메뉴 건너뛰기




Volumn 125, Issue 3, 2010, Pages 210-215

Factor XII: What does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 12; EPIDERMAL GROWTH FACTOR; FIBRONECTIN; PROTEINASE;

EID: 76949094364     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.thromres.2009.11.028     Document Type: Review
Times cited : (137)

References (66)
  • 1
    • 77049208954 scopus 로고
    • A familial hemorrhagic trait associated with a deficiency of a clot-promoting fraction of plasma
    • Ratnoff O.D., and Colopy J.E. A familial hemorrhagic trait associated with a deficiency of a clot-promoting fraction of plasma. J Clin Invest 34 4 (Apr 1955) 602-613
    • (1955) J Clin Invest , vol.34 , Issue.4 , pp. 602-613
    • Ratnoff, O.D.1    Colopy, J.E.2
  • 2
    • 37049242417 scopus 로고
    • Waterfall Sequence for Intrinsic Blood Clotting
    • Davie E.W., and Ratnoff O.D. Waterfall Sequence for Intrinsic Blood Clotting. Science 145 (Sep 18 1964) 1310-1312
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 3
    • 0019471542 scopus 로고
    • Activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B., Silverberg M., and Kaplan A.P. Activation of the classical pathway of complement by Hageman factor fragment. J Exp Med 153 3 (Mar 1 1981) 665-676
    • (1981) J Exp Med , vol.153 , Issue.3 , pp. 665-676
    • Ghebrehiwet, B.1    Silverberg, M.2    Kaplan, A.P.3
  • 4
    • 0024215593 scopus 로고
    • Assignment of human coagulation factor XII (fXII) to chromosome 5 by cDNA hybridization to DNA from somatic cell hybrids
    • Citarella F., Tripodi M., Fantoni A., Bernardi F., Romeo G., and Rocchi M. Assignment of human coagulation factor XII (fXII) to chromosome 5 by cDNA hybridization to DNA from somatic cell hybrids. Hum Genet 80 4 (Dec 1988) 397-398
    • (1988) Hum Genet , vol.80 , Issue.4 , pp. 397-398
    • Citarella, F.1    Tripodi, M.2    Fantoni, A.3    Bernardi, F.4    Romeo, G.5    Rocchi, M.6
  • 5
    • 0023265140 scopus 로고
    • Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region
    • Cool D.E., and MacGillivray R.T. Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region. J Biol Chem 262 28 (Oct 5 1987) 13662-13673
    • (1987) J Biol Chem , vol.262 , Issue.28 , pp. 13662-13673
    • Cool, D.E.1    MacGillivray, R.T.2
  • 7
    • 0020643475 scopus 로고
    • Cell surface interactions with extracellular materials
    • Yamada K.M. Cell surface interactions with extracellular materials. Annu Rev Biochem 52 (1983) 761-799
    • (1983) Annu Rev Biochem , vol.52 , pp. 761-799
    • Yamada, K.M.1
  • 8
    • 0024319165 scopus 로고
    • Mapping of a putative surface-binding site of human coagulation factor XII
    • Clarke B.J., Cote H.C., Cool D.E., Clark-Lewis I., Saito H., Pixley R.A., et al. Mapping of a putative surface-binding site of human coagulation factor XII. J Biol Chem 264 19 (Jul 5 1989) 11497-11502
    • (1989) J Biol Chem , vol.264 , Issue.19 , pp. 11497-11502
    • Clarke, B.J.1    Cote, H.C.2    Cool, D.E.3    Clark-Lewis, I.4    Saito, H.5    Pixley, R.A.6
  • 9
    • 0027208635 scopus 로고
    • Histidine residues are essential for the surface binding and autoactivation of human coagulation factor XII
    • Samuel M., Samuel E., and Villanueva G.B. Histidine residues are essential for the surface binding and autoactivation of human coagulation factor XII. Biochem Biophys Res Commun 191 1 (Feb 26 1993) 110-117
    • (1993) Biochem Biophys Res Commun , vol.191 , Issue.1 , pp. 110-117
    • Samuel, M.1    Samuel, E.2    Villanueva, G.B.3
