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Volumn 91, Issue 5, 2004, Pages 886-898

Penthalaris, a novel recombinant five-Kunitz tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick vector of Lyme disease, Ixodes scapularis

Author keywords

Anticoagulant; Inhibitor; Ixodes scapularis; Kunitz; Tick saliva; Tissue factor pathway

Indexed keywords

ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 7A; CHROMOGENIC SUBSTRATE; COMPLEMENTARY DNA; CYSTEINE; DIMER; ENZYME PRECURSOR; MONOMER; PENTHALARIS; PLACENTA PROTEIN 5; RECOMBINANT PROTEIN; RECOMBINANT TISSUE FACTOR PATHWAY INHIBITOR; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 2442483514     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th03-11-0715     Document Type: Article
Times cited : (106)

References (79)
  • 1
    • 0028932993 scopus 로고
    • Tissue factor pathway inhibitor and the revised theory of coagulation
    • Broze GJ Jr. Tissue factor pathway inhibitor and the revised theory of coagulation. Annu Rev Med 1995; 46: 103-12.
    • (1995) Annu. Rev. Med. , vol.46 , pp. 103-112
    • Broze Jr., G.J.1
  • 2
    • 0002056702 scopus 로고    scopus 로고
    • Coagulation cascade: An overview
    • Loscalzo J, Schafer AI (eds.): 2d ed. Baltimore, MD: Williams and Wilkins
    • Jenny NS, Mann KG. Coagulation cascade: an overview, in Loscalzo J, Schafer AI (eds.): Thrombosis and Hemorrhage, 2d ed. Baltimore, MD: Williams and Wilkins, 1998, 3-27.
    • (1998) Thrombosis and Hemorrhage , pp. 3-27
    • Jenny, N.S.1    Mann, K.G.2
  • 3
    • 0036271051 scopus 로고    scopus 로고
    • Orchestration of coagulation protease signaling by tissue factor
    • Riewald M, Ruf W. Orchestration of coagulation protease signaling by tissue factor. Trends Cardiovasc Med 2002; 12: 149-54.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 149-154
    • Riewald, M.1    Ruf, W.2
  • 4
    • 0006088037 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor
    • Loscalzo J, Schafer AI (eds.): 2d ed. Baltimore, MD: Williams and Wilkins
    • Broze GJ Jr. Tissue factor pathway inhibitor, in Loscalzo J, Schafer AI (eds.): Thrombosis and Hemorrhage, 2d ed. Baltimore, MD: Williams and Wilkins, 1998, 77-104.
    • (1998) Thrombosis and Hemorrhage , pp. 77-104
    • Broze Jr., G.J.1
  • 5
    • 0032697618 scopus 로고    scopus 로고
    • Biochemistry and physiology of blood coagulation
    • Mann KG. Biochemistry and physiology of blood coagulation. Thromb Haemost 1999; 82: 165-74.
    • (1999) Thromb. Haemost. , vol.82 , pp. 165-174
    • Mann, K.G.1
  • 6
    • 0034615559 scopus 로고    scopus 로고
    • Regulation of Blood coagulation
    • Esmon CT. Regulation of Blood coagulation. Biochim Biophys Acta 2000; 1477: 349-60.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 349-360
    • Esmon, C.T.1
  • 7
    • 0036021104 scopus 로고    scopus 로고
    • Identification of critical molecular interactions mediating heparin activation of antithrombin: Implications for the design of improved heparin anticoagulants
    • Olson ST, Bjork I, Bock SC. Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants. Trends Cardiovasc Med 2002; 12: 198-205.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 198-205
    • Olson, S.T.1    Bjork, I.2    Bock, S.C.3
  • 8
    • 0028784386 scopus 로고
    • Insight into the mechanism of action of heparin cofactor II
    • Tollefsen DM. Insight into the mechanism of action of heparin cofactor II. Thromb Haemost 1995; 74: 1209-14.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1209-1214
    • Tollefsen, D.M.1
  • 9
    • 1842521997 scopus 로고    scopus 로고
    • Control of coagulation reactions
    • Beutler E, Lichtman MA, Coller BS, Kipps TJ, Seligsohn U (eds): 6th ed. New York, NY. McGraw-Hill Companies, Inc
    • Griffin JH. Control of coagulation reactions. In: Beutler E, Lichtman MA, Coller BS, Kipps TJ, Seligsohn U (eds): Williams Hematology, 6th ed. New York, NY. McGraw-Hill Companies, Inc., 2001, 1435-49.
