메뉴 건너뛰기




Volumn 45, Issue , 2007, Pages 209-255

Chapter 6 A Journey with Bleeding Time Factor

Author keywords

ADAMTS 13.; factorVIII; multimer; platelets; Von Willebrand factor; VWD; VWF

Indexed keywords


EID: 44449172526     PISSN: 00698032     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0069-8032(07)45006-9     Document Type: Review
Times cited : (10)

References (140)
  • 2
    • 44449130048 scopus 로고    scopus 로고
    • von Willebrand, E.A. (1931) Über hereditäre Pseudohämophilie. Acta Med. Scand. LXXVI(fasc. IV-VI), 521-550 - An addendum refers to a similar case with ascent for three generations (Acta Med. Scand. 72, 104 (1929).
    • von Willebrand, E.A. (1931) Über hereditäre Pseudohämophilie. Acta Med. Scand. LXXVI(fasc. IV-VI), 521-550 - An addendum refers to a similar case with ascent for three generations (Acta Med. Scand. 72, 104 (1929).
  • 4
    • 0342665073 scopus 로고
    • Dual hemostatic Defect in pseudohemophilia
    • Alexander B., and Goldstein R. Dual hemostatic Defect in pseudohemophilia. J. Clin. Invest. 32 (1953) 551
    • (1953) J. Clin. Invest. , vol.32 , pp. 551
    • Alexander, B.1    Goldstein, R.2
  • 5
    • 17344372258 scopus 로고
    • Déficit en facteur antihémophilique A chez une fille, associé a un trouble du saignement
    • Larrieu M.-J., and Soulier J.P. Déficit en facteur antihémophilique A chez une fille, associé a un trouble du saignement. Rev. Hemat. 8 (1953) 361-370
    • (1953) Rev. Hemat. , vol.8 , pp. 361-370
    • Larrieu, M.-J.1    Soulier, J.P.2
  • 6
    • 0000673509 scopus 로고
    • Purification of human and bovine Fibrinogen
    • Blombäck B., and Blombäck M. Purification of human and bovine Fibrinogen. Ark. Kemi 10 (1956) 415-443
    • (1956) Ark. Kemi , vol.10 , pp. 415-443
    • Blombäck, B.1    Blombäck, M.2
  • 7
    • 6544221214 scopus 로고
    • Kvinnlig hämofili och dess behandling med humant antihämofiliglobulin
    • Nilsson I.M., Blombäck B., Blombäck M., and Svennerud S. Kvinnlig hämofili och dess behandling med humant antihämofiliglobulin. Nordisk Medicin 56 (1956) 1654-1662
    • (1956) Nordisk Medicin , vol.56 , pp. 1654-1662
    • Nilsson, I.M.1    Blombäck, B.2    Blombäck, M.3    Svennerud, S.4
  • 8
    • 0002857544 scopus 로고
    • On an inherited autosomal hemorrhagic diathesis with antihemophilic globulin (AHG) deficiency and prolonged bleeding time
    • Nilsson I.M., Blombäck M., and von Franken I. On an inherited autosomal hemorrhagic diathesis with antihemophilic globulin (AHG) deficiency and prolonged bleeding time. Acta Med. Scand. CLIX fasc. 1 (1957) 35-57
    • (1957) Acta Med. Scand. , vol.CLIX , Issue.fasc. 1 , pp. 35-57
    • Nilsson, I.M.1    Blombäck, M.2    von Franken, I.3
  • 9
    • 0004491249 scopus 로고
    • Von Willebrand's disease and its correction with human plasma fraction I-O
    • Nilsson I.M., Blombäck M., Jorpes E., Blombäck B., and Johansson S.-A. Von Willebrand's disease and its correction with human plasma fraction I-O. Acta Med. Scand. CLIX fasc. III (1957) 179-188
    • (1957) Acta Med. Scand. , vol.CLIX , Issue.fasc. III , pp. 179-188
    • Nilsson, I.M.1    Blombäck, M.2    Jorpes, E.3    Blombäck, B.4    Johansson, S.-A.5
  • 10
    • 84995181575 scopus 로고    scopus 로고
    • Blombäck, B. (1958) Studies on fibrinogen and antihaemophilic globulin, XIIth Conference of the Protein Foundation on blood cells and plasma proteins, Albany, NY, November 1957. Vox Sang., 3, 58.
    • Blombäck, B. (1958) Studies on fibrinogen and antihaemophilic globulin, XIIth Conference of the Protein Foundation on blood cells and plasma proteins, Albany, NY, November 1957. Vox Sang., 3, 58.
  • 11
    • 0001164136 scopus 로고
    • v. Willebrand's disease in Sweden: its pathogenesis and treatment
    • Nilsson I.M., Blombäck M., and Blombäck B. v. Willebrand's disease in Sweden: its pathogenesis and treatment. Acta Med. Scand. 164 fasc. 3 (1959) 263-278
    • (1959) Acta Med. Scand. , vol.164 , Issue.fasc. 3 , pp. 263-278
    • Nilsson, I.M.1    Blombäck, M.2    Blombäck, B.3
  • 12
    • 44449086476 scopus 로고
    • von Willebrand's disease in Sweden - occurrence, pathogenesis and treatment
    • Nilsson I.M., and Blombäck M. von Willebrand's disease in Sweden - occurrence, pathogenesis and treatment. Thromb. Diath. Haemorrhagica IX Suppl. 2 (1962) 103-118
    • (1962) Thromb. Diath. Haemorrhagica , vol.IX , Issue.SUPPL. 2 , pp. 103-118
    • Nilsson, I.M.1    Blombäck, M.2
  • 13
    • 44449179899 scopus 로고
    • Response to fractions in von Willebrand's disease
    • Brinkhous K.M. (Ed), University North Carolina Press, Chapel Hill
    • Blombäck M., Blombäck B., and Nilsson I.M. Response to fractions in von Willebrand's disease. In: Brinkhous K.M. (Ed). The Haemophilias (1964), University North Carolina Press, Chapel Hill 286-294
    • (1964) The Haemophilias , pp. 286-294
    • Blombäck, M.1    Blombäck, B.2    Nilsson, I.M.3
  • 14
    • 44449141036 scopus 로고
    • The use of plasma and plasma fractions in the treatment of a patient with von Willebrand's disease
    • Weiss H.J. The use of plasma and plasma fractions in the treatment of a patient with von Willebrand's disease. Vox Sang. 7 (1962) 267-280
    • (1962) Vox Sang. , vol.7 , pp. 267-280
    • Weiss, H.J.1
  • 15
    • 44449152632 scopus 로고
    • Von Willebrand's disease - a plasma deficiency cause of the prolonged bleeding time
    • Van Creveld S., and Mochtar I.A. Von Willebrand's disease - a plasma deficiency cause of the prolonged bleeding time. Ann. Paediatr. 194 (1960) 37-46
    • (1960) Ann. Paediatr. , vol.194 , pp. 37-46
    • Van Creveld, S.1    Mochtar, I.A.2
  • 17
    • 0001536999 scopus 로고
    • Transfusion studies in von Willebrand's disease: effect on bleeding time and factor VIII
    • Cornu P., Larrieu M.-J., Caen J., and Bernard J. Transfusion studies in von Willebrand's disease: effect on bleeding time and factor VIII. Brit J. Haematol. 9 (1963) 189-202
    • (1963) Brit J. Haematol. , vol.9 , pp. 189-202
    • Cornu, P.1    Larrieu, M.-J.2    Caen, J.3    Bernard, J.4
  • 18
    • 44449174118 scopus 로고    scopus 로고
    • Biggs, R. and Macfarlane, R.G. (eds.) (1962) von Willebrand's disease. In Human Blood Coagulation and Its Disorders, p. 280. Oxford, Blackwell.