  • 10
    • 0023258668 scopus 로고
    • A monoclonal antibody recognizing an icosapeptide sequence in the heavy chain of human factor XII inhibits surface-catalyzed activation
    • Pixley R.A., Stumpo L.G., Birkmeyer K., Silver L., and Colman R.W. A monoclonal antibody recognizing an icosapeptide sequence in the heavy chain of human factor XII inhibits surface-catalyzed activation. J Biol Chem 262 21 (Jul 25 1987) 10140-10145
    • (1987) J Biol Chem , vol.262 , Issue.21 , pp. 10140-10145
    • Pixley, R.A.1    Stumpo, L.G.2    Birkmeyer, K.3    Silver, L.4    Colman, R.W.5
  • 11
    • 0029967088 scopus 로고    scopus 로고
    • Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces
    • Citarella F., Ravon D.M., Pascucci B., Felici A., Fantoni A., and Hack C.E. Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces. Eur J Biochem 238 1 (May 15 1996) 240-249
    • (1996) Eur J Biochem , vol.238 , Issue.1 , pp. 240-249
    • Citarella, F.1    Ravon, D.M.2    Pascucci, B.3    Felici, A.4    Fantoni, A.5    Hack, C.E.6
  • 12
    • 0032402133 scopus 로고    scopus 로고
    • The second exon-encoded factor XII region is involved in the interaction of factor XII with factor XI and does not contribute to the binding site for negatively charged surfaces
    • Citarella F., Fedele G., Roem D., Fantoni A., and Hack C.E. The second exon-encoded factor XII region is involved in the interaction of factor XII with factor XI and does not contribute to the binding site for negatively charged surfaces. Blood 92 11 (Dec 1 1998) 4198-4206
    • (1998) Blood , vol.92 , Issue.11 , pp. 4198-4206
    • Citarella, F.1    Fedele, G.2    Roem, D.3    Fantoni, A.4    Hack, C.E.5
  • 13
    • 0027418234 scopus 로고
    • Identification and characterization of a binding site for factor XIIa in the Apple 4 domain of coagulation factor XI
    • Baglia F.A., Jameson B.A., and Walsh P.N. Identification and characterization of a binding site for factor XIIa in the Apple 4 domain of coagulation factor XI. J Biol Chem 268 6 (Feb 25 1993) 3838-3844
    • (1993) J Biol Chem , vol.268 , Issue.6 , pp. 3838-3844
    • Baglia, F.A.1    Jameson, B.A.2    Walsh, P.N.3
  • 14
    • 0037093204 scopus 로고    scopus 로고
    • Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes
    • Mahdi F., Madar Z.S., Figueroa C.D., and Schmaier A.H. Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes. Blood 99 10 (May 15 2002) 3585-3596
    • (2002) Blood , vol.99 , Issue.10 , pp. 3585-3596
    • Mahdi, F.1    Madar, Z.S.2    Figueroa, C.D.3    Schmaier, A.H.4
  • 15
    • 0028236815 scopus 로고
    • Assembly of contact-phase factors on the surface of the human neutrophil membrane
    • Henderson L.M., Figueroa C.D., Muller-Esterl W., and Bhoola K.D. Assembly of contact-phase factors on the surface of the human neutrophil membrane. Blood 84 2 (Jul 15 1994) 474-482
    • (1994) Blood , vol.84 , Issue.2 , pp. 474-482
    • Henderson, L.M.1    Figueroa, C.D.2    Muller-Esterl, W.3    Bhoola, K.D.4
  • 16
    • 0034725612 scopus 로고    scopus 로고
    • Human factor XII binding to the glycoprotein Ib-IX-V complex inhibits thrombin-induced platelet aggregation
    • Bradford H.N., Pixley R.A., and Colman R.W. Human factor XII binding to the glycoprotein Ib-IX-V complex inhibits thrombin-induced platelet aggregation. J Biol Chem 275 30 (Jul 28 2000) 22756-22763
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 22756-22763
    • Bradford, H.N.1    Pixley, R.A.2    Colman, R.W.3