    • (2001) Williams Hematology , pp. 1435-1449
    • Griffin, J.H.1
  • 10
    • 0023851665 scopus 로고
    • The lipoprotein-associated coagulation inhibitor that inhibits the FVII-tissue factor complex also inhibits FXa: Insight into its possible mechanism of action
    • Broze GJ Jr, Warren LA, Novotny WF, et al. The lipoprotein-associated coagulation inhibitor that inhibits the FVII-tissue factor complex also inhibits FXa: insight into its possible mechanism of action. Blood 1988; 71: 335-43.
    • (1988) Blood , vol.71 , pp. 335-343
    • Broze Jr., G.J.1    Warren, L.A.2    Novotny, W.F.3
  • 11
    • 0023924263 scopus 로고
    • Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains
    • Wun T-C, Kretzmer KK, Girard TJ, et al. Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains. J Biol Chem 1988; 263: 6001-4.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6001-6004
    • Wun, T.-C.1    Kretzmer, K.K.2    Girard, T.J.3
  • 12
    • 0025149085 scopus 로고
    • Recombinant human extrinsic pathway inhibitor. Production, isolation, and characterization of its inhibitory activity on tissue factor-initiated coagulation reactions
    • Pedersen AH, Nordfang O, Norris F, et al. Recombinant human extrinsic pathway inhibitor. Production, isolation, and characterization of its inhibitory activity on tissue factor-initiated coagulation reactions. J Biol Chem 1990; 254: 16786-93.
    • (1990) J. Biol. Chem. , vol.254 , pp. 16786-16793
    • Pedersen, A.H.1    Nordfang, O.2    Norris, F.3
  • 13
    • 0027456278 scopus 로고
    • Inhibitory properties of full-length and truncated recombinant tisuue factor pathway inhibitor (TFPI)
    • Hamamoto T, Yamamoto M, Nordfang O, et al. Inhibitory properties of full-length and truncated recombinant tisuue factor pathway inhibitor (TFPI). J Biol Chem 1993; 268: 8704-10.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8704-8710
    • Hamamoto, T.1    Yamamoto, M.2    Nordfang, O.3
  • 14
    • 0024535793 scopus 로고
    • Inhibition of FVIIa/tissue factor-induced blood coagulation: With particular emphasis upon a FXa-dependent inhibitory mechanism
    • Rapaport SI. Inhibition of FVIIa/tissue factor-induced blood coagulation: with particular emphasis upon a FXa-dependent inhibitory mechanism. Blood 1989; 73: 359-65.
    • (1989) Blood , vol.73 , pp. 359-365
    • Rapaport, S.I.1
  • 15
    • 0027724106 scopus 로고
    • Kinetics of FXa inhibition by tissue factor pathway inhibitor
    • Huang Z-F, Wun T-C, Broze GJ Jr. Kinetics of FXa inhibition by tissue factor pathway inhibitor. J Biol Chem 1993; 268: 26950-5.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26950-26955
    • Huang, Z.-F.1    Wun, T.-C.2    Broze Jr., G.J.3
  • 16
    • 0029143909 scopus 로고
    • Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor-VIIa with Xa-tissue factor pathway inhibitor
    • Rao LVM, Ruf W. Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor-VIIa with Xa-tissue factor pathway inhibitor. Biochemistry 1995; 34: 10867-71.
    • (1995) Biochemistry , vol.34 , pp. 10867-10871
    • Rao, L.V.M.1    Ruf, W.2
  • 17
    • 0024543984 scopus 로고
    • Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor
    • Girard TJ, Warren LA, Novotny WF, et al. Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature 1989; 338: 518-20.
