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Volumn 10, Issue 13, 1999, Pages 2091-2107

Advances toward gene therapy for hemophilia at the millennium

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9;

EID: 0033200188     PISSN: 10430342     EISSN: None     Source Type: Journal    
DOI: 10.1089/10430349950017095     Document Type: Review
Times cited : (78)

References (102)
  • 1
    • 0001311949 scopus 로고
    • The pathogenesis of hereditary hemophilia
    • ADDIS, T. (1911). The pathogenesis of hereditary hemophilia. J. Pathol. Bacteriol. 15, 427-452.
    • (1911) J. Pathol. Bacteriol. , vol.15 , pp. 427-452
    • Addis, T.1
  • 2
    • 0028260471 scopus 로고
    • Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169
    • AGARWALA, K.L., KAWABATA, S., TAKAO, T., MURATA, H., SHIMONISHI, Y., NISHIMURA, H., and IWANAGA, S. (1994). Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169. Biochemistry 33, 5167-5171.
    • (1994) Biochemistry , vol.33 , pp. 5167-5171
    • Agarwala, K.L.1    Kawabata, S.2    Takao, T.3    Murata, H.4    Shimonishi, Y.5    Nishimura, H.6    Iwanaga, S.7
  • 3
    • 0031734471 scopus 로고    scopus 로고
    • Stable and inheritable changes in genotype and phenotype of albino melanocytes induced by an RNA-DNA
    • ALEXEEV, V., and YOON, K. (1998). Stable and inheritable changes in genotype and phenotype of albino melanocytes induced by an RNA-DNA. Nature Biotechnol. 16, 1343-1346.
    • (1998) Nature Biotechnol. , vol.16 , pp. 1343-1346
    • Alexeev, V.1    Yoon, K.2
  • 4
    • 0031888019 scopus 로고    scopus 로고
    • Mutation at either Arg336 or Arg562 in factor VIII is insufficient for complete resistance to activated protein C (APC)-mediated inactivation: Implications for the APC resistance test
    • AMANO, K., MICHNICK, D.A., MOUSSALLI, M., and KAUFMAN, R.J. (1998). Mutation at either Arg336 or Arg562 in factor VIII is insufficient for complete resistance to activated protein C (APC)-mediated inactivation: Implications for the APC resistance test. Thromb. Haemost. 79, 557-563.
    • (1998) Thromb. Haemost. , vol.79 , pp. 557-563
    • Amano, K.1    Michnick, D.A.2    Moussalli, M.3    Kaufman, R.J.4
  • 6
    • 0028914687 scopus 로고
    • Strain related variations in adenovirally mediated transgene expression from mouse hepatocytes in vivo: Comparisons between immunocompetent and immunodeficient inbred strains
    • BARR, D., TUBB, J., FERGUSON, D., SCARIA, A., LIEBER, A., WILSON, C., PERKINS, J., and KAY, M.A. (1995). Strain related variations in adenovirally mediated transgene expression from mouse hepatocytes in vivo: Comparisons between immunocompetent and immunodeficient inbred strains. Gene Ther. 2, 151-155.
    • (1995) Gene Ther. , vol.2 , pp. 151-155
    • Barr, D.1    Tubb, J.2    Ferguson, D.3    Scaria, A.4    Lieber, A.5    Wilson, C.6    Perkins, J.7    Kay, M.A.8
  • 7
    • 0030855794 scopus 로고    scopus 로고
    • Second generation, B-domain deleted recombinant factor VIII
    • BERNTORP, E. (1997). Second generation, B-domain deleted recombinant factor VIII. Thromb. Haemost. 78, 256-260.
    • (1997) Thromb. Haemost. , vol.78 , pp. 256-260
    • Berntorp, E.1
  • 9
    • 0010597307 scopus 로고    scopus 로고
    • Identification of O-glycosylation, sulfation and phosphorylation sites in the activation peptide of human plasma factor IX
    • BOND, M.D., HUBERTY, M.C., JANKOWSKI, M.A., VATH, J.E., STRANG, A.-M., and SCOBLE, H.A. (1997). Identification of O-glycosylation, sulfation and phosphorylation sites in the activation peptide of human plasma factor IX. Blood 84, 531a.
    • (1997) Blood , vol.84
    • Bond, M.D.1    Huberty, M.C.2    Jankowski, M.A.3    Vath, J.E.4    Strang, A.-M.5    Scoble, H.A.6
  • 11
    • 0028801352 scopus 로고
    • X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
    • BRANDSTETTER, H., BAUER, M., HUBER, R., LOLLAR, P., and BODE, W. (1995). X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B. Proc. Natl. Acad. Sci. U.S.A. 92, 9796-9800.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 12
    • 0032525902 scopus 로고    scopus 로고
    • Therapeutic levels of human protein C in rats after retroviral vector-mediated hepatic gene therapy
    • CAI, S.-R., KENNEDY, S.C., BOWLING, W.M., FLYE, M.W., and PONDER, K.P. (1998). Therapeutic levels of human protein C in rats after retroviral vector-mediated hepatic gene therapy. J. Clin. Invest. 101, 2831-2841.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2831-2841
    • Cai, S.-R.1    Kennedy, S.C.2    Bowling, W.M.3    Flye, M.W.4    Ponder, K.P.5
  • 13
    • 0003294581 scopus 로고    scopus 로고
    • Residues 330-338 in catalytic domain of factor IX represent an interactive site for both factor VIIIa and factor X
    • CHANG, J.L., JIN, J.P., STRAIGHT, D.L., and STAFFORD, D.W. (1998). Residues 330-338 in catalytic domain of factor IX represent an interactive site for both factor VIIIa and factor X. Blood 92, 184a.