  • 17
    • 0032584066 scopus 로고    scopus 로고
    • Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cells
    • Hasan A.A., Zisman T., and Schmaier A.H. Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cells. Proc Natl Acad Sci U S A 95 7 (Mar 31 1998) 3615-3620
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.7 , pp. 3615-3620
    • Hasan, A.A.1    Zisman, T.2    Schmaier, A.H.3
  • 18
    • 0035871850 scopus 로고    scopus 로고
    • Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells
    • Mahdi F., Shariat-Madar Z., Todd III R.F., Figueroa C.D., and Schmaier A.H. Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells. Blood 97 8 (Apr 15 2001) 2342-2350
    • (2001) Blood , vol.97 , Issue.8 , pp. 2342-2350
    • Mahdi, F.1    Shariat-Madar, Z.2    Todd III, R.F.3    Figueroa, C.D.4    Schmaier, A.H.5
  • 19
    • 0030788208 scopus 로고    scopus 로고
    • Partial identification of the Zn2+-binding sites in factor XII and its activation derivatives
    • Rojkaer R., and Schousboe I. Partial identification of the Zn2+-binding sites in factor XII and its activation derivatives. Eur J Biochem 247 2 (Jul 15 1997) 491-496
    • (1997) Eur J Biochem , vol.247 , Issue.2 , pp. 491-496
    • Rojkaer, R.1    Schousboe, I.2
  • 20
    • 0022407061 scopus 로고
    • Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa
    • Cool D.E., Edgell C.J., Louie G.V., Zoller M.J., Brayer G.D., and MacGillivray R.T. Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. J Biol Chem 260 25 (Nov 5 1985) 13666-13676
    • (1985) J Biol Chem , vol.260 , Issue.25 , pp. 13666-13676
    • Cool, D.E.1    Edgell, C.J.2    Louie, G.V.3    Zoller, M.J.4    Brayer, G.D.5    MacGillivray, R.T.6
  • 21
    • 0023319784 scopus 로고
    • Epidermal growth factor
    • Cohen S. Epidermal growth factor. In Vitro Cell Dev Biol 23 4 (Apr 1987) 239-246
    • (1987) In Vitro Cell Dev Biol , vol.23 , Issue.4 , pp. 239-246
    • Cohen, S.1
  • 22
    • 0024230452 scopus 로고
    • Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor
    • Chien P., Pixley R.A., Stumpo L.G., Colman R.W., and Schreiber A.D. Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor. J Clin Invest 82 5 (Nov 1988) 1554-1559
    • (1988) J Clin Invest , vol.82 , Issue.5 , pp. 1554-1559
    • Chien, P.1    Pixley, R.A.2    Stumpo, L.G.3    Colman, R.W.4    Schreiber, A.D.5
  • 23
    • 0029970618 scopus 로고    scopus 로고
    • Factor XII-induced mitogenesis is mediated via a distinct signal transduction pathway that activates a mitogen-activated protein kinase
    • Gordon E.M., Venkatesan N., Salazar R., Tang H., Schmeidler-Sapiro K., Buckley S., et al. Factor XII-induced mitogenesis is mediated via a distinct signal transduction pathway that activates a mitogen-activated protein kinase. Proc Natl Acad Sci U S A 93 5 (Mar 5 1996) 2174-2179
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.5 , pp. 2174-2179
    • Gordon, E.M.1    Venkatesan, N.2    Salazar, R.3    Tang, H.4    Schmeidler-Sapiro, K.5    Buckley, S.6
  • 24
    • 0025729812 scopus 로고
    • Mitogenic effects of coagulation factor XII and factor XIIa on HepG2 cells
    • Schmeidler-Sapiro K.T., Ratnoff O.D., and Gordon E.M. Mitogenic effects of coagulation factor XII and factor XIIa on HepG2 cells. Proc Natl Acad Sci U S A 88 10 (May 15 1991) 4382-4385
    • (1991) Proc Natl Acad Sci U S A , vol.88 , Issue.10 , pp. 4382-4385
    • Schmeidler-Sapiro, K.T.1    Ratnoff, O.D.2    Gordon, E.M.3
  • 25
    • 21644457354 scopus 로고    scopus 로고
    • Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells
    • Fernando A.N., Fernando L.P., Fukuda Y., and Kaplan A.P. Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 289 1 (Jul 2005) H251-H257
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , Issue.1
    • Fernando, A.N.1    Fernando, L.P.2    Fukuda, Y.3    Kaplan, A.P.4
  • 26
    • 0034533548 scopus 로고    scopus 로고
    • Identification of a putative binding site for negatively charged surfaces in the fibronectin type II domain of human factor XII-an immunochemical and homology modeling approach
    • Citarella F., te Velthuis H., Helmer-Citterich M., and Hack C.E. Identification of a putative binding site for negatively charged surfaces in the fibronectin type II domain of human factor XII-an immunochemical and homology modeling approach. Thromb Haemost 84 6 (Dec 2000) 1057-1065
    • (2000) Thromb Haemost , vol.84 , Issue.6 , pp. 1057-1065
    • Citarella, F.1    te Velthuis, H.2    Helmer-Citterich, M.3    Hack, C.E.4
  • 27
    • 0017690677 scopus 로고
    • The binding and cleavage characteristics of human Hageman factor during contact activation. A comparison of normal plasma with plasmas deficient in factor XI, prekallikrein, or high molecular weight kininogen
    • Revak S.D., Cochrane C.G., and Griffin J.H. The binding and cleavage characteristics of human Hageman factor during contact activation. A comparison of normal plasma with plasmas deficient in factor XI, prekallikrein, or high molecular weight kininogen. J Clin Invest 59 6 (Jun 1977) 1167-1175
    • (1977) J Clin Invest , vol.59 , Issue.6 , pp. 1167-1175
    • Revak, S.D.1    Cochrane, C.G.2    Griffin, J.H.3
  • 28
    • 0020516777 scopus 로고
    • Amino acid sequence of human beta-factor XIIa
    • Fujikawa K., and McMullen B.A. Amino acid sequence of human beta-factor XIIa. J Biol Chem 258 18 (Sep 25 1983) 10924-10933
    • (1983) J Biol Chem , vol.258 , Issue.18 , pp. 10924-10933
    • Fujikawa, K.1    McMullen, B.A.2
  • 29
    • 0020076571 scopus 로고
    • The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein
    • Dunn J.T., Silverberg M., and Kaplan A.P. The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein. J Biol Chem 257 4 (Feb 25 1982) 1779-1784
    • (1982) J Biol Chem , vol.257 , Issue.4 , pp. 1779-1784
    • Dunn, J.T.1    Silverberg, M.2    Kaplan, A.P.3
  • 30
    • 0031878996 scopus 로고    scopus 로고
    • Factor XII does not initiate prekallikrein activation on endothelial cells
    • Rojkjaer R., Hasan A.A., Motta G., Schousboe I., and Schmaier A.H. Factor XII does not initiate prekallikrein activation on endothelial cells. Thromb Haemost 80 1 (Jul 1998) 74-81
    • (1998) Thromb Haemost , vol.80 , Issue.1 , pp. 74-81
    • Rojkjaer, R.1    Hasan, A.A.2    Motta, G.3    Schousboe, I.4    Schmaier, A.H.5
  • 31
    • 0018632212 scopus 로고
    • The autoactivation of rabbit Hageman factor
    • Wiggins R.C., and Cochrane C.C. The autoactivation of rabbit Hageman factor. J Exp Med 150 5 (Nov 1 1979) 1122-1133
    • (1979) J Exp Med , vol.150 , Issue.5 , pp. 1122-1133
    • Wiggins, R.C.1    Cochrane, C.C.2
  • 32
    • 0026701990 scopus 로고
    • Human factor XII (Hageman factor) autoactivation by dextran sulfate. Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies
    • Samuel M., Pixley R.A., Villanueva M.A., Colman R.W., and Villanueva G.B. Human factor XII (Hageman factor) autoactivation by dextran sulfate. Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies. J Biol Chem 267 27 (Sep 25 1992) 19691-19697