    • (1989) Nature , vol.338 , pp. 518-520
    • Girard, T.J.1    Warren, L.A.2    Novotny, W.F.3
  • 18
    • 0024991650 scopus 로고
    • Regulation of coagulation by multivalent Kunitz-type inhibitor
    • Broze GJ Jr, Girard, TH, Novotony, WF. Regulation of coagulation by multivalent Kunitz-type inhibitor. Biochemistry 1995; 29: 7539-46.
    • (1995) Biochemistry , vol.29 , pp. 7539-7546
    • Broze Jr., G.J.1    Girard, T.H.2    Novotony, W.F.3
  • 19
    • 0031649079 scopus 로고
    • Allosteric regulation of the cofactor dependent serine protease coagulation factor VIIa
    • Ruf W, Dickinson CD. Allosteric regulation of the cofactor dependent serine protease coagulation factor VIIa. Trends Cardiovasc Med 1988; 8: 350-6.
    • (1988) Trends Cardiovasc. Med. , vol.8 , pp. 350-356
    • Ruf, W.1    Dickinson, C.D.2
  • 20
    • 0037391809 scopus 로고    scopus 로고
    • Alternatively spliced human tissue factor: A circulating soluble, thrombogenic protein
    • Bogdanov VY, Balasubramanian V, Hathcock J, et al. Alternatively spliced human tissue factor: a circulating soluble, thrombogenic protein. Nat Med 2003; 9: 458-62.
    • (2003) Nat. Med. , vol.9 , pp. 458-462
    • Bogdanov, V.Y.1    Balasubramanian, V.2    Hathcock, J.3
  • 21
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues
    • Drake TA, Morrisey JH, Edgington TS. Selective cellular expression of tissue factor in human tissues. Am J Pathol 1989; 134: 1087-97.
    • (1989) Am. J. Pathol. , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrisey, J.H.2    Edgington, T.S.3
  • 22
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium
    • Bach R, Rifkin DB. Expression of tissue factor procoagulant activity: regulation by cytosolic calcium. Proc Natl Acad Sci USA 1990; 87: 6995-9.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6995-6999
    • Bach, R.1    Rifkin, D.B.2
  • 23
    • 0031005422 scopus 로고    scopus 로고
    • Mechanism of tissue factor activation on HL-60 cells
    • Bach RR, Moldow CF. Mechanism of tissue factor activation on HL-60 cells. Blood 1997; 89: 3270-6.
    • (1997) Blood , vol.89 , pp. 3270-3276
    • Bach, R.R.1    Moldow, C.F.2
  • 24
    • 0028235662 scopus 로고
    • Structural biology of tissue factor, the initiator of thrombogenesis in vivo
    • Ruf W, Edgington TS. Structural biology of tissue factor, the initiator of thrombogenesis in vivo. FASEB J 1994; 8: 385-90.
    • (1994) FASEB J. , vol.8 , pp. 385-390
    • Ruf, W.1    Edgington, T.S.2
  • 25
    • 0032975660 scopus 로고    scopus 로고
    • Cooperation between VEGF and TNF-α is necessary for exposure of active tissue factor on the surface of human endothelial cells
    • Camera M, Giesen PL, Fallon J. Cooperation between VEGF and TNF-α is necessary for exposure of active tissue factor on the surface of human endothelial cells. Arterioscler Thromb Vasc Biol 1999; 19: 531-7.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 531-537
    • Camera, M.1    Giesen, P.L.2    Fallon, J.3
  • 27
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro JM, Francischetti IM. Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives. Ann Rev Entomol 2003; 48: 73-88.
    • (2003) Ann. Rev. Entomol. , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 28
    • 0021984773 scopus 로고
    • Pheromones and other semiochemicals of the acari
    • Sonenshine DE. Pheromones and other semiochemicals of the acari. Annu Rev Entomol 1985; 30: 1-28.
    • (1985) Annu. Rev. Entomol. , vol.30 , pp. 1-28
    • Sonenshine, D.E.1
  • 29
    • 0037093065 scopus 로고    scopus 로고
    • Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: Identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex
    • Francischetti IMB, Valenzuela JG, Andersen JF, et al. Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex. Blood 2002; 99: 3602-12.