    • Biggs, R. and Macfarlane, R.G. (eds.) (1962) von Willebrand's disease. In Human Blood Coagulation and Its Disorders, p. 280. Oxford, Blackwell.
  • 19
    • 84982058255 scopus 로고
    • Platelet adhesion in vivo in patients with bleeding disorders
    • Borchgrevink C.F. Platelet adhesion in vivo in patients with bleeding disorders. Acta Med. Scand. 170 fasc. 2 (1961) 231-243
    • (1961) Acta Med. Scand. , vol.170 , Issue.fasc. 2 , pp. 231-243
    • Borchgrevink, C.F.1
  • 20
    • 0000203483 scopus 로고
    • Measurement of platelet adhesiveness: a simple in vitro technique demonstrating an abnormality in von Willebrand's disease
    • Salzman E.W. Measurement of platelet adhesiveness: a simple in vitro technique demonstrating an abnormality in von Willebrand's disease. J. Lab. Clin. Med. 62 (1963) 724-735
    • (1963) J. Lab. Clin. Med. , vol.62 , pp. 724-735
    • Salzman, E.W.1
  • 21
    • 33645957692 scopus 로고
    • In vitro abnormality of the blood in von Willebrand's disease correctable by normal plasma
    • Zucker M.B. In vitro abnormality of the blood in von Willebrand's disease correctable by normal plasma. Nature 197 (1963) 601-602
    • (1963) Nature , vol.197 , pp. 601-602
    • Zucker, M.B.1
  • 22
    • 0014048160 scopus 로고
    • Some interactions between human platelets and glass: von Willebrand's disease compared with normal
    • O'Brien J.R., and Heywood J.B. Some interactions between human platelets and glass: von Willebrand's disease compared with normal. J. Clin. Pathol. 20 (1967) 56-64
    • (1967) J. Clin. Pathol. , vol.20 , pp. 56-64
    • O'Brien, J.R.1    Heywood, J.B.2
  • 23
    • 0014769957 scopus 로고
    • Von Willebrand factor and platelet adhesiveness
    • Meyer D., and Larrieu M.-J. Von Willebrand factor and platelet adhesiveness. J. Clin. Pathol. 23 (1970) 228-231
    • (1970) J. Clin. Pathol. , vol.23 , pp. 228-231
    • Meyer, D.1    Larrieu, M.-J.2
  • 24
    • 44449119515 scopus 로고
    • The defect in von Willebrand's disease
    • Johnson S.A., and Seegers W.H. (Eds), Charles C. Thomas Publisher, Springfield, Illinois, USA
    • Stormorken H. The defect in von Willebrand's disease. In: Johnson S.A., and Seegers W.H. (Eds). Physiology of Hemostasis and Thrombosis (1967), Charles C. Thomas Publisher, Springfield, Illinois, USA 179-200
    • (1967) Physiology of Hemostasis and Thrombosis , pp. 179-200
    • Stormorken, H.1
  • 25
    • 0016180637 scopus 로고    scopus 로고
    • Hovig, T. and Stormorken, H. (1974) Ultrastructural studies on the platelet plug formation in bleeding time wounds from normal individuals and patients with von Willebrand's disease. Acta Path. Microbiol. Scand., Sect. A, Suppl. 248: 105-122.
    • Hovig, T. and Stormorken, H. (1974) Ultrastructural studies on the platelet plug formation in bleeding time wounds from normal individuals and patients with von Willebrand's disease. Acta Path. Microbiol. Scand., Sect. A, Suppl. 248: 105-122.
  • 26
    • 0014976247 scopus 로고
    • Immunologic differentiation of classic hemophilia (factor VIII deficiency) and von Willebrand's disease
    • Zimmerman T.S., Ratnoff O.D., and Powell A.E. Immunologic differentiation of classic hemophilia (factor VIII deficiency) and von Willebrand's disease. J. Clin. Invest. 50 (1971) 244-254
    • (1971) J. Clin. Invest. , vol.50 , pp. 244-254
    • Zimmerman, T.S.1    Ratnoff, O.D.2    Powell, A.E.3
  • 27
    • 0015713057 scopus 로고
    • The precence and reactions of high and lower-molecular-weight procoagulant factor VIII in the plasma of patients with von Willebrand's disease after treatment: significance for a structural hypothesis for factor VIII
    • Bloom A.L., Peake I.R., and Giddings J.C. The precence and reactions of high and lower-molecular-weight procoagulant factor VIII in the plasma of patients with von Willebrand's disease after treatment: significance for a structural hypothesis for factor VIII. Thromb. Res. 3 (1973) 389-404
    • (1973) Thromb. Res. , vol.3 , pp. 389-404
    • Bloom, A.L.1    Peake, I.R.2    Giddings, J.C.3
  • 28
    • 0015819659 scopus 로고
    • Factor VIII coagulant activity and factor VIII-like antigen: independent molecular entities
    • Zimmerman T.S., and Edgington T.S. Factor VIII coagulant activity and factor VIII-like antigen: independent molecular entities. J. Exp. Med. 138 (1973) 1015-1020
    • (1973) J. Exp. Med. , vol.138 , pp. 1015-1020
    • Zimmerman, T.S.1    Edgington, T.S.2
  • 29
    • 0015530864 scopus 로고
    • Antihaemophilic factor: separation of an active fragment following dissociation by salts or detergents
    • Owen W.G., and Wagner R.H. Antihaemophilic factor: separation of an active fragment following dissociation by salts or detergents. Thromb. Diath. Haemorrh. 27 (1972) 502-515
    • (1972) Thromb. Diath. Haemorrh. , vol.27 , pp. 502-515
    • Owen, W.G.1    Wagner, R.H.2
  • 31
    • 0011694667 scopus 로고
    • Synthesis of von Willebrand factor by cultured human endothelial cells
    • Jaffe E.A., Hoyer L.W., and Nachman R.L. Synthesis of von Willebrand factor by cultured human endothelial cells. Proc. Nat. Acad. Sci. U.S.A. 71 (1974) 1906-1909
    • (1974) Proc. Nat. Acad. Sci. U.S.A. , vol.71 , pp. 1906-1909
    • Jaffe, E.A.1    Hoyer, L.W.2    Nachman, R.L.3
  • 32
    • 0017658776 scopus 로고
    • Synthesis of factor VIII antigen by cultured guinea pig megakaryocytes
    • Nachman R., Levine R., and Jaffe E.A. Synthesis of factor VIII antigen by cultured guinea pig megakaryocytes. J. Clin. Invest. 60 (1977) 914-921
    • (1977) J. Clin. Invest. , vol.60 , pp. 914-921
    • Nachman, R.1    Levine, R.2    Jaffe, E.A.3
  • 33
    • 0018150726 scopus 로고
    • Purification of factor VIII:C by antigen-antibody chromatography
    • Holmberg L., and Ljung R. Purification of factor VIII:C by antigen-antibody chromatography. Thromb. Res. 12 (1978) 667-675
    • (1978) Thromb. Res. , vol.12 , pp. 667-675
    • Holmberg, L.1    Ljung, R.2
  • 34
    • 0018345568 scopus 로고
    • The properties of factor VIII coagulant activity prepared by immunoadsorbent chromatography
    • Tuddenham E.G.D., Trabold N.C., Collins J.A., and Hoyer L.W. The properties of factor VIII coagulant activity prepared by immunoadsorbent chromatography. J. Lab. Clin. Med. 93 (1979) 40-53
    • (1979) J. Lab. Clin. Med. , vol.93 , pp. 40-53
