메뉴 건너뛰기




Volumn 78, Issue 1, 1997, Pages 151-160

Inherited factor VII deficiency: Molecular genetics and pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 7; THROMBOPLASTIN;

EID: 0030813937     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1657519     Document Type: Conference Paper
Times cited : (91)

References (104)
  • 1
    • 0029794555 scopus 로고    scopus 로고
    • Targeted disruption of the murine tissue factor gene results in embryonic lethality
    • Toomey JR, Kratzer KE, Lasky NM, Stanton JJ, Broze GJ. Targeted disruption of the murine tissue factor gene results in embryonic lethality. Blood 1996; 88: 1583-1587.
    • (1996) Blood , vol.88 , pp. 1583-1587
    • Toomey, J.R.1    Kratzer, K.E.2    Lasky, N.M.3    Stanton, J.J.4    Broze, G.J.5
  • 2
    • 0027402655 scopus 로고
    • Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation
    • Morrissey JH, Macik BG, Neuenschwander PF, Comp PC.Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation. Blood 1993; 81: 734-744.
    • (1993) Blood , vol.81 , pp. 734-744
    • Morrissey, J.H.1    Macik, B.G.2    Neuenschwander, P.F.3    Comp, P.C.4
  • 4
    • 0020579182 scopus 로고
    • Factor VII and ischaemic heart disease: Epidemiologic evidence
    • Meade TW. Factor VII and ischaemic heart disease: epidemiologic evidence. Haemostasis 1983; 13: 178-185.
    • (1983) Haemostasis , vol.13 , pp. 178-185
    • Meade, T.W.1
  • 8
    • 0022410305 scopus 로고
    • Hereditary factor VII deficiency: Heterogeneity defined by combined functional and immunochemical analysis
    • Triplett DA, Brandt JT, Batard MA, Dixon JS, Fair DS. Hereditary factor VII deficiency: heterogeneity defined by combined functional and immunochemical analysis. Blood 1985; 66: 1284-1287.
    • (1985) Blood , vol.66 , pp. 1284-1287
    • Triplett, D.A.1    Brandt, J.T.2    Batard, M.A.3    Dixon, J.S.4    Fair, D.S.5
  • 10
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congenital clotting factor abnormalities
    • Goodnough LT, Saito H, Ratnoff OD. Thrombosis or myocardial infarction in congenital clotting factor abnormalities. Medicine 1983; 62: 248-255.
    • (1983) Medicine , vol.62 , pp. 248-255
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 11
    • 0029153854 scopus 로고
    • Inherited factor VII deficiency: Genetics and molecular pathology
    • Tuddenham EGD, Pemberton S, Cooper DN. Inherited factor VII deficiency: genetics and molecular pathology. Thromb. Haemost. 1995; 74: 313-321.
    • (1995) Thromb. Haemost. , vol.74 , pp. 313-321
    • Tuddenham, E.G.D.1    Pemberton, S.2    Cooper, D.N.3
  • 12
    • 0022411248 scopus 로고
    • Distribution of factor VIII mRNA and antigen in human liver and other tissues
    • Wion KL, Kelly D, Summerfield JA, Tuddenham EGD, Lawn RM. Distribution of factor VIII mRNA and antigen in human liver and other tissues. Nature 1985; 317: 726-729.
    • (1985) Nature , 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
  • 13
    • 0020556855 scopus 로고
    • Quantitation of factor VII in the plasma of normal and warfarin-treated individuals by radioimmunoassay
    • Fair DS. Quantitation of factor VII in the plasma of normal and warfarin-treated individuals by radioimmunoassay. Blood 1983; 62: 784-791.
    • (1983) Blood , vol.62 , pp. 784-791
    • Fair, D.S.1
  • 14
    • 0029951107 scopus 로고    scopus 로고
    • Site-directed mutagenesis but not g-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor
    • Persson E, Nielsen LS. Site-directed mutagenesis but not g-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor. FEBS Letts 1996; 385: 241-243.
