메뉴 건너뛰기




Volumn 152, Issue 4, 2008, Pages 165-177

Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain

Author keywords

[No Author keywords available]

Indexed keywords

CD47 ANTIGEN; ENOXAPARIN; HEPARIN; PADGEM PROTEIN; PHOSPHATIDYLSERINE; THROMBOSPONDIN 1;

EID: 54549115945     PISSN: 19315244     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.trsl.2008.07.007     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 0031948732 scopus 로고    scopus 로고
    • Phospholipid asymmetry in health and disease
    • Kuypers F.A. Phospholipid asymmetry in health and disease. Curr Opin Hematol 5 (1998) 122-131
    • (1998) Curr Opin Hematol , vol.5 , pp. 122-131
    • Kuypers, F.A.1
  • 2
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • Zwaal R.F.A., and Schroit A.J. Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89 (1997) 1121-1132
    • (1997) Blood , vol.89 , pp. 1121-1132
    • Zwaal, R.F.A.1    Schroit, A.J.2
  • 3
    • 33645845142 scopus 로고    scopus 로고
    • Phosphatidylserine recognition by phagocytes: a view to a kill
    • Wu Y., Tibrewal N., and Birge R.B. Phosphatidylserine recognition by phagocytes: a view to a kill. Trends Cell Biol 16 (2006) 189-197
    • (2006) Trends Cell Biol , vol.16 , pp. 189-197
    • Wu, Y.1    Tibrewal, N.2    Birge, R.B.3
  • 4
    • 0036493303 scopus 로고    scopus 로고
    • Role of erythrocyte phosphatidylserine in sickle red cell-endothelial adhesion
    • Setty B.N.Y., Kulkarni S., and Stuart M.J. Role of erythrocyte phosphatidylserine in sickle red cell-endothelial adhesion. Blood 99 (2002) 1564-1571
    • (2002) Blood , vol.99 , pp. 1564-1571
    • Setty, B.N.Y.1    Kulkarni, S.2    Stuart, M.J.3
  • 5
    • 0036434149 scopus 로고    scopus 로고
    • Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine
    • Eda S., and Sherman I.W. Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine. Cell Physiol Biochem 12 (2002) 373-384
    • (2002) Cell Physiol Biochem , vol.12 , pp. 373-384
    • Eda, S.1    Sherman, I.W.2
  • 6
    • 0036380903 scopus 로고    scopus 로고
    • Enhanced adherence of human uremic erythrocytes to vascular endothelium: role of phosphatidylserine exposure
    • Bonomini M., Sirolli V., Gizzi F., Di Stante S., Grilli A., and Felaco M. Enhanced adherence of human uremic erythrocytes to vascular endothelium: role of phosphatidylserine exposure. Kidney Intl 62 (2002) 1358-1363
    • (2002) Kidney Intl , vol.62 , pp. 1358-1363
    • Bonomini, M.1    Sirolli, V.2    Gizzi, F.3    Di Stante, S.4    Grilli, A.5    Felaco, M.6
  • 7
    • 0018885938 scopus 로고
    • Erythrocyte adherence to endothelium in sickle-cell anemia. A possible determinant of disease severity
    • Hebbel R.P., Boogaerts M.A., Eaton J.W., and Steinberg M.H. Erythrocyte adherence to endothelium in sickle-cell anemia. A possible determinant of disease severity. N Engl J Med 302 (1980) 992-995
    • (1980) N Engl J Med , vol.302 , pp. 992-995
    • Hebbel, R.P.1    Boogaerts, M.A.2    Eaton, J.W.3    Steinberg, M.H.4
  • 8
    • 0343339958 scopus 로고    scopus 로고
    • Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin
    • Manodori A.B., Barabino G.A., Lubin B.H., and Kuypers F.A. Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin. Blood 95 (2000) 1293-1300
    • (2000) Blood , vol.95 , pp. 1293-1300
    • Manodori, A.B.1    Barabino, G.A.2    Lubin, B.H.3    Kuypers, F.A.4
