메뉴 건너뛰기




Volumn 1, Issue 7, 2003, Pages 1525-1534

Molecular recognition in the protein C anticoagulant pathway

Author keywords

Factor V; Protein C; Protein S; Thrombomodulin

Indexed keywords

ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 5A; BLOOD CLOTTING FACTOR 8A; PEPTIDE; PROTEIN C; PROTHROMBIN; SERINE PROTEINASE;

EID: 18244417756     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1046/j.1538-7836.2003.00299.x     Document Type: Review
Times cited : (74)

References (89)
  • 1
    • 0242585716 scopus 로고    scopus 로고
    • Blood coagulation
    • Dahlbäck B. Blood coagulation. Lancet 2000; 355: 1627-32.
    • (2000) Lancet , vol.355 , pp. 1627-1632
    • Dahlbäck, B.1
  • 2
    • 0034925134 scopus 로고    scopus 로고
    • Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation
    • Esmon CT. Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation. Crit Care Med 2001; 29: S48-51.
    • (2001) Crit Care Med , vol.29
    • Esmon, C.T.1
  • 3
    • 0002866615 scopus 로고    scopus 로고
    • The protein C anticoagulant system. Stamatoyannopoulos
    • G, Majerus, PW, Perlmutter, RM, Varmus, H, eds. 3rd edn. Philadelphia: W.B. Saunders Co
    • Dahlbäck B, Stenflo J. The protein C anticoagulant system. In: Stamatoyannopoulos, G, Majerus, PW, Perlmutter, RM, Varmus, H, eds. The molecular Basis of Blood Diseases, 3rd edn. Philadelphia: W.B. Saunders Co, 2001: 614-56.
    • (2001) The molecular Basis of Blood Diseases , pp. 614-656
    • Dahlbäck, B.1    Stenflo, J.2
  • 4
    • 0036124011 scopus 로고    scopus 로고
    • Factor Vand thrombotic disease: description of a Janus-faced protein
    • Nicolaes GA, Dahlbäck B. Factor Vand thrombotic disease: description of a Janus-faced protein. Arterioscler Thromb Vasc Biol 2002; 22: 530-8.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 530-538
    • Nicolaes, G.A.1    Dahlbäck, B.2
  • 5
    • 0035030340 scopus 로고    scopus 로고
    • Factor V: Dr. Jekyll and Mr Hyde
    • Mann KG, Kalafatis M. Factor V: Dr. Jekyll and Mr Hyde. Adv Exp Med Biol 2001; 489: 31-43.
    • (2001) Adv Exp Med Biol , vol.489 , pp. 31-43
    • Mann, K.G.1    Kalafatis, M.2
  • 7
    • 0028959158 scopus 로고
    • Inherited thrombophilia. resistance to activated protein C as a pathogenic factor of venous thromboembolism
    • Dahlbäck B. Inherited thrombophilia. resistance to activated protein C as a pathogenic factor of venous thromboembolism. Blood 1995; 85: 607-14.
    • (1995) Blood , vol.85 , pp. 607-614
    • Dahlbäck, B.1
  • 9
    • 0034059213 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor
    • Esmon CT. The endothelial cell protein C receptor. Thromb Haemost 2000; 83: 639-43.
    • (2000) Thromb Haemost , vol.83 , pp. 639-643
    • Esmon, C.T.1
  • 10
    • 0028832910 scopus 로고
    • The protein C anticoagulant system: inherited defects as basis for venous thrombosis
    • Dahlbäck B. The protein C anticoagulant system: inherited defects as basis for venous thrombosis. Thromb Res 1995; 77: 1-43.
    • (1995) Thromb Res , vol.77 , pp. 1-43
    • Dahlbäck, B.1
  • 11
    • 0000306073 scopus 로고    scopus 로고
    • Vitamin K-dependent proteins in blood coagulation
    • Stamatoyannopoulos, G, Majerus, PW, Perlmutter, RM, Varmus, H, eds. 3rd edn. Philadelphia: W.B. Saunders Co
    • Stenflo J, Dahlbäck B. Vitamin K-dependent proteins in blood coagulation. In: Stamatoyannopoulos, G, Majerus, PW, Perlmutter, RM, Varmus, H, eds. The molecular Bais of Blood Diseases, 3rd edn. Philadelphia: W.B. Saunders Co., 2001: 579-613.
    • (2001) The molecular Bais of Blood Diseases , pp. 579-613
    • Stenflo, J.1    Dahlbäck, B.2
  • 13
    • 0033135017 scopus 로고    scopus 로고
    • Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site-directed mutagenesis, and computer modeling
    • Knobe KE, Berntsdotter A, Shen L, Morser J, Dahlbäck B, Villoutreix BO. Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site-directed mutagenesis, and computer modeling. Proteins 1999; 35: 218-34.
    • (1999) Proteins , vol.35 , pp. 218-234
    • Knobe, K.E.1    Berntsdotter, A.2    Shen, L.3    Morser, J.4    Dahlbäck, B.5    Villoutreix, B.O.6
  • 14
    • 0029787653 scopus 로고    scopus 로고
    • Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin
    • Gerlitz B, Grinnell BW. Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin. J Biol Chem 1996; 271: 22285-8.