    • (1992) J Biol Chem , vol.267 , Issue.27 , pp. 19691-19697
    • Samuel, M.1    Pixley, R.A.2    Villanueva, M.A.3    Colman, R.W.4    Villanueva, G.B.5
  • 33
    • 34248209006 scopus 로고    scopus 로고
    • Ordered adsorption of coagulation factor XII on negatively charged polymer surfaces probed by sum frequency generation vibrational spectroscopy
    • Chen X., Wang J., Paszti Z., Wang F., Schrauben J.N., Tarabara V.V., et al. Ordered adsorption of coagulation factor XII on negatively charged polymer surfaces probed by sum frequency generation vibrational spectroscopy. Anal Bioanal Chem 388 1 (May 2007) 65-72
    • (2007) Anal Bioanal Chem , vol.388 , Issue.1 , pp. 65-72
    • Chen, X.1    Wang, J.2    Paszti, Z.3    Wang, F.4    Schrauben, J.N.5    Tarabara, V.V.6
  • 34
    • 44849115945 scopus 로고    scopus 로고
    • Contaminated heparin associated with adverse clinical events and activation of the contact system
    • Kishimoto T.K., Viswanathan K., Ganguly T., Elankumaran S., Smith S., Pelzer K., et al. Contaminated heparin associated with adverse clinical events and activation of the contact system. N Engl J Med 358 23 (Jun 5 2008) 2457-2467
    • (2008) N Engl J Med , vol.358 , Issue.23 , pp. 2457-2467
    • Kishimoto, T.K.1    Viswanathan, K.2    Ganguly, T.3    Elankumaran, S.4    Smith, S.5    Pelzer, K.6
  • 37
    • 51349160073 scopus 로고    scopus 로고
    • Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation
    • Maas C., Govers-Riemslag J.W., Bouma B., Schiks B., Hazenberg B.P., Lokhorst H.M., et al. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. J Clin Invest 118 9 (Sep 2008) 3208-3218
    • (2008) J Clin Invest , vol.118 , Issue.9 , pp. 3208-3218
    • Maas, C.1    Govers-Riemslag, J.W.2    Bouma, B.3    Schiks, B.4    Hazenberg, B.P.5    Lokhorst, H.M.6
  • 39
    • 0021168136 scopus 로고
    • Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease
    • Matsumoto K., Yamamoto T., Kamata R., and Maeda H. Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease. J Biochem 96 3 (Sep 1984) 739-749
    • (1984) J Biochem , vol.96 , Issue.3 , pp. 739-749
    • Matsumoto, K.1    Yamamoto, T.2    Kamata, R.3    Maeda, H.4
  • 41
    • 0014883077 scopus 로고
    • Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified serum C1 inactivator
    • Forbes C.D., Pensky J., and Ratnoff O.D. Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified serum C1 inactivator. J Lab Clin Med 76 5 (Nov 1970) 809-815
    • (1970) J Lab Clin Med , vol.76 , Issue.5 , pp. 809-815
    • Forbes, C.D.1    Pensky, J.2    Ratnoff, O.D.3
  • 42
    • 0023212415 scopus 로고
    • Effect of negatively charged activating compounds on inactivation of factor XIIa by Cl inhibitor
    • Pixley R.A., Schmaier A., and Colman R.W. Effect of negatively charged activating compounds on inactivation of factor XIIa by Cl inhibitor. Arch Biochem Biophys 256 2 (Aug 1 1987) 490-498
    • (1987) Arch Biochem Biophys , vol.256 , Issue.2 , pp. 490-498
    • Pixley, R.A.1    Schmaier, A.2    Colman, R.W.3
  • 43
    • 0017167631 scopus 로고
    • Inhibition of activated factor XII by antithrombin-heparin cofactor
    • Stead N., Kaplan A.P., and Rosenberg R.D. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem 251 21 (1976 Nov 10) 6481-6488
    • (1976) J Biol Chem , vol.251 , Issue.21 , pp. 6481-6488
    • Stead, N.1    Kaplan, A.P.2    Rosenberg, R.D.3
  • 44
    • 0036122075 scopus 로고    scopus 로고