    • Tuddenham, E.G.D.1    Trabold, N.C.2    Collins, J.A.3    Hoyer, L.W.4
  • 35
    • 0018860405 scopus 로고
    • Preparation and properties of bovine factor VIII (Antihemophilic factor)
    • Vehar G.A., and Davie E.W. Preparation and properties of bovine factor VIII (Antihemophilic factor). Biochemistry 19 (1980) 401-410
    • (1980) Biochemistry , vol.19 , pp. 401-410
    • Vehar, G.A.1    Davie, E.W.2
  • 36
    • 0020440981 scopus 로고
    • Purification and characterization of a highly purified human factor VIII consisting of a single type of polypeptide chain
    • Fay P.J., Chavin S.I., Schroeder D., Young F.E., and Marder V.J. Purification and characterization of a highly purified human factor VIII consisting of a single type of polypeptide chain. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 7200-7204
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 7200-7204
    • Fay, P.J.1    Chavin, S.I.2    Schroeder, D.3    Young, F.E.4    Marder, V.J.5
  • 37
    • 0015247223 scopus 로고
    • Ristocetin - a new tool in the investigation of platelet aggregation
    • Howard M.A., and Firkin B.G. Ristocetin - a new tool in the investigation of platelet aggregation. Thromb. Diath. Haemorrh. 26 (1971) 362-369
    • (1971) Thromb. Diath. Haemorrh. , vol.26 , pp. 362-369
    • Howard, M.A.1    Firkin, B.G.2
  • 38
    • 0018123566 scopus 로고
    • Disulfide bonds and the quaternary structure of Factor VIII/von Willebrand factor
    • Counts R.B., Paskell S.L., and Elgee S.K. Disulfide bonds and the quaternary structure of Factor VIII/von Willebrand factor. J. Clin. Invest. 62 (1978) 702-709
    • (1978) J. Clin. Invest. , vol.62 , pp. 702-709
    • Counts, R.B.1    Paskell, S.L.2    Elgee, S.K.3
  • 39
    • 0018888146 scopus 로고
    • Multimeric structure of factorVIII/von Willebrand factor in von Willebrand's disease
    • Meyer D., Obert B., Pietu G., Lavergne J.M., and Zimmerman T.S. Multimeric structure of factorVIII/von Willebrand factor in von Willebrand's disease. J. Lab. Clin. Med. 95 (1980) 590-602
    • (1980) J. Lab. Clin. Med. , vol.95 , pp. 590-602
    • Meyer, D.1    Obert, B.2    Pietu, G.3    Lavergne, J.M.4    Zimmerman, T.S.5
  • 40
    • 0021683006 scopus 로고
    • Biosynthesis of von Willebrand protein by human endothelial cells: processing steps and the intracellular localization
    • Wagner D.D., and Marder V.J. Biosynthesis of von Willebrand protein by human endothelial cells: processing steps and the intracellular localization. J. Cell Biol. 99 (1984) 2123-2130
    • (1984) J. Cell Biol. , vol.99 , pp. 2123-2130
    • Wagner, D.D.1    Marder, V.J.2
  • 41
    • 0021131281 scopus 로고
    • Purification of the factor VIII complex
    • Thorell L., and Blombäck B. Purification of the factor VIII complex. Thromb. Res. 35 (1984) 431-450
    • (1984) Thromb. Res. , vol.35 , pp. 431-450
    • Thorell, L.1    Blombäck, B.2
  • 42
    • 0020608365 scopus 로고
    • An in vivo study of a new factor VIII high purity preparation
    • Thorell L., Blombäck M., and Blombäck B. An in vivo study of a new factor VIII high purity preparation. Thromb. Res. 31 (1983) 375-385
    • (1983) Thromb. Res. , vol.31 , pp. 375-385
    • Thorell, L.1    Blombäck, M.2    Blombäck, B.3
  • 47
    • 0022764677 scopus 로고
    • Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit
    • Verweij C.L., Diergaarde P.J., Hart M., and Pannekoek H. Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit. EMBO J. 5 (1986) 1839-1847
    • (1986) EMBO J. , vol.5 , pp. 1839-1847
    • Verweij, C.L.1    Diergaarde, P.J.2    Hart, M.3    Pannekoek, H.4
  • 48
    • 0017889090 scopus 로고
    • von Willebrand's disease antigen II: a new plasma and platelet antigen deficient in severe von Willebrand's disease
    • Montgomery R.R., and Zimmerman T.S. von Willebrand's disease antigen II: a new plasma and platelet antigen deficient in severe von Willebrand's disease. J. Clin. Invest. 61 (1978) 1498-1507
    • (1978) J. Clin. Invest. , vol.61 , pp. 1498-1507
    • Montgomery, R.R.1    Zimmerman, T.S.2
  • 49
    • 0022475523 scopus 로고
    • Human von Willebrand factor: a multivalent protein composed of identical subunits
    • Chopek M.W., Girma J.-P., Fujikawa K., Davie E.W., and Titani K. Human von Willebrand factor: a multivalent protein composed of identical subunits. Biochemistry 25 (1986) 3146-3155
    • (1986) Biochemistry , vol.25 , pp. 3146-3155
    • Chopek, M.W.1    Girma, J.-P.2    Fujikawa, K.3    Davie, E.W.4    Titani, K.5
  • 50
    • 0022547632 scopus 로고
    • Limited proteolysis of human von Willebrand factor by Staphylococcus aureus V-8 protease: isolation and partial characterization of a platelet-binding domain
    • Girma J.-P., Chopek M.W., Titani K., and Davie E.W. Limited proteolysis of human von Willebrand factor by Staphylococcus aureus V-8 protease: isolation and partial characterization of a platelet-binding domain. Biochemistry 25 (1986) 3156-3163
    • (1986) Biochemistry , vol.25 , pp. 3156-3163
    • Girma, J.-P.1    Chopek, M.W.2    Titani, K.3    Davie, E.W.4
  • 52
    • 0015906103 scopus 로고
    • Aggregation of human platelets by bovine or human factor VIII: role of carbohydrate side chains
    • Vermylen J., Donati M.B., de Gaetano G., and Verstraete M. Aggregation of human platelets by bovine or human factor VIII: role of carbohydrate side chains. Nature 244 (1973) 167-168
    • (1973) Nature , vol.244 , pp. 167-168
    • Vermylen, J.1    Donati, M.B.2    de Gaetano, G.3    Verstraete, M.4
  • 53
    • 0034682789 scopus 로고    scopus 로고
    • Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor
    • Katsumi A., Tuley E.A., Bodó I., and Sadler J.E. Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor. J. Biol. Chem. 275 (2000) 25585-25594
    • (2000) J. Biol. Chem. , vol.275 , pp. 25585-25594
    • Katsumi, A.1    Tuley, E.A.2    Bodó, I.3    Sadler, J.E.4
  • 54
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willeband factor A1 domain and implications for the binding of platelet glycoprotein Ib
    • Emsley J., Cruz M., Handin R., and Liddington R. Crystal structure of the von Willeband factor A1 domain and implications for the binding of platelet glycoprotein Ib. J. Biol. Chem. 273 (1998) 10396-10401
    • (1998) J. Biol. Chem. , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Handin, R.3    Liddington, R.4