    • (1996) J Biol Chem , vol.271 , pp. 22285-22288
    • Gerlitz, B.1    Grinnell, B.W.2
  • 15
    • 0035968239 scopus 로고    scopus 로고
    • Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C
    • Friedrich U, Blom AM, Dahlbäck B, Villoutreix BO. Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C. J Biol Chem 2001; 276: 24122-8.
    • (2001) J Biol Chem , vol.276 , pp. 24122-24128
    • Friedrich, U.1    Blom, A.M.2    Dahlbäck, B.3    Villoutreix, B.O.4
  • 16
    • 0029790055 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex
    • Stearns-Kurosawa DJ, Kurosawa S, Mollica JS, Ferrell GL, Esmon CT. The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex. Proc Natl Acad Sci USA 1996; 93: 10212-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10212-10216
    • Stearns-Kurosawa, D.J.1    Kurosawa, S.2    Mollica, J.S.3    Ferrell, G.L.4    Esmon, C.T.5
  • 17
    • 0035869411 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor plays an important role in protein C activation in vivo
    • Taylor FB Jr, Peer GT, Lockhart MS, Ferrell G, Esmon CT. Endothelial cell protein C receptor plays an important role in protein C activation in vivo. Blood 2001; 97: 1685-8.
    • (2001) Blood , vol.97 , pp. 1685-1688
    • Taylor Jr., F.B.1    Peer, G.T.2    Lockhart, M.S.3    Ferrell, G.4    Esmon, C.T.5
  • 19
    • 2642679231 scopus 로고    scopus 로고
    • Structural investigation of the A domains of human blood coagulation factor V by molecular modeling
    • Villoutreix BO, Dahlbäck B. Structural investigation of the A domains of human blood coagulation factor V by molecular modeling. Protein Sci 1998; 7: 1317-25.
    • (1998) Protein Sci , vol.7 , pp. 1317-1325
    • Villoutreix, B.O.1    Dahlbäck, B.2
  • 20
    • 0001238260 scopus 로고    scopus 로고
    • Molecular models for the C1 and C2 domains of factor V: new structurefunction insights
    • Villoutreix B, Bucher P, Hofmann K, Baumgartner S, Dahlbäck B. Molecular models for the C1 and C2 domains of factor V: new structurefunction insights. J Mol Model 1998; 4: 268-75.
    • (1998) J Mol Model , vol.4 , pp. 268-275
    • Villoutreix, B.1    Bucher, P.2    Hofmann, K.3    Baumgartner, S.4    Dahlbäck, B.5
  • 21
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin
    • Pemberton S, Lindley P, Zaitsev V, Card G, Tuddenham EG, Kemball-Cook G. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 1997 1998; 89: 2413-21.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3    Card, G.4    Tuddenham, E.G.5    Kemball-Cook, G.6
  • 22
    • 0031804517 scopus 로고    scopus 로고
    • The Factor VIII structure and mutation resource site: HAMSTeRS, version 4
    • Kemball-Cook G, Tuddenham EG, Wacey AI. The Factor VIII structure and mutation resource site: HAMSTeRS, version 4. Nucleic Acids Res 1998; 26: 216-9.
    • (1998) Nucleic Acids Res , vol.26 , pp. 216-219
    • Kemball-Cook, G.1    Tuddenham, E.G.2    Wacey, A.I.3
  • 23
    • 0032467348 scopus 로고    scopus 로고
    • Homology models of the C domains of blood coagulation factors V and VIII: a proposed membrane binding mode for FV and FVIII C2 domains
    • Pellequer JL, Gale AJ, Griffin JH, Getzoff ED. Homology models of the C domains of blood coagulation factors V and VIII: a proposed membrane binding mode for FV and FVIII C2 domains. Blood Cells Mol Dis 1998; 24: 448-61.
    • (1998) Blood Cells Mol Dis , vol.24 , pp. 448-461
    • Pellequer, J.L.1    Gale, A.J.2    Griffin, J.H.3    Getzoff, E.D.4
  • 24
    • 0033709870 scopus 로고    scopus 로고
    • Three-dimensional model of coagulation factor Va bound to activated protein C
    • Pellequer JL, Gale AJ, Getzoff ED, Griffin JH. Three-dimensional model of coagulation factor Va bound to activated protein C. Thromb Haemost 2000; 84: 849-57.
    • (2000) Thromb Haemost , vol.84 , pp. 849-857
    • Pellequer, J.L.1    Gale, A.J.2    Getzoff, E.D.3    Griffin, J.H.4
  • 25
    • 0037082464 scopus 로고    scopus 로고
    • 3-Dimensional structure of membrane-bound coagulation factor VIII: modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography
    • Stoilova-McPhie S, Villoutreix BO, Mertens K, Kemball-Cook G, Holzenburg A. 3-Dimensional structure of membrane-bound coagulation factor VIII: modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood 2002; 99: 1215-23.
    • (2002) Blood , vol.99 , pp. 1215-1223
    • Stoilova-McPhie, S.1    Villoutreix, B.O.2    Mertens, K.3    Kemball-Cook, G.4    Holzenburg, A.5
  • 26
    • 0036707993 scopus 로고    scopus 로고
    • Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C
    • Gale AJ, Xu X, Pellequer JL, Getzoff ED, Griffin JH. Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C. Protein Sci 2002; 11: 2091-101.