    • (2002) Blood , vol.99 , pp. 3602-3612
    • Francischetti, I.M.B.1    Valenzuela, J.G.2    Andersen, J.F.3
  • 30
    • 18744386088 scopus 로고    scopus 로고
    • A novel family of anticoagulants from the saliva of Ixodes scapularis
    • Narasimhan S, Koski RA, Beaulieu B, et al. A novel family of anticoagulants from the saliva of Ixodes scapularis. Insect Mol Biol 2002; 11: 641-50.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 641-650
    • Narasimhan, S.1    Koski, R.A.2    Beaulieu, B.3
  • 31
    • 0034705418 scopus 로고    scopus 로고
    • Purification, cloning, and expression of a novel salivary anticomplement protein from the tick, Ixodes scapularis
    • Valenzuela JG, Charlab R, Mather TN, et al. Purification, cloning, and expression of a novel salivary anticomplement protein from the tick, Ixodes scapularis. J Biol Chem 2000; 275: 8717-23.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8717-8723
    • Valenzuela, J.G.1    Charlab, R.2    Mather, T.N.3
  • 32
    • 0024214890 scopus 로고
    • Ixodes dammini: Evidence for salivary prostacyclin secretion
    • Ribeiro JMC, Makoul GT, Robinson DR. Ixodes dammini: evidence for salivary prostacyclin secretion. J Parasitol 1988; 74: 1068-9.
    • (1988) J. Parasitol. , vol.74 , pp. 1068-1069
    • Ribeiro, J.M.C.1    Makoul, G.T.2    Robinson, D.R.3
  • 33
    • 0037077268 scopus 로고    scopus 로고
    • Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold
    • Mans BJ, Louw AI, Neitz AW. Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold. J Biol Chem 2002; 277: 21371-8.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21371-21378
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 34
    • 0025329136 scopus 로고
    • Saliva of the tick Ixodes dammini inhibits neutrophil function
    • Ribeiro JMC, Weis JJ, Telford SR III. Saliva of the tick Ixodes dammini inhibits neutrophil function. Exp Parasitol 1990; 70: 382-8.
    • (1990) Exp. Parasitol. , vol.70 , pp. 382-388
    • Ribeiro, J.M.C.1    Weis, J.J.2    Telford III, S.R.3
  • 35
    • 0037904919 scopus 로고    scopus 로고
    • Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin-(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis
    • Francischetti IMB, Mather TN, Ribeiro JMC. Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin-(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem Biophys Res Commun 2003; 305: 869-75.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 869-875
    • Francischetti, I.M.B.1    Mather, T.N.2    Ribeiro, J.M.C.3
  • 36
    • 0014140723 scopus 로고
    • A modified method for obtaining tick oral secretion
    • Tatchell RJ. A modified method for obtaining tick oral secretion. J Parasitol 1967; 53: 1106-7.
    • (1967) J. Parasitol. , vol.53 , pp. 1106-1107
    • Tatchell, R.J.1
  • 37
    • 0036671719 scopus 로고    scopus 로고
    • Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae
    • Francischetti IMB, Valenzuela JG, Pham VM, et al. Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae. J Exp Biol 2002; 205: 2429-51.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2429-2451
    • Francischetti, I.M.B.1    Valenzuela, J.G.2    Pham, V.M.3
  • 39
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl Acids Res 1997; 25: 3389-402.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 40
    • 0030614959 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, et al. A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997; 10: 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 1994; 22: 4673-80.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • Page RDM. TREEVIEW: An application to display phylogenetic trees on personal computers. Computer Appl Biosci 1996; 12: 357-8.
    • (1996) Computer Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 43
    • 0032879138 scopus 로고    scopus 로고
    • Structural requirements for TFPI-mediated inhibition of neointimal thickening after balloon injury in the rat
    • Han X, Girard TJ, Baum P, et al. Structural requirements for TFPI-mediated inhibition of neointimal thickening after balloon injury in the rat. Arterioscler Thromb Vasc Biol 1999; 19: 2563-7.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2563-2567
    • Han, X.1    Girard, T.J.2    Baum, P.3
  • 45
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams JW, Morrison JF. The kinetics of reversible tight-binding inhibition. Methods Enzymol 1979; 63: 437-67.