  • 9
    • 0029347102 scopus 로고
    • Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1
    • Bornstein P. Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1. J Cell Biol 130 (1995) 503-506
    • (1995) J Cell Biol , vol.130 , pp. 503-506
    • Bornstein, P.1
  • 10
    • 0033734494 scopus 로고    scopus 로고
    • The cell biology of thrombospondin-1
    • Chen H., Herndon M.E., and Lawler J. The cell biology of thrombospondin-1. Matrix Biol 19 (2000) 597-614
    • (2000) Matrix Biol , vol.19 , pp. 597-614
    • Chen, H.1    Herndon, M.E.2    Lawler, J.3
  • 11
    • 0035178990 scopus 로고    scopus 로고
    • Thrombospondins: multifunctional regulators of cell interactions
    • Adams J.C. Thrombospondins: multifunctional regulators of cell interactions. Ann Rev Cell Dev Biol 17 (2001) 25-51
    • (2001) Ann Rev Cell Dev Biol , vol.17 , pp. 25-51
    • Adams, J.C.1
  • 12
    • 16544391915 scopus 로고    scopus 로고
    • The N-terminus of thrombospondin: the domain stands apart
    • Elzie C.A., and Murphy-Ullrich J.E. The N-terminus of thrombospondin: the domain stands apart. Int J Biochem Cell Biol 36 (2004) 1090-1101
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1090-1101
    • Elzie, C.A.1    Murphy-Ullrich, J.E.2
  • 14
    • 0019774169 scopus 로고
    • Isolation and characterization of a glycoprotein secreted by aortic endothelial cells in culture: apparent identity with platelet thrombospondin
    • McPherson J., Sage H., and Bornstein P. Isolation and characterization of a glycoprotein secreted by aortic endothelial cells in culture: apparent identity with platelet thrombospondin. J Biol Chem 256 (1981) 11330-11336
    • (1981) J Biol Chem , vol.256 , pp. 11330-11336
    • McPherson, J.1    Sage, H.2    Bornstein, P.3
  • 15
    • 0020313151 scopus 로고
    • Synthesis and secretion of thrombospondin by cultured human endothelial cells
    • Mosher D.F., Doyle M.J., and Jaffe E.A. Synthesis and secretion of thrombospondin by cultured human endothelial cells. J Cell Biol 93 (1982) 343-348
    • (1982) J Cell Biol , vol.93 , pp. 343-348
    • Mosher, D.F.1    Doyle, M.J.2    Jaffe, E.A.3
  • 17
    • 0032212293 scopus 로고    scopus 로고
    • Enhanced adherence of sickle erythrocytes to thrombin-treated endothelial cells involves interendothelial cell gap formation
    • Manodori A.B., Matsui N.M., Chen J.Y., and Embury S.H. Enhanced adherence of sickle erythrocytes to thrombin-treated endothelial cells involves interendothelial cell gap formation. Blood 92 (1998) 3445-3454
    • (1998) Blood , vol.92 , pp. 3445-3454
    • Manodori, A.B.1    Matsui, N.M.2    Chen, J.Y.3    Embury, S.H.4
  • 18
    • 0032898355 scopus 로고    scopus 로고
    • Mechanism of interaction of thrombospondin with human endothelium and inhibition of sickle erythrocyte adhesion to human endothelial cells by heparin
    • Gupta K., Gupta P., Solovey A., and Hebbel R.P. Mechanism of interaction of thrombospondin with human endothelium and inhibition of sickle erythrocyte adhesion to human endothelial cells by heparin. Biochim Biophys Acta 1453 (1999) 63-73
    • (1999) Biochim Biophys Acta , vol.1453 , pp. 63-73
    • Gupta, K.1    Gupta, P.2    Solovey, A.3    Hebbel, R.P.4
  • 19
    • 0023000529 scopus 로고
    • Monoclonal antibodies that recognize calcium-dependent structures of human thrombospondin: characterization and mapping of their epitopes