  • 55
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler J.E. Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 67 (1998) 395-424
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 57
    • 0022999369 scopus 로고
    • Substructure of human von Willebrand factor: proteolysis by V8 and characterization of two functional domains
    • Fretto L.J., Fowler W.E., McCaslin D.R., Erickson H.P., and McKee P.A. Substructure of human von Willebrand factor: proteolysis by V8 and characterization of two functional domains. J. Biol. Chem. 261 (1986) 15679-15689
    • (1986) J. Biol. Chem. , vol.261 , pp. 15679-15689
    • Fretto, L.J.1    Fowler, W.E.2    McCaslin, D.R.3    Erickson, H.P.4    McKee, P.A.5
  • 58
    • 0023149024 scopus 로고
    • Topology and order of formation of interchain disulfide bonds in von Willebrand factor
    • Wagner D.D., Lawrence S.O., Ohlsson-Wilhelm B.M., Fay P.J., and Marder V.J. Topology and order of formation of interchain disulfide bonds in von Willebrand factor. Blood 69 (1987) 27-32
    • (1987) Blood , vol.69 , pp. 27-32
    • Wagner, D.D.1    Lawrence, S.O.2    Ohlsson-Wilhelm, B.M.3    Fay, P.J.4    Marder, V.J.5
  • 60
    • 0025119629 scopus 로고
    • Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib
    • Girma J.P., Takahashi Y., Yoshioka A., Diaz J., and Meyer D. Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib. Thromb. Haemostasis 64 (1990) 326-332
    • (1990) Thromb. Haemostasis , vol.64 , pp. 326-332
    • Girma, J.P.1    Takahashi, Y.2    Yoshioka, A.3    Diaz, J.4    Meyer, D.5
  • 61
    • 0345427143 scopus 로고
    • Expression of variant von Willebrand factor (vWF) cDNA in heterologous cells: requirement of the pro-polypeptide in vWF multimer formation
    • Verweij C.L., Hart M., and Pannekoek H. Expression of variant von Willebrand factor (vWF) cDNA in heterologous cells: requirement of the pro-polypeptide in vWF multimer formation. EMBO J. 6 (1987) 2885-2890
    • (1987) EMBO J. , vol.6 , pp. 2885-2890
    • Verweij, C.L.1    Hart, M.2    Pannekoek, H.3
  • 62
    • 0025748557 scopus 로고
    • The role of von Willebrand factor multimers and propeptide cleavage in binding and stabilization of factor VIII
    • Wise R.J., Dorner A.J., Krane M., Pittman D.D., and Kaufman R.J. The role of von Willebrand factor multimers and propeptide cleavage in binding and stabilization of factor VIII. J. Biol. Chem. 266 (1991) 21948-21955
    • (1991) J. Biol. Chem. , vol.266 , pp. 21948-21955
    • Wise, R.J.1    Dorner, A.J.2    Krane, M.3    Pittman, D.D.4    Kaufman, R.J.5
  • 63
    • 0022415284 scopus 로고
    • Solution studies of the quaternary structure and assembly of human von Willebrand factor
    • Loscalzo J., Fisch M., and Handin1 R.I. Solution studies of the quaternary structure and assembly of human von Willebrand factor. Biochemistry 24 (1985) 4468-4475
    • (1985) Biochemistry , vol.24 , pp. 4468-4475
    • Loscalzo, J.1    Fisch, M.2    Handin1, R.I.3
  • 64
    • 0020355947 scopus 로고
    • Immunolocalization of von Willebrand Protein in Weibel-Palade bodies of human endothelial cells
    • Wagner D.D., Olmsted J.B., and Marder V.J. Immunolocalization of von Willebrand Protein in Weibel-Palade bodies of human endothelial cells. J. Cell Biol. 95 (1982) 355-360
    • (1982) J. Cell Biol. , vol.95 , pp. 355-360
    • Wagner, D.D.1    Olmsted, J.B.2    Marder, V.J.3
  • 66
    • 0017754787 scopus 로고
    • Stabilization of factor VIII in plasma by the von Willebrand factor
    • Weiss H.J., Sussman I.I., and Hoyer L.W. Stabilization of factor VIII in plasma by the von Willebrand factor. J. Clin. Invest. 60 (1977) 390-404
    • (1977) J. Clin. Invest. , vol.60 , pp. 390-404
    • Weiss, H.J.1    Sussman, I.I.2    Hoyer, L.W.3
  • 67
    • 0019958451 scopus 로고
    • Response to infusions of polyelectrolyte fractionated human factor VIII concentrate in human haemophilia A and von Willebrand's disease
    • Tuddenham E.G.D., Lane R.S., Rotblat F., Johnson A.J., Snape T.J., Middleton S., and Kernoff P.B.A. Response to infusions of polyelectrolyte fractionated human factor VIII concentrate in human haemophilia A and von Willebrand's disease. Brit. J. Haematol. 52 (1982) 259-267
    • (1982) Brit. J. Haematol. , vol.52 , pp. 259-267
    • Tuddenham, E.G.D.1    Lane, R.S.2    Rotblat, F.3    Johnson, A.J.4    Snape, T.J.5    Middleton, S.6    Kernoff, P.B.A.7
  • 68
    • 0022296676 scopus 로고
    • Purified human factor VIII procoagulant protein: comparative hemostatic response after infusions into hemophilic and von Willebrand disease dogs
    • Brinkhous K.M., Sandberg H., Garris J.B., Mattson C., Palm M., Griggs T., and Read M.S. Purified human factor VIII procoagulant protein: comparative hemostatic response after infusions into hemophilic and von Willebrand disease dogs. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 8752-8756
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 8752-8756
    • Brinkhous, K.M.1    Sandberg, H.2    Garris, J.B.3    Mattson, C.4    Palm, M.5    Griggs, T.6    Read, M.S.7
  • 69
    • 0023217139 scopus 로고
    • A major factor VIII binding domain resides within the amino-terminal 272 amino acid residues of von Willebrand factor
    • Foster P.A., Fulcher C.A., Marti T., Titani K., and Zimmerman T.S. A major factor VIII binding domain resides within the amino-terminal 272 amino acid residues of von Willebrand factor. J. Biol. Chem. 262 (1987) 8443-8446
    • (1987) J. Biol. Chem. , vol.262 , pp. 8443-8446
    • Foster, P.A.1    Fulcher, C.A.2    Marti, T.3    Titani, K.4    Zimmerman, T.S.5
  • 71
    • 0025991461 scopus 로고
    • The effect of plasma von Villebrand factor on the binding of human factor VIII to thrombin-activated human platelets
    • Nesheim M., Pittman D.D., Giles A.R., Fass D.N., Wang J.H., Slonosky D., and Kaufman R.J. The effect of plasma von Villebrand factor on the binding of human factor VIII to thrombin-activated human platelets. J. Biol. Chem. 266 (1991) 17815-17820
    • (1991) J. Biol. Chem. , vol.266 , 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
  • 72
    • 0018118813 scopus 로고
    • Effect of shear rate on platelet interaction with subendothelium in citrated and native blood. I. Shear rate-dependent decrease of adhesion in von Willebrand's disease and the Bernard-Soulier syndrome
