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Volumn 11, Issue 1, 2000, Pages 89-100

Mutations in a potential phospholipid binding loop in the C2 domain of factor V affecting the assembly of the prothrombinase complex

Author keywords

APC; Coagulation; Factor V; Prothrombinase; Structural prediction; Threading; Thrombosis

Indexed keywords

BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 8A; MONOCLONAL ANTIBODY; PHOSPHOLIPID;

EID: 0033953116     PISSN: 09575235     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001721-200001000-00010     Document Type: Article
Times cited : (41)

References (68)
  • 2
    • 0018909419 scopus 로고
    • Human coagulation factor V purification and thrombin-catalysed activation
    • 2. Dahlbäck B. Human coagulation factor V purification and thrombin-catalysed activation. J Clin Invest 1980; 66: 583-591.
    • (1980) J Clin Invest , vol.66 , pp. 583-591
    • Dahlbäck, B.1
  • 3
    • 0019862464 scopus 로고
    • Purification and characterisation of human coagulation factor V
    • 3. Kane WH, Majerus PW. Purification and characterisation of human coagulation factor V. J Biol Chem 1981; 256: 1002-1007.
    • (1981) J Biol Chem , vol.256 , pp. 1002-1007
    • Kane, W.H.1    Majerus, P.W.2
  • 4
    • 0020320628 scopus 로고
    • Thrombin-catalysed activation of human coagulation factor V
    • 4. Suzuki K, Dahlbäck B, Stenflo J. Thrombin-catalysed activation of human coagulation factor V. J Biol Chem 1982; 257: 6556-6564.
    • (1982) J Biol Chem , vol.257 , pp. 6556-6564
    • Suzuki, K.1    Dahlbäck, B.2    Stenflo, J.3
  • 5
    • 0025139882 scopus 로고
    • Activation of human factor V by factor Xa and thrombin
    • 5. Monkovic D, Tracy P. Activation of human factor V by factor Xa and thrombin. Biochemistry 1990; 29: 1118-1128.
    • (1990) Biochemistry , vol.29 , pp. 1118-1128
    • Monkovic, D.1    Tracy, P.2
  • 8
    • 0020414822 scopus 로고
    • Formation of a calcium-binding site on bovine activated factor V following recombination of the isolated subunits
    • 8. Guinto ER, Esmon CT. Formation of a calcium-binding site on bovine activated factor V following recombination of the isolated subunits. J Biol Chem 1982; 257: 10038-10043.
    • (1982) J Biol Chem , vol.257 , pp. 10038-10043
    • Guinto, E.R.1    Esmon, C.T.2
  • 9
    • 0018622772 scopus 로고
    • The contribution of bovine factor V and factor Va to the activity of the prothrombinase
    • 9. Nesheim ME, Taswell JB, Mann KG. The contribution of bovine factor V and factor Va to the activity of the prothrombinase. J Biol Chem 1979; 254: 10952-10962.
    • (1979) J Biol Chem , vol.254 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 11
    • 0028013675 scopus 로고
    • Factor Va-membrane interaction is mediated by two regions located on the light chain of the cofactor
    • 11. Kalafatis M, Rand MD, Mann KG. Factor Va-membrane interaction is mediated by two regions located on the light chain of the cofactor. Biochemistry 1994; 33: 486-493.
    • (1994) Biochemistry , vol.33 , pp. 486-493
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 12
    • 0027957287 scopus 로고
    • Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids
    • 12. Lecompte MF, Bouix G, Mann KG. Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids. J Biol Chem 1994; 269: 1905-1910.
    • (1994) J Biol Chem , vol.269 , pp. 1905-1910
    • Lecompte, M.F.1    Bouix, G.2    Mann, K.G.3
  • 14
    • 0030066652 scopus 로고    scopus 로고
    • Insights into the complex association of bovine factor V(a) with acidic-lipid-containing synthetic membranes
    • 14. Cutsforth GA, Koppaka V, Krishnaswamy S, Wu JR, Mann KG, Lentz BR. Insights into the complex association of bovine factor V(a) with acidic-lipid-containing synthetic membranes. Biophys J 1996; 70(6): 2938-2949.
    • (1996) Biophys J , vol.70 , Issue.6 , pp. 2938-2949
    • Cutsforth, G.A.1    Koppaka, V.2    Krishnaswamy, S.3    Wu, J.R.4    Mann, K.G.5    Lentz, B.R.6
  • 15
    • 0018780186 scopus 로고
    • Phospholipid-binding properties of bovine factor V and factor Va
    • 15. Bloom JW, Nesheim ME, Mann KG. Phospholipid-binding properties of bovine factor V and factor Va. Biochemistry 1979; 18: 4419-4425.
    • (1979) Biochemistry , vol.18 , pp. 4419-4425
    • Bloom, J.W.1    Nesheim, M.E.2    Mann, K.G.3
  • 16
