SEARCH

SEARCH BY CITATION

References

  • Agarwala KL, Kawabata SI, Takao T, Murata H, Shimonishi Y, Nishimura H, Iwanga S. 1994. Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169. Biochemistry 33: 51675171.
  • Ahmad SS, Rawala-Sheikh R, Cheung WF, Jameson BA, Stafford DW, Walsh PN. 1994. High affinity specific factor IXa binding to platelets is mediated in part by residues 3–11. Biochemistry 33: 1204812055.
  • Astermark J, Bjork I, Ohlin AK, Stenflo J. 1991. Structural requirements for Ca2+ binding to the γ-carboxyglutamic acid and epidermal growth factorlike regions of factor IX. J Biol Chem 266: 24302437.
  • Astermark J, Hogg PJ, Bjork I, Stenflo J. 1992. Effects of γ-carboxyglutamic acid and epidermal growth factor-like modules of factor IX on factor X activation. J Biol Chem 267: 32493256.
  • Astermark J, Hogg PJ, Stenflo J. 1994. The y-carboxyglutamic acid and epidermal growth factor-like modules of factor IXaβ. J Biol Chem 269: 36823689.
  • Barenholz Y, Gibbes D, Litman BJ, Goll J, Thompson TE, Carlson FD. 1977. A simple method for the preparation of homogeneous phospholipid vesicles. Biochemistry 16: 28062810.
  • Bharadwaj D, Harris RJ, Kisiel W, Smith KJ. 1995. Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity. J Biol Chem 270: 65376542.
  • Bond MD, Huberty MC, Jankowski MA, Vath JE, Strang AM, Scoble HA. 1994a. Identification of O-glycosylation, sulfation and phosphorylation sites in the activation peptide of human plasma factor IX. Blood 84 (Suppl 1): 53la.
  • Bond MD, Jankowski MA, Huberty MC, Patel H, Scoble HA. 1994b. Structural analysis of recombinant human factor IX. Blood 84 (Suppl 1): 194a.
  • Borowski M, Furie BC, Furie B. 1986. Prothrombin undergoes two metal-dependent conformational transitions required for phospholipid binding. J Biol Chem 261: 16241628.
  • Chen PS, Toribara TY, Warner H. 1956. Microdetermination of phosphorus. Anal Chem 28: 17561758.
  • Cheung W, Hamaguchi N, Smith KJ, Stafford DW. 1992. The binding of human factor IX to endothelial cells is mediated by residues 3–11. J Biol Chem 267: 2052920531.
  • Cheung WF, Stafford DW, Sugo T. 1996. Localization of a calcium-binding epitope to the amino terminal region of the Gla domain of human factor IX. Thromb Res 81: 6573.
  • Cheung WF, Wolberg AS, Stafford DW, Smith KJ. 1995. Localization of a metal-dependent epitope to the amino terminal residues 33–40 of human factor IX. Thromb Res 80: 419427.
  • Christiansen WT, Castellino FJ. 1994. Properties of recombinant chimeric human protein C and activated protein C containing the γ-carboxyglutamic acid and trailing helical stack domains of protein C replaced by those of human coagulation factor IX. Biochemistry 33: 59015911.
  • Christiansen WT, Geng JP, Castellino FJ. 1995. Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C. Biochemistry 34: 80828090.
  • Cohen SA, Strydom DJ. 1988. Amino acid analysis utilizing phenylisothiocyanate derivatives. Anal Biochem 174: 116.
  • Derian CK, VanDusen W, Przysiecki CT, Walsh PN, Berkner KL, Kaufman RJ, Friedman PA. 1989. Inhibitors of 2-ketoglutarate-dependent dioxygenases block aspartyl β-hydroxylation of recombinant human factor IX in several mammalian expression systems. J Biol Chem 264: 66156618.
  • DiScipio RG, Hermodson MA, Yates SG, Davie EW. 1977. A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S. Biochemistry 16: 698706.
  • Fernlund P, Stenflo J. 1983. Beta-hydroxyaspartic acid in vitamin K-dependent proteins. J Biol Chem 258: 1250912512.
  • Foster WB, Anagnostopoulos A, Bonam D, Costigan RJ, Knight A, Sterl KS, Switzer MB, Walsh RE. 1995. Development of a process for purification of recombinant human factor IX. Blood 86 (Suppl 1): 870a.
  • Freedman SJ, Blostein MD, Baleja J, Jacobs M, Furie BC, Furie B. 1996. Identification of the phospholipid binding site in the vitamin K-dependent protein factor IX. J Biol Chem 271: 1622716236.
  • Freedman SJ, Furie BC, Furie B, Baleja JD. 1995a. Structure of the factor IX Gla domain bound to calcium ions. Biochemistry 34: 1212612137.
  • Freedman SJ, Furie BC, Furie B, Baleja JD. 1995b. Structure of the metal-free y-carboxyglutamic acid-rich membrane binding region of factor IX by 2D NMR spectroscopy. J Biol Chem 270: 79807987.
  • Furie B, Furie BC. 1988. Molecular basis of blood coagulation. Cell 53: 505518.
  • Gianelli F, Green PM, Sommer SS, Lillicrap DP, Ludwig M, Schwaab R, Reitsma PH, Goosens M, Yoshioka A, Brownlee GG. 1994. Hemophilia B: Database of point mutations and short additions and deletions. Nucleic Acids Res 22: 35343546.
  • Gilbert GE, Furie BC, Furie B. 1990. Binding of factor VIII to phospholipid vesicles. J Biol Chem 265: 815822.
  • Harrison S, Clancy B, Brodeur S, Oakes P, Miller D, Drapeau D, Hamilton M, Charlebois T, Leonard M, McCarthy M, Zollner R, Adamson SR. 1995. Development of a serum-free process for recombinant factor IX expression in Chinese hamster ovary cells. Thromb Haemost 73: 1222.