    • (1998) Blood , vol.92
    • Chang, J.L.1    Jin, J.P.2    Straight, D.L.3    Stafford, D.W.4
  • 14
    • 0019957533 scopus 로고
    • Molecular cloning of the gene for human anti-haemophilic factor IX
    • CHOO, K.H., GOULD, K.G., REES, D.J., and BROWNLEE, G.G. (1982). Molecular cloning of the gene for human anti-haemophilic factor IX. Nature (London) 299, 178-180.
    • (1982) Nature (London) , vol.299 , pp. 178-180
    • Choo, K.H.1    Gould, K.G.2    Rees, D.J.3    Brownlee, G.G.4
  • 15
    • 0029943193 scopus 로고    scopus 로고
    • Sustained expression of therapeutic levels of human factor VIII in mice
    • CONNELLY, S., GARDNER, J.M., LYONS, R.M., McCLELLAND, A., and KALEKO, M. (1996a). Sustained expression of therapeutic levels of human factor VIII in mice. Blood 87, 4671-4677.
    • (1996) Blood , vol.87 , pp. 4671-4677
    • Connelly, S.1    Gardner, J.M.2    Lyons, R.M.3    McClelland, A.4    Kaleko, M.5
  • 16
    • 0030069229 scopus 로고    scopus 로고
    • High-level tissue-specific expression of functional human factor VIII in mice
    • CONNELLY, S., GARDNER, J.M., McCLELLAND, A., and KALEKO, M. (1996b). High-level tissue-specific expression of functional human factor VIII in mice. Hum. Gene Ther. 7, 183-195.
    • (1996) Hum. Gene Ther. , vol.7 , pp. 183-195
    • Connelly, S.1    Gardner, J.M.2    McClelland, A.3    Kaleko, M.4
  • 19
    • 0030850713 scopus 로고    scopus 로고
    • Resistance to activated protein C as risk factor for thrombosis: Molecular mechanisms, laboratory investigation, and clinical management
    • DAHLBACK, B. (1997). Resistance to activated protein C as risk factor for thrombosis: Molecular mechanisms, laboratory investigation, and clinical management. Semin Hematol. 34, 217-234.
    • (1997) Semin Hematol. , vol.34 , pp. 217-234
    • Dahlback, B.1
  • 20
    • 0028098218 scopus 로고
    • Inherited resistance to activated protein C is corrected by anticoagulant cofactor activity found to be a property of factor V
    • DAHLBACK, B., and HILDEBRAND, B. (1994). Inherited resistance to activated protein C is corrected by anticoagulant cofactor activity found to be a property of factor V. Proc. Natl. Acad. Sci. U.S.A. 91, 1396-1400.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1396-1400
    • Dahlback, B.1    Hildebrand, B.2
  • 21
    • 0023597393 scopus 로고
    • The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins
    • DORNER, A.J., BOLE, D.G., and KAUFMAN, R.J. (1987). The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J. Cell. Biol. 105, 2665-2674.
    • (1987) J. Cell. Biol. , vol.105 , pp. 2665-2674
    • Dorner, A.J.1    Bole, D.G.2    Kaufman, R.J.3
  • 22
    • 0025119643 scopus 로고
    • Protein dissociation from GRP78 and secretion is blocked by depletion of cellular ATP levels
    • DORNER, A.J., WASLEY, L.C., and KAUFMAN, R.J. (1990). Protein dissociation from GRP78 and secretion is blocked by depletion of cellular ATP levels. Proc. Natl. Acad. Sci. U.S.A. 87, 7429-7432.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7429-7432
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 23
    • 0029896502 scopus 로고    scopus 로고
    • The human clotting factor VIII cDNA contains an autonomously replicating sequence consensus- and matrix attachment region-like sequence that binds a nuclear factor, represses heterologous gene expression, and mediates the transcriptional effects of sodium butyrate
    • FALLAUX, F.J., HOEBEN, R.C., CRAMER, S.J., VAN DEN WOLLENBERG, D.J., BRIET, E., VAN ORMONDT, H., and VAN DER EB, A.J. (1996). The human clotting factor VIII cDNA contains an autonomously replicating sequence consensus- and matrix attachment region-like sequence that binds a nuclear factor, represses heterologous gene expression, and mediates the transcriptional effects of sodium butyrate. Mol. Cell. Biol. 16, 4264-4272.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4264-4272
    • Fallaux, F.J.1    Hoeben, R.C.2    Cramer, S.J.3    Van Den Wollenberg, D.J.4    Briet, E.5    Van Ormondt, H.6    Van Der Eb, A.J.7
  • 24
    • 0032563086 scopus 로고    scopus 로고
    • The A2 subunit of factor VIIIa modulates the active site of factor IXa
    • FAY, P.J., and KOSHIBU, K. (1998). The A2 subunit of factor VIIIa modulates the active site of factor IXa. J. Biol. Chem. 273, 19049-19054.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19049-19054
    • Fay, P.J.1    Koshibu, K.2
  • 25
    • 0026708655 scopus 로고
    • Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa
    • FAY, P.J., and SMUDZIN, T.M. (1992). Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa. J. Biol. Chem. 267, 13246-13250.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13246-13250
    • Fay, P.J.1    Smudzin, T.M.2
  • 26
    • 0025923490 scopus 로고
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit
    • FAY, P.J., HAIDARIS, P.J., and SMUDZIN, T.M. (1991). Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit. J. Biol. Chem. 266, 8957-8962.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8957-8962
    • Fay, P.J.1    Haidaris, P.J.2    Smudzin, T.M.3
  • 27
    • 0027938728 scopus 로고
    • Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site
    • FAY, P.J., BEATTIE, T., HUGGINS, C.F., and REGAN, L.M. (1994). Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site. J. Biol. Chem. 269, 20522-20527.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20522-20527
    • Fay, P.J.1    Beattie, T.2    Huggins, C.F.3    Regan, L.M.4
  • 28
    • 0030037846 scopus 로고    scopus 로고
    • Proteasome subunits X and Y alter peptides activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7
    • GACZYNSKA, M., GOLDBERG, A.L., TANAKA, K., HENDIL, K.B., and ROCK, K.L. (1996). Proteasome subunits X and Y alter peptides activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7. J. Biol. Chem. 271, 17275-17280.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17275-17280
    • Gaczynska, M.1    Goldberg, A.L.2    Tanaka, K.3    Hendil, K.B.4    Rock, K.L.5
  • 29
    • 0002624219 scopus 로고    scopus 로고
    • Assay of factor VIII antigen (VIII:CAg) in 294 haemophilia a patients by a new commercial ELISa using monoclonal antibodies
    • GIRMA, J.P., FRESSINAUD, E., HOULLIER, A., LAURIAN, Y., AMIRAL, J., and MEYER, D. (1998). Assay of factor VIII antigen (VIII:CAg) in 294 haemophilia A patients by a new commercial ELISA using monoclonal antibodies. Haemophilia 4, 98-103.
