메뉴 건너뛰기




Volumn 78, Issue 1, 1997, Pages 161-172

Inherited factor X deficiency: Molecular genetics and pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10;

EID: 0030804838     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1657520     Document Type: Conference Paper
Times cited : (84)

References (118)
  • 1
    • 0020622131 scopus 로고
    • Factor X abnormalities
    • Mammen EF. Factor X abnormalities. Sem Thromb Haemost 1983; 9:31-44.
    • (1983) Sem Thromb Haemost , vol.9 , pp. 31-44
    • Mammen, E.F.1
  • 2
    • 0022438103 scopus 로고
    • Tentative and updated classification of factor X variants
    • Girolami A. Tentative and updated classification of factor X variants. Acta Haemato 1986; 75:58-9.
    • (1986) Acta Haemato , vol.75 , pp. 58-59
    • Girolami, A.1
  • 3
    • 0014666302 scopus 로고
    • Abnormal forms of factor X
    • Denson KWE. Abnormal forms of factor X. Lancet 1969; 2:1256.
    • (1969) Lancet , vol.2 , pp. 1256
    • Denson, K.W.E.1
  • 4
    • 0021988726 scopus 로고
    • Heterogeneity of hereditary and acquired factor X deficiencies by combined immunochemical and functional analyses
    • Fair DS, Edgington TS. Heterogeneity of hereditary and acquired factor X deficiencies by combined immunochemical and functional analyses. Br J Haematol 1985; 59:235-48.
    • (1985) Br J Haematol , vol.59 , pp. 235-248
    • Fair, D.S.1    Edgington, T.S.2
  • 5
    • 1842396185 scopus 로고
    • Coagulation factor synthesis by the liver with special reference to factors V and VIII
    • Fondu P and Thijs O (eds). Martinus Nijhoff Boston
    • Giddings JC. Coagulation factor synthesis by the liver with special reference to factors V and VIII. In Fondu P and Thijs O (eds). Hemostatic Failure in Liver Disease. Martinus Nijhoff Boston, 1984; pp.5-21.
    • (1984) Hemostatic Failure in Liver Disease , pp. 5-21
    • Giddings, J.C.1
  • 6
    • 0020427478 scopus 로고
    • Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments
    • Graves CB, Munns TW, Willingham AK, Stauss AW. Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments. J Biol Chem 1982; 257:13108-13.
    • (1982) J Biol Chem , vol.257 , pp. 13108-13113
    • Graves, C.B.1    Munns, T.W.2    Willingham, A.K.3    Stauss, A.W.4
  • 7
    • 0021259955 scopus 로고
    • Human hepatoma cells secrete single chain factor X, prothrombin and antithrombin III
    • Fair DS, Bahnak BR. Human hepatoma cells secrete single chain factor X, prothrombin and antithrombin III. Blood 1984; 64: 194-204.
    • (1984) Blood , vol.64 , pp. 194-204
    • Fair, D.S.1    Bahnak, B.R.2
  • 8
    • 0018672139 scopus 로고
    • Combined functional and immunochemical analysis of normal and abnormal human factor X
    • Fair DS, Plow EF, Edgington TS. Combined functional and immunochemical analysis of normal and abnormal human factor X. J Clin Invest 1979; 64:884-94.
    • (1979) J Clin Invest , vol.64 , pp. 884-894
    • Fair, D.S.1    Plow, E.F.2    Edgington, T.S.3
  • 10
    • 0026588358 scopus 로고
    • Processing and trafficking of clotting factor X in the secretory pathway. Effects of warfarin
    • Stanton C, Wallin R. Processing and trafficking of clotting factor X in the secretory pathway. Effects of warfarin. Biochem J 1992; 284:25-31.
    • (1992) Biochem J , vol.284 , pp. 25-31
    • Stanton, C.1    Wallin, R.2
  • 11
    • 0001506214 scopus 로고
    • Activation of bovine factor X (Stuart factor): Conversion of activation of factor Xaa to Xab
    • Fujikawa K, Titani K, Davie EW. Activation of bovine factor X (Stuart factor): conversion of activation of factor Xaa to Xab. Proc Natl Acad Sci USA 1975:72:3359-63.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3359-3363
    • Fujikawa, K.1    Titani, K.2    Davie, E.W.3
  • 12
    • 0028101918 scopus 로고
    • Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa
    • Altieri DC. Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa. J Biol Chem 1994; 269:3139-42.
    • (1994) J Biol Chem , vol.269 , pp. 3139-3142
    • Altieri, D.C.1
  • 13
    • 0029095017 scopus 로고
    • Xa receptor EPR-1
    • Altieri DC. Xa receptor EPR-1. FASEB J 1995; 9:860-5.
    • (1995) FASEB J , vol.9 , pp. 860-865
    • Altieri, D.C.1
  • 14
    • 0030042202 scopus 로고    scopus 로고
    • Molecular dissection of effector cell protease receptor-1 recognition of factor Xa. Assignment of critical residues involved in antibody reactivity and ligand binding
    • Ambrosini G, Altieri DC. Molecular dissection of effector cell protease receptor-1 recognition of factor Xa. Assignment of critical residues involved in antibody reactivity and ligand binding. J Biol Chem 1996; 271:1243-8.