    • Weiss H.J., Turitto V.T., and Baumgartner H.R. Effect of shear rate on platelet interaction with subendothelium in citrated and native blood. I. Shear rate-dependent decrease of adhesion in von Willebrand's disease and the Bernard-Soulier syndrome. J. Lab. Clin. Med. 92 (1978) 750-764
    • (1978) J. Lab. Clin. Med. , vol.92 , pp. 750-764
    • Weiss, H.J.1    Turitto, V.T.2    Baumgartner, H.R.3
  • 73
    • 0018890631 scopus 로고
    • Shear rate dependent inhibition of platelet adhesion and aggregation on collagen surfaces by antibodies to human factor VIII/von Willebrand factor
    • Baumgartner H.R., Tschopp T.B., and Meyer D. Shear rate dependent inhibition of platelet adhesion and aggregation on collagen surfaces by antibodies to human factor VIII/von Willebrand factor. Br. J. Haematol. 44 (1980) 127-139
    • (1980) Br. J. Haematol. , vol.44 , pp. 127-139
    • Baumgartner, H.R.1    Tschopp, T.B.2    Meyer, D.3
  • 74
    • 0017357271 scopus 로고
    • Platelet interaction with collagen fibrils in flowing blood. II. Impaired adhesion-aggregation in bleeding disorders: a comparison with subendothelium
    • Baumgartner H.R., Tschopp T.B., and Weiss H.J. Platelet interaction with collagen fibrils in flowing blood. II. Impaired adhesion-aggregation in bleeding disorders: a comparison with subendothelium. Thromb. Haemostasis 37 (1977) 17-28
    • (1977) Thromb. Haemostasis , vol.37 , pp. 17-28
    • Baumgartner, H.R.1    Tschopp, T.B.2    Weiss, H.J.3
  • 75
    • 0018858006 scopus 로고
    • von Willebrand factor dependent platelet aggregation and adsorption of factor VIII related antigen by collagen
    • Nyman D. von Willebrand factor dependent platelet aggregation and adsorption of factor VIII related antigen by collagen. Thromb. Res. 17 (1980) 209-214
    • (1980) Thromb. Res. , vol.17 , pp. 209-214
    • Nyman, D.1
  • 76
    • 0018770590 scopus 로고
    • Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-von Willebrand factor bound to the subendothelium
    • Sakariassen K.S., Bolhuis P.A., and Sixma J.J. Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-von Willebrand factor bound to the subendothelium. Nature 279 (1979) 636-638
    • (1979) Nature , vol.279 , pp. 636-638
    • Sakariassen, K.S.1    Bolhuis, P.A.2    Sixma, J.J.3
  • 77
    • 0018827228 scopus 로고
    • Localization of factor VIII-related antigen in human vascular subendothelium
    • Rand J.H., Sussman I.I., Gordon R.E., Chu S.V., and Solomon V. Localization of factor VIII-related antigen in human vascular subendothelium. Blood 55 (1980) 752-756
    • (1980) Blood , vol.55 , pp. 752-756
    • Rand, J.H.1    Sussman, I.I.2    Gordon, R.E.3    Chu, S.V.4    Solomon, V.5
  • 79
    • 0022445644 scopus 로고
    • Mediation of platelet adhesion to fibrillar collagen in flowing blood by a proteolytic fragment of human von Willebrand factor
    • Sakariassen K.S., Fressinaud E., Girma J.-P., Baumgartner H.R., and Meyer D. Mediation of platelet adhesion to fibrillar collagen in flowing blood by a proteolytic fragment of human von Willebrand factor. Blood 67 (1986) 1515-1518
    • (1986) Blood , vol.67 , pp. 1515-1518
    • Sakariassen, K.S.1    Fressinaud, E.2    Girma, J.-P.3    Baumgartner, H.R.4    Meyer, D.5
  • 80
    • 0037039439 scopus 로고    scopus 로고
    • Functional self-association of von Willebrand factor during platelet adhesion under flow
    • Savage B., Sixma J.J., and Ruggeri Z.M. Functional self-association of von Willebrand factor during platelet adhesion under flow. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 425-430
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 425-430
    • Savage, B.1    Sixma, J.J.2    Ruggeri, Z.M.3
  • 81
    • 0017293424 scopus 로고
    • Platelet membrane glycoproteins implicated in ristocetin-induced aggregation: studies of the proteins on platelets from patients with Bernard-Soulier syndrome and von Willebrand's disease
    • Jenkins C.S.P., Phillips D.R., Clemetson K.J., Meyer D., Larrieu M.-J., and Lüscher E.F. Platelet membrane glycoproteins implicated in ristocetin-induced aggregation: studies of the proteins on platelets from patients with Bernard-Soulier syndrome and von Willebrand's disease. J. Clin. Invest. 57 (1976) 112-124
    • (1976) J. Clin. Invest. , vol.57 , pp. 112-124
    • Jenkins, C.S.P.1    Phillips, D.R.2    Clemetson, K.J.3    Meyer, D.4    Larrieu, M.-J.5    Lüscher, E.F.6
  • 82
    • 0017137264 scopus 로고
    • Platelet glycocalicin. II. Purification and characterization
    • Okumura T., Lombart C., and Jamieson G.A. Platelet glycocalicin. II. Purification and characterization. J. Biol. Chem. 251 (1976) 5950-5955
    • (1976) J. Biol. Chem. , vol.251 , pp. 5950-5955
    • Okumura, T.1    Lombart, C.2    Jamieson, G.A.3
  • 83
    • 0018863543 scopus 로고
    • Platelet glycocalicin: its membrane association and solubilization in aqueous media
    • Solum N.O., Hagen I., Filion-Myklebust C., and Stabaek T. Platelet glycocalicin: its membrane association and solubilization in aqueous media. Biochim. Biophys. Acta 597 (1980) 235-246
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 235-246
    • Solum, N.O.1    Hagen, I.2    Filion-Myklebust, C.3    Stabaek, T.4
  • 84
    • 0019568384 scopus 로고
    • Relationship between glycocalicin and glycoprotein Ib of human platelets
    • Clemetson K.J., Naim H.Y., and Lüscher E.F. Relationship between glycocalicin and glycoprotein Ib of human platelets. Proc. Natl. Acad. Sci. U.S.A. 78 (1981) 2712-2716
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2712-2716
    • Clemetson, K.J.1    Naim, H.Y.2    Lüscher, E.F.3
  • 86
    • 0022495893 scopus 로고
    • The role of platelet membrane glycoproteins Ib and IIb+IIIa in platelet adherence to human artery subendothelium
    • Sakariassen K.S., Nievelstein P.F.E.M., Coller B.S., and Sixma J.J. The role of platelet membrane glycoproteins Ib and IIb+IIIa in platelet adherence to human artery subendothelium. Br. J. Haematol. 63 (1986) 681-691
    • (1986) Br. J. Haematol. , vol.63 , pp. 681-691
    • Sakariassen, K.S.1    Nievelstein, P.F.E.M.2    Coller, B.S.3    Sixma, J.J.4
  • 87
    • 0021717485 scopus 로고
    • Platelet interaction with rabbit subendothelium in von Willebrand's disease: altered thrombus formation distinct from defective platelet adhesion