    • Dixit V.M., Galvin N.J., O'Rourke K.M., and Frazier W.A. Monoclonal antibodies that recognize calcium-dependent structures of human thrombospondin: characterization and mapping of their epitopes. J Biol Chem 261 (1986) 1962-1968
    • (1986) J Biol Chem , vol.261 , pp. 1962-1968
    • Dixit, V.M.1    Galvin, N.J.2    O'Rourke, K.M.3    Frazier, W.A.4
  • 20
    • 0021826587 scopus 로고
    • A monoclonal antibody against human thrombospondin inhibits platelet aggregation
    • Dixit V.M., Haverstick D.M., O'Rourke K.M., et al. A monoclonal antibody against human thrombospondin inhibits platelet aggregation. Proc Natl Acad Sci U S A 82 (1985) 3472-3476
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 3472-3476
    • Dixit, V.M.1    Haverstick, D.M.2    O'Rourke, K.M.3
  • 21
    • 0026329264 scopus 로고
    • Cell attachment activity of the carboxyl-terminal domain of human thrombospondin expressed in Escherichia coli
    • Kosfeld M.D., Pavlopoulos T.V., and Frazier W.A. Cell attachment activity of the carboxyl-terminal domain of human thrombospondin expressed in Escherichia coli. J Biol Chem 266 (1991) 24257-24259
    • (1991) J Biol Chem , vol.266 , pp. 24257-24259
    • Kosfeld, M.D.1    Pavlopoulos, T.V.2    Frazier, W.A.3
  • 22
    • 0030921686 scopus 로고    scopus 로고
    • Decorin inhibits cell attachment to thrombospondin-1 by binding to a KKTR-dependent cell adhesive site present within the N-terminal domain of thrombospondin-1
    • Merle B., Malaval L., Lawler J., Delmas P., and Clezardin P. Decorin inhibits cell attachment to thrombospondin-1 by binding to a KKTR-dependent cell adhesive site present within the N-terminal domain of thrombospondin-1. J Cellular Biochem 67 (1997) 75-83
    • (1997) J Cellular Biochem , vol.67 , pp. 75-83
    • Merle, B.1    Malaval, L.2    Lawler, J.3    Delmas, P.4    Clezardin, P.5
  • 23
    • 0031044918 scopus 로고    scopus 로고
    • Identification of cell adhesive active sites in the N-terminal domain of thrombospondin-1
    • Clezardin P., Lawler J., Amiral J., Quentin G., and Delmas P. Identification of cell adhesive active sites in the N-terminal domain of thrombospondin-1. Biochem J 321 (1997) 819-827
    • (1997) Biochem J , vol.321 , pp. 819-827
    • Clezardin, P.1    Lawler, J.2    Amiral, J.3    Quentin, G.4    Delmas, P.5
  • 24
    • 0030020463 scopus 로고    scopus 로고
    • Detection of altered membrane phospholipid asymmetry in subpopulations of human red blood cells using fluorescently labeled annexin V
    • Kuypers F.A., Lewis R.A., Hua M., et al. Detection of altered membrane phospholipid asymmetry in subpopulations of human red blood cells using fluorescently labeled annexin V. Blood 87 (1996) 1179-1187
    • (1996) Blood , vol.87 , pp. 1179-1187
    • Kuypers, F.A.1    Lewis, R.A.2    Hua, M.3
  • 25
    • 38349151904 scopus 로고    scopus 로고
    • Microvascular endothelial cells express a phosphatidylserine receptor: a functionally active receptor for phosphatidylserine-positive erythrocytes
    • Setty B.N.Y., and Gayen Betal S. Microvascular endothelial cells express a phosphatidylserine receptor: a functionally active receptor for phosphatidylserine-positive erythrocytes. Blood 111 (2008) 905-914
    • (2008) Blood , vol.111 , pp. 905-914
    • Setty, B.N.Y.1    Gayen Betal, S.2