    • (1996) J Biol Chem , vol.271 , pp. 1243-1248
    • Ambrosini, G.1    Altieri, D.C.2
  • 15
    • 0022535992 scopus 로고
    • Activation of coagulation releases endothelial cell mitogens
    • Gajdusek C, Carbon S, Ross R, Nawroth P, Stern D. Activation of coagulation releases endothelial cell mitogens. J Cell Biol 1986; 103:419-28.
    • (1986) J Cell Biol , vol.103 , pp. 419-428
    • Gajdusek, C.1    Carbon, S.2    Ross, R.3    Nawroth, P.4    Stern, D.5
  • 16
    • 0026535444 scopus 로고
    • Coagulation factors X, Xa and protein S as potent mitogens of cultured aortic smooth muscle cells
    • Gasic GP, Arenas CP, Gasic TB, Gasic GJ. Coagulation factors X, Xa and protein S as potent mitogens of cultured aortic smooth muscle cells. Proc Natl Acad Sci USA 1992; 89:2317-20.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2317-2320
    • Gasic, G.P.1    Arenas, C.P.2    Gasic, T.B.3    Gasic, G.J.4
  • 19
    • 0028168831 scopus 로고
    • 2+ binding site yet retains function
    • 2+ binding site yet retains function. J Biol Chem 1994; 269:21495-9.
    • (1994) J Biol Chem , vol.269 , pp. 21495-21499
    • Rezaie, A.R.1    Esmon, C.T.2
  • 21
    • 0030054839 scopus 로고    scopus 로고
    • A binding site on the surface of activated human platelets is shared by factor X and prothrombin
    • Scandura JM, Ahmad SS, Walsh PN. A binding site on the surface of activated human platelets is shared by factor X and prothrombin. Biochemistry 1996; 35:8890-902.
    • (1996) Biochemistry , vol.35 , pp. 8890-8902
    • Scandura, J.M.1    Ahmad, S.S.2    Walsh, P.N.3
  • 22
    • 0028045068 scopus 로고
    • Human monocytes support factor X activation by factor VIIa, independent of tissue factor: Implications for the therapeutic mechanism of high-dose factor VIIa in hemophilia
    • Hoffman M, Monroe DM, Roberts HR. Human monocytes support factor X activation by factor VIIa, independent of tissue factor: implications for the therapeutic mechanism of high-dose factor VIIa in hemophilia. Blood 1994; 83:38-42.
    • (1994) Blood , vol.83 , pp. 38-42
    • Hoffman, M.1    Monroe, D.M.2    Roberts, H.R.3
  • 23
    • 0028241067 scopus 로고
    • The activation of human blood coagulation factor X on the surface of endothelial cells: A comparison with various vascular cells, platelets and monocytes
    • Brinkman H-JM, Mertens K, Holthuis J, Zwart-Huinink LA, Grijm K, Van Mourik JA. The activation of human blood coagulation factor X on the surface of endothelial cells: a comparison with various vascular cells, platelets and monocytes. Brit J Haematol 1994; 87:332-42.
    • (1994) Brit J Haematol , vol.87 , pp. 332-342
    • Brinkman, H.-J.M.1    Mertens, K.2    Holthuis, J.3    Zwart-Huinink, L.A.4    Grijm, K.5    Van Mourik, J.A.6
  • 24
    • 0024346843 scopus 로고
    • Platelet receptor occupancy with factor IXa promotes factor X activation
    • Ahmad SS, Rawala-Sheikh R, Walsh P. Platelet receptor occupancy with factor IXa promotes factor X activation. J Biol Chem 1989; 264:20012-6.
    • (1989) J Biol Chem , vol.264 , pp. 20012-20016
    • Ahmad, S.S.1    Rawala-Sheikh, R.2    Walsh, P.3
  • 25
    • 0019831499 scopus 로고
    • The role of phospholipid and FVIIIa in the activation of bovine factor X
    • van Diejen G, Tans G, Rosing J, Hemker HC. The role of phospholipid and FVIIIa in the activation of bovine factor X. J Biol Chem 1981; 256:3433-42.
    • (1981) J Biol Chem , vol.256 , pp. 3433-3442
    • Van Diejen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4
  • 28
    • 0025010978 scopus 로고
    • Proteolytic activation of human factors IX and X by recombinant human factor VIIa: Effects of calcium, phospholipids and tissue factor
    • Komiyama Y, Pedersen AH, Kisiel W. Proteolytic activation of human factors IX and X by recombinant human factor VIIa: Effects of calcium, phospholipids and tissue factor. Biochemistry 1990; 29:9418-25.
    • (1990) Biochemistry , vol.29 , pp. 9418-9425
    • Komiyama, Y.1    Pedersen, A.H.2    Kisiel, W.3
  • 29
    • 0020654344 scopus 로고
    • A monoclonal antibody which inhibits the factor Va:Factor Xa interaction
    • Tucker MM, Foster WB, Katzmann JA, Mann KG. A monoclonal antibody which inhibits the factor Va:factor Xa interaction. J Biol Chem 1983; 258:1210-4.