    • (1996) FEBS Letts , vol.385 , pp. 241-243
    • Persson, E.1    Nielsen, L.S.2
  • 16
    • 0030068977 scopus 로고    scopus 로고
    • Kinetics of human factor VII activation
    • Butenas S, Mann KG. Kinetics of human factor VII activation. Biochemistry 1996; 35: 1904-1910.
    • (1996) Biochemistry , vol.35 , pp. 1904-1910
    • Butenas, S.1    Mann, K.G.2
  • 17
    • 0025778142 scopus 로고
    • A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z
    • Iwanaga S, Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T. A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Adv. Exp. Med. Biol. 1990; 281: 121-131.
    • (1990) Adv. Exp. Med. Biol. , vol.281 , pp. 121-131
    • Iwanaga, S.1    Nishimura, H.2    Kawabata, S.3    Kisiel, W.4    Hase, S.5    Ikenaka, T.6
  • 18
    • 0025764566 scopus 로고
    • Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine
    • Bjoern S, Foster DC, Thim L, Wiberg FC, Christensen M, Komiyama Y, Pedersen AH, Kisiel W. Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. J. Biol. Chem. 1991; 266:11051-11057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11051-11057
    • Bjoern, S.1    Foster, D.C.2    Thim, L.3    Wiberg, F.C.4    Christensen, M.5    Komiyama, Y.6    Pedersen, A.H.7    Kisiel, W.8
  • 19
    • 0023784390 scopus 로고
    • Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells
    • Thim L, Bjoern S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen AH, Hedner U. Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 1988; 27: 7785-7793.
    • (1988) Biochemistry , vol.27 , pp. 7785-7793
    • Thim, L.1    Bjoern, S.2    Christensen, M.3    Nicolaisen, E.M.4    Lund-Hansen, T.5    Pedersen, A.H.6    Hedner, U.7
  • 20
    • 0023851758 scopus 로고
    • Tissue factor and hemostasis
    • Nemerson Y. Tissue factor and hemostasis. Blood 1988; 71: 1-8.
    • (1988) Blood , vol.71 , pp. 1-8
    • Nemerson, Y.1
  • 21
    • 0025355427 scopus 로고
    • Synthesis, purification and characterization of an Arg152→Gln site directed mutant of recombinant human blood clotting factor VII
    • Wildgoose P, Berkner KL, Kisiel W. Synthesis, purification and characterization of an Arg152→Gln site directed mutant of recombinant human blood clotting factor VII. Biochemistry 1990; 29: 3413-3420.
    • (1990) Biochemistry , vol.29 , pp. 3413-3420
    • Wildgoose, P.1    Berkner, K.L.2    Kisiel, W.3
  • 22
    • 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: 9418-9425.
    • (1990) Biochemistry , vol.29 , pp. 9418-9425
    • Komiyama, Y.1    Pedersen, A.H.2    Kisiel, W.3
  • 23
    • 11944261500 scopus 로고
    • Hemophilia as a defect of the tissue factor pathway of blood coagulation. Effect of factors VIII and IX on factor X activation in a continuous flow reactor
    • Repke K, Gemmell CH, Guha A, Turitto VT, Broze GJ, Nemerson Y. Hemophilia as a defect of the tissue factor pathway of blood coagulation. Effect of factors VIII and IX on factor X activation in a continuous flow reactor. Proc. Natl. Acad. Sci. USA 1990; 87: 7623-7627.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7623-7627
    • Repke, K.1    Gemmell, C.H.2    Guha, A.3    Turitto, V.T.4    Broze, G.J.5    Nemerson, Y.6
  • 25
    • 0030068977 scopus 로고    scopus 로고
    • Kinetics of human factor VII activation
    • Butenas S, Mann KG. Kinetics of human factor VII activation-(Biochemistry 1996; 35: 1904-1910.