  • 26
    • 0035761409 scopus 로고    scopus 로고
    • Thrombophilia in sickle cell disease: the red cell connection
    • Setty B.N.Y., Rao A.K., and Stuart M.J. Thrombophilia in sickle cell disease: the red cell connection. Blood 98 (2001) 3228-3233
    • (2001) Blood , vol.98 , pp. 3228-3233
    • Setty, B.N.Y.1    Rao, A.K.2    Stuart, M.J.3
  • 27
    • 0035353182 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia: relationship to erythrocyte adhesion markers and adhesion
    • Setty B.N.Y., Kulkarni S., Dampier C.D., and Stuart M.J. Fetal hemoglobin in sickle cell anemia: relationship to erythrocyte adhesion markers and adhesion. Blood 97 (2001) 2568-2573
    • (2001) Blood , vol.97 , pp. 2568-2573
    • Setty, B.N.Y.1    Kulkarni, S.2    Dampier, C.D.3    Stuart, M.J.4
  • 28
    • 0029897658 scopus 로고    scopus 로고
    • Increased adhesion of erythrocytes to components of the extracellular matrix: isolation and characterization of a red blood cell lipid that binds thrombospondin and laminin
    • Hillery C.A., Du M.C., Montgomery R.R., and Scott J.P. Increased adhesion of erythrocytes to components of the extracellular matrix: isolation and characterization of a red blood cell lipid that binds thrombospondin and laminin. Blood 87 (1996) 4879-4886
    • (1996) Blood , vol.87 , pp. 4879-4886
    • Hillery, C.A.1    Du, M.C.2    Montgomery, R.R.3    Scott, J.P.4
  • 29
    • 0028324464 scopus 로고
    • Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P., and Pollard H.B. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim Biophys Acta 1197 (1994) 63-93
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 30
    • 0037111637 scopus 로고    scopus 로고
    • Heparin inhibits the flow adhesion of sickle red blood cells to P-selectin
    • Matsui N.M., Varki A., and Embury S.H. Heparin inhibits the flow adhesion of sickle red blood cells to P-selectin. Blood 100 (2002) 3790-3796
    • (2002) Blood , vol.100 , pp. 3790-3796
    • Matsui, N.M.1    Varki, A.2    Embury, S.H.3
  • 31
    • 0033558304 scopus 로고    scopus 로고
    • Anionic polysaccharides inhibit adhesion of sickle erythrocytes to the vascular endothelium and result in improved hemodynamic behavior
    • Barabino G.A., Liu X.D., Ewenstein B.M., and Kaul D.K. Anionic polysaccharides inhibit adhesion of sickle erythrocytes to the vascular endothelium and result in improved hemodynamic behavior. Blood 93 (1999) 1422-1429
    • (1999) Blood , vol.93 , pp. 1422-1429
    • Barabino, G.A.1    Liu, X.D.2    Ewenstein, B.M.3    Kaul, D.K.4
  • 33
    • 0027131853 scopus 로고
    • Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia
    • Joneckis C.C., Ackley R.L., Orringer E.P., Wayner E.A., and Parise L.V. Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia. Blood 82 (1993) 3548-3555
    • (1993) Blood , vol.82 , pp. 3548-3555
    • Joneckis, C.C.1    Ackley, R.L.2    Orringer, E.P.3    Wayner, E.A.4    Parise, L.V.5
  • 34
    • 0027184968 scopus 로고
    • Alpha 4 beta 1-integrin expression on sickle reticulocytes: vascular cell adhesion molecule-1-dependent binding to endothelium
    • Swerlick R.A., Eckman J.R., Kumar A., Jeitler M., and Wick T.M. Alpha 4 beta 1-integrin expression on sickle reticulocytes: vascular cell adhesion molecule-1-dependent binding to endothelium. Blood 82 (1993) 1891-1899
    • (1993) Blood , vol.82 , pp. 1891-1899
