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Volumn 288, Issue 41, 2013, Pages 29394-29402

Zn2+ mediates high affinity binding of heparin to the αc domain of fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

ANTICOAGULANT ACTIVITIES; DEGRADATION PRODUCTS; HEPARIN BINDING; HEPARIN-BINDING SITE; HIGH AFFINITY BINDING; NON-SPECIFIC BINDING; PEPTIDE ANALOGS; PLASMA PROTEIN;

EID: 84885593825     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.469916     Document Type: Article
Times cited : (24)

References (50)
  • 3
    • 0027520062 scopus 로고
    • Comparison of the non-specific binding of unfractionated heparin and low molecular weight heparin (Enoxaparin) to plasma proteins
    • Young, E., Cosmi, B., Weitz, J., and Hirsh, J. (1993) Comparison of the non-specific binding of unfractionated heparin and low molecular weight heparin (Enoxaparin) to plasma proteins. Thromb. Haemost. 70, 625-630
    • (1993) Thromb. Haemost , vol.70 , pp. 625-630
    • Young, E.1    Cosmi, B.2    Weitz, J.3    Hirsh, J.4
  • 4
    • 0032489379 scopus 로고    scopus 로고
    • Histidine-proline-rich glycoprotein as a plasma pH sensor. Modulation of its interaction with glycosaminoglycans by pH and metals
    • Borza, D. B., and Morgan, W. T. (1998) Histidine-proline-rich glycoprotein as a plasma pH sensor. Modulation of its interaction with glycosaminoglycans by pH and metals. J. Biol. Chem. 273, 5493-5499
    • (1998) J. Biol. Chem , vol.273 , pp. 5493-5499
    • Borza, D.B.1    Morgan, W.T.2
  • 5
    • 0024511155 scopus 로고
    • Binding of heparin to human high molecular weight kininogen
    • Björk, I., Olson, S. T., Sheffer, R. G., and Shore, J. D. (1989) Binding of heparin to human high molecular weight kininogen. Biochemistry 28, 1213-1221
    • (1989) Biochemistry , vol.28 , pp. 1213-1221
    • Björk, I.1    Olson, S.T.2    Sheffer, R.G.3    Shore, J.D.4
  • 6
    • 0024670167 scopus 로고
    • Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III: Implications for heparin efficacy
    • Hogg, P. J., and Jackson, C. M. (1989) Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III: implications for heparin efficacy. Proc. Natl. Acad. Sci. U.S.A. 86, 3619-3623
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 3619-3623
    • Hogg, P.J.1    Jackson, C.M.2
  • 7
    • 0031439715 scopus 로고    scopus 로고
    • Molecular basis for the resistance of fibrin-bound thrombin to inactivation by heparin/serpin complexes
    • Becker, D. L., Fredenburgh, J. C., Stafford, A. R., and Weitz, J. I. (1997) Molecular basis for the resistance of fibrin-bound thrombin to inactivation by heparin/serpin complexes. Adv. Exp. Med. Biol. 425, 55-66
    • (1997) Adv. Exp. Med. Biol , vol.425 , pp. 55-66
    • Becker, D.L.1    Fredenburgh, J.C.2    Stafford, A.R.3    Weitz, J.I.4
  • 8
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and Falchuk, K. H. (1993) The biochemical basis of zinc physiology. Physiol. Rev. 73, 79-118
    • (1993) Physiol. Rev , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 9
    • 84874778287 scopus 로고    scopus 로고
    • Zinc: An important cofactor in haemostasis and thrombosis
    • Vu, T. T., Fredenburgh, J. C., and Weitz, J. I. (2013) Zinc: An important cofactor in haemostasis and thrombosis. Thromb. Haemost. 109, 421-430
    • (2013) Thromb. Haemost , vol.109 , pp. 421-430
    • Vu, T.T.1    Fredenburgh, J.C.2    Weitz, J.I.3
