RSS-Feed abonnieren
Bitte kopieren Sie die angezeigte URL und fügen sie dann in Ihren RSS-Reader ein.
https://www.thieme-connect.de/rss/thieme/de/10.1055-s-00035024.xml
Thromb Haemost 1997; 78(01): 161-172
DOI: 10.1055/s-0038-1657520
DOI: 10.1055/s-0038-1657520
Molecular defects in rare bleeding disorders
Inherited Factor X Deficiency: Molecular Genetics and Pathophysiology
Weitere Informationen
Publikationsverlauf
Publikationsdatum:
12. Juli 2018 (online)
-
References
- 1 Mammen EF. Factor X abnormalities. Sem Thromb Haemost 1983; 9: 31-44
- 2 Girolami A. Tentative and updated classification of factor X variants. Acta Haemato 1986; 75: 58-59
- 3 Denson KWE. Abnormal forms of factor X. Lancet 1969; 2: 1256
- 4 Fair DS, Edgington TS. Heterogeneity of hereditary and acquired factor X deficiencies by combined immunochemical and functional analyses. Br J Haematol 1985; 59: 235-248
- 5 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. 05-21
- 6 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: 13108-13113
- 7 Fair DS, Bahnak BR. Human hepatoma cells secrete single chain factor X, prothrombin and antithrombin III. Blood 1984; 64: 194-204
- 8 Fair DS, Plow EF, Edgington TS. Combined functional and immunochemical analysis of normal and abnormal human factor X. J Clin Invest 1979; 64: 884-894
- 9 Henkens CM, Bom VJ, Van der Schaaf W, Pelsma PM, Sibinga CT, de Kam PJ, Van der Meer J. Plasma levels of protein S, protein C and factor X:effects of sex, hormonal state and age. Thromb Haemost 1995; 74: 1271-1275
- 10 Stanton C, Wallin R. Processing and trafficking of clotting factor X in the secretory pathway. Effects of warfarin. Biochem J 1992; 284: 25-31
- 11 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: 3359-3363
- 12 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: 3139-3142
- 13 Altieri DC. Xa receptor EPR-1. FASEB J 1995; 9: 860-865
- 14 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: 1243-1248
- 15 Gajdusek C, Carbon S, Ross R, Nawroth P, Stem D. Activation of coagulation releases endothelial cell mitogens. J Cell Biol 1986; 103: 419-428
- 16 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: 2317-2320
- 17 Nicholson AC, Nachman RL, Altieri DC, Summers BD, Ruf W, Edgington TS, Hajjar DP. Effector cell protease receptor-1 is a vascular receptor for coagulation factor Xa. J Biol Chem 1996; 271: 28407-2813
- 18 Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W. Structure of human des(l-45) factor Xa at 2.2A resolution. J Mol Biol 1993; 232: 947-966
- 19 Rezaie AR, Esmon CT. Asp70→Lys mutant of factor X lacks high affinity Ca2+ binding site yet retains function. J Biol Chem 1994; 269: 21495-21499
- 20 Sunnerhagen M, Forsen S, Hoffren A-M, Drakenberg T, Teleman O, Stenflo J. Structure of the Ca2+-free GLA domain sheds light on membrane binding of blood coagulation proteins. Nature Struct Biol 1995; 2: 504-509
- 21 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: 8890-8902
- 22 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
- 23 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: 332-342
- 24 Ahmad SS, Rawala-Sheikh R, Walsh P. Platelet receptor occupancy with factor IXa promotes factor X activation. J Biol Chem 1989; 264: 20012-20016
- 25 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: 3433-3442
- 26 ten Cate H, Bauer KA, Levi M, Edgington TS, Sublett RD, Barzegar S, Kass BL, Rosenberg RD. The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor. J Clin Invest 1993; 92: 1207-1212
- 27 Huang Q, Neuenschwander PF, Rezaie AR, Morrissey JH. Substrate recognition by tissue factor-factor VIIa. J Biol Chem 1996; 271: 21752-21757
- 28 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
- 29 Tucker MM, Foster WB, Katzmann JA, Mann KG. A monoclonal antibody which inhibits the factor Va:factor Xa interaction. J Biol Chem 1983; 258: 1210-1214