    • (1998) Haemophilia , vol.4 , pp. 98-103
    • Girma, J.P.1    Fressinaud, E.2    Houllier, A.3    Laurian, Y.4    Amiral, J.5    Meyer, D.6
  • 30
    • 0031698579 scopus 로고    scopus 로고
    • Problems and prospects in gene therapy for hemophilia
    • HERZOG, R.W., and HIGH, K.A. (1998). Problems and prospects in gene therapy for hemophilia. Curr. Opin. Hematol. 5, 321-326.
    • (1998) Curr. Opin. Hematol. , vol.5 , pp. 321-326
    • Herzog, R.W.1    High, K.A.2
  • 32
    • 0024367339 scopus 로고
    • Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombin
    • HILL-EUBANKS, D.C., PARKER, C.G., and LOLLAR, P. (1989). Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombin. Proc. Natl. Acad. Sci. U.S.A. 86, 6508-6512.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6508-6512
    • Hill-Eubanks, D.C.1    Parker, C.G.2    Lollar, P.3
  • 35
    • 0031969428 scopus 로고    scopus 로고
    • Transduction of dendritic cells by DNA viral vectors directs the immune response to transgene products in muscle fibers
    • JOOSS, K., YANG, Y., FISHER, K.J., and WILSON, J.M. (1998). Transduction of dendritic cells by DNA viral vectors directs the immune response to transgene products in muscle fibers. J. Virol. 72, 4212-4223.
    • (1998) J. Virol. , vol.72 , pp. 4212-4223
    • Jooss, K.1    Yang, Y.2    Fisher, K.J.3    Wilson, J.M.4
  • 36
    • 2442742364 scopus 로고    scopus 로고
    • Post-translational modifications required for coagulation factor secretion and function
    • KAUFMAN, R.J. (1998). Post-translational modifications required for coagulation factor secretion and function. Thromb. Haemost. 12, 1812-1824.
    • (1998) Thromb. Haemost. , vol.12 , pp. 1812-1824
    • Kaufman, R.J.1
  • 37
    • 0023918719 scopus 로고
    • Synthesis processing and secretion of factor VIII expressed in mammalian cells
    • KAUFMAN, R.J., WASLEY, L.C., and DORNER, A.J. (1988). Synthesis processing and secretion of factor VIII expressed in mammalian cells. J. Biol. Chem. 263, 6352-6362.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 38
    • 0024597022 scopus 로고
    • The effect of von Willebrand factor co-expression on the synthesis and secretion of factor VIII in Chinese hamster ovary cells
    • KAUFMAN, R.J., WASLEY, L.C., DAVIES, M.V., WISE, R.J., and ISRAEL, D.I. (1989). The effect of von Willebrand factor co-expression on the synthesis and secretion of factor VIII in Chinese hamster ovary cells. Mol. Cell. Biol. 9, 1233-1242.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1233-1242
    • Kaufman, R.J.1    Wasley, L.C.2    Davies, M.V.3    Wise, R.J.4    Israel, D.I.5
  • 39
    • 0032960838 scopus 로고    scopus 로고
    • Von Willebrand factor elevates plasma factor VIII without induction of factor VIII messenger RNA in the liver
    • KAUFMAN, R.J., DORNER, A.J., and FASS, D.N. (1999). von Willebrand factor elevates plasma factor VIII without induction of factor VIII messenger RNA in the liver. Blood 93, 193-197.
    • (1999) Blood , vol.93 , pp. 193-197
    • Kaufman, R.J.1    Dorner, A.J.2    Fass, D.N.3
  • 41
    • 0021173723 scopus 로고
    • Localization of factor VIIIC: Antigen in guinea-pig tissues and isolated liver cell fractions
    • KELLY, D.A., SUMMERFIELD, J.A., and TUDDENHAM, E.G. (1984). Localization of factor VIIIC: Antigen in guinea-pig tissues and isolated liver cell fractions. Br. J. Haematol. 56, 535-543.