    • Increased vascular permeability in C1 inhibitor-deficient mice mediated by the bradykinin type 2 receptor
    • Han E.D., MacFarlane R.C., Mulligan A.N., Scafidi J., and Davis III A.E. Increased vascular permeability in C1 inhibitor-deficient mice mediated by the bradykinin type 2 receptor. J Clin Invest 109 8 (2002 Apr) 1057-1063
    • (2002) J Clin Invest , vol.109 , Issue.8 , pp. 1057-1063
    • Han, E.D.1    MacFarlane, R.C.2    Mulligan, A.N.3    Scafidi, J.4    Davis III, A.E.5
  • 45
    • 33845219794 scopus 로고    scopus 로고
    • Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III
    • Cichon S., Martin L., Hennies H.C., Muller F., Van Driessche K., Karpushova A., et al. Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet 79 6 (2006 Dec) 1098-1104
    • (2006) Am J Hum Genet , vol.79 , Issue.6 , pp. 1098-1104
    • Cichon, S.1    Martin, L.2    Hennies, H.C.3    Muller, F.4    Van Driessche, K.5    Karpushova, A.6
  • 46
    • 0028827650 scopus 로고
    • Molecular basis of estrogen regulation of Hageman factor XII gene expression
    • Farsetti A., Misiti S., Citarella F., Felici A., Andreoli M., Fantoni A., et al. Molecular basis of estrogen regulation of Hageman factor XII gene expression. Endocrinology 136 11 (1995 Nov) 5076-5083
    • (1995) Endocrinology , vol.136 , Issue.11 , pp. 5076-5083
    • Farsetti, A.1    Misiti, S.2    Citarella, F.3    Felici, A.4    Andreoli, M.5    Fantoni, A.6
  • 47
    • 0031765962 scopus 로고    scopus 로고
    • Orphan receptor hepatocyte nuclear factor-4 antagonizes estrogen receptor alpha-mediated induction of human coagulation factor XII gene
    • Farsetti A., Moretti F., Narducci M., Misiti S., Nanni S., Andreoli M., et al. Orphan receptor hepatocyte nuclear factor-4 antagonizes estrogen receptor alpha-mediated induction of human coagulation factor XII gene. Endocrinology 139 11 (1998 Nov) 4581-4589
    • (1998) Endocrinology , vol.139 , Issue.11 , pp. 4581-4589
    • Farsetti, A.1    Moretti, F.2    Narducci, M.3    Misiti, S.4    Nanni, S.5    Andreoli, M.6
  • 48
    • 33645416119 scopus 로고    scopus 로고
    • Role of hepatocyte nuclear factor 4alpha in control of blood coagulation factor gene expression
    • Inoue Y., Peters L.L., Yim S.H., Inoue J., and Gonzalez F.J. Role of hepatocyte nuclear factor 4alpha in control of blood coagulation factor gene expression. J Mol Med 84 4 (Apr 2006) 334-344
    • (2006) J Mol Med , vol.84 , Issue.4 , pp. 334-344
    • Inoue, Y.1    Peters, L.L.2    Yim, S.H.3    Inoue, J.4    Gonzalez, F.J.5
  • 50
    • 72949143661 scopus 로고
    • The partial thromboplastin time with kaolin. A simple screening test for first stage plasma clotting factor deficiencies
    • Proctor R.R., and Rapaport S.I. The partial thromboplastin time with kaolin. A simple screening test for first stage plasma clotting factor deficiencies. Am J Clin Pathol 36 (Sep 1961) 212-219
    • (1961) Am J Clin Pathol , vol.36 , pp. 212-219
    • Proctor, R.R.1    Rapaport, S.I.2
  • 51
    • 22944462705 scopus 로고    scopus 로고
    • Defective thrombus formation in mice lacking coagulation factor XII
    • Renne T., Pozgajova M., Gruner S., Schuh K., Pauer H.U., Burfeind P., et al. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med 202 2 (Jul 18 2005) 271-281
    • (2005) J Exp Med , vol.202 , Issue.2 , pp. 271-281
    • Renne, T.1    Pozgajova, M.2    Gruner, S.3    Schuh, K.4    Pauer, H.U.5    Burfeind, P.6
  • 52
    • 33645066112 scopus 로고    scopus 로고
    • Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis
    • Kleinschnitz C., Stoll G., Bendszus M., Schuh K., Pauer H.U., Burfeind P., et al. Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis. J Exp Med 203 3 (Mar 20 2006) 513-518
    • (2006) J Exp Med , vol.203 , Issue.3 , pp. 513-518
    • Kleinschnitz, C.1    Stoll, G.2    Bendszus, M.3    Schuh, K.4    Pauer, H.U.5    Burfeind, P.6
  • 53
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer W.M., Mannhalter C., Feichtinger C., Rubi K., and Fischer M. The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost 68 3 (Sep 7 1992) 285-290
    • (1992) Thromb Haemost , vol.68 , Issue.3 , pp. 285-290
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3    Rubi, K.4    Fischer, M.5
  • 54
    • 0028234054 scopus 로고
    • John Hageman's factor and deep-vein thrombosis: Leiden thrombophilia Study
    • Koster T., Rosendaal F.R., Briet E., and Vandenbroucke J.P. John Hageman's factor and deep-vein thrombosis: Leiden thrombophilia Study. Br J Haematol 87 2 (Jun 1994) 422-424
    • (1994) Br J Haematol , vol.87 , Issue.2 , pp. 422-424
    • Koster, T.1    Rosendaal, F.R.2    Briet, E.3    Vandenbroucke, J.P.4
  • 55
    • 3242748377 scopus 로고    scopus 로고
    • Homozygosity of the T allele of the 46 C->T polymorphism in the F12 gene is a risk factor for ischemic stroke in the Spanish population
    • Santamaria A., Mateo J., Tirado I., Oliver A., Belvis R., Marti-Fabregas J., et al. Homozygosity of the T allele of the 46 C->T polymorphism in the F12 gene is a risk factor for ischemic stroke in the Spanish population. Stroke 35 8 (Aug 2004) 1795-1799
    • (2004) Stroke , vol.35 , Issue.8 , pp. 1795-1799
    • Santamaria, A.1    Mateo, J.2    Tirado, I.3    Oliver, A.4    Belvis, R.5    Marti-Fabregas, J.6
  • 56
    • 18244384262 scopus 로고    scopus 로고
    • A quantitative-trait locus in the human factor XII gene influences both plasma factor XII levels and susceptibility to thrombotic disease
    • Soria J.M., Almasy L., Souto J.C., Bacq D., Buil A., Faure A., et al. A quantitative-trait locus in the human factor XII gene influences both plasma factor XII levels and susceptibility to thrombotic disease. Am J Hum Genet 70 3 (Mar 2002) 567-574
    • (2002) Am J Hum Genet , vol.70 , Issue.3 , pp. 567-574
    • Soria, J.M.1    Almasy, L.2    Souto, J.C.3    Bacq, D.4    Buil, A.5    Faure, A.6
  • 57
    • 0036840704 scopus 로고    scopus 로고
    • Association of the factor XII 46C>T polymorphism with risk of coronary heart disease (CHD) in the WOSCOPS study
    • Zito F., Lowe G.D., Rumley A., McMahon A.D., and Humphries S.E. Association of the factor XII 46C>T polymorphism with risk of coronary heart disease (CHD) in the WOSCOPS study. Atherosclerosis 165 1 (Nov 2002) 153-158
    • (2002) Atherosclerosis , vol.165 , Issue.1 , pp. 153-158
    • Zito, F.1    Lowe, G.D.2    Rumley, A.3    McMahon, A.D.4    Humphries, S.E.5
  • 58
    • 0035543840 scopus 로고    scopus 로고
    • Homozygosity for the C->T polymorphism at nucleotide 46 in the 5' untranslated region of the factor XII gene protects from development of acute coronary syndrome
    • Endler G., Mannhalter C., Sunder-Plassmann H., Lalouschek W., Kapiotis S., Exner M., et al. Homozygosity for the C->T polymorphism at nucleotide 46 in the 5' untranslated region of the factor XII gene protects from development of acute coronary syndrome. Br J Haematol 115 4 (Dec 2001) 1007-1009
    • (2001) Br J Haematol , vol.115 , Issue.4 , pp. 1007-1009