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • 16. Higgins DL, Mann KG. The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J Biol Chem 1983; 258: 6503-6508.
    • (1983) J Biol Chem , vol.258 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 17
    • 0020549866 scopus 로고
    • Interaction of bovine blood clotting factor Va and its subunits with phospholipid vesicles
    • 17. Van de Waart P, Bruls H, Hemker HC. Interaction of bovine blood clotting factor Va and its subunits with phospholipidvesicles. Biochemistry 1983;22:2427-2432.
    • (1983) Biochemistry , vol.22 , pp. 2427-2432
    • Van De Waart, P.1    Bruls, H.2    Hemker, H.C.3
  • 18
    • 0021734651 scopus 로고
    • Membrane binding properties of blood coagulation Factor V and derived peptides
    • 18. Pusey ML, Nelsestuen GL. Membrane binding properties of blood coagulation Factor V and derived peptides. Biochemistry 1984; 23: 6202-6210.
    • (1984) Biochemistry , vol.23 , pp. 6202-6210
    • Pusey, M.L.1    Nelsestuen, G.L.2
  • 19
    • 0020448997 scopus 로고
    • Factor Va-factor Xa interaction. Effects of phospholipid vesicles of varying composition
    • 19. Lindhout T, Govers Riemslag JW, van de Waart P, Hemker HC, Rosing, J. Factor Va-factor Xa interaction. Effects of phospholipid vesicles of varying composition. Biochemistry 1982; 21: 5494-5502.
    • (1982) Biochemistry , vol.21 , pp. 5494-5502
    • Lindhout, T.1    Govers Riemslag, J.W.2    Van De Waart, P.3    Hemker, H.C.4    Rosing, J.5
  • 20
    • 0027956509 scopus 로고
    • Structure of membrane-bound human factor Va
    • 20. Stoylova S, Mann KG, Brisson A. Structure of membrane-bound human factor Va. FEBS Lett 1994; 351: 330-334.
    • (1994) FEBS Lett , vol.351 , pp. 330-334
    • Stoylova, S.1    Mann, K.G.2    Brisson, A.3
  • 21
    • 0026709656 scopus 로고
    • Deletion analysis of recombinant human factor V. Evidence for a phosphatidylserine binding site in the second C-type domain
    • 21. Ortel TL, Devore Carter D, Quinn Allen M, Kane WH. Deletion analysis of recombinant human factor V. Evidence for a phosphatidylserine binding site in the second C-type domain. J Biol Chem 1992; 267: 4189-4198.
    • (1992) J Biol Chem , vol.267 , pp. 4189-4198
    • Ortel, T.L.1    Devore Carter, D.2    Quinn Allen, M.3    Kane, W.H.4
  • 22
    • 1842356814 scopus 로고
    • Prothrombinase complex assembly on the platelet surface is mediated through the 74,000-dalton component of factor Va
    • 22. Tracy PB, Mann KG. Prothrombinase complex assembly on the platelet surface is mediated through the 74,000-dalton component of factor Va. Proc Natl Acad Sci USA 1983; 80: 2380-2384.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2380-2384
    • Tracy, P.B.1    Mann, K.G.2
  • 23
    • 0021755607 scopus 로고
    • Interaction of prothrombin with factor Va-phospholipid complexes
    • 23. van de Waart P, Hemker HC, Lindhout T. Interaction of prothrombin with factor Va-phospholipid complexes. Biochemistry 1984; 23: 2838-2842.
    • (1984) Biochemistry , vol.23 , pp. 2838-2842
    • Van De Waart, P.1    Hemker, H.C.2    Lindhout, T.3
  • 24
    • 0023949710 scopus 로고
    • The binding of factor Va to phospholipid vesicles
    • 24. Krishnaswamy S, Mann KG. The binding of factor Va to phospholipid vesicles. J Biol Chem 1988; 263: 5714-5723.
    • (1988) J Biol Chem , vol.263 , pp. 5714-5723
    • Krishnaswamy, S.1    Mann, K.G.2
  • 25
    • 0028176740 scopus 로고
    • Localization of functionally important epitopes within the second C-type domain of coagulation factor V using recombinant chimeras
    • 25. Ortel TL, Quinn-Allen MA, Keller FG, Peterson JA, Larocca D, Kane WH. Localization of functionally important epitopes within the second C-type domain of coagulation factor V using recombinant chimeras. J Biol Chem 1994; 269: 15898-15905.
    • (1994) J Biol Chem , vol.269 , pp. 15898-15905
    • Ortel, T.L.1    Quinn-Allen, M.A.2    Keller, F.G.3    Peterson, J.A.4    Larocca, D.5    Kane, W.H.6
  • 26
    • 0033117450 scopus 로고    scopus 로고
    • Clinical and laboratory manifestations of anti-factor V antibodies
    • 26. Ortel TL. Clinical and laboratory manifestations ofanti-factor V antibodies. J Lab Clin Med 1999; 133: 326-334.
    • (1999) J Lab Clin Med , vol.133 , pp. 326-334
    • Ortel, T.L.1
  • 27
    • 0027442867 scopus 로고
    • Characterization of two forms of human factor Va with different cofactor activities