    • (2002) Protein Sci , vol.11 , pp. 2091-2101
    • Gale, A.J.1    Xu, X.2    Pellequer, J.L.3    Getzoff, E.D.4    Griffin, J.H.5
  • 29
    • 0033953116 scopus 로고    scopus 로고
    • Mutations in a potential phospholipid binding loop in the C2 domain of factor V affecting the assembly of the prothrombinase complex
    • Nicolaes GA, Villoutreix BO, Dahlbäck B. Mutations in a potential phospholipid binding loop in the C2 domain of factor V affecting the assembly of the prothrombinase complex. Blood Coagul Fibrinolysis 2000; 11: 89-100.
    • (2000) Blood Coagul Fibrinolysis , vol.11 , pp. 89-100
    • Nicolaes, G.A.1    Villoutreix, B.O.2    Dahlbäck, B.3
  • 30
    • 0001252591 scopus 로고    scopus 로고
    • Identification of functionally important amino acid residues within the C2-domain of human factor V using alaninescanning mutagenesis
    • Kim SW, Quinn-Allen MA, Camp JT, Macedo-Ribeiro S, Fuentes-Prior P, Bode W, Kane WH. Identification of functionally important amino acid residues within the C2-domain of human factor V using alaninescanning mutagenesis. Biochemistry 2000; 39: 1951-8.
    • (2000) Biochemistry , vol.39 , pp. 1951-1958
    • Kim, S.W.1    Quinn-Allen, M.A.2    Camp, J.T.3    Macedo-Ribeiro, S.4    Fuentes-Prior, P.5    Bode, W.6    Kane, W.H.7
  • 31
    • 0037155149 scopus 로고    scopus 로고
    • Four hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs
    • Gilbert GE, Kaufman RJ, Arena AA, Miao H, Pipe SW. Four hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs. J Biol Chem 2002; 277: 6374-81.
    • (2002) J Biol Chem , vol.277 , pp. 6374-6381
    • Gilbert, G.E.1    Kaufman, R.J.2    Arena, A.A.3    Miao, H.4    Pipe, S.W.5
  • 32
    • 0035412387 scopus 로고    scopus 로고
    • Structure of a factor VIII C2 domain-immunoglobulin G4kappa Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII
    • Spiegel PC Jr, Jacquemin M, Saint-Remy JM, Stoddard BL, Pratt KP. Structure of a factor VIII C2 domain-immunoglobulin G4kappa Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII. Blood 2001; 98: 13-9.
    • (2001) Blood , vol.98 , pp. 13-19
    • Spiegel Jr., P.C.1    Jacquemin, M.2    Saint-Remy, J.M.3    Stoddard, B.L.4    Pratt, K.P.5
  • 33
    • 0033602920 scopus 로고    scopus 로고
    • A model describing the inactivation of factor Va by APC: bond cleavage, fragment dissociation, and product inhibition
    • Hockin MF, Cawthern KM, Kalafatis M, Mann KG. A model describing the inactivation of factor Va by APC: bond cleavage, fragment dissociation, and product inhibition. Biochemistry 1999; 38: 6918-34.
    • (1999) Biochemistry , vol.38 , pp. 6918-6934
    • Hockin, M.F.1    Cawthern, K.M.2    Kalafatis, M.3    Mann, K.G.4
  • 35
    • 0025888388 scopus 로고
    • Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. Identification of cleavage sites and correlation of proteolysis with cofactor activity
    • Fay PJ, Smudzin TM, Walker FJ. Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. Identification of cleavage sites and correlation of proteolysis with cofactor activity. J Biol Chem 1991; 266: 20139-45.
    • (1991) J Biol Chem , vol.266 , pp. 20139-20145
    • Fay, P.J.1    Smudzin, T.M.2    Walker, F.J.3
  • 36
    • 0032697629 scopus 로고    scopus 로고
    • Regulation of factor VIIIa in the intrinsic factor Xase
    • Fay PJ. Regulation of factor VIIIa in the intrinsic factor Xase. Thromb Haemost 1999; 82: 193-200.
    • (1999) Thromb Haemost , vol.82 , pp. 193-200
    • Fay, P.J.1
  • 37
    • 0029133654 scopus 로고
    • Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C
    • Nicolaes GA, Tans G, Thomassen MC, 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: 21158-66.
    • (1995) J Biol Chem , vol.270 , pp. 21158-21166
    • Nicolaes, G.A.1    Tans, G.2    Thomassen, M.C.3    Hemker, H.C.4    Pabinger, I.5    Varadi, K.6    Schwarz, H.P.7    Rosing, J.8
  • 38
    • 0028810678 scopus 로고
    • Effects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein C
    • Rosing J, Hoekema L, Nicolaes GA, Thomassen MC, Hemker HC, Varadi K, Schwarz HP, Tans G. Effects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein C. J Biol Chem 1995; 270: 27852-8.
    • (1995) J Biol Chem , vol.270 , pp. 27852-27858
    • Rosing, J.1    Hoekema, L.2    Nicolaes, G.A.3    Thomassen, M.C.4    Hemker, H.C.5    Varadi, K.6    Schwarz, H.P.7    Tans, G.8
  • 39
    • 0034661942 scopus 로고    scopus 로고
    • The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites
    • Gale AJ, Heeb MJ, Griffin JH. The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites. Blood 2000; 96: 585-93.