    • (1983) J Biol Chem , vol.258 , pp. 1210-1214
    • Tucker, M.M.1    Foster, W.B.2    Katzmann, J.A.3    Mann, K.G.4
  • 30
    • 0023185058 scopus 로고
    • Epitope mapping of functional domains of human factor V with murine monoclonal antibodies
    • Annamalai AE, Rao RK, Chin HCC et al. Epitope mapping of functional domains of human factor V with murine monoclonal antibodies. Blood 1987; 70:139-46.
    • (1987) Blood , vol.70 , pp. 139-146
    • Annamalai, A.E.1    Rao, R.K.2    Chin, H.C.C.3
  • 31
    • 0021322174 scopus 로고
    • Comparison of coagulation factor Xa and des-(1-44) factor Xa in the assembly of prothrombinase
    • Skogen WF, Esmon CT, Cox AC. Comparison of coagulation factor Xa and des-(1-44) factor Xa in the assembly of prothrombinase. J Biol Chem 1984; 259:2306-10.
    • (1984) J Biol Chem , vol.259 , pp. 2306-2310
    • Skogen, W.F.1    Esmon, C.T.2    Cox, A.C.3
  • 32
    • 0025812794 scopus 로고
    • The γ-carboxyglutamic acid and epidermal growth factor-like domains of factor X
    • Persson E, Valcarce C, Stenflo J. The γ-carboxyglutamic acid and epidermal growth factor-like domains of factor X. J Biol Chem 1991; 266:2453-8.
    • (1991) J Biol Chem , vol.266 , pp. 2453-2458
    • Persson, E.1    Valcarce, C.2    Stenflo, J.3
  • 33
    • 0029036487 scopus 로고
    • Factor Xa-factor Va complex assembles in two dimensions with unexpectedly high affinity: An experimental and theoretical analysis
    • Ye J, Esmon CT. Factor Xa-factor Va complex assembles in two dimensions with unexpectedly high affinity: an experimental and theoretical analysis. Biochemistry 1995; 34:6448-53.
    • (1995) Biochemistry , vol.34 , pp. 6448-6453
    • Ye, J.1    Esmon, C.T.2
  • 35
    • 0026695765 scopus 로고
    • Construction, expression and characterization of a chimera of factor IX and factor X
    • Hertzberg MS, Ben-Tal O, Furie B, Furie BC. Construction, expression and characterization of a chimera of factor IX and factor X. J Biol Chem 1992; 267:14759-66.
    • (1992) J Biol Chem , vol.267 , pp. 14759-14766
    • Hertzberg, M.S.1    Ben-Tal, O.2    Furie, B.3    Furie, B.C.4
  • 36
    • 0026710630 scopus 로고
    • Molecular recognition sites on factor Xa which participate in the prothrombinase complex
    • Chattopadhyay A, James HL, Fair DS. Molecular recognition sites on factor Xa which participate in the prothrombinase complex. J Biol Chem 1992; 267:12323-9.
    • (1992) J Biol Chem , vol.267 , pp. 12323-12329
    • Chattopadhyay, A.1    James, H.L.2    Fair, D.S.3
  • 37
    • 0029131205 scopus 로고
    • Characterization of the binding of factor Xa to fibrinogen/fibrin derivatives and localization of the factor Xa binding site on fibrinogen
    • Iino M, Takeya H, Takemitsu T, Nakagaki T, Gabazza EC, Suzuki K. Characterization of the binding of factor Xa to fibrinogen/fibrin derivatives and localization of the factor Xa binding site on fibrinogen. Eur J Biochem 1995; 232:90-7.
    • (1995) Eur J Biochem , vol.232 , pp. 90-97
    • Iino, M.1    Takeya, H.2    Takemitsu, T.3    Nakagaki, T.4    Gabazza, E.C.5    Suzuki, K.6
  • 38
    • 0027199974 scopus 로고
    • Importance of factor Xa in determining the procoagulant activity of whole-blood clots
    • Eisenberg PR, Siegel JE, Abendschein DR, Miletich JP. Importance of factor Xa in determining the procoagulant activity of whole-blood clots. J Clin Invest 1993; 91:1877-83.
    • (1993) J Clin Invest , vol.91 , pp. 1877-1883
    • Eisenberg, P.R.1    Siegel, J.E.2    Abendschein, D.R.3    Miletich, J.P.4
  • 39
    • 0029028011 scopus 로고
    • Prothrombinase components can accelerate tissue plasminogen activator-catalyzed plasminogen activation
    • Pryzdial ELG, Bajzar L, Nesheim ME. Prothrombinase components can accelerate tissue plasminogen activator-catalyzed plasminogen activation. J Biol Chem 1995; 270:17871-7.
    • (1995) J Biol Chem , vol.270 , pp. 17871-17877
    • Pryzdial, E.L.G.1    Bajzar, L.2    Nesheim, M.E.3
  • 40
    • 0029938845 scopus 로고    scopus 로고
    • Autoproteolysis or plasmin-mediated cleavage of factor Xaα exposes a plasminogen binding site and inhibits coagulation
    • Pryzdial ELG, Kessler GE. Autoproteolysis or plasmin-mediated cleavage of factor Xaα exposes a plasminogen binding site and inhibits coagulation. J Biol Chem 1996; 271:16614-20.