    • Turitto V.T., Weiss H.J., and Baumgartner H.R. Platelet interaction with rabbit subendothelium in von Willebrand's disease: altered thrombus formation distinct from defective platelet adhesion. J. Clin. Invest. 74 (1984) 1730-1740
    • (1984) J. Clin. Invest. , vol.74 , pp. 1730-1740
    • Turitto, V.T.1    Weiss, H.J.2    Baumgartner, H.R.3
  • 90
    • 0032483550 scopus 로고    scopus 로고
    • Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • Savage B., Almus-Jacobs F., and Ruggeri Z.M. Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell 94 (1998) 657-666
    • (1998) Cell , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 91
    • 0021206578 scopus 로고
    • Inhibition of von Willebrand factor-platelet interaction by fibrinogen
    • Piétu G., Cherel G., Margurie G., and Meyer D. Inhibition of von Willebrand factor-platelet interaction by fibrinogen. Nature 308 (1984) 648-649
    • (1984) Nature , vol.308 , pp. 648-649
    • Piétu, G.1    Cherel, G.2    Margurie, G.3    Meyer, D.4
  • 92
    • 0034662164 scopus 로고    scopus 로고
    • Homozygous truncation of the fibrinogen Aα chain within the coiled coil causes congenital afibrinogenemia
    • Fellowes A.P., Brennan S.O., Holme R., Stormorken H., Brosstad F.R., and George P.M. Homozygous truncation of the fibrinogen Aα chain within the coiled coil causes congenital afibrinogenemia. Blood 96 (2000) 773-775
    • (2000) Blood , vol.96 , pp. 773-775
    • Fellowes, A.P.1    Brennan, S.O.2    Holme, R.3    Stormorken, H.4    Brosstad, F.R.5    George, P.M.6
  • 93
    • 0015693918 scopus 로고
    • Factor VIII on the vascular intima: possible importance in haemostasis and thrombosis
    • Bloom A.L., Giddings J.C., and Wilks C.J. Factor VIII on the vascular intima: possible importance in haemostasis and thrombosis. Nature New Biol. 241 (1973) 217-219
    • (1973) Nature New Biol. , vol.241 , pp. 217-219
    • Bloom, A.L.1    Giddings, J.C.2    Wilks, C.J.3
  • 95
    • 0034669991 scopus 로고    scopus 로고
    • Platelets adhere to and translocate on von Willebrand factor presented by endothelium in stimulated veins
    • André P., Denis C.V., Ware J., Saffaripour S., Hynes R.O., Ruggeri Z.M., and Wagner D.D. Platelets adhere to and translocate on von Willebrand factor presented by endothelium in stimulated veins. Blood 96 (2000) 3322-3328
    • (2000) Blood , vol.96 , pp. 3322-3328
    • André, P.1    Denis, C.V.2    Ware, J.3    Saffaripour, S.4    Hynes, R.O.5    Ruggeri, Z.M.6    Wagner, D.D.7
  • 96
    • 0026806511 scopus 로고
    • Localization and characterization of a heparin binding domain peptide of human von Willebrand factor
    • Sobel M., Soler D.F., Kermode J.C., and Harris R.B. Localization and characterization of a heparin binding domain peptide of human von Willebrand factor. J. Biol. Chem. 267 (1992) 8857-8862
    • (1992) J. Biol. Chem. , vol.267 , pp. 8857-8862
    • Sobel, M.1    Soler, D.F.2    Kermode, J.C.3    Harris, R.B.4
  • 97
    • 0037188383 scopus 로고    scopus 로고
    • Two clusters of charged residues located in the electropositive face of Von Willebrand factor A1 domain are essential for heparin binding
    • Rastegar-Lari G., Villoutreix B.O., Ribba A.-S., Legendre P., Meyer D., and Baruch D. Two clusters of charged residues located in the electropositive face of Von Willebrand factor A1 domain are essential for heparin binding. Biochemistry 41 (2002) 6668-6678
    • (2002) Biochemistry , vol.41 , pp. 6668-6678
    • Rastegar-Lari, G.1    Villoutreix, B.O.2    Ribba, A.-S.3    Legendre, P.4    Meyer, D.5    Baruch, D.6
  • 98
    • 0027185452 scopus 로고
    • Mutations of von Willebrand factor gene in families with von Willebrand disease in the Åland Islands
    • Zhang Z.P., Blombäck M., Nyman D., and Anvret M. Mutations of von Willebrand factor gene in families with von Willebrand disease in the Åland Islands. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 7937-7940
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7937-7940
    • Zhang, Z.P.1    Blombäck, M.2    Nyman, D.3    Anvret, M.4
  • 99
    • 0029135286 scopus 로고
    • Effects of the mutant von Willebrand factor gene in von Willebrand disease
    • Zhang Z., Lindstedt M., Blombäck M., and Anvret M. Effects of the mutant von Willebrand factor gene in von Willebrand disease. Hum. Genet. 96 (1995) 388-394
    • (1995) Hum. Genet. , vol.96 , pp. 388-394
    • Zhang, Z.1    Lindstedt, M.2    Blombäck, M.3    Anvret, M.4
  • 101
    • 14544302314 scopus 로고    scopus 로고
    • New concepts in von Willwbrand disease
    • Sadler J.E. New concepts in von Willwbrand disease. Annu. Rev. Med. 56 (2005) 173-191
    • (2005) Annu. Rev. Med. , vol.56 , pp. 173-191
    • Sadler, J.E.1
  • 102
    • 0016147023 scopus 로고
    • Inherited variants of factor VIII-related protein in von Willebrand's disease
    • Peake I.R., Bloom A.L., and Giddings J.C. Inherited variants of factor VIII-related protein in von Willebrand's disease. N. Engl. J. Med. 291 (1974) 113-117
    • (1974) N. Engl. J. Med. , vol.291 , pp. 113-117
    • Peake, I.R.1    Bloom, A.L.2    Giddings, J.C.3
  • 103
    • 0022517442 scopus 로고
    • Subunit composition of plasma von Willebrand factor. Cleavage is present in nomal individuals, increased in IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individual oligomers (Types IIC, IID and IIE)
    • Zimmerman T.S., Dent J.A., Ruggeri Z.M., and Nannini L.H. Subunit composition of plasma von Willebrand factor. Cleavage is present in nomal individuals, increased in IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individual oligomers (Types IIC, IID and IIE). J. Clin Invest. 77 (1986) 947-951
    • (1986) J. Clin Invest. , vol.77 , pp. 947-951
    • Zimmerman, T.S.1    Dent, J.A.2    Ruggeri, Z.M.3    Nannini, L.H.4
  • 104
    • 0030980679 scopus 로고    scopus 로고
    • Proteolytic cleavage of recombinant Type 2A von Willebrand factor mutants R834W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-I
    • Tsai H.-M., Sussman I.I., Ginsburg D., Lankhof H., Sixma J.J., and Nagel R.L. Proteolytic cleavage of recombinant Type 2A von Willebrand factor mutants R834W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-I. Blood 89 (1997) 1954-1962
    • (1997) Blood , vol.89 , pp. 1954-1962