    • (1996) Biochemistry , vol.35 , pp. 1904-1910
    • Butenas, S.1    Mann, K.G.2
  • 26
    • 0029917898 scopus 로고    scopus 로고
    • Studies of the activation of factor VII bound to tissue factor
    • Rao LV, Williams T, Rapaport SI. Studies of the activation of factor VII bound to tissue factor. Blood 1996; 87: 3738-3748.
    • (1996) Blood , vol.87 , pp. 3738-3748
    • Rao, L.V.1    Williams, T.2    Rapaport, S.I.3
  • 28
    • 0028094639 scopus 로고
    • Structure of the extracellular domain of human tisue factor: Location of the factor VIIa binding site
    • Muller YA, Ultsch MH, Kelley RF, de Vos AM. Structure of the extracellular domain of human tisue factor: location of the factor VIIa binding site. Biochemistry 1994; 33: 10864-10870.
    • (1994) Biochemistry , vol.33 , pp. 10864-10870
    • Muller, Y.A.1    Ultsch, M.H.2    Kelley, R.F.3    De Vos, A.M.4
  • 29
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf W, Schullek JR, Stone MJ, Edgington TS. Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry 1994; 33: 1565-1572.
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3    Edgington, T.S.4
  • 30
    • 0028019121 scopus 로고
    • Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis
    • Gibbs, CS, McCurdy SN, Leung LLK, Paborsky LR. Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis. Biochemistry 1994; 33: 14003-14010.
    • (1994) Biochemistry , vol.33 , pp. 14003-14010
    • Gibbs, C.S.1    McCurdy, S.N.2    Leung, L.L.K.3    Paborsky, L.R.4
  • 31
    • 0029992658 scopus 로고    scopus 로고
    • Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa
    • Dickinson CD, Kelly CR, Ruf W. Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa. Proc. Natl. Acad. Sci. USA 1996; 93: 14379-14384.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14379-14384
    • Dickinson, C.D.1    Kelly, C.R.2    Ruf, W.3
  • 32
    • 0029156910 scopus 로고
    • The roles of factor VII's structural domains in tissue factor binding
    • Chang JY, Stafford DW, Straight DL. The roles of factor VII's structural domains in tissue factor binding. Biochemistry 1995; 34: 12227-12232.
    • (1995) Biochemistry , vol.34 , pp. 12227-12232
    • Chang, J.Y.1    Stafford, D.W.2    Straight, D.L.3
  • 33
    • 0029903723 scopus 로고    scopus 로고
    • The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor
    • McCallum CD, Hapak RC, Neuenschwander PF, Morrissey JH, Johnson AE. The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor. J. Biol. Chem. 1996; 271: 28168-28175.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28168-28175
    • McCallum, C.D.1    Hapak, R.C.2    Neuenschwander, P.F.3    Morrissey, J.H.4    Johnson, A.E.5
  • 36
    • 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: 7395-7401.
    • (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
  • 38
    • 1842356609 scopus 로고    scopus 로고
    • unpublished results
    • D.S. Millar, unpublished results.
    • Millar, D.S.1
  • 39
    • 0027400886 scopus 로고
    • Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII
    • Brothers AB, Clarke BJ, Sheffield WP, Blajchman MA. Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII. Thromb. Res. 1993; 69: 231-238.
    • (1993) Thromb. Res. , vol.69 , pp. 231-238
    • Brothers, A.B.1    Clarke, B.J.2    Sheffield, W.P.3    Blajchman, M.A.4
  • 41
    • 0028357936 scopus 로고
    • Analysis of the partial nucleotide sequences and deuced 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 deuced primary structures of the protease domains of mammalian blood coagulation factors VII and X. Eur. J. Haematol. 1994; 52: 162-168.
    • (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
  • 42
    • 0030442463 scopus 로고    scopus 로고
    • Nucleotide structure and characterization of the murine blood coagulation factor VII gene
    • 199
    • Idusogie E, Rosen ED, Carmeliet P, Collen D, Castellino FJ. Nucleotide structure and characterization of the murine blood coagulation factor VII gene. Thromb. Haemost. 199; 76:957964.