  • 10
    • 84867457102 scopus 로고    scopus 로고
    • By increasing the affinity of heparin for fibrin, Zn2+ promotes the formation of a ternary heparinthrombin- fibrin complex that protects thrombin from inhibition by antithrombin
    • Chan, H. H., Leslie, B. A., Stafford, A. R., Roberts, R. S., Al-Aswad, N. N., Fredenburgh, J. C., and Weitz, J. I. (2012) By increasing the affinity of heparin for fibrin, Zn2+ promotes the formation of a ternary heparinthrombin- fibrin complex that protects thrombin from inhibition by antithrombin. Biochemistry 51, 7964-7973
    • (2012) Biochemistry , vol.51 , pp. 7964-7973
    • Chan, H.H.1    Leslie, B.A.2    Stafford, A.R.3    Roberts, R.S.4    Al-Aswad, N.N.5    Fredenburgh, J.C.6    Weitz, J.I.7
  • 11
    • 0022499723 scopus 로고
    • Binding of zinc ions to heparin. Analysis by equilibrium dialysis suggests the occurrence of two, entropy-driven, processes
    • Woodhead, N. E., Long, W. F., and Williamson, F. B. (1986) Binding of zinc ions to heparin. Analysis by equilibrium dialysis suggests the occurrence of two, entropy-driven, processes. Biochem. J. 237, 281-284
    • (1986) Biochem. J , vol.237 , pp. 281-284
    • Woodhead, N.E.1    Long, W.F.2    Williamson, F.B.3
  • 12
    • 0023679995 scopus 로고
    • Zinc binding to fibrinogen and fibrin
    • Marx, G. (1988) Zinc binding to fibrinogen and fibrin. Arch. Biochem. Biophys. 266, 285-288
    • (1988) Arch. Biochem. Biophys , vol.266 , pp. 285-288
    • Marx, G.1
  • 13
    • 41449105828 scopus 로고    scopus 로고
    • Bivalent binding to γa/γ'-fibrin engages both exosites of thrombin and protects it from inhibition by the antithrombin-heparin complex
    • Fredenburgh, J. C., Stafford, A. R., Leslie, B. A., and Weitz, J. I. (2008) Bivalent binding to γA/γ'-fibrin engages both exosites of thrombin and protects it from inhibition by the antithrombin-heparin complex. J. Biol. Chem. 283, 2470-2477
    • (2008) J. Biol. Chem , vol.283 , pp. 2470-2477
    • Fredenburgh, J.C.1    Stafford, A.R.2    Leslie, B.A.3    Weitz, J.I.4
  • 14
    • 33645547820 scopus 로고    scopus 로고
    • Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin
    • Schaefer, A. V., Leslie, B. A., Rischke, J. A., Stafford, A. R., Fredenburgh, J. C., and Weitz, J. I. (2006) Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin. Biochemistry 45, 4257-4265
    • (2006) Biochemistry , vol.45 , pp. 4257-4265
    • Schaefer, A.V.1    Leslie, B.A.2    Rischke, J.A.3    Stafford, A.R.4    Fredenburgh, J.C.5    Weitz, J.I.6
  • 15
    • 0037821812 scopus 로고    scopus 로고
    • Evidence that both exosites on thrombin participate in its high affinity interaction with fibrin
    • Pospisil, C. H., Stafford, A. R., Fredenburgh, J. C., and Weitz, J. I. (2003) Evidence that both exosites on thrombin participate in its high affinity interaction with fibrin. J. Biol. Chem. 278, 21584-21591
    • (2003) J. Biol. Chem , vol.278 , pp. 21584-21591
    • Pospisil, C.H.1    Stafford, A.R.2    Fredenburgh, J.C.3    Weitz, J.I.4
  • 16
    • 0020566458 scopus 로고
    • Monoclonal antibodies to α-chain regions of human fibrinogen that participate in polymer formation
    • Ehrlich, P. H., Sobel, J. H., Moustafa, Z. A., and Canfield, R. E. (1983) Monoclonal antibodies to α-chain regions of human fibrinogen that participate in polymer formation. Biochemistry 22, 4184-4192
    • (1983) Biochemistry , vol.22 , pp. 4184-4192