    • (1984) Br. J. Haematol. , vol.56 , pp. 535-543
    • Kelly, D.A.1    Summerfield, J.A.2    Tuddenham, E.G.3
  • 42
    • 0029098922 scopus 로고
    • Sequences within the coding regions of clotting factor VIII and CFTR block transcriptional elongation
    • KOEBERL, D.D., HALBERT, C.L., KRUMM, A., and MILLER, A.D. (1995). Sequences within the coding regions of clotting factor VIII and CFTR block transcriptional elongation. Hum. Gene Ther. 6, 469-479.
    • (1995) Hum. Gene Ther. , vol.6 , pp. 469-479
    • Koeberl, D.D.1    Halbert, C.L.2    Krumm, A.3    Miller, A.D.4
  • 43
    • 0031019819 scopus 로고    scopus 로고
    • Persistent expression of human clotting factor IX from mouse liver after intravenous injection of adeno-associated virus vectors
    • KOEBERL, D.D., ALEXANDER, I.E., HALBERT, C.L., RUSSELL, D.W., and MILLER, A.D. (1997). Persistent expression of human clotting factor IX from mouse liver after intravenous injection of adeno-associated virus vectors. Proc. Natl. Acad. Sci. U.S.A. 94, 1426-1431.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1426-1431
    • Koeberl, D.D.1    Alexander, I.E.2    Halbert, C.L.3    Russell, D.W.4    Miller, A.D.5
  • 44
    • 0019156474 scopus 로고
    • Thrombotic stroke associated with elevated plasma factor VIII
    • KOSIK, K.S., and FURIE, B. (1980). Thrombotic stroke associated with elevated plasma factor VIII. Ann. Neurol. 8, 435-437.
    • (1980) Ann. Neurol. , vol.8 , pp. 435-437
    • Kosik, K.S.1    Furie, B.2
  • 45
    • 0028814316 scopus 로고
    • Role of clotting factor VIII in effect of von Willebrand factor on occurrence of deep-vein thrombosis
    • KOSTER, T., BLANN, A.D., BRIET, E., VANDENBROUCKE, J.P., and ROSENDAAL, F.R. (1995). Role of clotting factor VIII in effect of von Willebrand factor on occurrence of deep-vein thrombosis. Lancet 345, 152-155.
    • (1995) Lancet , vol.345 , pp. 152-155
    • Koster, T.1    Blann, A.D.2    Briet, E.3    Vandenbroucke, J.P.4    Rosendaal, F.R.5
  • 46
    • 0031953132 scopus 로고    scopus 로고
    • In vivo site-directed mutagenesis of the factor IX gene by chimeric RNA/DNA oligonucleotides
    • KREN, B.T., BANDYOPADHYAY, P., and STEER, C.J. (1998). In vivo site-directed mutagenesis of the factor IX gene by chimeric RNA/DNA oligonucleotides. Nature Med. 4, 285-290.
    • (1998) Nature Med. , vol.4 , pp. 285-290
    • Kren, B.T.1    Bandyopadhyay, P.2    Steer, C.J.3
  • 47
    • 0343941338 scopus 로고
    • Isolation and characterization of a cDNa coding for human factor IX
    • KURACHI, K., and DAVIE, E.W. (1982). Isolation and characterization of a cDNA coding for human factor IX. Proc. Natl. Acad. Sci. U.S.A. 79, 6461-6464.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 6461-6464
    • Kurachi, K.1    Davie, E.W.2
  • 48
    • 0027520025 scopus 로고
    • Inversions disrupting the factor VIII gene as a common cause of severe hemophilia A
    • LAKICH, D., KAZAZIAN, H.H., ANTONARAKIS, S.E., and GITSCHIER, J. (1993). Inversions disrupting the factor VIII gene as a common cause of severe hemophilia A. Nature Genet. 5, 236-241.
    • (1993) Nature Genet. , vol.5 , pp. 236-241
    • Lakich, D.1    Kazazian, H.H.2    Antonarakis, S.E.3    Gitschier, J.4
  • 49
    • 0001556240 scopus 로고
    • Haemorrhagid diathesis. Successful transfusion of blood
    • LANE, S. (1840). Haemorrhagid diathesis. Successful transfusion of blood. Lancet 1, 185-188.
    • (1840) Lancet , vol.1 , pp. 185-188
    • Lane, S.1
  • 50
    • 0029670912 scopus 로고    scopus 로고
    • The sequence of Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX
    • LENTING, P.J., VAN DE LOO, J.W., DONATH, M.J., VAN MOURIK, J.A., and MERTENS, K. (1996). The sequence of Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX. J. Biol. Chem. 271, 1935-1940.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1935-1940
    • Lenting, P.J.1    Van De Loo, J.W.2    Donath, M.J.3    Van Mourik, J.A.4    Mertens, K.5
  • 52
    • 0028261727 scopus 로고
    • Transplantation of spleen cells in patients with hemophilia A. A report of 20 cases
    • LIU, L., XIA, S., and SEIFERT, J. (1994). Transplantation of spleen cells in patients with hemophilia A. A report of 20 cases. Transplant. Int. 7, 201-206.
    • (1994) Transplant. Int. , vol.7 , pp. 201-206
    • Liu, L.1    Xia, S.2    Seifert, J.3
  • 53
    • 0030858423 scopus 로고    scopus 로고
    • Analysis of factor VIII inhibitors using hybrid human/porcine factor VIII
    • LOLLAR, P. (1997). Analysis of factor VIII inhibitors using hybrid human/porcine factor VIII. Thromb. Haemost. 78, 647-651.