    • Thromb. Haemost. , vol.76 , pp. 957-964
    • Idusogie, E.1    Rosen, E.D.2    Carmeliet, P.3    Collen, D.4    Castellino, F.J.5
  • 45
    • 0025860324 scopus 로고
    • A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals
    • Green F, Kelleher C, Wilkes H, Temple A, Meade T, Humphries S. A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals. Arterioscl. Thromb. 1991; 11: 540-546.
    • (1991) Arterioscl. Thromb. , vol.11 , pp. 540-546
    • Green, F.1    Kelleher, C.2    Wilkes, H.3    Temple, A.4    Meade, T.5    Humphries, S.6
  • 46
    • 0026716531 scopus 로고
    • Genetic and environmental determinants of factor VII coagulant activity in different ethnic groups at differing risk of coronary heart disease
    • Lane A, Cruikshank JK, Stewart J, Henderson A, Humphries S, Green F. Genetic and environmental determinants of factor VII coagulant activity in different ethnic groups at differing risk of coronary heart disease. Atherosclerosis 1992; 94: 43-50.
    • (1992) Atherosclerosis , vol.94 , pp. 43-50
    • Lane, A.1    Cruikshank, J.K.2    Stewart, J.3    Henderson, A.4    Humphries, S.5    Green, F.6
  • 47
    • 0028107482 scopus 로고
    • Factor VII coagulant activity and antigen levels in healthy men are determined by interaction between factor VII genotype and plasma triglyceride concentration
    • Humphries SE, Lane A, Green FR, Cooper J, Miller GJ. Factor VII coagulant activity and antigen levels in healthy men are determined by interaction between factor VII genotype and plasma triglyceride concentration. Arterioscl. Thromb. 1994; 14: 193-198.
    • (1994) Arterioscl. Thromb. , vol.14 , pp. 193-198
    • Humphries, S.E.1    Lane, A.2    Green, F.R.3    Cooper, J.4    Miller, G.J.5
  • 48
    • 0027947548 scopus 로고
    • Elevated levels of factor VII activity in the postprandial state: Effect of the factor VII Arg-Gln polymorphism
    • Silveria A, Green F, Karpe F, BlombÑck M, Humphries S, Hamsten A. Elevated levels of factor VII activity in the postprandial state: effect of the factor VII Arg-Gln polymorphism. Thromb. Haemost. 1994; 72: 734-739.
    • (1994) Thromb. Haemost. , vol.72 , pp. 734-739
    • Silveria, A.1    Green, F.2    Karpe, F.3    BlombÑck, M.4    Humphries, S.5    Hamsten, A.6
  • 51
    • 0030066703 scopus 로고    scopus 로고
    • The factor VII Arg/Gln353 polymorphism determines factor VII coagulant activity in patients with myocardial infarction (MI) and control subjects in Belfast and in France but is not a strong indicator of MI risk in the ECTIM study
    • Lane A, Green F, Scarabin PY, Nicaud V, Bara L, Humphries S, Evans A, Luc G, Cambou JP, Arveiler D, Cambien F. The factor VII Arg/Gln353 polymorphism determines factor VII coagulant activity in patients with myocardial infarction (MI) and control subjects in Belfast and in France but is not a strong indicator of MI risk in the ECTIM study. Atherosclerosis 1996; 119: 119-127.
    • (1996) Atherosclerosis , vol.119 , pp. 119-127
    • Lane, A.1    Green, F.2    Scarabin, P.Y.3    Nicaud, V.4    Bara, L.5    Humphries, S.6    Evans, A.7    Luc, G.8    Cambou, J.P.9    Arveiler, D.10    Cambien, F.11
  • 53
    • 0029836469 scopus 로고    scopus 로고
    • Association of factor VII:C levels with environmental and genetic factors in patients with ischaemic heart disease and coronary atheroma characterized by angiography
    • Heywood DM, Ossei-Gerning N, Grant PJ. Association of factor VII:C levels with environmental and genetic factors in patients with ischaemic heart disease and coronary atheroma characterized by angiography. Thromb. Haemost. 1996; 76: 161-165.