    • (1996) J Biol Chem , vol.271 , pp. 16614-16620
    • Pryzdial, E.L.G.1    Kessler, G.E.2
  • 41
    • 0030008810 scopus 로고    scopus 로고
    • Kinetics of blood coagulation factor Xaα autoproteolytic conversion to factor Xaβ
    • Pryzdial ELG, Kessler GE. Kinetics of blood coagulation factor Xaα autoproteolytic conversion to factor Xaβ. J Biol Chem 1996; 271: 16621-6.
    • (1996) J Biol Chem , vol.271 , pp. 16621-16626
    • Pryzdial, E.L.G.1    Kessler, G.E.2
  • 42
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • Huang Z-F, Wun T-C, Broze GJ. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem 1993; 268:26950-5.
    • (1993) J Biol Chem , vol.268 , pp. 26950-26955
    • Huang, Z.-F.1    Wun, T.-C.2    Broze, G.J.3
  • 43
    • 0028154010 scopus 로고
    • Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor
    • Lindhout T, Willems G, Blezer R, Hemker HC. Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor. Biochem J 1994; 297:131-6.
    • (1994) Biochem J , vol.297 , pp. 131-136
    • Lindhout, T.1    Willems, G.2    Blezer, R.3    Hemker, H.C.4
  • 44
    • 0028932993 scopus 로고
    • Tissue factor pathway inhibitor and the revised theory of coagulation
    • Broze GJ. Tissue factor pathway inhibitor and the revised theory of coagulation. Annu Rev Med 1995; 46:103-12.
    • (1995) Annu Rev Med , vol.46 , pp. 103-112
    • Broze, G.J.1
  • 45
    • 0029983760 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis of coagulation factor Xa requires cell surface-bound tissue factor pathway inhibitor
    • Ho G, Toomey JR, Broze GJ, Schwartz AL. Receptor-mediated endocytosis of coagulation factor Xa requires cell surface-bound tissue factor pathway inhibitor. J Biol Chem 1996; 271:9497-502.
    • (1996) J Biol Chem , vol.271 , pp. 9497-9502
    • Ho, G.1    Toomey, J.R.2    Broze, G.J.3    Schwartz, A.L.4
  • 46
    • 0021233471 scopus 로고
    • Inhibition of human activated factor X by antithrombin III and α-proteinase inhibitor in human plasma
    • Gitel SN, Medina VM, Wessler S. Inhibition of human activated factor X by antithrombin III and α-proteinase inhibitor in human plasma. J Biol Chem 1984; 259:6890-5.
    • (1984) J Biol Chem , vol.259 , pp. 6890-6895
    • Gitel, S.N.1    Medina, V.M.2    Wessler, S.3
  • 47
    • 0027199974 scopus 로고
    • Importance of factor Xa in determining the procoagulant activity of whole-blood clots
    • Eisenberg PR, Siegel JE, Abendschein DR, Miletich JP. Importance of factor Xa in determining the procoagulant activity of whole-blood clots. J Clin Invest 1993; 91:1877-83.
    • (1993) J Clin Invest , vol.91 , pp. 1877-1883
    • Eisenberg, P.R.1    Siegel, J.E.2    Abendschein, D.R.3    Miletich, J.P.4
  • 48
    • 0028072085 scopus 로고
    • Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator
    • Barrow RT, Parker ET, Krishnaswamy S, Lollar P. Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator. J Biol Chem 1994; 269:26796-800.
    • (1994) J Biol Chem , vol.269 , pp. 26796-26800
    • Barrow, R.T.1    Parker, E.T.2    Krishnaswamy, S.3    Lollar, P.4
  • 49
    • 0023731990 scopus 로고
    • Kinetics of inactivation of membrane bound factor Va by activated protein C. Protein S modulates factor Xa ptotection
    • Solymoss S, Tucker MM, Tracy PB. Kinetics of inactivation of membrane bound factor Va by activated protein C. Protein S modulates factor Xa ptotection. J Biol Chem 1988; 263:14884-90.
    • (1988) J Biol Chem , vol.263 , pp. 14884-14890
    • Solymoss, S.1    Tucker, M.M.2    Tracy, P.B.3
  • 51
    • 0028855424 scopus 로고
    • Inhibition of the intrinsic factor X activating complex by protein S: Evidence for a specific binding of protein S to factor VIII
    • Koppelman SJ, Hackeng TM, Sixma JJ, Bouma BN. Inhibition of the intrinsic factor X activating complex by protein S: evidence for a specific binding of protein S to factor VIII. Blood 1995; 86: 1062-71.
    • (1995) Blood , vol.86 , pp. 1062-1071
    • Koppelman, S.J.1    Hackeng, T.M.2    Sixma, J.J.3    Bouma, B.N.4
  • 52
    • 0029118512 scopus 로고
    • Synergistic inhibition of the intrinsic factor X activation activation by protein S and C4b-binding protein
    • Koppelman SJ, van't Veer C, Sixma JJ, Bouma BN. Synergistic inhibition of the intrinsic factor X activation activation by protein S and C4b-binding protein. Blood 1995; 86:2653-60.