- 30 Annamalai AE, Rao RK, Chin HCC. et al Epitope mapping of functional domains of human factor V with murine monoclonal antibodies. Blood 1987; 70: 139-146
- 31 Skogen WF, Esmon CT, Cox AC. Comparison of coagulation factor Xa and des-(l-44) factor Xa in the assembly of prothrombinase. J Biol Chem 1984; 259: 2306-2310
- 32 Persson E, Valcarce C, Stenflo J. The γ-carboxyglutamic acid and epidermal growth factor-like domains of factor X. J Biol Chem 1991; 266: 2453-2458
- 33 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: 6448-6453
- 34 Nicolaes GAF, Tans G, Thomassen CLGD, Hemker HC, Pabinger I, Varadi K, Schwarz HP, Rosing J. Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C. J Biol Chem 1995; 270: 21158-21166
- 35 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: 14759-14766
- 36 Chattopadhyay A, James HL, Fair DS. Molecular recognition sites on factor Xa which participate in the prothrombinase complex. J Biol Chem 1992; 267: 12323-12329
- 37 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: 90-97
- 38 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: 1877-1883
- 39 Pryzdial ELG, Bajzar L, Nesheim ME. Prothrombinase components can accelerate tissue plasminogen activator-catalyzed plasminogen activation. J Biol Chem 1995; 270: 17871-17877
- 40 Pryzdial ELG, Kessler GE. Autoproteolysis or plasmin-mediated cleavage of factor Xaa exposes a plasminogen binding site and inhibits coagulation. J Biol Chem 1996; 271: 16614-16620
- 41 Pryzdial ELG, Kessler GE. Kinetics of blood coagulation factor Xaα autoproteolytic conversion to factor Xaβ. J Biol Chem 1996; 271: 16621-16626
- 42 Huang Z-F, Wun T-C, Broze GJ. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem 1993; 268: 26950-26955
- 43 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: 131-136
- 44 Broze GJ. Tissue factor pathway inhibitor and the revised theory of coagulation. Annu Rev Med 1995; 46: 103-112
- 45 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: 9497-9502
- 46 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: 6890-6895
- 47 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: 1877-1883
- 48 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: 26796-2800
- 49 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: 14884-14890
- 50 Heeb MJ, Rosing J, Bakker HM, Fernandez JA, Tans G, Griffin JH. Protein S binds to and inhibits factor Xa. Proc Natl Acad Sci USA 1994; 91: 2728-2732
- 51 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: 1062-1071
- 52 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: 2653-2660
- 53 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: 21051-21058
- 54 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: 5098-5102
- 55 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: 291-294
- 56 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: 4481-4492
- 57 Murakawa M, Okamuia 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: 162-168
- 58 Stanton C, Ross RP, Hutson S, Wallin R. Processing and expression of rat and human clotting factor X-encoding cDNAs. Gene 1996; 169: 269-273
- 59 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: 517-519
- 60 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: 351-370
- 61 Jaye M, Ricca G, Kaplan R, Howk R, Mudd R, Ngo KY, Fair DS, Drohan W. Polymorphism associated with the coagulation factor X gene. Nucleic Acids Res 1985; 13: 8286
- 62 Hassan HJ, Guerriero R, Chelucci C, Leonardi A, Mattia G, Leone G, Mariani G, Mannucci PM, Peschle C. Multiple polymorphism sites in factor X locus. Blood 1988; 71: 1353-1356
- 63 Hay CW, Robertson KA, Fung MR, MacGillivray RTA. RFLPs for Pstl and EcoRl in the human blood clotting factor X gene. Nucleic Acids Res 1986; 14: 5118