    • (2000) Blood , vol.96 , pp. 585-593
    • Gale, A.J.1    Heeb, M.J.2    Griffin, J.H.3
  • 40
    • 0035933906 scopus 로고    scopus 로고
    • Secondary substrate-binding exosite in the serine protease domain of activated protein C important for cleavage at Arg-506 but not at Arg-306 in factor Va
    • Friedrich U, Nicolaes GA, Villoutreix BO, Dahlbäck B. Secondary substrate-binding exosite in the serine protease domain of activated protein C important for cleavage at Arg-506 but not at Arg-306 in factor Va. J Biol Chem 2001; 276: 23105-8.
    • (2001) J Biol Chem , vol.276 , pp. 23105-23108
    • Friedrich, U.1    Nicolaes, G.A.2    Villoutreix, B.O.3    Dahlbäck, B.4
  • 41
    • 0035853784 scopus 로고    scopus 로고
    • Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA
    • Fay PJ, Mastri M, Koszelak ME, Wakabayashi H. Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA. J Biol Chem 2001; 276: 12434-9.
    • (2001) J Biol Chem , vol.276 , pp. 12434-12439
    • Fay, P.J.1    Mastri, M.2    Koszelak, M.E.3    Wakabayashi, H.4
  • 42
    • 0028290275 scopus 로고
    • Factor Vand protein S, as synergistic cofactors to activated protein C, in degradation of factor VIIIa
    • Shen L, Dahlbäck B. Factor Vand protein S, as synergistic cofactors to activated protein C, in degradation of factor VIIIa. J Biol Chem 1994; 269: 18735-8.
    • (1994) J Biol Chem , vol.269 , pp. 18735-18738
    • Shen, L.1    Dahlbäck, B.2
  • 43
    • 0030821008 scopus 로고    scopus 로고
    • Synergistic cofactor function of factor V and protein S to activated protein C in the inactivation of the factor VIIIa - factor IXa complex- species specific interactions of components of the protein C anticoagulant system
    • Shen L, He X, Dahlbäck B. Synergistic cofactor function of factor V and protein S to activated protein C in the inactivation of the factor VIIIa - factor IXa complex- species specific interactions of components of the protein C anticoagulant system. Thromb Haemost 1997; 78: 1030-6.
    • (1997) Thromb Haemost , vol.78 , pp. 1030-1036
    • Shen, L.1    He, X.2    Dahlbäck, B.3
  • 44
    • 0029792536 scopus 로고    scopus 로고
    • Factor V enhances the cofactor function of protein S in the APC-mediated inactivation of factor VIII: influence of the factor VR506Q mutation
    • Varadi K, Rosing J, Tans G, Pabinger I, Keil B, Schwarz HP. Factor V enhances the cofactor function of protein S in the APC-mediated inactivation of factor VIII: influence of the factor VR506Q mutation. Thromb Haemost 1996; 76: 208-14.
    • (1996) Thromb Haemost , vol.76 , pp. 208-214
    • Varadi, K.1    Rosing, J.2    Tans, G.3    Pabinger, I.4    Keil, B.5    Schwarz, H.P.6
  • 45
    • 0033561431 scopus 로고    scopus 로고
    • Cleavage of factorVat Arg 506 by activated protein C and the expression of anticoagulant activity of factor V
    • Thorelli E, Kaufman RJ, Dahlbäck B. Cleavage of factorVat Arg 506 by activated protein C and the expression of anticoagulant activity of factor V. Blood 1999; 93: 2552-8.
    • (1999) Blood , vol.93 , pp. 2552-2558
    • Thorelli, E.1    Kaufman, R.J.2    Dahlbäck, B.3
  • 46
    • 0032569021 scopus 로고    scopus 로고
    • The C-terminal region of the factor V B-domain is crucial for the anticoagulant activity of factor V
    • Thorelli E, Kaufman RJ, Dahlbäck B. The C-terminal region of the factor V B-domain is crucial for the anticoagulant activity of factor V. J Biol Chem 1998; 273: 16140-5.
    • (1998) J Biol Chem , vol.273 , pp. 16140-16145
    • Thorelli, E.1    Kaufman, R.J.2    Dahlbäck, B.3
  • 47
    • 0026631565 scopus 로고
    • Protein S and thrombotic disease
    • Walker FJ. Protein S and thrombotic disease. Proc Soc Exp Biol Med 1992; 200: 285-95.
    • (1992) Proc Soc Exp Biol Med , vol.200 , pp. 285-295
    • Walker, F.J.1
  • 48
    • 0025303669 scopus 로고
    • Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies
    • Dahlbäck B, Hildebrand B, Malm J. Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies. J Biol Chem 1990; 265: 8127-35.
    • (1990) J Biol Chem , vol.265 , pp. 8127-8135
    • Dahlbäck, B.1    Hildebrand, B.2    Malm, J.3
  • 49
    • 0028809322 scopus 로고
    • Expression and functional characterization of chimeras between human and bovine vitamin-K-dependent protein-S-defining modules important for the species specificity of the activated protein C cofactor activity
    • He X, Shen L, Dahlbäck B. Expression and functional characterization of chimeras between human and bovine vitamin-K-dependent protein-S-defining modules important for the species specificity of the activated protein C cofactor activity. Eur J Biochem 1995; 227: 433-40.