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 46
    • 0025010978 scopus 로고
    • Proteolytic activation of human factors IX and X by recombinant human FVIIa: Effects of calcium, phospholipids, and tissue factor
    • Komiyama Y, Pedersen AH, Kisiel W. Proteolytic activation of human factors IX and X by recombinant human FVIIa: effects of calcium, phospholipids, and tissue factor. Biochemistry 1991; 29: 9418-25.
    • (1991) Biochemistry , vol.29 , pp. 9418-9425
    • Komiyama, Y.1    Pedersen, A.H.2    Kisiel, W.3
  • 47
    • 0035971227 scopus 로고    scopus 로고
    • Role of zymogen and activated FX as scaffolds for the inhibition of the blood coagulation FVIIa-tissue factor complex by recombinant nematode anticoagulant protein c2
    • Bergun PW, Cruikshank A, Maki SL, et al. Role of zymogen and activated FX as scaffolds for the inhibition of the blood coagulation FVIIa-tissue factor complex by recombinant nematode anticoagulant protein c2. J Biol Chem 2001; 276: 10063-71.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10063-10071
    • Bergun, P.W.1    Cruikshank, A.2    Maki, S.L.3
  • 48
    • 0034665994 scopus 로고    scopus 로고
    • Exosite interactions determine the affinity of FX for the extrinsic Xase complex
    • Baugh RJ, Dickinson CD, Ruf W, et al. Exosite interactions determine the affinity of FX for the extrinsic Xase complex. J Biol Chem 2000; 275: 28826-33.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28826-28833
    • Baugh, R.J.1    Dickinson, C.D.2    Ruf, W.3
  • 49
    • 0025998507 scopus 로고
    • Proteinase-protein inhibitor interaction
    • Bode W, Huber R. Proteinase-protein inhibitor interaction. Biomed Biochim Acta 1991; 50: 437-46.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 437-446
    • Bode, W.1    Huber, R.2
  • 50
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution
    • Huber R, Kukla D, Bode W, et al. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution. J Mol Biol 1974; 89: 73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3
  • 52
    • 0027363207 scopus 로고
    • Structural requirements for tissue factor pathway inhibitor interactions with factor Xa and heparin
    • Wesselschmidt R, Likert K, Huang Z, et al. Structural requirements for tissue factor pathway inhibitor interactions with factor Xa and heparin. Blood Coagul Fibrinolysis 1993; 4: 661-9.
    • (1993) Blood Coagul. Fibrinolysis , vol.4 , pp. 661-669
    • Wesselschmidt, R.1    Likert, K.2    Huang, Z.3
  • 53
    • 0026668480 scopus 로고
    • Tissue factor pathway inhibitor: The carboxy-terminus is required for optimal inhibition of FXa
    • Wesselschmidt R, Likert K, Girard T, et al. Tissue factor pathway inhibitor: the carboxy-terminus is required for optimal inhibition of FXa. Blood 1992; 79: 2004-10.
    • (1992) Blood , vol.79 , pp. 2004-2010
    • Wesselschmidt, R.1    Likert, K.2    Girard, T.3
  • 54
    • 0028969172 scopus 로고
    • The carboxy terminus of tissue factor pathway inhibitor is required for interacting with hepatoma cells in vitro and in vivo
    • Warshawasky I, Bu G, Mast A, et al. The carboxy terminus of tissue factor pathway inhibitor is required for interacting with hepatoma cells in vitro and in vivo. J Clin Invest 1995; 95: 1173-81.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1173-1181
    • Warshawasky, I.1    Bu, G.2    Mast, A.3
  • 55
    • 0035853735 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor inhibits endothelial cell proliferation via association with the very low density lipoprotein receptor
    • Hembrough TA, Ruiz JF, Papathanassiu AE, et al. Tissue factor pathway inhibitor inhibits endothelial cell proliferation via association with the very low density lipoprotein receptor. J Biol Chem 2001; 276: 12241-8.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12241-12248
    • Hembrough, T.A.1    Ruiz, J.F.2    Papathanassiu, A.E.3
  • 56
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko AP. Recognition between flexible protein molecules: induced and assisted folding. J Mol Recognit 2001; 14: 42-61.