    • (1996) Thromb. Haemost. , vol.76 , pp. 161-165
    • Heywood, D.M.1    Ossei-Gerning, N.2    Grant, P.J.3
  • 54
    • 0028170627 scopus 로고
    • Association of factor VII genotype with plasma factor VII activity and antigen levels in healthy Indian adults and interaction with triglycerides
    • Saha N, Liu Y, Heng CK, Hong S, Low PS, Tay JS. Association of factor VII genotype with plasma factor VII activity and antigen levels in healthy Indian adults and interaction with triglycerides. Arterioscl. Thromb. 1994; 14: 1923-1927.
    • (1994) Arterioscl. Thromb. , vol.14 , pp. 1923-1927
    • Saha, N.1    Liu, Y.2    Heng, C.K.3    Hong, S.4    Low, P.S.5    Tay, J.S.6
  • 55
    • 0029043916 scopus 로고
    • Genetic polymorphism (Arg353ÆGln) in coagulation factor VII gene and factor VII levels (coagulant activity, antigen and binding ability to tissue factor) in 101 healthy Japanese
    • Takamiya O. Genetic polymorphism (Arg353ÆGln) in coagulation factor VII gene and factor VII levels (coagulant activity, antigen and binding ability to tissue factor) in 101 healthy Japanese. Scand. J. Clin. Lab. Invest. 1995; 55: 211-215.
    • (1995) Scand. J. Clin. Lab. Invest. , vol.55 , pp. 211-215
    • Takamiya, O.1
  • 56
    • 0343213918 scopus 로고
    • Reduced plasma factor VII coagulant activity due to the Arg353Gln polymorphism in the factor VII gene results from defective secretion
    • Arbini AA, Bauer KA. Reduced plasma factor VII coagulant activity due to the Arg353Gln polymorphism in the factor VII gene results from defective secretion. Blood 1994; 84 Suppl.1: 86a.
    • (1994) Blood , vol.84 , Issue.1 SUPPL.
    • Arbini, A.A.1    Bauer, K.A.2
  • 57
    • 0026716531 scopus 로고
    • Genetic and environmental determinants of factor VII coagulant activity in different ethnic groups at differing risk of coronary heart disease
    • Lane A, Cruickshank JK, Mitchell J, Henderson A, Humphries S, Green F. Genetic and environmental determinants of factor VII coagulant activity in different ethnic groups at differing risk of coronary heart disease. Atherosclerosis 1992; 94: 43-50.
    • (1992) Atherosclerosis , vol.94 , pp. 43-50
    • Lane, A.1    Cruickshank, J.K.2    Mitchell, J.3    Henderson, A.4    Humphries, S.5    Green, F.6
  • 58
    • 0028107482 scopus 로고
    • Factor VII coagulant activity and antigen levels in men are determined by interaction between factor VII genotype and plasma triglyceride concentration
    • Humphries SE, Lane A, Green F, Cooper J, Miller G. Factor VII coagulant activity and antigen levels in men are determined by interaction between factor VII genotype and plasma triglyceride concentration. Arterioscl. Thromb. 1994; 14: 193-198.
    • (1994) Arterioscl. Thromb. , vol.14 , pp. 193-198
    • Humphries, S.E.1    Lane, A.2    Green, F.3    Cooper, J.4    Miller, G.5
  • 61
    • 0027537854 scopus 로고
    • A polymorphism in the 5′ region of coagulation factor VII gene (F7) caused by an inserted decanucleotide
    • Marchetti G, Patracchini P, Papacchini M, Ferrati M, Bernardi F. A polymorphism in the 5′ region of coagulation factor VII gene (F7) caused by an inserted decanucleotide. Hum. Genet. 1993; 90: 575-576.