    • (1995) Blood , vol.86 , pp. 2653-2660
    • Koppelman, S.J.1    Van't Veer, C.2    Sixma, J.J.3    Bouma, B.N.4
  • 53
    • 0028030891 scopus 로고
    • Human protein S inhibits prothrombinase complex activity on endothelial cells and platelets via direct interactions with factors Va and Xa
    • Hackeng TM, van't Veer C, Meijers JCM, Bouma BN. Human protein S inhibits prothrombinase complex activity on endothelial cells and platelets via direct interactions with factors Va and Xa. J Biol Chem 1994; 269:21051-8.
    • (1994) J Biol Chem , vol.269 , pp. 21051-21058
    • Hackeng, T.M.1    Van't Veer, C.2    Meijers, J.C.M.3    Bouma, B.N.4
  • 54
    • 0022871419 scopus 로고
    • Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C
    • Leytus SP, Foster DC, Kurachi K, Davie EW. Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986; 25: 5098-102.
    • (1986) Biochemistry , vol.25 , pp. 5098-5102
    • Leytus, S.P.1    Foster, D.C.2    Kurachi, K.3    Davie, E.W.4
  • 55
    • 0025910104 scopus 로고
    • Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X
    • Messier TL, Pittman DD, Long GL, Kaufman RJ, Church WR. Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. Gene 1991; 99:291-4.
    • (1991) Gene , vol.99 , pp. 291-294
    • Messier, T.L.1    Pittman, D.D.2    Long, G.L.3    Kaufman, R.J.4    Church, W.R.5
  • 56
    • 0021760465 scopus 로고
    • Blood coagulation factor X mRNa encodes a single polypeptide chain containing a prepro leader sequence
    • Fung MR, Campbell RM, MacGillivray RTA. Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence. Nucleic Acids Res 1984; 12:4481-92.
    • (1984) Nucleic Acids Res , vol.12 , pp. 4481-4492
    • Fung, M.R.1    Campbell, R.M.2    MacGillivray, R.T.A.3
  • 57
    • 0028357936 scopus 로고
    • Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X
    • Murakawa M, Okamura T, Kamura T, Kuroiwa M, Harada M, Niho Y. Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X. Eur J Haematol 1994; 52:162-8.
    • (1994) Eur J Haematol , vol.52 , pp. 162-168
    • Murakawa, M.1    Okamura, T.2    Kamura, T.3    Kuroiwa, M.4    Harada, M.5    Niho, Y.6
  • 58
    • 0029998990 scopus 로고    scopus 로고
    • Processing and expression of rat and human clotting factor X-encoding cDNAs
    • Stanton C, Ross RP, Hutson S, Wallin R. Processing and expression of rat and human clotting factor X-encoding cDNAs. Gene 1996; 169: 269-73.
    • (1996) Gene , vol.169 , pp. 269-273
    • Stanton, C.1    Ross, R.P.2    Hutson, S.3    Wallin, R.4
  • 59
    • 0024843766 scopus 로고
    • Cloning and characterization of the 5′ end (exon 1) of the gene encoding human factor X
    • Jagadeeswaran P, Reddy SK, Rao KJ, Hamsabhushanam K, Lyman G. Cloning and characterization of the 5′ end (exon 1) of the gene encoding human factor X. Gene 1989; 84:517-9.
    • (1989) Gene , vol.84 , pp. 517-519
    • Jagadeeswaran, P.1    Reddy, S.K.2    Rao, K.J.3    Hamsabhushanam, K.4    Lyman, G.5
  • 60
    • 0029737765 scopus 로고    scopus 로고
    • Molecular reconstruction and homology modelling of the catalytic domain of the common ancestor of the haemostatic vitamin K-dependent serine proteinases
    • Krawczak M, Wacey A, Cooper DN. Molecular reconstruction and homology modelling of the catalytic domain of the common ancestor of the haemostatic vitamin K-dependent serine proteinases. Hum Genet 1996; 98:351-70.
    • (1996) Hum Genet , vol.98 , pp. 351-370
    • Krawczak, M.1    Wacey, A.2    Cooper, D.N.3
  • 65
    • 0022181227 scopus 로고
    • The structural gene for human coagulation factor X is located on chromosome 13q34
    • Scambler PJ, Williamson R. The structural gene for human coagulation factor X is located on chromosome 13q34. Cytogenet. Cell Genet 1985; 39:231-3.
    • (1985) Cytogenet. Cell Genet , vol.39 , pp. 231-233
    • Scambler, P.J.1    Williamson, R.2
  • 66
    • 0022504302 scopus 로고
    • Mapping through somatic cell hybrids and cDNA probes of protein C to chromosome 2, factor X to chromosome 13 and α1-acid glycoprotein to chromosome 9
    • Rocchi M, Roncuzzi L, Santamaria R, Archidiacono N, Dente L, Romeo G. Mapping through somatic cell hybrids and cDNA probes of protein C to chromosome 2, factor X to chromosome 13 and α1-acid glycoprotein to chromosome 9. Hum Genet 1986; 74:30-3.