    • (2001) J. Mol. Recognit. , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 58
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of FXa critical for heparin and factor Va binding
    • Rezaie AR. Identification of basic residues in the heparin-binding exosite of FXa critical for heparin and factor Va binding. J Biol Chem 2000; 275: 3320-7.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3320-3327
    • Rezaie, A.R.1
  • 59
    • 0030767267 scopus 로고    scopus 로고
    • Exosites determine macromolecular substrate recognition by prothrombinase
    • Krishnaswamy S, Betz A. Exosites determine macromolecular substrate recognition by prothrombinase. Biochemistry 1997; 36: 12080-6.
    • (1997) Biochemistry , vol.36 , pp. 12080-12086
    • Krishnaswamy, S.1    Betz, A.2
  • 60
    • 0027218342 scopus 로고
    • Molecular recognition in biological systems: From activation to inhibition
    • Kossiakoff AA, Hynes T, de Vos A. Molecular recognition in biological systems: from activation to inhibition. Biochem Soc Trans 1993; 21: 614-8.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 614-618
    • Kossiakoff, A.A.1    Hynes, T.2    de Vos, A.3
  • 61
    • 0026568164 scopus 로고
    • Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage
    • Roberts BL, Markland W, Ley AC, et al. Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage. Proc Natl Acad Sci USA 1992; 89: 2429-33.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2429-2433
    • Roberts, B.L.1    Markland, W.2    Ley, A.C.3
  • 62
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L, Smith DE, Arcuri KE, et al. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 1990; 248: 593-6.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3
  • 63
    • 0027216868 scopus 로고
    • Structural and functional characterization of tick anticoagulant peptide (TAP): A potent and selective inhibitor of blood coagulation factor Xa
    • Vlasuk GP. Structural and functional characterization of tick anticoagulant peptide (TAP): a potent and selective inhibitor of blood coagulation factor Xa. Thromb Haemost 1993; 70: 212-6.
    • (1993) Thromb. Haemost. , vol.70 , pp. 212-216
    • Vlasuk, G.P.1
  • 64
    • 0029957955 scopus 로고    scopus 로고
    • The ornithodorin-thrombin crystal structure, a key to the TAP enigma?
    • van de Locht A, Stubbs MT, Bode W, et al. The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J 1996; 15:6011-7.
    • (1996) EMBO J. , vol.15 , pp. 6011-6017
    • van de Locht, A.1    Stubbs, M.T.2    Bode, W.3
  • 65
    • 0032538320 scopus 로고    scopus 로고
    • Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa
    • Wei A, Alexander RS, Duke J, et al. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J Mol Biol 1998; 283: 147-54.
    • (1998) J. Mol. Biol. , vol.283 , pp. 147-154
    • Wei, A.1    Alexander, R.S.2    Duke, J.3
  • 66
    • 0027432559 scopus 로고
    • Purification and characterization of inhibitors of blood coagulation factor Xa from hematophagous organisms
    • Dunwiddie CT, Waxman L, Vlasuk GP, et al. Purification and characterization of inhibitors of blood coagulation factor Xa from hematophagous organisms. Methods Enzymol 1993; 223: 291-312.
    • (1993) Methods Enzymol. , vol.223 , pp. 291-312
    • Dunwiddie, C.T.1    Waxman, L.2    Vlasuk, G.P.3
  • 67
    • 0028930192 scopus 로고
    • Identification and characterization of variants of tick anticoagulant peptide with increased inhibitory potency toward human factor Xa
    • Mao SS, Huang J, Welebob C, et al. Identification and characterization of variants of tick anticoagulant peptide with increased inhibitory potency toward human factor Xa. Biochemistry 1995; 34: 5098-103.
    • (1995) Biochemistry , vol.34 , pp. 5098-5103
    • Mao, S.S.1    Huang, J.2    Welebob, C.3
  • 68
    • 0028319879 scopus 로고
    • Analysis of cysteine residues and disulfide bonds
    • Aitken A. Analysis of cysteine residues and disulfide bonds. Methods Mol Biol 1994; 32: 351-430.