  • Jacobs M, Freedman SJ, Furie BC, Furie B. 1994. Membrane binding properties of the factor IX y-carboxyglutamic acid-rich domain prepared by chemical synthesis. J Biol Chem 269: 2549425501.
  • Jorgensen MJ, Cantor AB, Furie BC, Furie B. 1987. Expression of completely y-carboxylated recombinant human prothrombin. J Biol Chem 262: 67296734.
  • Kaufman RJ, Wasley LC, Furie BC, Furie B, Shoemaker CB. 1986. Expression, purification, and characterization of recombinant γ-carboxylated human factor IX. J Biol Chem 261: 96229628.
  • Koeberl DD, Bottema CDK, Buerstedde JM, Sommer SS. 1989. Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG. Am J Hum Genet 45: 448457.
  • Liebman HA, Furie BC, Furie B. 1987. The factor IX phospholipid-binding site is required for calcium-dependent activation of factor IX by factor XIa. J Biol Chem 262: 76057612.
  • Limentani SA, Roth DA, Furie BC, Furie B. 1993. Recombinant blood clotting proteins for treatment of hemorrhagic disorders. Semin Thromb Hemost 19: 6272.
  • Nelsestuen GL, Broderius M, Martin G. 1976. Role of y-carboxyglutamic acid. Cation specificity of prothrombin and factor X-phospholipid binding. J Biol Chem 251: 68866893.
  • Nelsestuen GL, Zytkovicz TH. 1974. The mode of action of vitamin K. Identification of gamma-carboxyglutamic acid as a component of prothrombin. J Biol Chem 249: 63476350.
  • Neuenschwander P, Jesty J. 1988. A comparison of phospholipid and platelets in the activation of human factor VIII by thrombin and factor Xa, and in the activation of factor X. Blood 72: 17611770.
  • Pendurthi UR, Tukey RH, Rao LVM. 1992. Characterization of rabbit factor IX cDNA. Thromb Res 65: 177186.
  • Proctor RR, Rapaport SI. 1961. The partial thromboplastin time with kaolin. Am J Clin Pathol 36: 212219.
  • Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stuart D. 1995. The structure of a Ca2+ binding epidermal growth factor-like domain: Its role in protein-protein interaction. Cell 82: 131141.
  • Ratcliffe JV, Furie B, Furie BC. 1993. The importance of specific γ-carboxyglutamic acid residues in prothrombin: Evaluation by site-specific mutagenesis. J Biol Chem 268: 2433924345.
  • Rick ME. 1982. Activation of factor VIII by factor IXa. Blood 60: 744751.
  • Ryan J, Wolitzky B, Heimer E, Lambrose T, Felix A, Tam JP, Huang LH, Naworth P, Wilner G, Kisiel W, Nelsestuen GL, Stem DM. 1989. Structural determinants of the factor IX molecule mediating interaction with the endothelial cell binding site are distinct from those involved in phospholipid binding. J Biol Chem 264: 2028320287.
  • Soriano-Garcia M, Padmanabhan K, de Vos AM, Tulinsky A. 1992. The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry 31: 25542566.
  • Stenflo J, Fernlund P, Egan W, Roepstorff P. 1974. Vitamin K-dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci USA 71: 27302733.
  • Stem DM, Drillings M, Nossel HL, Hurlet-Jensen A, LaGamma KS, Owen J. 1983. Binding of factors IX and IXa to cultured vascular endothelial cells. Proc Natl Acad Sci USA 80: 41194123.
  • Thim L, Bjoem S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen AH, Hedner U. 1988. Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 27: 77857793.
  • Vermeer C. 1990. Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase. Biochem J 266: 625636.
  • Vysotchin A, Medved LV, Ingham KC. 1993. Domain structure and domain-domain interactions in human coagulation factor IX. J Biol Chem 268: 84368446.
  • Ware J, Diuguid DL, Liebman HA, Rabiet MJ, Kasper CK, Furie BC, Furie B, Stafford DW. 1989. Factor IX San Dimas: Substitution of glutamine for arginine-4 in the propeptide leads to incomplete γ-carboxylation and altered phospholipid binding properties. J Biol Chem 264: 1140111406.
  • Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ. 1993. PACE/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J Biol Chem 268: 84588465.
  • White G, Shapiro A, Ragni M, Kaye J, Tubridy K, McCarthy K, Courter S. 1995. Phase I/II pharmacokinetics, safety and efficacy data of recombinant human factor IX in previously treated patients with hemophilia B. Blood 86 (Suppl 1): 193a.
  • Yao SN, DeSilva AH, Kurachi S, Samuelson LC, Kurachi K. 1991. Characterization of a mouse factor IX cDNA and developmental regulation of the factor IX gene expression in liver. Thromb Haemost 65: 5258.
  • Zhang L, Castellino FJ. 1993. The contributions of individual γ-carboxyglutamic acid residues in the calcium-dependent binding of recombinant human protein C to acidic phospholipid vesicles. J Biol Chem 268: 1204012045.
  • Zhang L, Jhingan A, Castellino FJ. 1992. Role of individual γ-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activity. Blood 80: 945952.