    • Tsai, H.-M.1    Sussman, I.I.2    Ginsburg, D.3    Lankhof, H.4    Sixma, J.J.5    Nagel, R.L.6
  • 105
    • 0018871618 scopus 로고
    • Heightened interaction between platelets and factor VIII/von Willebrand factor in a new subtype of von Willebrand's disease
    • Ruggeri Z.M., Pareti F.I., Mannucci P.M., Ciavarella N., and Zimmerman T.S. Heightened interaction between platelets and factor VIII/von Willebrand factor in a new subtype of von Willebrand's disease. N. Engl. J. Med. 302 (1980) 1047-1051
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1047-1051
    • Ruggeri, Z.M.1    Pareti, F.I.2    Mannucci, P.M.3    Ciavarella, N.4    Zimmerman, T.S.5
  • 106
    • 0027258360 scopus 로고
    • von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure
    • Holmberg L., Dent J.A., Schneppenheim R., Budde U., Ware J., and Ruggeri Z.M. von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure. J. Clin. Invest. 91 (1993) 2169-2177
    • (1993) J. Clin. Invest. , vol.91 , pp. 2169-2177
    • Holmberg, L.1    Dent, J.A.2    Schneppenheim, R.3    Budde, U.4    Ware, J.5    Ruggeri, Z.M.6
  • 108
    • 0024425034 scopus 로고
    • New variant of von Willebrand disease with defective binding to factor VIII
    • Nishino M., Girma J.-P., Rothschild C., Fressinaud E., and Meyer D. New variant of von Willebrand disease with defective binding to factor VIII. Blood 74 (1989) 1591-1599
    • (1989) Blood , vol.74 , pp. 1591-1599
    • Nishino, M.1    Girma, J.-P.2    Rothschild, C.3    Fressinaud, E.4    Meyer, D.5
  • 109
    • 0037328171 scopus 로고    scopus 로고
    • Hilbert, L., Jorieux, S., Proulle, V., Favier, R., Goudemand, J., Parquet, A., Meyer, D., Fressinaud, E., Mazurier, C. and the INSERM network on molecular abnormalities in von Willebrand disease. (2003) Two novel mutations, Q1053 H and C1060R, located in the D3 domain of von Willebrand factor, are responsible for decreased F VIII-binding capacity. Br. J. Haematol. 120, 627-632.
    • Hilbert, L., Jorieux, S., Proulle, V., Favier, R., Goudemand, J., Parquet, A., Meyer, D., Fressinaud, E., Mazurier, C. and the INSERM network on molecular abnormalities in von Willebrand disease. (2003) Two novel mutations, Q1053 H and C1060R, located in the D3 domain of von Willebrand factor, are responsible for decreased F VIII-binding capacity. Br. J. Haematol. 120, 627-632.
  • 110
    • 0002978048 scopus 로고
    • Hyaline thrombosis of the terminal arterioles and capillaries: a hitherto undescribed disease
    • Moschcowitz E. Hyaline thrombosis of the terminal arterioles and capillaries: a hitherto undescribed disease. Proc. New York Pathol. Soc. 24 (1924) 21-24
    • (1924) Proc. New York Pathol. Soc. , vol.24 , pp. 21-24
    • Moschcowitz, E.1
  • 111
    • 0002041785 scopus 로고
    • An acute febrile anemia and thrombocytopenic purpura with diffuse platelet thromboses of capillaries and arterioles
    • Baehr G., Klemperer P., and Schifrin A. An acute febrile anemia and thrombocytopenic purpura with diffuse platelet thromboses of capillaries and arterioles. Trans. Assoc. Am. Physician 65 (1936) 43-58
    • (1936) Trans. Assoc. Am. Physician , vol.65 , pp. 43-58
    • Baehr, G.1    Klemperer, P.2    Schifrin, A.3
  • 112
    • 0015818285 scopus 로고
    • Thrombotic thrombocytopenic purpura: report of a case with disseminated intravascular platelet aggregation
    • Neame P.B., Lechago J., Ling E.T., and Koval A. Thrombotic thrombocytopenic purpura: report of a case with disseminated intravascular platelet aggregation. Blood 42 (1973) 805-814
    • (1973) Blood , vol.42 , pp. 805-814
    • Neame, P.B.1    Lechago, J.2    Ling, E.T.3    Koval, A.4
  • 113
    • 0021858462 scopus 로고
    • Immunohistochemistry of vascular lesion in thrombotic thrombocytopenic purpura, with special reference to factor VIII related antigen
    • Asada Y., Sumiyoshi A., Hayashi T., Suzumiya J., and Kaketani K. Immunohistochemistry of vascular lesion in thrombotic thrombocytopenic purpura, with special reference to factor VIII related antigen. Thromb. Res. 38 (1985) 469-479
    • (1985) Thromb. Res. , vol.38 , pp. 469-479
    • Asada, Y.1    Sumiyoshi, A.2    Hayashi, T.3    Suzumiya, J.4    Kaketani, K.5
  • 115
    • 0024734977 scopus 로고
    • Abnormalities of von Willebrand factor multimers in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome
    • Moake J.L., and McPherson P.D. Abnormalities of von Willebrand factor multimers in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome. Am. J. Med. 87 (1989) 9N-15N
    • (1989) Am. J. Med. , vol.87
    • Moake, J.L.1    McPherson, P.D.2
  • 116
    • 0029043071 scopus 로고
    • Thrombotic thrombocytopenia induced in dogs and pigs: the role of plasma and platelet vWF in animal models of thrombotic thrombocytopenic purpura
    • Sanders Jr. W.E., Reddick R.L., Nichols T.C., Brinkhous K.M., and Read M.S. Thrombotic thrombocytopenia induced in dogs and pigs: the role of plasma and platelet vWF in animal models of thrombotic thrombocytopenic purpura. Arterioscl. Thromb. Vas. Biol. 15 (1995) 793-800
    • (1995) Arterioscl. Thromb. Vas. Biol. , vol.15 , pp. 793-800
    • Sanders Jr., W.E.1    Reddick, R.L.2    Nichols, T.C.3    Brinkhous, K.M.4    Read, M.S.5
  • 117
    • 0022852282 scopus 로고
    • Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation
    • Moake J.L., Turner N.A., Stathopoulos N.A., Nolasco L.H., and Hellums J.D. Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation. J. Clin. Invest. 78 (1986) 1456-1461
    • (1986) J. Clin. Invest. , vol.78 , pp. 1456-1461
    • Moake, J.L.1    Turner, N.A.2    Stathopoulos, N.A.3    Nolasco, L.H.4    Hellums, J.D.5
  • 118
    • 0024356269 scopus 로고
    • Multimeric composition of endothelial cell-derived von Willebrand factor
    • Tsai H.-M., Nagel R.L., Hatcher V.B., and Sussman I.I. Multimeric composition of endothelial cell-derived von Willebrand factor. Blood 73 (1989) 2074-2076
    • (1989) Blood , vol.73 , pp. 2074-2076
    • Tsai, H.-M.1    Nagel, R.L.2    Hatcher, V.B.3    Sussman, I.I.4
  • 119
    • 0025044664 scopus 로고
    • Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in Type IIA von Willebrand factor
    • Dent J.A., Berkowitz S.D., Ware J., Kasper C.K., and Ruggeri Z.M. Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in Type IIA von Willebrand factor. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 6306-6310