    • (1997) Thromb. Haemost. , vol.78 , pp. 647-651
    • Lollar, P.1
  • 54
    • 0024576076 scopus 로고
    • Subunit structure of thrombin-activated porcine factor VIII
    • LOLLAR, P., and PARKER, C.G. (1987). Subunit structure of thrombin-activated porcine factor VIII. Biochemistry 28, 666-674.
    • (1987) Biochemistry , vol.28 , pp. 666-674
    • Lollar, P.1    Parker, C.G.2
  • 55
    • 0025101070 scopus 로고
    • pH-dependent denaturation of tnrombin-activated porcine factor VIII
    • LOLLAR, P., and PARKER, C.G. (1990). pH-dependent denaturation of tnrombin-activated porcine factor VIII. J. Biol. Chem. 265, 1688-1692.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1688-1692
    • Lollar, P.1    Parker, C.G.2
  • 56
    • 0025866980 scopus 로고
    • Structural basis for the decreased procoagulant activity of human factor VIII compared to the porcine homolog
    • LOLLAR, P., and PARKER, C.G. (1991). Structural basis for the decreased procoagulant activity of human factor VIII compared to the porcine homolog. J. Biol. Chem. 265, 12481-12486.
    • (1991) J. Biol. Chem. , vol.265 , pp. 12481-12486
    • Lollar, P.1    Parker, C.G.2
  • 57
    • 0033559706 scopus 로고    scopus 로고
    • The rhesus macaque as an animal model for hemophilia B gene therapy
    • LOZIER, J.N., METZGER, M.E., DONAHUE, R.E., and MORGAN, R.A. (1999). The rhesus macaque as an animal model for hemophilia B gene therapy. Blood 93, 1875-1881.
    • (1999) Blood , vol.93 , pp. 1875-1881
    • Lozier, J.N.1    Metzger, M.E.2    Donahue, R.E.3    Morgan, R.A.4
  • 58
    • 0030764556 scopus 로고    scopus 로고
    • Prophylaxis in children with hemophilia: Is it the optimal treatment?
    • LUSHER, J.M. (1997). Prophylaxis in children with hemophilia: Is it the optimal treatment? Thromb. Haemost. 78, 726-729.
    • (1997) Thromb. Haemost. , vol.78 , pp. 726-729
    • Lusher, J.M.1
  • 59
    • 0027237331 scopus 로고
    • Sequences in the coding region of clotting factor VIII act as dominant inhibitors of RNA accumulation and protein production
    • LYNCH, C.M., ISRAEL, D.I., KAUFMAN, R.J., and MILLER, A.D. (1993). Sequences in the coding region of clotting factor VIII act as dominant inhibitors of RNA accumulation and protein production. Hum. Gene Ther. 4, 259-272.
    • (1993) Hum. Gene Ther. , vol.4 , pp. 259-272
    • Lynch, C.M.1    Israel, D.I.2    Kaufman, R.J.3    Miller, A.D.4
  • 60
    • 0023757497 scopus 로고
    • Desmopressin: A nontransfusional form of treatment for congenital and acquired bleeding disorders
    • MANNUCCI, P.M. (1988). Desmopressin: A nontransfusional form of treatment for congenital and acquired bleeding disorders. Blood 72, 1449-1455.
    • (1988) Blood , vol.72 , pp. 1449-1455
    • Mannucci, P.M.1
  • 61
    • 0026650784 scopus 로고
    • Comparison of four virus-inactivated plasma concentrates for treatment of severe von Willebrand disease: A cross-over randomized trial
    • MANNUCCI, P.M., TENCONI, P.M., CASTAMAN, G., and RODEGHIERO, F. (1992). Comparison of four virus-inactivated plasma concentrates for treatment of severe von Willebrand disease: A cross-over randomized trial. Blood 79, 3130-3137.
    • (1992) Blood , vol.79 , pp. 3130-3137
    • Mannucci, P.M.1    Tenconi, P.M.2    Castaman, G.3    Rodeghiero, F.4
  • 62
    • 0028937341 scopus 로고
    • A 110 amino acid region within the A1-domain of coagulation factor VIII inhibits secretion from mammalian cells
    • MARQUETTE, K.A., PITTMAN, D.D., and KAUFMAN, R.J. (1995). A 110 amino acid region within the A1-domain of coagulation factor VIII inhibits secretion from mammalian cells. J. Biol. Chem. 270, 10297-10303.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10297-10303
    • Marquette, K.A.1    Pittman, D.D.2    Kaufman, R.J.3
  • 63
    • 0033603299 scopus 로고    scopus 로고
    • Protease and EGF1 domains of factor IXa
    • MATHUR, A., and BAJAJ, S.P. (1999). Protease and EGF1 domains of factor IXa. J. Biol. Chem. 274, 18477-18486.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18477-18486
    • Mathur, A.1    Bajaj, S.P.2
  • 64
    • 0028058606 scopus 로고
    • Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage
    • MICHNICK, D.A., PITTMAN, D.D., and KAUFMAN, R.J. (1993). Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage. J. Biol. Chem. 269, 20095-20102.