    • Ehrlich, P.H.1    Sobel, J.H.2    Moustafa, Z.A.3    Canfield, R.E.4
  • 17
    • 0025313097 scopus 로고
    • Interaction of integrins αvβ3 and glycoprotein IIb-IIIa with fibrinogen. Differential peptide recognition accounts for distinct binding sites
    • Smith, J. W., Ruggeri, Z. M., Kunicki, T. J., and Cheresh, D. A. (1990) Interaction of integrins αvβ3 and glycoprotein IIb-IIIa with fibrinogen. Differential peptide recognition accounts for distinct binding sites. J. Biol. Chem. 265, 12267-12271
    • (1990) J. Biol. Chem , vol.265 , pp. 12267-12271
    • Smith, J.W.1    Ruggeri, Z.M.2    Kunicki, T.J.3    Cheresh, D.A.4
  • 18
    • 76449121417 scopus 로고    scopus 로고
    • Decreased plasmin resistance by clots of a homophenotypic AαR 16H fibrinogen (Kingsport, slower fibrinopeptide A than fibrinopeptide B release)
    • Galanakis, D. K., Neerman-Arbez, M., Kudryk, B., and Henschen, A. (2010) Decreased plasmin resistance by clots of a homophenotypic AαR 16H fibrinogen (Kingsport, slower fibrinopeptide A than fibrinopeptide B release). Blood Coagul. Fibrinolysis 21, 135-139
    • (2010) Blood Coagul. Fibrinolysis , vol.21 , pp. 135-139
    • Galanakis, D.K.1    Neerman-Arbez, M.2    Kudryk, B.3    Henschen, A.4
  • 19
    • 0037112671 scopus 로고    scopus 로고
    • Proteinheparin interactions measured by BIAcore 2000 are affected by the method of heparin immobilization
    • Osmond, R. I., Kett, W. C., Skett, S. E., and Coombe, D. R. (2002) Proteinheparin interactions measured by BIAcore 2000 are affected by the method of heparin immobilization. Anal. Biochem. 310, 199-207
    • (2002) Anal. Biochem , vol.310 , pp. 199-207
    • Osmond, R.I.1    Kett, W.C.2    Skett, S.E.3    Coombe, D.R.4
  • 20
    • 34047199215 scopus 로고    scopus 로고
    • In the presence of phospholipids, glycosaminoglycans potentiate factor Xa-mediated protein C activation by modulating factor Xa activity
    • McRae, S. J., Stafford, A. R., Fredenburgh, J. C., and Weitz, J. I. (2007) In the presence of phospholipids, glycosaminoglycans potentiate factor Xa-mediated protein C activation by modulating factor Xa activity. Biochemistry 46, 4195-4203
    • (2007) Biochemistry , vol.46 , pp. 4195-4203
    • McRae, S.J.1    Stafford, A.R.2    Fredenburgh, J.C.3    Weitz, J.I.4
  • 21
    • 0025667113 scopus 로고
    • The dissociation constants and stoichiometries of the interactions of Lys-plasminogen and chloromethyl ketone derivatives of tissue plasminogen activator and the variant ΔfEIX with intact fibrin
    • Nesheim, M., Fredenburgh, J. C., and Larsen, G. R. (1990) The dissociation constants and stoichiometries of the interactions of Lys-plasminogen and chloromethyl ketone derivatives of tissue plasminogen activator and the variant ΔFEIX with intact fibrin. J. Biol. Chem. 265, 21541-21548
    • (1990) J. Biol. Chem , vol.265 , pp. 21541-21548
    • Nesheim, M.1    Fredenburgh, J.C.2    Larsen, G.R.3
  • 22
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Olson, S. T., Björk, I., and Shore, J. D. (1993) Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol. 222, 525-559
    • (1993) Methods Enzymol , vol.222 , pp. 525-559
    • Olson, S.T.1    Björk, I.2    Shore, J.D.3
  • 23
    • 0025096662 scopus 로고
    • Heparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombinfibrin polymer-heparin ternary complex