    • (1995) Eur J Biochem , vol.227 , pp. 433-440
    • He, X.1    Shen, L.2    Dahlbäck, B.3
  • 50
    • 0032538548 scopus 로고    scopus 로고
    • Amino acid residues in thrombin-sensitive region and first epidermal growth factor domain of vitamin K-dependent protein S determining specificity of the activated protein C cofactor function
    • He X, Shen L, Villoutreix BO, Dahlbäck B. Amino acid residues in thrombin-sensitive region and first epidermal growth factor domain of vitamin K-dependent protein S determining specificity of the activated protein C cofactor function. J Biol Chem 1998; 273: 27449-58.
    • (1998) J Biol Chem , vol.273 , pp. 27449-27458
    • He, X.1    Shen, L.2    Villoutreix, B.O.3    Dahlbäck, B.4
  • 51
    • 0032145758 scopus 로고    scopus 로고
    • Chemical synthesis of human protein S thrombin-sensitive module and first epidermal growth factor module
    • Hackeng TM, Dawson PE, Kent SB, Griffin JH. Chemical synthesis of human protein S thrombin-sensitive module and first epidermal growth factor module. Biopolymers 1998; 46: 53-63.
    • (1998) Biopolymers , vol.46 , pp. 53-63
    • Hackeng, T.M.1    Dawson, P.E.2    Kent, S.B.3    Griffin, J.H.4
  • 52
    • 84858768011 scopus 로고    scopus 로고
    • Deletion or replacement of the second EGF-like domain of protein S results in loss of APC cofactor activity
    • Mille-Baker B, Rezende SM, Simmonds RE, Lane DA, Laffan MA. Deletion or replacement of the second EGF-like domain of protein S results in loss of APC cofactor activity. Blood 2002; 10: 10.
    • (2002) Blood , vol.10 , pp. 10
    • Mille-Baker, B.1    Rezende, S.M.2    Simmonds, R.E.3    Lane, D.A.4    Laffan, M.A.5
  • 53
    • 0033854083 scopus 로고    scopus 로고
    • The second laminin G-type domain of protein S is indispensable for expression of full cofactor activity in activated protein C-catalysed inactivation of factor Va and factor VIIIa
    • Evenäs P, Garcia de Frutos P, Nicolaes GA, Dahlbäck B. The second laminin G-type domain of protein S is indispensable for expression of full cofactor activity in activated protein C-catalysed inactivation of factor Va and factor VIIIa. Thromb Haemost 2000; 84: 271-7.
    • (2000) Thromb Haemost , vol.84 , pp. 271-277
    • Evenäs, P.1    Garcia de Frutos, P.2    Nicolaes, G.A.3    Dahlbäck, B.4
  • 54
    • 0030951464 scopus 로고    scopus 로고
    • Binding site for C4b-binding protein in vitamin K-dependent protein S fully contained in carboxy-terminal laminin-G-type repeats. A study using recombinant factor IX-protein S chimeras and surface plasmon resonance
    • He X, Shen L, Malmborg AC, Smith KJ, Dahlbäck B, Linse S. Binding site for C4b-binding protein in vitamin K-dependent protein S fully contained in carboxy-terminal laminin-G-type repeats. A study using recombinant factor IX-protein S chimeras and surface plasmon resonance. Biochemistry 1997; 36: 3745-54.
    • (1997) Biochemistry , vol.36 , pp. 3745-3754
    • He, X.1    Shen, L.2    Malmborg, A.C.3    Smith, K.J.4    Dahlbäck, B.5    Linse, S.6
  • 55
    • 0033573154 scopus 로고    scopus 로고
    • Both G-type domains of protein S are required for the high-affinity interaction with C4b-binding protein
    • Evenäs P, Garcia De Frutos P, Linse S, Dahlbäck B. Both G-type domains of protein S are required for the high-affinity interaction with C4b-binding protein. Eur J Biochem 1999; 266: 935-42.
    • (1999) Eur J Biochem , vol.266 , pp. 935-942
    • Evenäs, P.1    Garcia De Frutos, P.2    Linse, S.3    Dahlbäck, B.4
  • 57
    • 0035830943 scopus 로고    scopus 로고
    • Localization of a hydrophobic binding site for anticoagulant protein S on the beta-chain of complement regulator C4b-binding protein
    • Webb JH, Villoutreix BO, Dahlbäck B, Blom AM. Localization of a hydrophobic binding site for anticoagulant protein S on the beta-chain of complement regulator C4b-binding protein. J Biol Chem 2001; 276: 4330-7.
    • (2001) J Biol Chem , vol.276 , pp. 4330-4337
    • Webb, J.H.1    Villoutreix, B.O.2    Dahlbäck, B.3    Blom, A.M.4
  • 58
    • 0024459550 scopus 로고
    • Characterization of a synthetic peptide that inhibits the interaction between protein S and C4b-binding protein
    • Walker FJ. Characterization of a synthetic peptide that inhibits the interaction between protein S and C4b-binding protein. J Biol Chem 1989; 264: 17645-8.
    • (1989) J Biol Chem , vol.264 , pp. 17645-17648
    • Walker, F.J.1
  • 60
    • 0030947233 scopus 로고    scopus 로고
    • A region of vitamin Kdependent protein S that binds to C4b binding protein (C4 BP) identified using bacteriophage peptide display libraries
    • Linse S, Härdig Y, Schultz DA, Dahlbäck B. A region of vitamin Kdependent protein S that binds to C4b binding protein (C4 BP) identified using bacteriophage peptide display libraries. J Biol Chem 1997; 272: 14658-65.