    • (1994) Methods Mol. Biol. , vol.32 , pp. 351-430
    • Aitken, A.1
  • 69
    • 0029148567 scopus 로고
    • Kinetics of the inhibition of tissue factor-FVIIa by tissue factor pathway inhibitor
    • Lindhout T, Fransen J, Willems G. Kinetics of the inhibition of tissue factor-FVIIa by tissue factor pathway inhibitor. Thromb Haemost 1995; 74: 910-5.
    • (1995) Thromb. Haemost. , vol.74 , pp. 910-915
    • Lindhout, T.1    Fransen, J.2    Willems, G.3
  • 70
    • 0005232458 scopus 로고
    • The isolation and purification of a bovine-plasma protein which is substrate for the coagulation fraction of Russell's viper venom
    • Esnouf MP, Williams WJ. The isolation and purification of a bovine-plasma protein which is substrate for the coagulation fraction of Russell's viper venom. Biochem J 1962; 84: 62-71.
    • (1962) Biochem. J. , vol.84 , pp. 62-71
    • Esnouf, M.P.1    Williams, W.J.2
  • 71
    • 0014386609 scopus 로고
    • Studies on bovine factor X. II. Observations on some alterations in zone electrophoresis and chromatographic behavior occurring during purification
    • Jackson CM, Hanahan DJ. Studies on bovine factor X. II. Observations on some alterations in zone electrophoresis and chromatographic behavior occurring during purification. Biochemistry 1968; 7: 4506-17.
    • (1968) Biochemistry , vol.7 , pp. 4506-4517
    • Jackson, C.M.1    Hanahan, D.J.2
  • 72
    • 0034720739 scopus 로고    scopus 로고
    • The tissue factor region that interacts with substrates FIX and FX
    • Kirchhofer D, Lipari MT, Moran P, et al. The tissue factor region that interacts with substrates FIX and FX. Biochemistry 2000; 3: 7380-7.
    • (2000) Biochemistry , vol.3 , pp. 7380-7387
    • Kirchhofer, D.1    Lipari, M.T.2    Moran, P.3
  • 73
    • 0029992658 scopus 로고    scopus 로고
    • Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease FVIIa
    • Dickinson CD, Kelly CR, Ruf W. Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease FVIIa. Proc Natl Acad Sci USA 1996; 93: 14379-84.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14379-14384
    • Dickinson, C.D.1    Kelly, C.R.2    Ruf, W.3
  • 74
    • 0025756188 scopus 로고
    • Self-association of tissue factor as revealed by chemical crosslinking
    • Roy S, Paborsky LR, Vehar GA. Self-association of tissue factor as revealed by chemical crosslinking. J Biol Chem 1991; 266: 4665-8.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4665-4668
    • Roy, S.1    Paborsky, L.R.2    Vehar, G.A.3
  • 75
    • 0019957155 scopus 로고
    • Binding of human factor VII and VIIa to monocytes
    • Broze GJ Jr. Binding of human factor VII and VIIa to monocytes. J Clin Invest 1982; 70: 526-35.
    • (1982) J. Clin. Invest. , vol.70 , pp. 526-535
    • Broze Jr., G.J.1
  • 76
    • 0026650453 scopus 로고
    • Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces
    • Le DT, Rapaport SI, Rao LVM. Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces. J Biol Chem 1992; 267: 15447-54.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15447-15454
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.M.3
  • 77
    • 0034933683 scopus 로고    scopus 로고
    • Mechanism coupling of protease signaling and initiation of coagulation by tissue factor
    • Riewald M, Ruf W. Mechanism coupling of protease signaling and initiation of coagulation by tissue factor. Proc Natl Acad Sci USA 2003; 98: 7742-7.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7742-7747
    • Riewald, M.1    Ruf, W.2
  • 78
    • 0034624973 scopus 로고    scopus 로고
    • Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa
    • Camerer E, Huang W, Coughlin SR. Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa. Proc Natl Acad Sci USA 2000; 97: 5255-60.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5255-5260
    • Camerer, E.1    Huang, W.2    Coughlin, S.R.3
  • 79
    • 0035128439 scopus 로고    scopus 로고
    • New anticoagulant drugs
    • Weitz JI, Hirsh J. New anticoagulant drugs. Chest 2001; 119: 95S-107S.
    • (2001) Chest , vol.119
    • Weitz, J.I.1    Hirsh, J.2


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