    • Swerlick, R.A.1    Eckman, J.R.2    Kumar, A.3    Jeitler, M.4    Wick, T.M.5
  • 35
    • 0035313429 scopus 로고    scopus 로고
    • Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin
    • Brittain J.E., Milnar K.J., Anderson C.S., Orringer E.P., and Parise L.V. Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin. Blood 97 (2001) 2159-2164
    • (2001) Blood , vol.97 , pp. 2159-2164
    • Brittain, J.E.1    Milnar, K.J.2    Anderson, C.S.3    Orringer, E.P.4    Parise, L.V.5
  • 36
    • 0034978033 scopus 로고    scopus 로고
    • Activation of sickle red blood cell adhesion via integrin-associated protein/CD47-induced signal transduction
    • Brittain J.E., Milnar K.J., Anderson C.S., Orringer E.P., and Parise L.V. Activation of sickle red blood cell adhesion via integrin-associated protein/CD47-induced signal transduction. J Clin Invest 107 (2001) 1555-1562
    • (2001) J Clin Invest , vol.107 , pp. 1555-1562
    • Brittain, J.E.1    Milnar, K.J.2    Anderson, C.S.3    Orringer, E.P.4    Parise, L.V.5
  • 37
    • 0033534462 scopus 로고    scopus 로고
    • Critical factors in basal cell adhesion molecule/Lutheran-mediated adhesion to laminin
    • Zen Q., Cottman M., Truskey G., Fraser R., and Telen M.J. Critical factors in basal cell adhesion molecule/Lutheran-mediated adhesion to laminin. J Biol Chem 274 (1999) 728-734
    • (1999) J Biol Chem , vol.274 , pp. 728-734
    • Zen, Q.1    Cottman, M.2    Truskey, G.3    Fraser, R.4    Telen, M.J.5
  • 38
    • 0032103286 scopus 로고    scopus 로고
    • Basal cell adhesion molecule/Lutheran protein. The receptor critical for sickle cell adhesion to laminin
    • Udani M., Zen Q., Cottman M., et al. Basal cell adhesion molecule/Lutheran protein. The receptor critical for sickle cell adhesion to laminin. J Clin Invest 101 (1998) 2550-2558
    • (1998) J Clin Invest , vol.101 , pp. 2550-2558
    • Udani, M.1    Zen, Q.2    Cottman, M.3
  • 39
    • 0029119077 scopus 로고
    • Conformational changes in adhesive proteins modulate their adhesive function
    • Ugarova T., Agbanyo F.R., and Plow E.F. Conformational changes in adhesive proteins modulate their adhesive function. Thromb Haem 74 (1995) 253-257
    • (1995) Thromb Haem , vol.74 , pp. 253-257
    • Ugarova, T.1    Agbanyo, F.R.2    Plow, E.F.3
  • 40
    • 0021032073 scopus 로고
    • Cooperative binding of calcium to thrombospondin: the effect of calcium on the circular dichroism and limited tryptic digestion of thrombospondin
    • Lawler J., and Simons E.R. Cooperative binding of calcium to thrombospondin: the effect of calcium on the circular dichroism and limited tryptic digestion of thrombospondin. J Biol Chem 258 (1983) 12098-12101
    • (1983) J Biol Chem , vol.258 , pp. 12098-12101
    • Lawler, J.1    Simons, E.R.2
  • 42
    • 0025109879 scopus 로고
    • Free Thiols of platelet thrombospondin: evidence for disulfide isomerization
    • Speziale M.V., and Detwiler T.C. Free Thiols of platelet thrombospondin: evidence for disulfide isomerization. J Biol Chem 265 (1990) 17859-17867
    • (1990) J Biol Chem , vol.265 , pp. 17859-17867
    • Speziale, M.V.1    Detwiler, T.C.2
  • 44
    • 0030008933 scopus 로고    scopus 로고
    • Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions
    • Joneckis C.C., Shock D.D., Cunningham M.L., Orringer E.P., and Parise L.V. Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions. Blood 87 (1996) 4862-4870