    • (1997) J Biol Chem , vol.272 , pp. 14658-14665
    • Linse, S.1    Härdig, Y.2    Schultz, D.A.3    Dahlbäck, B.4
  • 61
    • 0037177873 scopus 로고    scopus 로고
    • Structural requirements of anticoagulant protein S for its binding to the complement regulator C4b-binding protein
    • Giri TK, Linse S, Garcia de Frutos P, Yamazaki T, Villoutreix BO, Dahlbäck B. Structural requirements of anticoagulant protein S for its binding to the complement regulator C4b-binding protein. J Biol Chem 2002; 277: 15099-106.
    • (2002) J Biol Chem , vol.277 , pp. 15099-15106
    • Giri, T.K.1    Linse, S.2    Garcia de Frutos, P.3    Yamazaki, T.4    Villoutreix, B.O.5    Dahlbäck, B.6
  • 62
    • 0035342451 scopus 로고    scopus 로고
    • Threedimensional model of the SHBG-like region of anticoagulant protein S. new structure-function insights
    • Villoutreix BO, Dahlbäck B, Borgel D, Gandrille S, Muller YA. Threedimensional model of the SHBG-like region of anticoagulant protein S. new structure-function insights. Proteins 2001; 43: 203-16.
    • (2001) Proteins , vol.43 , pp. 203-216
    • Villoutreix, B.O.1    Dahlbäck, B.2    Borgel, D.3    Gandrille, S.4    Muller, Y.A.5
  • 63
    • 0037113999 scopus 로고    scopus 로고
    • Crystal Structure of a C-terminal fragment of growth arrest-specific protein Gas6. Receptor Tyrosine kinase activation by laminin G-like domains
    • Sasaki T, Knyazev PG, Cheburkin Y, Gohring W, Tisi D, Ullrich A, Timpl R, Hohenester E. Crystal Structure of a C-terminal fragment of growth arrest-specific protein Gas6. Receptor Tyrosine kinase activation by laminin G-like domains. J Biol Chem 2002; 277: 44164-70.
    • (2002) J Biol Chem , vol.277 , pp. 44164-44170
    • Sasaki, T.1    Knyazev, P.G.2    Cheburkin, Y.3    Gohring, W.4    Tisi, D.5    Ullrich, A.6    Timpl, R.7    Hohenester, E.8
  • 64
    • 0033024329 scopus 로고    scopus 로고
    • The complement regulator C4b-binding protein analyzed by molecular modeling, bioinformatics and computer-aided experimental design
    • Villoutreix BO, Blom AM, Webb J, Dahlbäck B. The complement regulator C4b-binding protein analyzed by molecular modeling, bioinformatics and computer-aided experimental design. Immunopharmacology 1999; 42: 121-34.
    • (1999) Immunopharmacology , vol.42 , pp. 121-134
    • Villoutreix, B.O.1    Blom, A.M.2    Webb, J.3    Dahlbäck, B.4
  • 65
    • 0345215157 scopus 로고    scopus 로고
    • Structural investigation of C4b-binding protein by molecular modeling: localization of putative binding sites
    • Villoutreix BO, Härdig Y, Wallqvist A, Covell DG, Garcia de Frutos P, Dahlbäck B. Structural investigation of C4b-binding protein by molecular modeling: localization of putative binding sites. Proteins 1998; 31: 391-405.
    • (1998) Proteins , vol.31 , pp. 391-405
    • Villoutreix, B.O.1    Härdig, Y.2    Wallqvist, A.3    Covell, D.G.4    Garcia de Frutos, P.5    Dahlbäck, B.6
  • 66
    • 0029808210 scopus 로고    scopus 로고
    • The amino-terminal module of the C4b-binding protein beta-chain contains the protein S-binding site
    • Härdig Y, Dahlbäck B. The amino-terminal module of the C4b-binding protein beta-chain contains the protein S-binding site. J Biol Chem 1996; 271: 20861-7.
    • (1996) J Biol Chem , vol.271 , pp. 20861-20867
    • Härdig, Y.1    Dahlbäck, B.2
  • 67
    • 0037221375 scopus 로고    scopus 로고
    • Role of CCP2 of the C4b-binding protein b-chain in protein S binding evaluated by mutagenesis and monoclonal antibodies
    • Webb JH, Villoutreix BO, Dahlbäck B, Blom AM. Role of CCP2 of the C4b-binding protein b-chain in protein S binding evaluated by mutagenesis and monoclonal antibodies. Eur J Biochem 2003; 270: 93-100.
    • (2003) Eur J Biochem , vol.270 , pp. 93-100
    • Webb, J.H.1    Villoutreix, B.O.2    Dahlbäck, B.3    Blom, A.M.4
  • 68
    • 0033382422 scopus 로고    scopus 로고
    • C4 BP b-chain SCR-2 specifically contributes to the interaction of protein S with C4 BP b-chain SCR-1
    • van de Poel RHL, Meijers JCM, Dahlbäck B, Bouma BN. C4 BP b-chain SCR-2 specifically contributes to the interaction of protein S with C4 BP b-chain SCR-1. Blood Cell Molecules Dis 1999; 25: 279-86.