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6306-6310
    • Dent, J.A.1    Berkowitz, S.D.2    Ware, J.3    Kasper, C.K.4    Ruggeri, Z.M.5
  • 120
    • 0026069774 scopus 로고
    • Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit
    • Dent J.A., Galbusera M., and Ruggeri Z.M. Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit. J. Clin. Invest. 88 (1991) 774-782
    • (1991) J. Clin. Invest. , vol.88 , pp. 774-782
    • Dent, J.A.1    Galbusera, M.2    Ruggeri, Z.M.3
  • 121
    • 0027172201 scopus 로고
    • Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers
    • Furlan M., Robles R., Affolter D., Meyer D., Baillod P., and Lämmle B. Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 7503-7507
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7503-7507
    • Furlan, M.1    Robles, R.2    Affolter, D.3    Meyer, D.4    Baillod, P.5    Lämmle, B.6
  • 122
    • 0024369489 scopus 로고
    • Cryosupernatant regulates accumulation of unusually large vWF multimers from endothelial cells
    • Frangos J.A., Moake J.L., Nolasco L., Phillips M.D., and McIntire L.V. Cryosupernatant regulates accumulation of unusually large vWF multimers from endothelial cells. Am. J. Physiol. 256 (1989) H1635-H1644
    • (1989) Am. J. Physiol. , vol.256
    • Frangos, J.A.1    Moake, J.L.2    Nolasco, L.3    Phillips, M.D.4    McIntire, L.V.5
  • 123
    • 0028266474 scopus 로고
    • Shear stress enhances the proteolysis of von Willebrand factor in normal plasma
    • Tsai H.-M., Sussman I.I., and Nagel R.L. Shear stress enhances the proteolysis of von Willebrand factor in normal plasma. Blood 83 (1994) 2171-2179
    • (1994) Blood , vol.83 , pp. 2171-2179
    • Tsai, H.-M.1    Sussman, I.I.2    Nagel, R.L.3
  • 124
    • 0029878123 scopus 로고    scopus 로고
    • Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion
    • Tsai H.-M. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. Blood 87 (1996) 4235-4244
    • (1996) Blood , vol.87 , pp. 4235-4244
    • Tsai, H.-M.1
  • 125
    • 0029925856 scopus 로고    scopus 로고
    • Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis
    • Furlan M., Robles R., and Lämmle B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood 87 (1996) 4223-4234
    • (1996) Blood , vol.87 , pp. 4223-4234
    • Furlan, M.1    Robles, R.2    Lämmle, B.3
  • 127
    • 0035885972 scopus 로고    scopus 로고
    • Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family
    • Fujikawa K., Suzuki H., MacMullen B., and Chung D. Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood 98 (2001) 1662-1666
    • (2001) Blood , vol.98 , pp. 1662-1666
    • Fujikawa, K.1    Suzuki, H.2    MacMullen, B.3    Chung, D.4
  • 131
    • 0032569840 scopus 로고    scopus 로고
    • Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura
    • Tsai H.-M., and Chun-Yet Lian E. Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura. N. Engl. J. Med. 339 (1998) 1585-1594
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1585-1594
    • Tsai, H.-M.1    Chun-Yet Lian, E.2
  • 132
    • 0344942587 scopus 로고    scopus 로고
    • Decreased level of von Willebrand factor-cleaving protease in coronary heart disease and thrombotic thrombocytopenic purpura: study of a simplified method for assaying the enzyme activity based on ristocetin-induced platelet aggregation
    • Yoo G., Blombäck M., Schenk-Gustafsson K., and He S. Decreased level of von Willebrand factor-cleaving protease in coronary heart disease and thrombotic thrombocytopenic purpura: study of a simplified method for assaying the enzyme activity based on ristocetin-induced platelet aggregation. Br. J. Haematol. 121 (2003) 123-129
    • (2003) Br. J. Haematol. , vol.121 , pp. 123-129
    • Yoo, G.1    Blombäck, M.2    Schenk-Gustafsson, K.3    He, S.4
  • 133
    • 0942276833 scopus 로고    scopus 로고
    • VWF73, a region from D1596 to R 1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13
    • Kokame K., Matsumoto M., Fujimura Y., and Miyata T. VWF73, a region from D1596 to R 1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13. Blood 103 (2004) 607-612
    • (2004) Blood , vol.103 , pp. 607-612
    • Kokame, K.1    Matsumoto, M.2    Fujimura, Y.3    Miyata, T.4
  • 134
  • 135
    • 0346095396 scopus 로고    scopus 로고
    • Cleavage of von Willebrand factor by ADAMTS-13 on endothelial cells
    • Lópes J.A., and Dong J.-f. Cleavage of von Willebrand factor by ADAMTS-13 on endothelial cells. Semin. Hematol. 41 (2004) 15-23
    • (2004) Semin. Hematol. , vol.41 , pp. 15-23
    • Lópes, J.A.1    Dong, J.-f.2
  • 136
    • 3242676770 scopus 로고    scopus 로고
    • Binding of platelet glycoprotein 1bα to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS 13
    • Nishio K., Anderson P.J., Zheng X.L., and Sadler J.E. Binding of platelet glycoprotein 1bα to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS 13. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 10578-10583
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10578-10583
    • Nishio, K.1    Anderson, P.J.2    Zheng, X.L.3    Sadler, J.E.4
  • 137
    • 0032801365 scopus 로고    scopus 로고
    • Modulation by heparin of the interaction of the A1 domain of von Willebrand factor with glycoprotein Ib
    • Perrault C., Ajzenberg N., Legendre P., Rastegar-Lari G., Meyer D., Lopez J.A., and Baruch D. Modulation by heparin of the interaction of the A1 domain of von Willebrand factor with glycoprotein Ib. Blood 94 (1999) 4186-4194
    • (1999) Blood , vol.94 , pp. 4186-4194
    • Perrault, C.1    Ajzenberg, N.2    Legendre, P.3    Rastegar-Lari, G.4    Meyer, D.5    Lopez, J.A.6    Baruch, D.7
  • 138
    • 0015954388 scopus 로고
    • Enzymatic reduction of disulfide bonds in fibrin-ogen by the thioredoxin system I. Identification of reduced bonds and studies on reoxidation process
    • Blombäck B., Blombäck M., Finkbeiner W., Holmgren A., Kowalska-Loth B., and Olovson G. Enzymatic reduction of disulfide bonds in fibrin-ogen by the thioredoxin system I. Identification of reduced bonds and studies on reoxidation process. Thromb. Res. 4 (1974) 55-75
    • (1974) Thromb. Res. , vol.4 , pp. 55-75
    • Blombäck, B.1    Blombäck, M.2    Finkbeiner, W.3    Holmgren, A.4    Kowalska-Loth, B.5    Olovson, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.