    • (1996) Blood , vol.87 , pp. 4862-4870
    • Joneckis, C.C.1    Shock, D.D.2    Cunningham, M.L.3    Orringer, E.P.4    Parise, L.V.5
  • 45
    • 0031147997 scopus 로고    scopus 로고
    • Platelet activation and platelet-erythrocyte aggregation in patients with sickle cell anemia
    • Wun T., Paglieroni T., Tablin F., Welborn J., Nelson K., and Cheung A. Platelet activation and platelet-erythrocyte aggregation in patients with sickle cell anemia. J Lab Clin Med 129 (1997) 507-516
    • (1997) J Lab Clin Med , vol.129 , pp. 507-516
    • Wun, T.1    Paglieroni, T.2    Tablin, F.3    Welborn, J.4    Nelson, K.5    Cheung, A.6
  • 46
    • 0033093026 scopus 로고    scopus 로고
    • Platelet-erythrocyte adhesion in sickle cell disease
    • Wun T., Paglieroni T., and Field C.L. Platelet-erythrocyte adhesion in sickle cell disease. J Investig Med 47 (1999) 121-127
    • (1999) J Investig Med , vol.47 , pp. 121-127
    • Wun, T.1    Paglieroni, T.2    Field, C.L.3
  • 47
    • 0029998910 scopus 로고    scopus 로고
    • Sickle erythrocytes adhere to polymorphonuclear neutrophils and activate the neutrophil respiratory burst
    • Hofstra T.C., Karla V.K., Meiselman H.J., and Coates T.D. Sickle erythrocytes adhere to polymorphonuclear neutrophils and activate the neutrophil respiratory burst. Blood 87 (1996) 4440-4447
    • (1996) Blood , vol.87 , pp. 4440-4447
    • Hofstra, T.C.1    Karla, V.K.2    Meiselman, H.J.3    Coates, T.D.4
  • 48
    • 0028339074 scopus 로고
    • Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1
    • Adams J.C., and Lawler J. Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1. Mol Biol Cell 5 (1994) 423-437
    • (1994) Mol Biol Cell , vol.5 , pp. 423-437
    • Adams, J.C.1    Lawler, J.2
  • 49
    • 0028785452 scopus 로고
    • Heparin: mechanism of action, pharmacokinetics, dosing considerations, monitoring, efficacy, and safety
    • Hirsh J., Raschke R., Warkentin T.E., Dalen J.E., Deykin D., and Poller L. Heparin: mechanism of action, pharmacokinetics, dosing considerations, monitoring, efficacy, and safety. Chest 108 (1995) 258S-275S
    • (1995) Chest , vol.108
    • Hirsh, J.1    Raschke, R.2    Warkentin, T.E.3    Dalen, J.E.4    Deykin, D.5    Poller, L.6
  • 50
    • 0035125405 scopus 로고    scopus 로고
    • Heparin and low-molecular-weight heparin: mechanisms of action, pharmacokinetics, dosing, monitoring, efficacy, and safety
    • Hirsh J., Warkentin T.E., Shaughnessy S.G., et al. Heparin and low-molecular-weight heparin: mechanisms of action, pharmacokinetics, dosing, monitoring, efficacy, and safety. Chest 119 (2001) 64S-94S
    • (2001) Chest , vol.119
    • Hirsh, J.1    Warkentin, T.E.2    Shaughnessy, S.G.3
  • 51
    • 0036474098 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of the prophylactic dose of enoxaparin once daily over 4 days in patients with renal impairment
    • Ger-Jan C.M., Sanderink G.-J.C.M., Guimart C.G., and Ozoux M.-L. Pharmacokinetics and pharmacodynamics of the prophylactic dose of enoxaparin once daily over 4 days in patients with renal impairment. Thrombosis Res 105 (2002) 225-231
    • (2002) Thrombosis Res , vol.105 , pp. 225-231
    • Ger-Jan, C.M.1    Sanderink, G.-J.C.M.2    Guimart, C.G.3    Ozoux, M.-L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.