    • (1993) Hum. Genet. , vol.90 , pp. 575-576
    • Marchetti, G.1    Patracchini, P.2    Papacchini, M.3    Ferrati, M.4    Bernardi, F.5
  • 63
    • 0029919365 scopus 로고    scopus 로고
    • Low plasma levels of factor VIIc and antigen are more strongly associated with the 10 base pair promoter (-323) insertion than the glutamine 353 variant
    • Humphries S, Temple A, Lane A, Green F, Cooper J, Miller G. Low plasma levels of factor VIIc and antigen are more strongly associated with the 10 base pair promoter (-323) insertion than the glutamine 353 variant. Thromb. Haemost. 1996; 75: 567-572.
    • (1996) Thromb. Haemost. , vol.75 , pp. 567-572
    • Humphries, S.1    Temple, A.2    Lane, A.3    Green, F.4    Cooper, J.5    Miller, G.6
  • 64
    • 0030071173 scopus 로고    scopus 로고
    • Functional characterization of the human factor VII 5′-flanking region
    • Pollak ES, Hung H-L, Godin W, Overton GC, High KA. Functional characterization of the human factor VII 5′-flanking region. J. Biol. Chem. 1996; 271: 1738-1747.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1738-1747
    • Pollak, E.S.1    Hung, H.-L.2    Godin, W.3    Overton, G.C.4    High, K.A.5
  • 65
    • 0029129331 scopus 로고
    • Orphan nuclear receptor HNF-4 binds to the human coagulation factor VII promoter
    • Erdmann D, Heim J. Orphan nuclear receptor HNF-4 binds to the human coagulation factor VII promoter. J. Biol. Chem. 1995; 270: 22988-22996.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22988-22996
    • Erdmann, D.1    Heim, J.2
  • 67
    • 0031043580 scopus 로고    scopus 로고
    • The 10-base-pair insertion in the promoter of the factor VII gene is not associated with lower levels of factor VIIC in Afrocarribeans
    • Temple A, Luong LA, Cruickshank K, Humphries SE. The 10-base-pair insertion in the promoter of the factor VII gene is not associated with lower levels of factor VIIC in Afrocarribeans. Thromb. Haemost. 1997; 77: 213-214.
    • (1997) Thromb. Haemost. , vol.77 , pp. 213-214
    • Temple, A.1    Luong, L.A.2    Cruickshank, K.3    Humphries, S.E.4
  • 68
    • 0023932377 scopus 로고
    • The human factor VII gene is polymorphic due to variation in repeat copy number in a minisatellite
    • O'Hara PJ, Grant FJ. The human factor VII gene is polymorphic due to variation in repeat copy number in a minisatellite. Gene 1988; 66: 147-158.
    • (1988) Gene , vol.66 , pp. 147-158
    • O'Hara, P.J.1    Grant, F.J.2
  • 71
  • 73
    • 0026510949 scopus 로고
    • Transforming growth factor b inhibits expression of fibrinogen and factor VII in a hepatoma cell line
    • Hassan HJ, Chelucci C, Peschle C, Sorrentino V. Transforming growth factor b inhibits expression of fibrinogen and factor VII in a hepatoma cell line. Thromb. Haemost. 1992; 67: 478-483.
    • (1992) Thromb. Haemost. , vol.67 , pp. 478-483
    • Hassan, H.J.1    Chelucci, C.2    Peschle, C.3    Sorrentino, V.4
  • 82
    • 0025871447 scopus 로고
    • Purification and characterization of factor VII 304-Gln: A variant molecule with reduced activity isolated from a clinically unaffected male
    • O'Brien DP, Gale KM, Anderson JS, McVey JH, Miller GJ, Meade TW, Tuddenham EGD. Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male. Blood 1991; 78: 132-140.