    • Hogg, P. J., and Jackson, C. M. (1990) Heparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombinfibrin polymer-heparin ternary complex. J. Biol. Chem. 265, 241-247
    • (1990) J. Biol. Chem , vol.265 , pp. 241-247
    • Hogg, P.J.1    Jackson, C.M.2
  • 24
    • 0035584032 scopus 로고    scopus 로고
    • Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance
    • Gestwicki, J. E., Hsieh, H. V., and Pitner, J. B. (2001) Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance. Anal. Chem. 73, 5732-5737
    • (2001) Anal. Chem , vol.73 , pp. 5732-5737
    • Gestwicki, J.E.1    Hsieh, H.V.2    Pitner, J.B.3
  • 25
    • 79251535901 scopus 로고    scopus 로고
    • Metals affect the structure and activity of human plasminogen activator inhibitor-1. II. Binding affinity and conformational changes
    • Thompson, L. C., Goswami, S., and Peterson, C. B. (2011) Metals affect the structure and activity of human plasminogen activator inhibitor-1. II. Binding affinity and conformational changes. Protein Sci. 20, 366-378
    • (2011) Protein Sci , vol.20 , pp. 366-378
    • Thompson, L.C.1    Goswami, S.2    Peterson, C.B.3
  • 26
    • 78650710112 scopus 로고    scopus 로고
    • Zn(II) complexes of glutathione disulfide: Structural bases of elevated stabilities
    • Krezel, A., Wójcik, J., Maciejczyk, M., and Bal, W. (2011) Zn(II) complexes of glutathione disulfide: Structural bases of elevated stabilities. Inorg. Chem. 50, 72-85
    • (2011) Inorg. Chem , vol.50 , pp. 72-85
    • Krezel, A.1    Wójcik, J.2    Maciejczyk, M.3    Bal, W.4
  • 27
    • 0033525536 scopus 로고    scopus 로고
    • Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II
    • Becker, D. L., Fredenburgh, J. C., Stafford, A. R., and Weitz, J. I. (1999) Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II. J. Biol. Chem. 274, 6226-6233
    • (1999) J. Biol. Chem , vol.274 , pp. 6226-6233
    • Becker, D.L.1    Fredenburgh, J.C.2    Stafford, A.R.3    Weitz, J.I.4
  • 28
    • 0029847785 scopus 로고    scopus 로고
    • Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin β chain
    • Odrljin, T. M., Shainoff, J. R., Lawrence, S. O., and Simpson-Haidaris, P. J. (1996) Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin β chain. Blood 88, 2050-2061
    • (1996) Blood , vol.88 , pp. 2050-2061
    • Odrljin, T.M.1    Shainoff, J.R.2    Lawrence, S.O.3    Simpson-Haidaris, P.J.4
  • 29
    • 0037663710 scopus 로고    scopus 로고
    • Interaction of fibrin(ogen) with heparin: Further characterization and localization of the heparin-binding site
    • Yakovlev, S., Gorlatov, S., Ingham, K., and Medved, L. (2003) Interaction of fibrin(ogen) with heparin: Further characterization and localization of the heparin-binding site. Biochemistry 42, 7709-7716
    • (2003) Biochemistry , vol.42 , pp. 7709-7716
    • Yakovlev, S.1    Gorlatov, S.2    Ingham, K.3    Medved, L.4
  • 30
    • 0010513386 scopus 로고
    • Heparin binding sites are located in a 40-kD γ-chain and a 36kD β-chain fragment isolated from human fibrinogen
    • Mohri, H., Iwamatsu, A., and Ohkubo, T. (1994) Heparin binding sites are located in a 40-kD γ-chain and a 36kD β-chain fragment isolated from human fibrinogen. J. Thromb. Thrombolysis 1, 49-54
    • (1994) J. Thromb. Thrombolysis , vol.1 , pp. 49-54
    • Mohri, H.1    Iwamatsu, A.2    Ohkubo, T.3
  • 31
    • 0021031042 scopus 로고
    • Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation
    • Leung, L. L., Harpel, P. C., Nachman, R. L., and Rabellino, E. M. (1983) Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation. Blood 62, 1016-1021
    • (1983) Blood , vol.62 , pp. 1016-1021
    • Leung, L.L.1    Harpel, P.C.2    Nachman, R.L.3    Rabellino, E.M.4
  • 32
    • 0020068668 scopus 로고
    • Structural features of fibrinogen associated with binding to chelated zinc
    • Scully, M. F., and Kakkar, V. V. (1982) Structural features of fibrinogen associated with binding to chelated zinc. Biochim. Biophys. Acta 700, 130-135
    • (1982) Biochim. Biophys. Acta , vol.700 , pp. 130-135
    • Scully, M.F.1    Kakkar, V.V.2
  • 33
    • 0024584913 scopus 로고
    • Molecular modeling of proteinglycosaminoglycan interactions
    • Cardin, A. D., and Weintraub, H. J. (1989) Molecular modeling of proteinglycosaminoglycan interactions. Arteriosclerosis 9, 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 34
    • 0020357050 scopus 로고
    • The interaction of zinc, nickel and cadmium with serum albumin and histidine-rich glycoprotein assessed by equilibrium dialysis and immunoadsorbent chromatography
    • Guthans, S. L., and Morgan, W. T. (1982) The interaction of zinc, nickel and cadmium with serum albumin and histidine-rich glycoprotein assessed by equilibrium dialysis and immunoadsorbent chromatography. Arch. Biochem. Biophys. 218, 320-328
    • (1982) Arch. Biochem. Biophys , vol.218 , pp. 320-328
    • Guthans, S.L.1    Morgan, W.T.2
  • 35
    • 33646684033 scopus 로고    scopus 로고
    • Zinc potentiates the antibacterial effects of histidine-rich peptides against Enterococcus faecalis
    • Rydengård, V., Andersson Nordahl, E., and Schmidtchen, A. (2006) Zinc potentiates the antibacterial effects of histidine-rich peptides against Enterococcus faecalis. FEBS J. 273, 2399-2406
    • (2006) FEBS J , vol.273 , pp. 2399-2406
    • Rydengård, V.1    Andersson Nordahl, E.2    Schmidtchen, A.3
  • 36
    • 33644530354 scopus 로고    scopus 로고
    • Solution1HNMRinvestigation of Zn2+ and Cd2+ binding to amyloid-β peptide (Aβ) of Alzheimer's disease
    • Syme, C. D., and Viles, J. H. (2006) Solution1HNMRinvestigation of Zn2+ and Cd2+ binding to amyloid-β peptide (Aβ) of Alzheimer's disease. Biochim. Biophys. Acta 1764, 246-256
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 246-256
    • Syme, C.D.1    Viles, J.H.2
  • 38
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and Auld, D. S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29, 5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 39
    • 0037464489 scopus 로고    scopus 로고
    • Zinc ions promote the interaction between heparin and heparin cofactor II
    • Eckert, R., and Ragg, H. (2003) Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Lett. 541, 121-125
    • (2003) FEBS Lett , vol.541 , pp. 121-125
    • Eckert, R.1    Ragg, H.2
  • 41
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • González-Iglesias, R., Pajares, M. A., Ocal, C., Espinosa, J. C., Oesch, B., and Gasset, M. (2002) Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J. Mol. Biol. 319, 527-540
    • (2002) J. Mol. Biol , vol.319 , pp. 527-540
    • González-Iglesias, R.1    Pajares, M.A.2    Ocal, C.3    Espinosa, J.C.4    Oesch, B.5    Gasset, M.6
  • 42
    • 0019431688 scopus 로고
    • Selective binding of zinc ions to heparin rather than to other glycosaminoglycans