    • (1993) J. Biol. Chem. , vol.269 , pp. 20095-20102
    • Michnick, D.A.1    Pittman, D.D.2    Kaufman, R.J.3
  • 65
    • 0033534406 scopus 로고    scopus 로고
    • Mvwf, A dominant modifier of murine von Willebrand factor: Results from altered lineage-specific expression of a glycosyltransferase
    • MOHLKE, K., PURKAYASTHA, A., WESTERICK, R., SMITH, P., PETRYNIAK, B., LOWE, J., and GINSBURG, D. (1999). Mvwf, A dominant modifier of murine von Willebrand factor: Results from altered lineage-specific expression of a glycosyltransferase. Cell 96, 111-120.
    • (1999) Cell , vol.96 , pp. 111-120
    • Mohlke, K.1    Purkayastha, A.2    Westerick, R.3    Smith, P.4    Petryniak, B.5    Lowe, J.6    Ginsburg, D.7
  • 66
    • 0031983639 scopus 로고    scopus 로고
    • Direct intramuscular injection with recombinant AAV vectors results in sustained expression in a dog model of hemophilia
    • MONAHAN, P.E., SAMULSKI, R.J., TAZELAAR, J., XIAO, X., NICHOLS, T.C., BELLINGER, D.A., READ, M.S., and WALSH, C.E. (1998). Direct intramuscular injection with recombinant AAV vectors results in sustained expression in a dog model of hemophilia. Gene Ther. 5, 40-49.
    • (1998) Gene Ther. , vol.5 , pp. 40-49
    • Monahan, P.E.1    Samulski, R.J.2    Tazelaar, J.3    Xiao, X.4    Nichols, T.C.5    Bellinger, D.A.6    Read, M.S.7    Walsh, C.E.8
  • 67
    • 0003303712 scopus 로고    scopus 로고
    • A role for whole blood clotting time as a sensitive screening test for F. VIII and F. IX replacement
    • MUSTAFA, R.L., ELWELL, D.R., RUSSELL, K.E., NICHOLS, T.C., and READ, M.S. (1998). A role for whole blood clotting time as a sensitive screening test for F. VIII and F. IX replacement. Blood 92, 96a.
    • (1998) Blood , vol.92
    • Mustafa, R.L.1    Elwell, D.R.2    Russell, K.E.3    Nichols, T.C.4    Read, M.S.5
  • 69
    • 0026701391 scopus 로고
    • Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue
    • NISHIMURA, H., TAKAO, T., HASE, S., SHIMONISHI, Y., and IWANAGA, S. (1992). Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. J. Biol. Chem. 267, 17520-17525.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17520-17525
    • Nishimura, H.1    Takao, T.2    Hase, S.3    Shimonishi, Y.4    Iwanaga, S.5
  • 70
    • 0023864433 scopus 로고
    • Generation of active coagulation factor VIII from isolated subunits
    • NORDFANG, O., and EZBAN, M. (1988). Generation of active coagulation factor VIII from isolated subunits. J. Biol. Chem. 263, 1115-1118.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1115-1118
    • Nordfang, O.1    Ezban, M.2
  • 71
    • 0003110303 scopus 로고
    • An account of an hemorrhagic disposition existing in certain families
    • OTTO, J.E. (1803). An account of an hemorrhagic disposition existing in certain families. Med. Repository 6, 1.
    • (1803) Med. Repository , vol.6 , pp. 1
    • Otto, J.E.1
  • 72
    • 0018198995 scopus 로고
    • Survival of 125 iodine-labeled factor VIII in normals and patients with classic hemophilia. Observations on the heterogeneity of human factor VIII
    • OVER, J., SIXMA, J.J., BRUINE, M.H., TRIESCHNIGG, M.C., VLOOSWIJK, R.A., BEESER-VISSER, N.H., and BOUMA, B.N. (1978). Survival of 125 iodine-labeled factor VIII in normals and patients with classic hemophilia. Observations on the heterogeneity of human factor VIII. J. Clin. Invest. 62, 223-234.
    • (1978) J. Clin. Invest. , vol.62 , pp. 223-234
    • Over, J.1    Sixma, J.J.2    Bruine, M.H.3    Trieschnigg, M.C.4    Vlooswijk, R.A.5    Beeser-Visser, N.H.6    Bouma, B.N.7
  • 73
    • 0000334774 scopus 로고
    • Hemophilia. II. Some properties of a substance obtained from normal human plasma effective in accelerating the coagulation of hemophilic blood
    • PATEK, A.J., and TAYLOR, F.H.L. (1937), Hemophilia. II. Some properties of a substance obtained from normal human plasma effective in accelerating the coagulation of hemophilic blood. J. Clin. Invest. 16, 113-124.
    • (1937) J. Clin. Invest. , vol.16 , pp. 113-124
    • Patek, A.J.1    Taylor, F.H.L.2
  • 74
    • 0032467348 scopus 로고    scopus 로고
    • Homology models of the C domains of blood coagulation factors V and VIII: A proposed membrane binding mode for FV and FVIII C2 domains
    • PELLEQUER, J.L., GALE, A.J., GRIFFIN, J.H., and GETZOFF, E.D. (1998). Homology models of the C domains of blood coagulation factors V and VIII: A proposed membrane binding mode for FV and FVIII C2 domains. Blood Cells Mol. Dis. 24, 448-461.