    • (1986) Hum Genet , vol.74 , pp. 30-33
    • Rocchi, M.1    Roncuzzi, L.2    Santamaria, R.3    Archidiacono, N.4    Dente, L.5    Romeo, G.6
  • 68
    • 0026767457 scopus 로고
    • Liver-specific expression of the gene coding for human factor X, a blood coagulation factor
    • Miao CH, Leytus SP, Chung DW, Davie EW. Liver-specific expression of the gene coding for human factor X, a blood coagulation factor. J Biol Chem 1992; 267:7395-401.
    • (1992) J Biol Chem , vol.267 , pp. 7395-7401
    • Miao, C.H.1    Leytus, S.P.2    Chung, D.W.3    Davie, E.W.4
  • 70
    • 0030028515 scopus 로고    scopus 로고
    • Liver-enriched transcription factor HNF-4 and ubiquitous factor NF-Y are critical for expression of blood coagulation factor X
    • Hung HL, High KA. Liver-enriched transcription factor HNF-4 and ubiquitous factor NF-Y are critical for expression of blood coagulation factor X. J Biol Chem 1996; 271:2323-31.
    • (1996) J Biol Chem , vol.271 , pp. 2323-2331
    • Hung, H.L.1    High, K.A.2
  • 72
    • 0343505606 scopus 로고
    • Characterization of an almost full-length cDNA coding for human blood coagulation factor X
    • Fung MR, Hay CW, MacGillivray RTA. Characterization of an almost full-length cDNA coding for human blood coagulation factor X. Proc Natl Acad Sci USA 1985; 82:3591-5.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3591-3595
    • Fung, M.R.1    Hay, C.W.2    MacGillivray, R.T.A.3
  • 73
    • 85069111608 scopus 로고
    • Functional characterization of the 5′ regulatory region of the human factor X gene
    • Huang M-N, High KA. Functional characterization of the 5′ regulatory region of the human factor X gene. Thromb Haemost 1991; 65:726.
    • (1991) Thromb Haemost , vol.65 , pp. 726
    • Huang, M.-N.1    High, K.A.2
  • 74
  • 76
    • 0000436892 scopus 로고
    • Stuart clotting defect. Segregation of a hereditary hemorrhagic state from the heterozygous heretofore called 'stable factor' (SPCA, proconvertin factor VII deficiency)
    • Hougie C, Barrow HM, Graham JB. Stuart clotting defect. Segregation of a hereditary hemorrhagic state from the heterozygous heretofore called 'stable factor' (SPCA, proconvertin factor VII deficiency). J Clin Invest 1957; 36:485-93.
    • (1957) J Clin Invest , vol.36 , pp. 485-493
    • Hougie, C.1    Barrow, H.M.2    Graham, J.B.3
  • 77
    • 0018672139 scopus 로고
    • Combined functional and immunochemical analysis of normal and abnormal human factor X
    • Fair DS, Plow EF, Edgington TS. Combined functional and immunochemical analysis of normal and abnormal human factor X. J Clin Invest 1979; 64:884-94.
    • (1979) J Clin Invest , vol.64 , pp. 884-894
    • Fair, D.S.1    Plow, E.F.2    Edgington, T.S.3
  • 81
    • 0014834193 scopus 로고
    • A new congenital haemorrhagic condition due to the presence of an abnormal factor X (Factor X Friuli). Study of a large kindred
    • Girolami A, Molaro G, Lazzarin M, Brunetti A, Scarpa R. A new congenital haemorrhagic condition due to the presence of an abnormal factor X (Factor X Friuli). Study of a large kindred. Br J Haematol 1970; 19:179-92.
    • (1970) Br J Haematol , vol.19 , pp. 179-192
    • Girolami, A.1    Molaro, G.2    Lazzarin, M.3    Brunetti, A.4    Scarpa, R.5
  • 82
    • 0014978576 scopus 로고
    • Prothrombin level and activity in the abnormal factor X (Factor X Friuli) hemorrhagic disorder
    • Girolami A, Sticchi A, Brunetti A. Prothrombin level and activity in the abnormal factor X (Factor X Friuli) hemorrhagic disorder. Thromb Diath Haemhorrag 1971; 25:147-56.
    • (1971) Thromb Diath Haemhorrag , vol.25 , pp. 147-156
    • Girolami, A.1    Sticchi, A.2    Brunetti, A.3
  • 84
    • 0020662202 scopus 로고
    • A family with heterozygous factor X Friuli defect outside Friuli
    • Girolami A, Lazzarin M, Procidano M, Luzzatto G. A family with heterozygous factor X Friuli defect outside Friuli. Blut 1983; 46: 149-55.
    • (1983) Blut , vol.46 , pp. 149-155
    • Girolami, A.1    Lazzarin, M.2    Procidano, M.3    Luzzatto, G.4
  • 86
    • 0024410307 scopus 로고
    • Isolation and characterization of the factor X Friuli variant
    • Fair DS, Revak DJ, Hubbard JG, Girolami A. Isolation and characterization of the factor X Friuli variant. Blood 1989; 73:2108-16.
    • (1989) Blood , vol.73 , pp. 2108-2116
    • Fair, D.S.1    Revak, D.J.2    Hubbard, J.G.3    Girolami, A.4
  • 87
    • 0029990233 scopus 로고    scopus 로고
    • Characterization of recombinant human coagulation factor X Friuli
    • Kim DJ, Girolami A, James HL. Characterization of recombinant human coagulation factor X Friuli. Thromb Haemost 1996; 75: 313-7.