    • Endler, G.1    Mannhalter, C.2    Sunder-Plassmann, H.3    Lalouschek, W.4    Kapiotis, S.5    Exner, M.6
  • 59
    • 0036269750 scopus 로고    scopus 로고
    • Activated factor XII levels and factor XII 46C>T genotype in relation to coronary artery calcification in patients with type 1 diabetes and healthy subjects
    • Colhoun H.M., Zito F., Norman Chan N., Rubens M.B., Fuller J.H., and Humphries S.E. Activated factor XII levels and factor XII 46C>T genotype in relation to coronary artery calcification in patients with type 1 diabetes and healthy subjects. Atherosclerosis 163 2 (Aug 2002) 363-369
    • (2002) Atherosclerosis , vol.163 , Issue.2 , pp. 363-369
    • Colhoun, H.M.1    Zito, F.2    Norman Chan, N.3    Rubens, M.B.4    Fuller, J.H.5    Humphries, S.E.6
  • 60
    • 33845497457 scopus 로고    scopus 로고
    • Levels of intrinsic coagulation factors and the risk of myocardial infarction among men: Opposite and synergistic effects of factors XI and XII
    • Doggen C.J., Rosendaal F.R., and Meijers J.C. Levels of intrinsic coagulation factors and the risk of myocardial infarction among men: Opposite and synergistic effects of factors XI and XII. Blood 108 13 (Dec 15 2006) 4045-4051
    • (2006) Blood , vol.108 , Issue.13 , pp. 4045-4051
    • Doggen, C.J.1    Rosendaal, F.R.2    Meijers, J.C.3
  • 61
    • 34250170510 scopus 로고    scopus 로고
    • The intrinsic pathway of coagulation: a target for treating thromboembolic disease?
    • Gailani D., and Renne T. The intrinsic pathway of coagulation: a target for treating thromboembolic disease?. J Thromb Haemost 5 6 (Jun 2007) 1106-1112
    • (2007) J Thromb Haemost , vol.5 , Issue.6 , pp. 1106-1112
    • Gailani, D.1    Renne, T.2
  • 63
    • 0032850195 scopus 로고    scopus 로고
    • Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4alpha1
    • Sladek F.M., Ruse Jr. M.D., Nepomuceno L., Huang S.M., and Stallcup M.R. Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4alpha1. Mol Cell Biol 19 10 (Oct 1999) 6509-6522
    • (1999) Mol Cell Biol , vol.19 , Issue.10 , pp. 6509-6522
    • Sladek, F.M.1    Ruse Jr., M.D.2    Nepomuceno, L.3    Huang, S.M.4    Stallcup, M.R.5
  • 64
    • 0021859293 scopus 로고
    • Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)
    • McMullen B.A., and Fujikawa K. Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J Biol Chem 260 9 (May 10 1985) 5328-5341
    • (1985) J Biol Chem , vol.260 , Issue.9 , pp. 5328-5341
    • McMullen, B.A.1    Fujikawa, K.2
  • 65
    • 0027496212 scopus 로고
    • Contact activation in human plasma is triggered by zinc ion modulation of factor XII (Hageman factor)
    • Schousboe I. Contact activation in human plasma is triggered by zinc ion modulation of factor XII (Hageman factor). Blood Coagul Fibrinolysis 4 5 (Oct 1993) 671-678
    • (1993) Blood Coagul Fibrinolysis , vol.4 , Issue.5 , pp. 671-678
    • Schousboe, I.1
  • 66
    • 0028856725 scopus 로고
    • Monoclonal antibody F1 binds to the kringle domain of factor XII and induces enhanced susceptibility for cleavage by kallikrein
    • Ravon D.M., Citarella F., Lubbers Y.T., Pascucci B., and Hack C.E. Monoclonal antibody F1 binds to the kringle domain of factor XII and induces enhanced susceptibility for cleavage by kallikrein. Blood 86 11 (Dec 1 1995) 4134-4143
    • (1995) Blood , vol.86 , Issue.11 , pp. 4134-4143
    • Ravon, D.M.1    Citarella, F.2    Lubbers, Y.T.3    Pascucci, B.4    Hack, C.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.