- 64 Wallmark A, Rose VL, Ho C, High KA. A NlalV polymorphism within the human factor X gene. Nucleic Acids Res 1991; 19: 4022
- 65 Scambler PJ, Williamson R. The structural gene for human coagulation factor X is located on chromosome 13q34. Cytogenet. Cell Genet 1985; 39: 231-233
- 66 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 αl-acid glycoprotein to chromosome 9. Hum Genet 1986; 74: 30-33
- 67 Royle NJ, Fung MR, MacGillivray RTA, Hamerton JL. The gene for clotting factor 10 is mapped to 13q32-qter. Cytogenet. Cell Genet 1986; 41: 185-188
- 68 Miao CH, Leytus SP, Chung DW, Davie EW. Liver-specific expression of the gene coding for human factorX, a blood coagulation factor. J Biol Chem 1992; 267: 7395-7401
- 69 Bahnak BR, Howk R, Morrissey JH, Ricca GA, Edgington TS, Jaye MC, Drohan WW, Fair DS. Steady state levels of factor X mRNA in liver and HepG2 cells. Blood 1987; 69: 224-230
- 70 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: 2323-2331
- 71 Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW. Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci USA 1984; 81: 3699-3702
- 72 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: 3591-3595
- 73 Huang M-N, High KA. Functional characterization of the 5’ regulatory region of the human factor X gene. Thromb Haemost 1991; 65: 726
- 74 Huang M-N, Hung H-L, Stanfield-Oakley SA, High KA. Characterization of the human blood coagulation factor X promoter. J Biol Chem 1992; 267: 15440-15446
- 75 Telfer TP, Denson KW, Wright DR. A ’new’ coagulation defect. Br J Haematol 1956; 2: 308-316
- 76 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: 485-493
- 77 Fair DS, Plow EF, Edgington TS. Combined functional and immunochemical analysis of normal and abnormal human factor X. J Clin Invest 1979; 64: 884-894
- 78 Bemardi F, Marchetti G, Patracchini P, Volinia S, Gemmati D, Simioni P, Girolami A. Partial gene deletion in a family with factor X deficiency. Blood 1989; 73: 2123-2127
- 79 Wieland K, Millar DS, Grundy CB, Mibashan RS, Kakkar VV, Cooper DN. Molecular genetic analysis of factor X deficiency :gene deletion and germline mosaicism. Hum Genet 1991; 86: 273-278
- 80 Reddy SV, Zhou Z-Q, Rao KJ, Scott JP, Watzke H, High KA, Jagadeeswaran P. Molecular characterization of human factor XsanAntonio . Blood 1989; 74: 1486-1490
- 81 Girolami A, Molaro G, Lazzarin M, Brunetti A, Scarpa R. A new congenital haemonhagie condition due to the presence of an abnormal factor X (Factor X Friuli). Study of a large kindred. Br J Haematol 1970; 19: 179-192
- 82 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: 147-156
- 83 Girolami A, Molaro G, Falomo R. Factor X Friuli coagulation disorder. Acta Haematol 1975; 54: 120-125
- 84 Girolami A, Lazzarin M, Procidano M, Luzzatto G. A family with heterozygous factor X Friuli defect outside Friuli. Blut 1983; 46: 149-155
- 85 Fair D, Revak D, Edgington T, Girolami A. Structural studies on the factor X Friuli variant. Thromb Haemost 1983; 50: 279-284
- 86 Fair DS, Revak DJ, Hubbard JG, Girolami A. Isolation and characterization of the factor X Friuli variant. Blood 1989; 73: 2108-2116
- 87 Kim DJ, Girolami A, James HL. Characterization of recombinant human coagulation factor X Friuli. Thromb Haemost 1996; 75: 313-317
- 88 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: 317-323
- 89 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: 28601-28606
- 90 Giannelli F, Green PM, Sommer SS, Poon M-C, Ludwig M, Schwaab R, Reitsma PH, Goossens M, Yoshioka A, Brownlee GG. Haemophilia B (sixth edition): a database of point mutations and short additions and deletions. Nucleic Acids Res 24: 103-118
- 91 Bernardi F, Castaman G, Redaelli R, Pinotti M, Lunghi B, Rodeghiero F, Marchetti G. Topologically equivalent mutations causing dysfunctional coagulation factors VII 294Ala→Val) and X (334Ser→Pro). Hum Molec Genet 1994; 3: 1175-1177