    • (1998) Blood Cells Mol. Dis. , vol.24 , pp. 448-461
    • Pellequer, J.L.1    Gale, A.J.2    Griffin, J.H.3    Getzoff, E.D.4
  • 75
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated a domains of human factor VIII based on the crystal structure of human ceruloplasmin
    • PEMBERTON, S.. LINDLEY, P., ZAITSEV, V., CARD, G., TUDDENHAM, E.G.D., and KEMBALL-COOK, G. (1997). A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 89, 2413-2421.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3    Card, G.4    Tuddenham, E.G.D.5    Kemball-Cook, G.6
  • 76
    • 0030664471 scopus 로고    scopus 로고
    • Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa
    • PIPE, S.W., and KAUFMAN, R.J. (1997). Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa. Proc. Natl. Acad. Sci. U.S.A. 94, 11851-11856.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11851-11856
    • Pipe, S.W.1    Kaufman, R.J.2
  • 77
    • 0032478644 scopus 로고    scopus 로고
    • Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
    • PIPE, S.W., MORRIS, J.A., SHAH, J., and KAUFMAN, R.J. (1998). Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J. Biol. Chem. 273, 8537-8544.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8537-8544
    • Pipe, S.W.1    Morris, J.A.2    Shah, J.3    Kaufman, R.J.4
  • 78
    • 0032932325 scopus 로고    scopus 로고
    • Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for nonproteolytic inactivation of factor VIIIa in vivo
    • PIPE, S.W., EICKHORST, A.N., MCKINLEY, E.L., SAENKO, E.L., and KAUFMAN, R.J. (1999). Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for nonproteolytic inactivation of factor VIIIa in vivo. Blood 93, 176-183.
    • (1999) Blood , vol.93 , pp. 176-183
    • Pipe, S.W.1    Eickhorst, A.N.2    Mckinley, E.L.3    Saenko, E.L.4    Kaufman, R.J.5
  • 79
    • 1842408993 scopus 로고
    • The proteolytic requirements for activation and inactivation of antihemophilic factor (factor VIII)
    • PITTMAN, D.D., and KAUFMAN, R.J. (1988). The proteolytic requirements for activation and inactivation of antihemophilic factor (factor VIII). Proc. Natl. Acad. Sci. U.S.A. 85, 2429-2433.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2429-2433
    • Pittman, D.D.1    Kaufman, R.J.2
  • 80
    • 0027319588 scopus 로고
    • Biochemical, immunological, and in vivo functional characterization of B-domain deleted factor VIII
    • PITTMAN, D.D., ALDERMAN, E.A., TOMKINSON, K.N., WANG, J.H., GILES, A.R., and KAUFMAN, R.J. (1993). Biochemical, immunological, and in vivo functional characterization of B-domain deleted factor VIII. Blood 81, 2925-2935.
    • (1993) Blood , vol.81 , pp. 2925-2935
    • Pittman, D.D.1    Alderman, E.A.2    Tomkinson, K.N.3    Wang, J.H.4    Giles, A.R.5    Kaufman, R.J.6
  • 81
    • 0028933042 scopus 로고
    • Cleavage of factor VIII light chain is required for maximal generation of factor VIIIa activity
    • REGAN, L.M., and FAY, P.J. (1995). Cleavage of factor VIII light chain is required for maximal generation of factor VIIIa activity. J. Biol. Chem. 270, 8546-8552.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8546-8552
    • Regan, L.M.1    Fay, P.J.2
  • 83
    • 0014499005 scopus 로고
    • Hemophilia in the Talmud and rabbinic writings
    • ROSNER, F. (1969). Hemophilia in the Talmud and rabbinic writings. Ann. Intern. Med. 70, 833-837.
    • (1969) Ann. Intern. Med. , vol.70 , pp. 833-837
    • Rosner, F.1
  • 85
    • 0024451521 scopus 로고
    • Localization of epitopes for human factor VIII inhibitor antibodies by immunoblotting and antibody neutralization
    • SCANDELLA, D., MATTINGLY, M., DE GRAAF, S., and FULCHER, C.A. (1989). Localization of epitopes for human factor VIII inhibitor antibodies by immunoblotting and antibody neutralization. Blood 74, 1618-1626.
    • (1989) Blood , vol.74 , pp. 1618-1626
    • Scandella, D.1    Mattingly, M.2    De Graaf, S.3    Fulcher, C.A.4
  • 88
    • 0025087144 scopus 로고
    • DNA cloning of a mouse mammary epithelial cell surface protein reveals the existence of epidermal growth factor-like domains linked to factor VIII-like sequences
    • STUBBS, J.D., LEKUTIS, C., SINGER, K.L., BUI, A., YUZUKI, D., SRINIVASAN, U., and PARRY, G. (1990). cDNA cloning of a mouse mammary epithelial cell surface protein reveals the existence of epidermal growth factor-like domains linked to factor VIII-like sequences. Proc. Natl. Acad. Sci. U.S.A. 87, 8417-8421.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8417-8421
    • Stubbs, J.D.1    Lekutis, C.2    Singer, K.L.3    Bui, A.4    Yuzuki, D.5    Srinivasan, U.6    Parry, G.7
  • 89
    • 0030821993 scopus 로고    scopus 로고
    • Mutagenesis of a potential BiP binding site enhances secretion of coagulation factor VIII
    • SWAROOP, M., MOUSSALLI, M., PIPE, S.W., and KAUFMAN, R.J. (1997). Mutagenesis of a potential BiP binding site enhances secretion of coagulation factor VIII. J. Biol. Chem. 272, 24121-24124.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24121-24124
    • Swaroop, M.1    Moussalli, M.2    Pipe, S.W.3    Kaufman, R.J.4
  • 90
    • 0030783138 scopus 로고    scopus 로고
    • Identification and functional requirement of Cu(II) and its ligands within coagulation factor VIII
    • TAGLIAVACCA, L., MOON, N., DUNHAM, W.R., and KAUFMAN, R.J. (1997). Identification and functional requirement of Cu(II) and its ligands within coagulation factor VIII. J. Biol. Chem. 272, 27428-27434.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27428-27434
    • Tagliavacca, L.1    Moon, N.2    Dunham, W.R.3    Kaufman, R.J.4
  • 93
    • 0027502870 scopus 로고
    • PACE/furin processes the vitamin K-dependent pro-factor IX precursor within the secretory pathway
    • WASLEY, L.C., REHEMTULLA, A., BRISTOL, J.A., and KAUFMAN, R.J. (1993). PACE/furin processes the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J. Biol. Chem. 268, 8458-8465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8458-8465
    • Wasley, L.C.1    Rehemtulla, A.2    Bristol, J.A.3    Kaufman, R.J.4
  • 94
    • 0017754787 scopus 로고
    • Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease
    • WEISS, H.J., SUSSMAN, I.I., and HOYER, L.W. (1977). Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease. J. Clin. Invest. 60, 390-404.
