메뉴 건너뛰기




Volumn 425, Issue 11, 2013, Pages 1961-1981

Structural and functional studies of γ-carboxyglutamic acid domains of factor VIIa and activated protein C: Role of magnesium at physiological calcium

Author keywords

activated Protein C; factor VIIa; surface plasmon resonance; carboxyglutamic acid domains

Indexed keywords

4 CARBOXYGLUTAMIC ACID; ACTIVATED PROTEIN C; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 5A; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 9; CALCIUM ION; ENDOTHELIAL PROTEIN C RECEPTOR; MAGNESIUM ION; THROMBOPLASTIN;

EID: 84877723864     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.02.017     Document Type: Article
Times cited : (25)

References (75)
  • 2
    • 0346435111 scopus 로고    scopus 로고
    • A brief historical review of the waterfall/cascade of blood coagulation
    • E.W. Davie A brief historical review of the waterfall/cascade of blood coagulation J. Biol. Chem. 278 2003 50819 50832
    • (2003) J. Biol. Chem. , vol.278 , pp. 50819-50832
    • Davie, E.W.1
  • 3
    • 82555181621 scopus 로고    scopus 로고
    • The structure-function relationship of activated protein C. Lessons from natural and engineered mutations
    • K.C. Wildhagen, E. Lutgens, S.T. Loubele, H. ten Cate, and G.A. Nicolaes The structure-function relationship of activated protein C. Lessons from natural and engineered mutations Thromb. Haemost. 106 2011 1034 1045
    • (2011) Thromb. Haemost. , vol.106 , pp. 1034-1045
    • Wildhagen, K.C.1    Lutgens, E.2    Loubele, S.T.3    Ten Cate, H.4    Nicolaes, G.A.5
  • 4
    • 84859718853 scopus 로고    scopus 로고
    • Protein C anticoagulant system - Anti-inflammatory effects
    • C.T. Esmon Protein C anticoagulant system - anti-inflammatory effects Semin. Immunopathol. 34 2012 127 132
    • (2012) Semin. Immunopathol. , vol.34 , pp. 127-132
    • Esmon, C.T.1
  • 6
    • 0028986860 scopus 로고
    • Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy
    • S.J. Freedman, B.C. Furie, B. Furie, and J.D. Baleja Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy J. Biol. Chem. 270 1995 7980 7987
    • (1995) J. Biol. Chem. , vol.270 , pp. 7980-7987
    • Freedman, S.J.1    Furie, B.C.2    Furie, B.3    Baleja, J.D.4
  • 7
    • 0029083550 scopus 로고
    • Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX
    • S.J. Freedman, B.C. Furie, B. Furie, and J.D. Baleja Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX Biochemistry 34 1995 12126 12137
    • (1995) Biochemistry , vol.34 , pp. 12126-12137
    • Freedman, S.J.1    Furie, B.C.2    Furie, B.3    Baleja, J.D.4
  • 9
    • 0017620084 scopus 로고
    • Differentiation of metal ion-induced transitions of prothrombin fragment 1
    • F.G. Prendergast, and K.G. Mann Differentiation of metal ion-induced transitions of prothrombin fragment 1 J. Biol. Chem. 252 1977 840 850
    • (1977) J. Biol. Chem. , vol.252 , pp. 840-850
    • Prendergast, F.G.1    Mann, K.G.2
  • 10
    • 0025879190 scopus 로고
    • 2 + binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains
    • 2 + binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains J. Biol. Chem. 266 1991 2444 2452
    • (1991) J. Biol. Chem. , vol.266 , pp. 2444-2452
    • Persson, E.1    Björk, I.2    Stenflo, J.3
  • 11
    • 0028940777 scopus 로고
    • Human protein C and activated protein C components of the human anticoagulation system
    • F.J. Castellino Human protein C and activated protein C components of the human anticoagulation system Trends Cardiovasc. Med. 5 1995 55 62
    • (1995) Trends Cardiovasc. Med. , vol.5 , pp. 55-62
    • Castellino, F.J.1
  • 13
    • 67949112761 scopus 로고    scopus 로고
    • Role of magnesium in factor XIa catalyzed activation of factor IX: Calcium binding to factor IX under physiologic magnesium
    • S. Agah, and S.P. Bajaj Role of magnesium in factor XIa catalyzed activation of factor IX: calcium binding to factor IX under physiologic magnesium J. Thromb. Haemost. 7 2009 1426 1428
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1426-1428
    • Agah, S.1    Bajaj, S.P.2