    • (1999) Blood Cell Molecules Dis , vol.25 , pp. 279-286
    • van de Poel, R.H.L.1    Meijers, J.C.M.2    Dahlbäck, B.3    Bouma, B.N.4
  • 69
    • 0036721697 scopus 로고    scopus 로고
    • Vitamin K-dependent protein S localizing complement regulator C4b-binding protein to the surface of apoptotic cells
    • Webb JH, Blom AM, Dahlbäck B. Vitamin K-dependent protein S localizing complement regulator C4b-binding protein to the surface of apoptotic cells. J Immunol 2002; 169: 2580-6.
    • (2002) J Immunol , vol.169 , pp. 2580-2586
    • Webb, J.H.1    Blom, A.M.2    Dahlbäck, B.3
  • 70
    • 0029833850 scopus 로고    scopus 로고
    • Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va
    • Heeb MJ, Kojima Y, Hackeng TM, Griffin JH. Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va. Protein Sci 1996; 5: 1883-9.
    • (1996) Protein Sci , vol.5 , pp. 1883-1889
    • Heeb, M.J.1    Kojima, Y.2    Hackeng, T.M.3    Griffin, J.H.4
  • 71
    • 0032511045 scopus 로고    scopus 로고
    • Binding site for blood coagulation factor Xa involving residues 311-325 in factor Va
    • Kojima Y, Heeb MJ, Gale AJ, Hackeng TM, Griffin JH. Binding site for blood coagulation factor Xa involving residues 311-325 in factor Va. J Biol Chem 1998; 273: 14900-5.
    • (1998) J Biol Chem , vol.273 , pp. 14900-14905
    • Kojima, Y.1    Heeb, M.J.2    Gale, A.J.3    Hackeng, T.M.4    Griffin, J.H.5
  • 72
    • 0034623962 scopus 로고    scopus 로고
    • Directed glycosylation of human coagulation factor X at residue 333. Insight into factor Va-dependent prothrombin catalysis
    • Cook BC, Rudolph AE, Kurumbail RG, Porche-Sorbet R, Miletich JP. Directed glycosylation of human coagulation factor X at residue 333. Insight into factor Va-dependent prothrombin catalysis. J Biol Chem 2000; 275: 38774-9.
    • (2000) J Biol Chem , vol.275 , pp. 38774-38779
    • Cook, B.C.1    Rudolph, A.E.2    Kurumbail, R.G.3    Porche-Sorbet, R.4    Miletich, J.P.5
  • 73
    • 0035895875 scopus 로고    scopus 로고
    • Definition of a factor Va binding site in factor Xa
    • Rudolph AE, Porche-Sorbet R, Miletich JP. Definition of a factor Va binding site in factor Xa. J Biol Chem 2001; 276: 5123-8.
    • (2001) J Biol Chem , vol.276 , pp. 5123-5128
    • Rudolph, A.E.1    Porche-Sorbet, R.2    Miletich, J.P.3
  • 74
    • 0037159218 scopus 로고    scopus 로고
    • Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va: amino acid residues 323-331 of factor V represent an interactive site for activated factor X
    • Kalafatis M, Beck DO. Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va: amino acid residues 323-331 of factor V represent an interactive site for activated factor X. Biochemistry 2002; 41: 12715-28.
    • (2002) Biochemistry , vol.41 , pp. 12715-12728
    • Kalafatis, M.1    Beck, D.O.2
  • 75
    • 0347997285 scopus 로고    scopus 로고
    • Defining the factor Xa-binding site on factor Va by site-directed glycosylation
    • Steen M, Villoutreix BO, Norstrom EA, Yamazaki T, Dahlbäck B. Defining the factor Xa-binding site on factor Va by site-directed glycosylation. J Biol Chem 2002; 277: 50022-9.
    • (2002) J Biol Chem , vol.277 , pp. 50022-50029
    • Steen, M.1    Villoutreix, B.O.2    Norstrom, E.A.3    Yamazaki, T.4    Dahlbäck, B.5
  • 76
    • 0037064117 scopus 로고    scopus 로고
    • Thrombin-mediated proteolysis of factor V resulting in Gradual B-domain release and exposure of the factor Xa-binding site
    • Steen M, Dahlbäck B. Thrombin-mediated proteolysis of factor V resulting in Gradual B-domain release and exposure of the factor Xa-binding site. J Biol Chem 2002; 277: 38424-30.
    • (2002) J Biol Chem , vol.277 , pp. 38424-38430
    • Steen, M.1    Dahlbäck, B.2
  • 77
    • 0035844226 scopus 로고    scopus 로고
    • Factor IXa: factor VIIIa interaction: helix 330-338 of factor IXa interacts with residues 558-565 and spatially adjacent regions of the A2 subunit of factor VIIIa
    • Bajaj SP, Schmidt AE, Mathur A, Padmanabhan K, Zhong D, Mastri M, Fay PJ. Factor IXa: factor VIIIa interaction: helix 330-338 of factor IXa interacts with residues 558-565 and spatially adjacent regions of the A2 subunit of factor VIIIa. J Biol Chem 2001; 276: 16302-9.
