugihara T., Kiyota M., Yamamoto S., Ishida T., Maruyama I., Antithrombotic effect of recombinant human soluble thrombomodulin on endotoxin-induced disseminated intravascular coagulation in rats. Thrombosis Research 1993 71 4 325 335 2-s2.0-0027291336 10.1016/0049-3848(93)90201-X (Pubitemid 23222875)
    • (1993) Thrombosis Research , vol.71 , Issue.4 , pp. 325-335
    • Gonda, Y.1    Hirata, S.2    Saitoh, K.3    Aoki, Y.4    Mohri, M.5    Gomi, K.6    Sugihara, T.7    Kiyota, M.8    Yamamoto, S.9    Ishida, T.10    Maruyama, I.11
  • 91
    • 0028853552 scopus 로고
    • Recombinant human soluble thrombomodulin reduces endotoxin-induced pulmonary vascular injury via protein C activation in rats
    • 2-s2.0-0028853552
    • Uchiba M., Okajima K., Murakami K., Nawa K., Okabe H., Takatsuki K., Recombinant human soluble thrombomodulin reduces endotoxin-induced pulmonary vascular injury via protein C activation in rats. Thrombosis and Haemostasis 1995 74 5 1265 1270 2-s2.0-0028853552
    • (1995) Thrombosis and Haemostasis , vol.74 , Issue.5 , pp. 1265-1270
    • Uchiba, M.1    Okajima, K.2    Murakami, K.3    Nawa, K.4    Okabe, H.5    Takatsuki, K.6
  • 92
    • 0034064131 scopus 로고    scopus 로고
    • Neuroprotection by recombinant thrombomodulin
    • Taoka Y., Okajima K., Uchiba M., Johno M., Neuroprotection by recombinant thrombomodulin. Thrombosis and Haemostasis 2000 83 3 462 468 2-s2.0-0034064131 (Pubitemid 30148362)
    • (2000) Thrombosis and Haemostasis , vol.83 , Issue.3 , pp. 462-468
    • Taoka, Y.1    Okajima, K.2    Uchiba, M.3    Johno, M.4
  • 93
  • 94
    • 44449114876 scopus 로고    scopus 로고
    • Intrarenal administration of recombinant human soluble thrombomodulin ameliorates ischaemic acute renal failure
    • DOI 10.1093/ndt/gfm563
    • Ozaki T., Anas C., Maruyama S., Yamamoto T., Yasuda K., Morita Y., Ito Y., Gotoh M., Yuzawa Y., Matsuo S., Intrarenal administration of recombinant human soluble thrombomodulin ameliorates ischaemic acute renal failure. Nephrology Dialysis Transplantation 2008 23 1 110 119 2-s2.0-44449114876 10.1093/ndt/gfm563 (Pubitemid 351767375)
    • (2008) Nephrology Dialysis Transplantation , vol.23 , Issue.1 , pp. 110-119
    • Ozaki, T.1    Anas, C.2    Maruyama, S.3    Yamamoto, T.4    Yasuda, K.5    Morita, Y.6    Ito, Y.7    Gotoh, M.8    Yuzawa, Y.9    Matsuo, S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.