  • 14
    • 0036673868 scopus 로고    scopus 로고
    • PH effects on measurements of ionized calcium and ionized magnesium in blood
    • S. Wang, E.H. McDonnell, F.A. Sedor, and J.G. Toffaletti pH effects on measurements of ionized calcium and ionized magnesium in blood Arch. Pathol. Lab. Med. 126 2002 947 950
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 947-950
    • Wang, S.1    McDonnell, E.H.2    Sedor, F.A.3    Toffaletti, J.G.4
  • 15
    • 0029027653 scopus 로고
    • Regulation of the tertiary structure and function of coagulation factor IX by magnesium (II) ions
    • F. Sekiya, T. Yamashita, H. Atoda, Y. Komiyama, and T. Morita Regulation of the tertiary structure and function of coagulation factor IX by magnesium (II) ions J. Biol. Chem. 270 1995 14325 14331
    • (1995) J. Biol. Chem. , vol.270 , pp. 14325-14331
    • Sekiya, F.1    Yamashita, T.2    Atoda, H.3    Komiyama, Y.4    Morita, T.5
  • 16
    • 0030565412 scopus 로고    scopus 로고
    • Localization of the specific binding site for magnesium (II) ions in factor IX
    • F. Sekiya, M. Yoshida, T. Yamashita, and T. Morita Localization of the specific binding site for magnesium (II) ions in factor IX FEBS Lett. 392 1996 205 208
    • (1996) FEBS Lett. , vol.392 , pp. 205-208
    • Sekiya, F.1    Yoshida, M.2    Yamashita, T.3    Morita, T.4
  • 18
    • 77449130501 scopus 로고    scopus 로고
    • Contribution of magnesium in binding of factor IXa to the phospholipid surface: Implications for vitamin K-dependent coagulation proteins
    • A.S. Messer, W.H. Velander, and S.P. Bajaj Contribution of magnesium in binding of factor IXa to the phospholipid surface: implications for vitamin K-dependent coagulation proteins J. Thromb. Haemost. 7 2009 2151 2153
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 2151-2153
    • Messer, A.S.1    Velander, W.H.2    Bajaj, S.P.3
  • 20
    • 34548070184 scopus 로고    scopus 로고
    • Mg(2 +) binding to the Gla domain of factor X influences the interaction with tissue factor
    • E. Persson, and A. Ostergaard Mg(2 +) binding to the Gla domain of factor X influences the interaction with tissue factor J. Thromb. Haemost. 5 2007 1977 1978
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1977-1978
    • Persson, E.1    Ostergaard, A.2
  • 21
    • 58149141636 scopus 로고    scopus 로고
    • Anticoagulant mechanism of factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis
    • M. Ishikawa, M. Kumashiro, Y. Yamazaki, H. Atoda, and T. Morita Anticoagulant mechanism of factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis J. Biochem. 145 2009 123 128
    • (2009) J. Biochem. , vol.145 , pp. 123-128
    • Ishikawa, M.1    Kumashiro, M.2    Yamazaki, Y.3    Atoda, H.4    Morita, T.5
  • 22
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • D.W. Banner, A. D'Arcy, C. Chène, F.K. Winkler, A. Guha, and W.H. Konigsberg The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor Nature 380 1996 41 46
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chène, C.3    Winkler, F.K.4    Guha, A.5    Konigsberg, W.H.6
  • 23
    • 0033573837 scopus 로고    scopus 로고
    • Importance of factor VIIa Gla-domain residue Arg-36 for recognition of the macromolecular substrate factor X Gla-domain
    • W. Ruf, J. Shobe, S.M. Rao, C.D. Dickinson, A. Olson, and T.S. Edgington Importance of factor VIIa Gla-domain residue Arg-36 for recognition of the macromolecular substrate factor X Gla-domain Biochemistry 38 1999 1957 1966
    • (1999) Biochemistry , vol.38 , pp. 1957-1966
    • Ruf, W.1    Shobe, J.2    Rao, S.M.3    Dickinson, C.D.4    Olson, A.5    Edgington, T.S.6
  • 24
    • 0026540132 scopus 로고
    • Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII
    • W. Ruf, D.J. Miles, A. Rehemtulla, and T.S. Edgington Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII J. Biol. Chem. 267 1992 22206 22210
    • (1992) J. Biol. Chem. , vol.267 , pp. 22206-22210
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3    Edgington, T.S.4
  • 25
    • 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