    • (1991) Blood , vol.78 , pp. 132-140
    • O'Brien, D.P.1    Gale, K.M.2    Anderson, J.S.3    McVey, J.H.4    Miller, G.J.5    Meade, T.W.6    Tuddenham, E.G.D.7
  • 83
  • 84
    • 1842316974 scopus 로고    scopus 로고
    • Two new missense mutations (P134T and A244V) in the the coagulation factor VII gene
    • in press
    • AlShinawi C, Scerri C, Galdies R, Aquilina A, Felice AE. Two new missense mutations (P134T and A244V) in the the coagulation factor VII gene. Hum. Mutation 1997; in press.
    • (1997) Hum. Mutation
    • AlShinawi, C.1    Scerri, C.2    Galdies, R.3    Aquilina, A.4    Felice, A.E.5
  • 89
    • 0029665491 scopus 로고    scopus 로고
    • A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule
    • Arbini AA, Mannucci PM, Bauer KA. A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 1996; 87: 5085-5094.
    • (1996) Blood , vol.87 , pp. 5085-5094
    • Arbini, A.A.1    Mannucci, P.M.2    Bauer, K.A.3
  • 90
    • 0031026003 scopus 로고    scopus 로고
    • Severe factor VII deficiency due to a mutation disrupting a hepatocyte nuclear factor 4 binding site in the factor VII promoter
    • Arbini AA, Pollak ES, Bayleran JK, High KA, Bauer KA. Severe factor VII deficiency due to a mutation disrupting a hepatocyte nuclear factor 4 binding site in the factor VII promoter. Blood 1997; 89: 176-182.
    • (1997) Blood , vol.89 , pp. 176-182
    • Arbini, A.A.1    Pollak, E.S.2    Bayleran, J.K.3    High, K.A.4    Bauer, K.A.5
  • 91
    • 0006528141 scopus 로고
    • Mutations in the factor VII gene of Norwegian FVII deficient patients
    • Kavlie A, Wright MS, Stormorken H, Prydz H. Mutations in the factor VII gene of Norwegian FVII deficient patients. Thromb. Haemost. 1993; 69: 612.
    • (1993) Thromb. Haemost. , vol.69 , pp. 612
    • Kavlie, A.1    Wright, M.S.2    Stormorken, H.3    Prydz, H.4
  • 92
    • 1842311277 scopus 로고    scopus 로고
    • Factor VII Coimbra: A novel splice site mutation in the human factor VII gene
    • Rosa H, Diniz MJ, Lavinha J. Factor VII Coimbra: a novel splice site mutation in the human factor VII gene. Eur. J. Hum. Genet. 1996; 4 Suppl. 1: 72.
    • (1996) Eur. J. Hum. Genet. , vol.4 , Issue.1 SUPPL. , pp. 72
    • Rosa, H.1    Diniz, M.J.2    Lavinha, J.3
  • 93
    • 0006584897 scopus 로고
    • Factor VII Hamilton: A novel type 2 mutation located at residue 57 in the first EGF domain of human factor VII
    • Chen Q, Clarke BJ, Blajchman MA, Ofusu FA. Factor VII Hamilton: a novel type 2 mutation located at residue 57 in the first EGF domain of human factor VII. Thromb. Haemost. 1993; 69: 1291.
    • (1993) Thromb. Haemost. , vol.69 , pp. 1291
    • Chen, Q.1    Clarke, B.J.2    Blajchman, M.A.3    Ofusu, F.A.4
  • 95
    • 0028988004 scopus 로고
    • Factor VII Shinjo: A dysfunctional factor VII variant homozygous for the substitution Gln for Arg at position 79
    • Takamiya O, Abe S, Yoshioka A, Nakajima K, McVey JH, Tuddenham EGD. Factor VII Shinjo: a dysfunctional factor VII variant homozygous for the substitution Gln for Arg at position 79. Haemostasis 1995; 25: 89-97.