    • (1977) J. Clin. Invest. , vol.60 , pp. 390-404
    • Weiss, H.J.1    Sussman, I.I.2    Hoyer, L.W.3
  • 95
    • 0032973849 scopus 로고    scopus 로고
    • Utilization of previously treated patients (PTPs), noninfected patients (NIPs), and previously untreated patients (PUPs) in the evaluation of Subcommittee on Factor VIII and Factor IX of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis
    • WHITE, G.C., DIMICHELE, D., MERTENS, K., NEGRIER, C., PEAKE, I.R., PROWSE, C., SCHWAAB, R., YOSHIOKA, A., and INGERSLEV, J. (1999). Utilization of previously treated patients (PTPs), noninfected patients (NIPs), and previously untreated patients (PUPs) in the evaluation of Subcommittee on Factor VIII and Factor IX of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb. Haemost. 81, 462.
    • (1999) Thromb. Haemost. , vol.81 , pp. 462
    • White, G.C.1    Dimichele, D.2    Mertens, K.3    Negrier, C.4    Peake, I.R.5    Prowse, C.6    Schwaab, R.7    Yoshioka, A.8    Ingerslev, J.9
  • 96
    • 0022411248 scopus 로고
    • Distribution of factor VIII mRNA and antigen in human liver and other tissues
    • WION, K.L., KELLY, D., SUMMERFIELD, J.A., TUDDENHAM, E.G.D., and LAWN, R.M. (1985). Distribution of factor VIII mRNA and antigen in human liver and other tissues. Nature (London) 317, 726-729.
    • (1985) Nature (London) , vol.317 , pp. 726-729
    • Wion, K.L.1    Kelly, D.2    Summerfield, J.A.3    Tuddenham, E.G.D.4    Lawn, R.M.5
  • 97
    • 0025748557 scopus 로고
    • The role of von Willebrand factor multimerization and propeptide cleavage in the binding and stabilization of factor VIII
    • WISE, R.J., DORNER, A.J., KRANE, M., PITTMAN, D.D., and KAUFMAN, R.J. (1991). The role of von Willebrand factor multimerization and propeptide cleavage in the binding and stabilization of factor VIII. J. Biol. Chem. 266, 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
  • 99
    • 9244220682 scopus 로고    scopus 로고
    • Immune responses to viral antigens versus transgene product in the elimination of recombinant adenovirus-infected hepatocytes in vivo
    • YANG, Y., JOOSS, K.U., SU, Q., ERTL, H.C., and WILSON, J.M. (1996). Immune responses to viral antigens versus transgene product in the elimination of recombinant adenovirus-infected hepatocytes in vivo. Gene Ther. 3, 137-144.
    • (1996) Gene Ther. , vol.3 , pp. 137-144
    • Yang, Y.1    Jooss, K.U.2    Su, Q.3    Ertl, H.C.4    Wilson, J.M.5
  • 100
    • 17344367454 scopus 로고    scopus 로고
    • Evaluating the potential of germ line transmission after intravenous administration of recombinant adenovirus in the C3H mouse
    • YE, X., GAO, G.P., PABIN, C., RAPER, S.E., and WILSON, J.M. (1998). Evaluating the potential of germ line transmission after intravenous administration of recombinant adenovirus in the C3H mouse. Hum. Gene Ther. 9, 2135-2142.
    • (1998) Hum. Gene Ther. , vol.9 , pp. 2135-2142
    • Ye, X.1    Gao, G.P.2    Pabin, C.3    Raper, S.E.4    Wilson, J.M.5
  • 101
    • 0022257323 scopus 로고
    • Nucleotide sequence of the gene for human factor IX (antihemophilic factor B)
    • YOSHITAKE, S., SCHACH, B.G., FOSTER, D.C., DAVIE, E.W., and KURACHI, K. (1985). Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 24, 3736-3750.
    • (1985) Biochemistry , vol.24 , pp. 3736-3750
    • Yoshitake, S.1    Schach, B.G.2    Foster, D.C.3    Davie, E.W.4    Kurachi, K.5
  • 102
    • 0022401607 scopus 로고
    • Ultrastructural localization of factor VIII procoagulant antigen in human liver hepatocytes
    • ZELECHOWSKA, M.G., VAN MOURIK, J.A., and BRODNIEWICZPROBA, T. (1985). Ultrastructural localization of factor VIII procoagulant antigen in human liver hepatocytes. Nature (London) 317, 729-730.
    • (1985) Nature (London) , vol.317 , pp. 729-730
    • Zelechowska, M.G.1    Van Mourik, J.A.2    Brodniewiczproba, T.3


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