    • L.V. Rao, and W. Ruf 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 34 1995 10867 10871
    • (1995) Biochemistry , vol.34 , pp. 10867-10871
    • Rao, L.V.1    Ruf, W.2
  • 26
    • 0029786640 scopus 로고    scopus 로고
    • Substrate recognition by tissue factor-factor VIIa. Evidence for interaction of residues Lys165 and Lys166 of tissue factor with the 4-carboxyglutamate-rich domain of factor X
    • Q. Huang, P.F. Neuenschwander, A.R. Rezaie, and J.H. Morrissey Substrate recognition by tissue factor-factor VIIa. Evidence for interaction of residues Lys165 and Lys166 of tissue factor with the 4-carboxyglutamate-rich domain of factor X J. Biol. Chem. 271 1996 21752 21757
    • (1996) J. Biol. Chem. , vol.271 , pp. 21752-21757
    • Huang, Q.1    Neuenschwander, P.F.2    Rezaie, A.R.3    Morrissey, J.H.4
  • 28
    • 0347291894 scopus 로고
    • Absolute hardness: Companion parameter to absolute electronegativity
    • R.G. Parr, and R.G. Pearson Absolute hardness: companion parameter to absolute electronegativity J. Am. Chem. Soc. 105 1983 7512 7516
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 7512-7516
    • Parr, R.G.1    Pearson, R.G.2
  • 29
    • 77951096477 scopus 로고    scopus 로고
    • Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. I. Application to blood coagulation: Direct cation-protein electronic effects vs. indirect interactions through water networks
    • B. de Courcy, L.G. Pedersen, O. Parisel, N. Gresh, B. Silvi, J. Pilmé, and J.P. Piquemal Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. I. Application to blood coagulation: direct cation-protein electronic effects vs. indirect interactions through water networks J. Chem. Theory Comput. 6 2010 1048 1063
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 1048-1063
    • De Courcy, B.1    Pedersen, L.G.2    Parisel, O.3    Gresh, N.4    Silvi, B.5    Pilmé, J.6    Piquemal, J.P.7
  • 30
    • 37549054088 scopus 로고    scopus 로고
    • 2 + in membrane binding of blood coagulation factors
    • 2 + in membrane binding of blood coagulation factors Structure 16 2008 72 81
    • (2008) Structure , vol.16 , pp. 72-81
    • Ohkubo, Y.Z.1    Tajkhorshid, E.2
  • 31
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • A.W. Shaw, V.S. Pureza, S.G. Sligar, and J.H. Morrissey The local phospholipid environment modulates the activation of blood clotting J. Biol. Chem. 282 2007 6556 6563
    • (2007) J. Biol. Chem. , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 32
    • 0030036599 scopus 로고    scopus 로고
    • Dynamic features of prothrombin interaction with phospholipid vesicles of different size and composition: Implications for protein-membrane contact
    • Y. Lu, and G.L. Nelsestuen Dynamic features of prothrombin interaction with phospholipid vesicles of different size and composition: implications for protein-membrane contact Biochemistry 35 1996 8193 8200
    • (1996) Biochemistry , vol.35 , pp. 8193-8200
    • Lu, Y.1    Nelsestuen, G.L.2
  • 33
    • 0033178858 scopus 로고    scopus 로고
    • Membrane association with multiple calcium ions: Vitamin-K-dependent proteins, annexins and pentraxins
    • G.L. Nelsestuen, and B.G. Ostrowski Membrane association with multiple calcium ions: vitamin-K-dependent proteins, annexins and pentraxins Curr. Opin. Struct. Biol. 9 1999 433 437
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 433-437
    • Nelsestuen, G.L.1    Ostrowski, B.G.2
  • 34
    • 0036318358 scopus 로고    scopus 로고
    • Interaction of bovine coagulation factor X and its glutamic-acid- containing fragments with phospholipid membranes. A surface plasmon resonance study
    • E.M. Erb, J. Stenflo, and T. Drakenberg Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study. Eur. J. Biochem. 269 2002 3041 3046
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3041-3046
    • Erb, E.M.1    Stenflo, J.2    Drakenberg, T.3
  • 35
    • 0041819513 scopus 로고    scopus 로고
    • Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins
    • M. Huang, A.C. Rigby, X. Morelli, M.A. Grant, G. Huang, and B. Furie Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins Nat. Struct. Biol. 10 2003 751 756
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 751-756
    • Huang, M.1    Rigby, A.C.2    Morelli, X.3    Grant, M.A.4    Huang, G.5    Furie, B.6
  • 36
    • 79960639587 scopus 로고    scopus 로고
    • Nanoscale studies of protein-membrane interactions in blood clotting
    • J.H. Morrissey, E. Tajkhorshid, and C.M. Rienstra Nanoscale studies of protein-membrane interactions in blood clotting J. Thromb. Haemost. 9 2011 162 167
    • (2011) J. Thromb. Haemost. , vol.9 , pp. 162-167
    • Morrissey, J.H.1    Tajkhorshid, E.2    Rienstra, C.M.3
  • 39
    • 0034050886 scopus 로고    scopus 로고
    • Mechanisms by which soluble endothelial cell protein C receptor modulates protein C and activated protein C function
    • P.C. Liaw, P.F. Neuenschwander, M.D. Smirnov, and C.T. Esmon Mechanisms by which soluble endothelial cell protein C receptor modulates protein C and activated protein C function J. Biol. Chem. 275 2000 5447 5452
    • (2000) J. Biol. Chem. , vol.275 , pp. 5447-5452
    • Liaw, P.C.1    Neuenschwander, P.F.2    Smirnov, M.D.3    Esmon, C.T.4
  • 40
    • 0035788254 scopus 로고    scopus 로고
    • Applications of anomalous scattering from S atoms for improved phasing of protein diffraction data collected at Cu Kα wavelength
    • C. Yang, and J.W. Pflugrath Applications of anomalous scattering from S atoms for improved phasing of protein diffraction data collected at Cu Kα wavelength Acta Crystallogr., Sect. D 57 2001 1480 1490
    • (2001) Acta Crystallogr., Sect. D , vol.57 , pp. 1480-1490
    • Yang, C.1    Pflugrath, J.W.2
  • 41
    • 0028267187 scopus 로고
    • Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C
    • T.L. Colpitts, and F.J. Castellino Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C Biochemistry 33 1994 3501 3508
    • (1994) Biochemistry , vol.33 , pp. 3501-3508
    • Colpitts, T.L.1    Castellino, F.J.2
  • 42
    • 0037047347 scopus 로고    scopus 로고
    • 2 + site in the protease domain of human activated protein C (APC). Sodium ion in the APC crystal structure is coordinated to four carbonyl groups from two separate loops
    • 2 + site in the protease domain of human activated protein C (APC). Sodium ion in the APC crystal structure is coordinated to four carbonyl groups from two separate loops J. Biol. Chem. 277 2002 28987 28995
    • (2002) J. Biol. Chem. , vol.277 , pp. 28987-28995
    • Schmidt, A.E.1    Padmanabhan, K.2    Underwood, M.C.3    Bode, W.4    Mather, T.5    Bajaj, S.P.6
  • 43
    • 0027972573 scopus 로고
    • Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C
    • M.D. Smirnov, and C.T. Esmon Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C J. Biol. Chem. 269 1994 816 819
    • (1994) J. Biol. Chem. , vol.269 , pp. 816-819
    • Smirnov, M.D.1    Esmon, C.T.2
  • 44
    • 0032762628 scopus 로고    scopus 로고
    • Enhancement of vitamin-K-dependent protein function by modification of the gamma-carboxyglutamic acid domain: Studies of protein C and factor VII
    • G.L. Nelsestuen Enhancement of vitamin-K-dependent protein function by modification of the gamma-carboxyglutamic acid domain: studies of protein C and factor VII Trends Cardiovasc. Med. 9 1999 162 167
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 162-167
    • Nelsestuen, G.L.1
  • 45
    • 34249722192 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor acts as a cellular receptor for factor VIIa on endothelium
    • S. Ghosh, U.R. Pendurthi, A. Steinoe, C.T. Esmon, and L.V. Rao Endothelial cell protein C receptor acts as a cellular receptor for factor VIIa on endothelium J. Biol. Chem. 282 2007 11849 11857
    • (2007) J. Biol. Chem. , vol.282 , pp. 11849-11857
    • Ghosh, S.1    Pendurthi, U.R.2    Steinoe, A.3    Esmon, C.T.4    Rao, L.V.5
  • 46
    • 27844553842 scopus 로고    scopus 로고
    • Chemical hardness and density functional theory
    • R.G. Pearson Chemical hardness and density functional theory J. Chem. Sci. 117 2005 369 377