    • (1996) Thromb Haemost , vol.75 , pp. 313-317
    • Kim, D.J.1    Girolami, A.2    James, H.L.3
  • 88
    • 0026020326 scopus 로고
    • Molecular defect in coagulation factor X Friuli results from a substitution of serine for proline at position 343
    • James HL, Girolami A, Fair DS. Molecular defect in coagulation factor X Friuli results from a substitution of serine for proline at position 343. Blood 1991; 77:317-23.
    • (1991) Blood , vol.77 , pp. 317-323
    • James, H.L.1    Girolami, A.2    Fair, D.S.3
  • 89
    • 0029661263 scopus 로고    scopus 로고
    • Factor X St Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein
    • Rudolph AE, Mullane MP, Porche-Sorbet R, Tsuda S, Miletich JP. Factor X St Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. J Biol Chem 1996; 271:28601-6.
    • (1996) J Biol Chem , vol.271 , pp. 28601-28606
    • Rudolph, A.E.1    Mullane, M.P.2    Porche-Sorbet, R.3    Tsuda, S.4    Miletich, J.P.5
  • 92
    • 0009742233 scopus 로고
    • Molecular defect (Gla26-Asp) and its functional consequences in a hereditary factor X deficiency (Factor X Malmo 4)
    • Wallmark A, Larson P, Ljung R, Monroe D, High K. Molecular defect (Gla26-Asp) and its functional consequences in a hereditary factor X deficiency (Factor X Malmo 4). Blood 1991; 78 Suppl. 1:60a.
    • (1991) Blood , vol.78 , Issue.1 SUPPL.
    • Wallmark, A.1    Larson, P.2    Ljung, R.3    Monroe, D.4    High, K.5
  • 93
    • 0023789852 scopus 로고
    • Factor X Roma: A congenital factor X variant defective at different degrees in the intrinsic and the extrinsic activation
    • De Stefano V, Leone G, Ferrelli R, Hassan HJ, Macioce G, Bizzi B. Factor X Roma: a congenital factor X variant defective at different degrees in the intrinsic and the extrinsic activation. Brit J Haematol 1988; 69:387-91.
    • (1988) Brit J Haematol , vol.69 , pp. 387-391
    • De Stefano, V.1    Leone, G.2    Ferrelli, R.3    Hassan, H.J.4    Macioce, G.5    Bizzi, B.6
  • 95
    • 0029640083 scopus 로고
    • Factors X Wenatchee I and II:Compound heterozygosity involving two variant proteins
    • Kim DJ, Thompson AR, Nash DR, James HL. Factors X Wenatchee I and II:compound heterozygosity involving two variant proteins. Biochim Biophys Acta 1995; 1271:327-34.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 327-334
    • Kim, D.J.1    Thompson, A.R.2    Nash, D.R.3    James, H.L.4
  • 97
    • 0029918581 scopus 로고    scopus 로고
    • Factor X Stockton: A mild bleeding diathesis associated with an active site mutation in factor X
    • Messier TL, Wong CY, Bovill EG, Long GL, Church WR. Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X. Blood Coag Fibrinol 1996; 7: 5-14.
    • (1996) Blood Coag Fibrinol , vol.7 , pp. 5-14
    • Messier, T.L.1    Wong, C.Y.2    Bovill, E.G.3    Long, G.L.4    Church, W.R.5
  • 99
    • 0028984931 scopus 로고
    • Factor X Ketchikan: A variant molecule in which Gly replaces a Gla residue at position 14 in the light chain
    • Kim DJ, Thompson AR, James HL. Factor X Ketchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain. Hum Genet 1995; 95:212-4.
    • (1995) Hum Genet , vol.95 , pp. 212-214
    • Kim, D.J.1    Thompson, A.R.2    James, H.L.3
  • 100
    • 0025919758 scopus 로고
    • Factor X Santo Domingo. Evidence that the severe clinical phenotype arises from a mutation blocking secretion
    • Watzke HH, Wallmark A, Hamaguchi N, Giardina P, Stafford DW, High KA. Factor X Santo Domingo. Evidence that the severe clinical phenotype arises from a mutation blocking secretion. J Clin Invest 1991; 88:1685-9.
    • (1991) J Clin Invest , vol.88 , pp. 1685-1689
    • Watzke, H.H.1    Wallmark, A.2    Hamaguchi, N.3    Giardina, P.4    Stafford, D.W.5    High, K.A.6
  • 101
    • 0027471438 scopus 로고
    • Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum
    • Racchi M, Watzke HH, High KA, Lively MO. Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum. J Biol Chem 1993; 268:5735-40.
    • (1993) J Biol Chem , vol.268 , pp. 5735-5740
    • Racchi, M.1    Watzke, H.H.2    High, K.A.3    Lively, M.O.4
  • 102
    • 0025503855 scopus 로고
    • Targeting of proteins into the eukaryotic secretory pathway: Signal peptide structure/function relationships
    • Nothwehr SF, Gordon JI. Targeting of proteins into the eukaryotic secretory pathway: signal peptide structure/function relationships. BioEssays 1990; 12:479-84.