    • Parrish, R. F., and Fair, W. R. (1981) Selective binding of zinc ions to heparin rather than to other glycosaminoglycans. Biochem. J. 193, 407-410
    • (1981) Biochem. J , vol.193 , pp. 407-410
    • Parrish, R.F.1    Fair, W.R.2
  • 43
    • 0026598679 scopus 로고
    • Modulation of protein C inhibitor activity by histidine-rich glycoprotein and platelet factor 4: Role of zinc and calcium ions in the heparin-neutralizing ability of histidine-rich glycoprotein
    • Kazama, Y., and Koide, T. (1992) Modulation of protein C inhibitor activity by histidine-rich glycoprotein and platelet factor 4: role of zinc and calcium ions in the heparin-neutralizing ability of histidine-rich glycoprotein. Thromb. Haemost. 67, 50-55
    • (1992) Thromb. Haemost , vol.67 , pp. 50-55
    • Kazama, Y.1    Koide, T.2
  • 44
    • 0020672569 scopus 로고
    • Neutralization of heparin activity by binding to human histidine-rich glycoprotein
    • Lijnen, H. R., Hoylaerts, M., and Collen, D. (1983) Neutralization of heparin activity by binding to human histidine-rich glycoprotein. Thromb. Res. 29, 443-446
    • (1983) Thromb. Res , vol.29 , pp. 443-446
    • Lijnen, H.R.1    Hoylaerts, M.2    Collen, D.3
  • 45
    • 0030971085 scopus 로고    scopus 로고
    • Zinc as a cofactor for heparin neutralization by histidine-rich glycoprotein
    • Kluszynski, B. A., Kim, C., and Faulk, W. P. (1997) Zinc as a cofactor for heparin neutralization by histidine-rich glycoprotein. J. Biol. Chem. 272, 13541-13547
    • (1997) J. Biol. Chem , vol.272 , pp. 13541-13547
    • Kluszynski, B.A.1    Kim, C.2    Faulk, W.P.3
  • 46
    • 0022999181 scopus 로고
    • Neutralization of heparin-related saccharides by histidine-rich glycoprotein and platelet factor 4
    • Lane, D. A., Pejler, G., Flynn, A. M., Thompson, E. A., and Lindahl, U. (1986) Neutralization of heparin-related saccharides by histidine-rich glycoprotein and platelet factor 4. J. Biol. Chem. 261, 3980-3986
    • (1986) J. Biol. Chem , vol.261 , pp. 3980-3986
    • Lane, D.A.1    Pejler, G.2    Flynn, A.M.3    Thompson, E.A.4    Lindahl, U.5
  • 49
    • 33747702876 scopus 로고    scopus 로고
    • High resolution structures of p-aminobenzamidine- and benzamidine- VIIa/soluble tissue factor: Unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa
    • Bajaj, S. P., Schmidt, A. E., Agah, S., Bajaj, M. S., and Padmanabhan, K. (2006) High resolution structures of p-aminobenzamidine- and benzamidine- VIIa/soluble tissue factor: unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa. J. Biol. Chem. 281, 24873-24888
    • (2006) J. Biol. Chem , vol.281 , pp. 24873-24888
    • Bajaj, S.P.1    Schmidt, A.E.2    Agah, S.3    Bajaj, M.S.4    Padmanabhan, K.5
  • 50
    • 68549127071 scopus 로고    scopus 로고
    • Plasma protein S contains zinc essential for efficient activated protein C-independent anticoagulant activity and binding to factor Xa, but not for efficient binding to tissue factor pathway inhibitor
    • Heeb, M. J., Prashun, D., Griffin, J. H., and Bouma, B. N. (2009) Plasma protein S contains zinc essential for efficient activated protein C-independent anticoagulant activity and binding to factor Xa, but not for efficient binding to tissue factor pathway inhibitor. FASEB J. 23, 2244-2253
    • (2009) FASEB J , vol.23 , pp. 2244-2253
    • Heeb, M.J.1    Prashun, D.2    Griffin, J.H.3    Bouma, B.N.4


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