    • (2005) J. Chem. Sci. , vol.117 , pp. 369-377
    • Pearson, R.G.1
  • 48
  • 49
    • 0032553444 scopus 로고    scopus 로고
    • Enhancement of human protein C function by site-directed mutagenesis of the gamma-carboxyglutamic acid domain
    • L. Shen, A.M. Shah, B. Dahlbäck, and G.L. Nelsestuen Enhancement of human protein C function by site-directed mutagenesis of the gamma-carboxyglutamic acid domain J. Biol. Chem. 273 1998 31086 31091
    • (1998) J. Biol. Chem. , vol.273 , pp. 31086-31091
    • Shen, L.1    Shah, A.M.2    Dahlbäck, B.3    Nelsestuen, G.L.4
  • 50
    • 0037424297 scopus 로고    scopus 로고
    • Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site
    • S.B. Harvey, M.D. Stone, M.B. Martinez, and G.L. Nelsestuen Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site J. Biol. Chem. 278 2003 8363 8369
    • (2003) J. Biol. Chem. , vol.278 , pp. 8363-8369
    • Harvey, S.B.1    Stone, M.D.2    Martinez, M.B.3    Nelsestuen, G.L.4
  • 52
    • 77949324716 scopus 로고    scopus 로고
    • Recent estimates of the structure of the factor VIIa (FVIIa)/tissue factor (TF) and factor Xa (FXa) ternary complex
    • C.J. Lee, V. Chandrasekaran, S. Wu, R.E. Duke, and L.G. Pedersen Recent estimates of the structure of the factor VIIa (FVIIa)/tissue factor (TF) and factor Xa (FXa) ternary complex Thromb. Res. 125 2010 S7 S10
    • (2010) Thromb. Res. , vol.125
    • Lee, C.J.1    Chandrasekaran, V.2    Wu, S.3    Duke, R.E.4    Pedersen, L.G.5
  • 53
    • 34250703112 scopus 로고    scopus 로고
    • Fibronectin-adherent monocytes express tissue factor and tissue factor pathway inhibitor whereas endotoxin-stimulated monocytes primarily express tissue factor: Physiologic and pathologic implications
    • M.S. Bajaj, M. Ghosh, and S.P. Bajaj Fibronectin-adherent monocytes express tissue factor and tissue factor pathway inhibitor whereas endotoxin-stimulated monocytes primarily express tissue factor: physiologic and pathologic implications J. Thromb. Haemost. 5 2007 1493 1499
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1493-1499
    • Bajaj, M.S.1    Ghosh, M.2    Bajaj, S.P.3
  • 54
    • 0015028817 scopus 로고
    • Cytochemical identification of monocytes and granulocytes
    • L.T. Yam, C.Y. Li, and W.H. Crosby Cytochemical identification of monocytes and granulocytes Am. J. Clin. Pathol. 55 1971 283 290
    • (1971) Am. J. Clin. Pathol. , vol.55 , pp. 283-290
    • Yam, L.T.1    Li, C.Y.2    Crosby, W.H.3
  • 55
    • 0012521621 scopus 로고
    • A method for viable cell count
    • S. Tolnai A method for viable cell count Methods Cell Sci. 1 1975 37 38
    • (1975) Methods Cell Sci. , vol.1 , pp. 37-38
    • Tolnai, S.1
  • 57
    • 0019785751 scopus 로고
    • A simplified procedure for purification of human prothrombin, factor IX and factor X
    • S.P. Bajaj, S.I. Rapaport, and C. Prodanos A simplified procedure for purification of human prothrombin, factor IX and factor X Prep. Biochem. 11 1981 397 412
    • (1981) Prep. Biochem. , vol.11 , pp. 397-412
    • Bajaj, S.P.1    Rapaport, S.I.2    Prodanos, C.3
  • 58
    • 0015239274 scopus 로고
    • Studies on the chemical and enzymatic modification of glycoproteins. A general method for the tritiation of sialic acid-containing glycoproteins
    • L. Van Lenten, and G. Ashwell Studies on the chemical and enzymatic modification of glycoproteins. A general method for the tritiation of sialic acid-containing glycoproteins J. Biol. Chem. 246 1971 1889 1894
    • (1971) J. Biol. Chem. , vol.246 , pp. 1889-1894
    • Van Lenten, L.1    Ashwell, G.2
  • 59
  • 60
    • 0037135531 scopus 로고    scopus 로고
    • Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase
    • S.K. Buddai, L. Toulokhonova, P.W. Bergum, G.P. Vlasuk, and S. Krishnaswamy Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase J. Biol. Chem. 277 2002 26689 26698
    • (2002) J. Biol. Chem. , vol.277 , pp. 26689-26698
    • Buddai, S.K.1    Toulokhonova, L.2    Bergum, P.W.3    Vlasuk, G.P.4    Krishnaswamy, S.5
  • 61
    • 0033603299 scopus 로고    scopus 로고
    • Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa
    • A. Mathur, and S.P. Bajaj Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa J. Biol. Chem. 274 1999 18477 18486
    • (1999) J. Biol. Chem. , vol.274 , pp. 18477-18486
    • Mathur, A.1    Bajaj, S.P.2
  • 62
    • 0019958515 scopus 로고
    • Decarboxylation of gamma-carboxyglutamic acid residues in human prothrombin. Stoichiometry of calcium binding to gamma-carboxyglutamic acid in prothrombin
    • S.P. Bajaj, P.A. Price, and W.A. Russell Decarboxylation of gamma-carboxyglutamic acid residues in human prothrombin. Stoichiometry of calcium binding to gamma-carboxyglutamic acid in prothrombin J. Biol. Chem. 257 1982 3726 3731
    • (1982) J. Biol. Chem. , vol.257 , pp. 3726-3731
    • Bajaj, S.P.1    Price, P.A.2    Russell, W.A.3
  • 63
    • 34447524033 scopus 로고    scopus 로고
    • Substitution of the Gla domain in factor X with that of protein C impairs its interaction with factor VIIa/tissue factor: Lack of comparable effect by similar substitution in factor IX
    • M. Ndonwi, G.J. Broze Jr., S. Agah, A.E. Schmidt, and S.P. Bajaj Substitution of the Gla domain in factor X with that of protein C impairs its interaction with factor VIIa/tissue factor: lack of comparable effect by similar substitution in factor IX J. Biol. Chem. 282 2007 15632 15644
    • (2007) J. Biol. Chem. , vol.282 , pp. 15632-15644
    • Ndonwi, M.1    Broze, Jr.G.J.2    Agah, S.3    Schmidt, A.E.4    Bajaj, S.P.5
  • 65
    • 0029908173 scopus 로고    scopus 로고
    • Functional consequences of mutations in amino acid residues that stabilize calcium binding to the first epidermal growth factor homology domain of human protein C
    • J.P. Geng, C.H. Cheng, and F.J. Castellino Functional consequences of mutations in amino acid residues that stabilize calcium binding to the first epidermal growth factor homology domain of human protein C Thromb. Haemost. 76 1996 720 728
    • (1996) Thromb. Haemost. , vol.76 , pp. 720-728
    • Geng, J.P.1    Cheng, C.H.2    Castellino, F.J.3
  • 66
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human alpha-thrombin: Interaction with d-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • W. Bode, I. Mayr, U. Baumann, R. Huber, S.R. Stone, and J. Hofsteenge The refined 1.9 Å crystal structure of human alpha-thrombin: interaction with d-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment EMBO J. 8 1989 3467 3475
    • (1989) EMBO J. , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 67
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 68
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 69
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallogr., Sect. A 50 1994 157 163
    • (1994) Acta Crystallogr., Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 72
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 760-763
  • 73
    • 0034630369 scopus 로고    scopus 로고
    • Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip
    • E.M. Erb, X. Chen, S. Allen, C.J. Roberts, S.J. Tendler, M.C. Davies, and S. Forsén Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip Anal. Biochem. 280 2000 29 35
    • (2000) Anal. Biochem. , vol.280 , pp. 29-35
    • Erb, E.M.1    Chen, X.2    Allen, S.3    Roberts, C.J.4    Tendler, S.J.5    Davies, M.C.6    Forsén, S.7
  • 74
    • 0023518606 scopus 로고
    • The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex
    • E.J. Husten, C.T. Esmon, and A.E. Johnson The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex J. Biol. Chem. 262 1987 12953 12961
    • (1987) J. Biol. Chem. , vol.262 , pp. 12953-12961
    • Husten, E.J.1    Esmon, C.T.2    Johnson, A.E.3
  • 75
    • 0000807711 scopus 로고
    • The determination of inorganic phosphate in the presence of labile phosphate esters
    • O.H. Lowry, and J.A. Lopez The determination of inorganic phosphate in the presence of labile phosphate esters J. Biol. Chem. 162 1946 421 428
    • (1946) J. Biol. Chem. , vol.162 , pp. 421-428
    • Lowry, O.H.1    Lopez, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.