    • (1990) BioEssays , vol.12 , pp. 479-484
    • Nothwehr, S.F.1    Gordon, J.I.2
  • 103
    • 0025287330 scopus 로고
    • Comparative modelling methods:Application to the family of the mammalian serine proteases
    • Greer J. Comparative modelling methods:application to the family of the mammalian serine proteases. Proteins Struct Funct Genet 1990; 7:317-34.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 317-334
    • Greer, J.1
  • 105
    • 0029112076 scopus 로고
    • Molecular bases of CRM+ factor X deficiency:A frequent mutation (Ser334Pro) in the catalytic domain and substitution (Glu102Lys) in the second EGF-like domain
    • Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio MG, Ruggieri M, Rodeghiero F, Bernardi F. Molecular bases of CRM+ factor X deficiency:a frequent mutation (Ser334Pro) in the catalytic domain and substitution (Glu102Lys) in the second EGF-like domain. Brit J Haematol 1995; 90:910-5.
    • (1995) Brit J Haematol , vol.90 , pp. 910-915
    • Marchetti, G.1    Castaman, G.2    Pinotti, M.3    Lunghi, B.4    Di Iasio, M.G.5    Ruggieri, M.6    Rodeghiero, F.7    Bernardi, F.8
  • 107
    • 0024292694 scopus 로고
    • Molecular basis of coagulation
    • Furie B, Furie BC. Molecular basis of coagulation. Cell 1988; 53:505-18.
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 108
    • 0021112692 scopus 로고
    • Beta-hydroxyaspartic acid in vitamin K-dependent proteins
    • Fernlund P, Stenflo J. Beta-hydroxyaspartic acid in vitamin K-dependent proteins. J Biol Chem 1983; 258:12509-12.
    • (1983) J Biol Chem , vol.258 , pp. 12509-12512
    • Fernlund, P.1    Stenflo, J.2
  • 109
    • 0028929274 scopus 로고
    • Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site
    • Nakagawa H, Takahashi N, Fujikawa K, Kawamura Y, Iino M, Takeya H, Ogawa H, Suzuki K. Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site. Glycoconjugate J 1995; 12:173-81.
    • (1995) Glycoconjugate J , vol.12 , pp. 173-181
    • Nakagawa, H.1    Takahashi, N.2    Fujikawa, K.3    Kawamura, Y.4    Iino, M.5    Takeya, H.6    Ogawa, H.7    Suzuki, K.8
  • 110
    • 0027537465 scopus 로고
    • Carbohydrate residues modulate the activation of coagulation factor X
    • Sinha U, Wolf DL. Carbohydrate residues modulate the activation of coagulation factor X. J Biol Chem 1993; 268:3048-51.
    • (1993) J Biol Chem , vol.268 , pp. 3048-3051
    • Sinha, U.1    Wolf, D.L.2
  • 111
    • 0028968261 scopus 로고
    • Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity
    • Bharadwaj D, Harris RJ, Kisiel W, Smith KJ. Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity. J Biol Chem 1995; 270:6537-42.
    • (1995) J Biol Chem , vol.270 , pp. 6537-6542
    • Bharadwaj, D.1    Harris, R.J.2    Kisiel, W.3    Smith, K.J.4
  • 112
    • 0023239941 scopus 로고
    • The factor IX phospholipid-binding site is required for calcium-dependent activation of factor factor IX by factor XIa
    • Liebman HA, Furie BC, Furie B. The factor IX phospholipid-binding site is required for calcium-dependent activation of factor factor IX by factor XIa. J Biol Chem 1986; 262:7605-12.
    • (1986) J Biol Chem , vol.262 , pp. 7605-7612
    • Liebman, H.A.1    Furie, B.C.2    Furie, B.3
  • 113
    • 0022979292 scopus 로고
    • Preparation and properties of derivatives of bovine factor X and factor Xa from which the γ-carboxyglutamic acid domain has been removed
    • Morita T, Jackson CM. Preparation and properties of derivatives of bovine factor X and factor Xa from which the γ-carboxyglutamic acid domain has been removed. J Biol Chem 1986; 261:4015-23.
    • (1986) J Biol Chem , vol.261 , pp. 4015-4023
    • Morita, T.1    Jackson, C.M.2
  • 114
    • 0024454718 scopus 로고
    • Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X
    • Persson E, Selander M, Linse S, Drakenberg T, Ohlin A-K, Stenflo J. Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. J Biol Chem 1989; 264:16897-904.
    • (1989) J Biol Chem , vol.264 , pp. 16897-16904
    • Persson, E.1    Selander, M.2    Linse, S.3    Drakenberg, T.4    Ohlin, A.-K.5    Stenflo, J.6
  • 116
    • 0028172935 scopus 로고    scopus 로고
    • Calcium-dependent interaction between γ-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X
    • Valcarce C, Holmgren A, Stenflo J. Calcium-dependent interaction between γ-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X. J Biol Chem 269:26011-6.
    • J Biol Chem , vol.269 , pp. 26011-26016
    • Valcarce, C.1    Holmgren, A.2    Stenflo, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.