- 92 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. 01) 60a
- 93 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: 387-391
- 94 Odom MW, Leone G, De Stefano V, Montiel MM, Boland EJ, Anderson J, Jagadeeswaran P. Five novel point mutations:two causing haemophilia B and three causing factor X deficiency. Molec Cell Probes 1994; 8: 63-65
- 95 Kim DJ, Thompson AR, Nash DR, James HL. Factors X Wenatchee I and ILcompound heterozygosity involving two variant proteins. Biochim Biophys Acta 1995; 1271: 327-334
- 96 Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stewart D. The structure of a Ca2+-binding epidermal growth factor-like domain:its role in protein-protein interactions. Cell 1995; 82: 131-141
- 97 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
- 98 Watzke HH, Lechner K, Roberts HR, Reddy SV, Wesch DJ, Friedman P, Mahr G, Jagadeeswaran P, Monroe DM, High KA. Molecular defect (Gla+14→Lys) and its functional consequences in a hereditary factor X deficiency (Factor X “Vorarlberg”). J Biol Chem 1990; 265: 11982-11989
- 99 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: 212-214
- 100 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: 1685-1689
- 101 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: 5735-5740
- 102 Nothwehr SF, Gordon JI. Targeting of proteins into the eukaryotic secretory pathway: signal peptide structure/function relationships. BioEssays 1990; 12: 479-484
- 103 Greer J. Comparative modelling methods application to the family of the mammalian serine proteases. Proteins Struct Funct Genet 1990; 7: 317-334
- 104 Wallmark A, Ho C, Monroe DM, Tengbom L, High KA. Molecular defect in F.X ‘Öckerӧ’, a mild congenital F.X deficiency. Thromb Haemost 1991; 65: 1263
- 105 Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio MG, Ruggieri M, Rodeghiero F, Bemardi F. Molecular bases of CRM+ factor X deficiency:a frequent mutation (Ser334Pro) in the catalytic domain and substitution (Glul02Lys) in the second EGF-like domain. Brit J Haematol 1995; 90: 910-915
- 106 Tuddenham EGD, Cooper DN. The Molecular Genetics of Haemostasis and its Inherited Disorders. Oxford University Press; 1994
- 107 Furie B, Furie BC. Molecular basis of coagulation. Cell 1988; 53: 505-518
- 108 Fernlund P, Stenflo J. Beta-hydroxyaspartic acid in vitamin K- dependent proteins. J Biol Chem 1983; 258: 12509-12512
- 109 Nakagawa H, Takahashi N, Fujikawa K, Kawamura Y, lino 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: 173-181
- 110 Sinha U, Wolf DL. Carbohydrate residues modulate the activation of coagulation factor X. J Biol Chem 1993; 268: 3048-3051
- 111 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: 6537-6542
- 112 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: 7605-7612
- 113 Morita T, Jackson CM. Preparation and properties of derivatives of bovine factor X and factor Xa from which the ϒ-carboxyglutamic acid domain has been removed. J Biol Chem 1986; 261: 4015-23
- 114 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: 16897-1904
- 115 Selander-Sunnerhagen M, Persson E, Dahlqvist I, Drakenberg T, Mayhew M, Robin M, Handford P, Tilley JW, Campbell ID, Brownlee GG. The effect of aspartate hydroxylation on calcium binding to epidermal growth factor-like modules in coagulation factors IX and X. J Biol Chem 1993; 268: 23339-44
- 116 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: 26011-26016
- 117 MacGillivray RTA, Fung MR. Molecular biology of factor X. Bailliere’s Clin.Haematol 1989; 2: 897-917
- 118 Bezeaud A, Miyata T, Helley D, Zeng YZ, Kato H, Aillaud MF, Juhan-Vague I, Guillin MC. Functional consequences of the Ser334→Pro mutation in a human factor X variant (factor X Marseille). Eur J Biochem 1995; 234: 140-147