    • (1995) Haemostasis , vol.25 , pp. 89-97
    • Takamiya, O.1    Abe, S.2    Yoshioka, A.3    Nakajima, K.4    McVey, J.H.5    Tuddenham, E.G.D.6
  • 97
    • 0006560279 scopus 로고
    • Molecular characterization of human factor VII Kansas (GK704): Substitution of Gln100 by Arg in one allele and of Arg304 by Gln possibly in the other allele
    • Kuppuswamy MN, Sabharwal AK, Birktoft JJ, Bajaj SP. Molecular characterization of human factor VII Kansas (GK704): substitution of Gln100 by Arg in one allele and of Arg304 by Gln possibly in the other allele. Thromb. Haemost. 1993; 69: 1292.
    • (1993) Thromb. Haemost. , vol.69 , pp. 1292
    • Kuppuswamy, M.N.1    Sabharwal, A.K.2    Birktoft, J.J.3    Bajaj, S.P.4
  • 98
    • 0027337367 scopus 로고
    • A missense mutation (178Cys→Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene
    • Marchetti G, Ferrati M, Patracchini P, Redaelli R, Bernardi F. A missense mutation (178Cys→Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene. Hum. Molec. Genet. 1993; 2: 1055-1056.
    • (1993) Hum. Molec. Genet. , vol.2 , pp. 1055-1056
    • Marchetti, G.1    Ferrati, M.2    Patracchini, P.3    Redaelli, R.4    Bernardi, F.5
  • 99
  • 100
    • 0028175691 scopus 로고
    • Factor VII Mie: Homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg (247) (CGC) in the catalytic domain
    • Ohiwa M, Hayashi T, Wada H, Minamikawa K, Shirakawa S, Suzuki K. Factor VII Mie: homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg (247) (CGC) in the catalytic domain. Thromb. Haemost. 1994; 71: 773-777.
    • (1994) Thromb. Haemost. , vol.71 , pp. 773-777
    • Ohiwa, M.1    Hayashi, T.2    Wada, H.3    Minamikawa, K.4    Shirakawa, S.5    Suzuki, K.6
  • 101
    • 0028059812 scopus 로고
    • Molecular analysis of Polish patients with factor VII deficiency
    • Arbini AA, Bodkin D, Lopaciuk S, Bauer KA. Molecular analysis of Polish patients with factor VII deficiency. Blood 1994; 84: 2214-2220.
    • (1994) Blood , vol.84 , pp. 2214-2220
    • Arbini, A.A.1    Bodkin, D.2    Lopaciuk, S.3    Bauer, K.A.4
  • 102
    • 0027528846 scopus 로고
    • The dysfunction of coagulation factor VII Padua results from substitution of arginine 304 by glutamine
    • James HL, Girolami A, Hubbard JG, Kumar A, Fair DS. The dysfunction of coagulation factor VII Padua results from substitution of arginine 304 by glutamine. Biochim. Biophys. Acta 1993; 1172: 301-305.
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 301-305
    • James, H.L.1    Girolami, A.2    Hubbard, J.G.3    Kumar, A.4    Fair, D.S.5
  • 103
    • 0028340150 scopus 로고
    • Impaired human tissue factor-mediated activity in blood clotting factor VII Nagoya (Arg304→Trp)
    • Matsushita T, Kojima T, Emi N, Takahashi I, Saito H. Impaired human tissue factor-mediated activity in blood clotting factor VII Nagoya (Arg304→Trp). J. Biol. Chem. 1994; 269: 7355-7363.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7355-7363
    • Matsushita, T.1    Kojima, T.2    Emi, N.3    Takahashi, I.4    Saito, H.5
  • 104
    • 0029866660 scopus 로고    scopus 로고
    • Factor VII G331D: A variant molecule involving replacement of a residue in the substrate-binding region of the catalytic domain
    • Zheng D-O, Shurafa M, James HL. Factor VII G331D: a variant molecule involving replacement of a residue in the substrate-binding region of the catalytic domain. Blood Coag. Fibrinol. 1996; 7: 93-96.
    • (1996) Blood Coag. Fibrinol. , vol.7 , pp. 93-96
    • Zheng, D.-O.1    Shurafa, M.2    James, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.