    • (2001) J Biol Chem , vol.276 , pp. 16302-16309
    • Bajaj, S.P.1    Schmidt, A.E.2    Mathur, A.3    Padmanabhan, K.4    Zhong, D.5    Mastri, M.6    Fay, P.J.7
  • 78
    • 0032722436 scopus 로고    scopus 로고
    • Factor VIII-factor IX interactions: molecular sites involved in enzyme-cofactor complex assembly
    • Mertens K, Celie PH, Kolkman JA, Lenting PJ. Factor VIII-factor IX interactions: molecular sites involved in enzyme-cofactor complex assembly. Thromb Haemost 1999; 82: 209-17.
    • (1999) Thromb Haemost , vol.82 , pp. 209-217
    • Mertens, K.1    Celie, P.H.2    Kolkman, J.A.3    Lenting, P.J.4
  • 79
    • 0037036401 scopus 로고    scopus 로고
    • The connecting segment between both epidermal growth factor-like domains in blood coagulation factor IX contributes to stimulation by factor VIIIa and its isolated A2 domain
    • Celie PH, Van Stempvoort G, Fribourg C, Schurgers LJ, Lenting PJ, Mertens K. The connecting segment between both epidermal growth factor-like domains in blood coagulation factor IX contributes to stimulation by factor VIIIa and its isolated A2 domain. J Biol Chem 2002; 277: 20214-20.
    • (2002) J Biol Chem , vol.277 , pp. 20214-20220
    • Celie, P.H.1    Van Stempvoort, G.2    Fribourg, C.3    Schurgers, L.J.4    Lenting, P.J.5    Mertens, K.6
  • 80
    • 0037144428 scopus 로고    scopus 로고
    • The Nterminal epidermal growth factor-like domain of coagulation factor IX. Probing its functions in the activation of factor IX and factor X with a monoclonal antibody
    • Persson KE, Villoutreix BO, Thämlitz AM, Knobe KE, Stenflo J. The Nterminal epidermal growth factor-like domain of coagulation factor IX. Probing its functions in the activation of factor IX and factor X with a monoclonal antibody. J Biol Chem 2002; 277: 35616-24.
    • (2002) J Biol Chem , vol.277 , pp. 35616-35624
    • Persson, K.E.1    Villoutreix, B.O.2    Thämlitz, A.M.3    Knobe, K.E.4    Stenflo, J.5
  • 83
    • 0032773568 scopus 로고    scopus 로고
    • Involvement of Lys 62 (217) and Lys 63 (218): of human anticoagulant protein C in heparin stimulation of inhibition by the protein C inhibitor
    • Shen L, Villoutreix BO, Dahlbäck B. Involvement of Lys 62 (217) and Lys, 1999; 63 (218): of human anticoagulant protein C in heparin stimulation of inhibition by the protein C inhibitor. Thromb Haemost; 82: 72-9.
    • (1999) Thromb Haemost , vol.82 , pp. 72-79
    • Shen, L.1    Villoutreix, B.O.2    Dahlbäck, B.3
  • 84
    • 0037076527 scopus 로고    scopus 로고
    • Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C
    • Yang L, Manithody C, Rezaie AR. Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C. Biochemistry 2002; 41: 6149-57.
    • (2002) Biochemistry , vol.41 , pp. 6149-6157
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 85
    • 0037047277 scopus 로고    scopus 로고
    • Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C
    • Gale AJ, Tsavaler A, Griffin JH. Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C. J Biol Chem 2002; 277: 28836-40.
    • (2002) J Biol Chem , vol.277 , pp. 28836-28840
    • Gale, A.J.1    Tsavaler, A.2    Griffin, J.H.3
  • 86
    • 0032716327 scopus 로고    scopus 로고
    • Structural prediction and analysis of endothelial cell protein C/activated protein C receptor
    • Villoutreix BO, Blom AM, Dahlbäck B. Structural prediction and analysis of endothelial cell protein C/activated protein C receptor. Protein Eng 1999; 12: 833-40.
    • (1999) Protein Eng , vol.12 , pp. 833-840
    • Villoutreix, B.O.1    Blom, A.M.2    Dahlbäck, B.3
  • 87
    • 0029874551 scopus 로고    scopus 로고
    • Protein fold recognition using sequencederived predictions
    • Fischer D, Eisenberg D. Protein fold recognition using sequencederived predictions. Protein Sci 1996; 5: 947-55.
    • (1996) Protein Sci , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 88
    • 0031137254 scopus 로고    scopus 로고
    • A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S. from biostructural pathology to species-specific cofactor activity
    • Villoutreix BO, Teleman O, Dahlbäck B. A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S. from biostructural pathology to species-specific cofactor activity. J Comput Aided Mol Des 1997; 11: 293-304.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 293-304
    • Villoutreix, B.O.1    Teleman, O.2    Dahlbäck, B.3
  • 89
    • 0031743385 scopus 로고    scopus 로고
    • Topological studies of the amino terminal modules of vitamin Kdependent protein S using monoclonal antibody epitope mapping and molecular modeling
    • Giri TK, Villoutreix BO, Wallqvist A, Dahlbäck B, de Frutos PG. Topological studies of the amino terminal modules of vitamin Kdependent protein S using monoclonal antibody epitope mapping and molecular modeling. Thromb Haemost 1998; 80: 798-804.
    • (1998) Thromb Haemost , vol.80 , pp. 798-804
    • Giri, T.K.1    Villoutreix, B.O.2    Wallqvist, A.3    Dahlbäck, B.4    de Frutos, P.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.