    • 27. Rosing J, Bakker HM, Thomassen MCLGD, Hemker HC, Tans G. Characterization of two forms of human factor Va with different cofactor activities. J Biol Chem 1993; 268: 21130-21136.
    • (1993) J Biol Chem , vol.268 , pp. 21130-21136
    • Rosing, J.1    Bakker, H.M.2    Thomassen, M.C.L.G.D.3    Hemker, H.C.4    Tans, G.5
  • 28
    • 0000197941 scopus 로고    scopus 로고
    • Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex
    • 28. Kim SW, Ortel TL, Quinn-Allen MA, Yoo L, Worfolf L, Zhai X, et al. Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex. Biochemistry 1999; 38: 11448-11545.
    • (1999) Biochemistry , vol.38 , pp. 11448-11545
    • Kim, S.W.1    Ortel, T.L.2    Quinn-Allen, M.A.3    Yoo, L.4    Worfolf, L.5    Zhai, X.6
  • 29
    • 0033549927 scopus 로고    scopus 로고
    • Partial glycosylation of Asn2181 in human factor V as a cause of molecular and functional heterogeneity, modulation of glycosylation efficiency by mutagenesis of the consensus sequence for N-linked glycosylation
    • 29. Nicolaes GAF, Villoutreix BO, Dahlbäck B. Partial glycosylation of Asn2181 in human factor V as a cause of molecular and functional heterogeneity, modulation of glycosylation efficiency by mutagenesis of the consensus sequence for N-linked glycosylation. Biochemistry 1999; 38: 13584-13591.
    • (1999) Biochemistry , vol.38 , pp. 13584-13591
    • Nicolaes, G.A.F.1    Villoutreix, B.O.2    Dahlbäck, B.3
  • 30
    • 0004484218 scopus 로고
    • Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin
    • 30. Kane WH, Davie EW. Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin. Proc Natl Acad Sci USA 1986; 83: 6800-6804.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6800-6804
    • Kane, W.H.1    Davie, E.W.2
  • 31
    • 0031826798 scopus 로고    scopus 로고
    • The discoidin domain family revisited: New members from prokaryotes and a homology-based fold prediction
    • 31. Baumgartner S, Hofmann K, Chiquet Ehrismann R, Bucher P. The discoidin domain family revisited: new members from prokaryotes and a homology-based fold prediction. Protein Sci 1998; 7: 1626-1631.
    • (1998) Protein Sci , vol.7 , pp. 1626-1631
    • Baumgartner, S.1    Hofmann, K.2    Chiquet Ehrismann, R.3    Bucher, P.4
  • 32
    • 0001238260 scopus 로고    scopus 로고
    • Molecular models for the two discoidin domains of human blood coagulation factor V
    • 32. Villoutreix BO, Bucher P, Hofmann K, Baumgartner S, Dahlbäck B. Molecular models for the two discoidin domains of human blood coagulation factor V. J Mol Model 1998; 4: 268-275.
    • (1998) J Mol Model , vol.4 , pp. 268-275
    • Villoutreix, B.O.1    Bucher, P.2    Hofmann, K.3    Baumgartner, S.4    Dahlbäck, B.5
  • 33
    • 0032467348 scopus 로고    scopus 로고
    • Homology models of the C domains of blood coagulation factors V and VIII: A proposed membrane binding mode for FV and FVIII C2 domains
    • 33. Pellequer JL, Gale AJ, Griffin JH, Getzoff ED. Homology models of the C domains of blood coagulation factors V and VIII: a proposed membrane binding mode for FV and FVIII C2 domains. Blood Cell Mol Dis 1998; 24: 448-461
    • (1998) Blood Cell Mol Dis , vol.24 , pp. 448-461
    • Pellequer, J.L.1    Gale, A.J.2    Griffin, J.H.3    Getzoff, E.D.4
  • 34
    • 0028290823 scopus 로고
    • Crystal structure of a free radical enzyme, galactose oxidase
    • 34. Ito N, Phillips SE, Yadav KD, Knowles PF. Crystal structure of a free radical enzyme, galactose oxidase. J Mol Biol 1994; 238: 794-814.
    • (1994) J Mol Biol , vol.238 , pp. 794-814
    • Ito, N.1    Phillips, S.E.2    Yadav, K.D.3    Knowles, P.F.4
  • 35
    • 0020628416 scopus 로고
    • Inactivation of human coagulation factor V by activated protein C
    • 35. Suzuki K, Stenflo J, Dahlbäck B, Teodorsson B. Inactivation of human coagulation factor V by activated protein C. J Biol Chem 1983; 258: 1914-1920.
    • (1983) J Biol Chem , vol.258 , pp. 1914-1920
    • Suzuki, K.1    Stenflo, J.2    Dahlbäck, B.3    Teodorsson, B.4
  • 36
    • 0029133654 scopus 로고
    • Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein
    • 36. Nicolaes GAF, Tans G, Thomassen MCLGD, Hemker HC, Pabinger I, Varadi K, et al. Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein. J Biol Chem 1995; 270: 21158-21166.
    • (1995) J Biol Chem , vol.270 , pp. 21158-21166
    • Nicolaes, G.A.F.1    Tans, G.2    Thomassen, M.C.L.G.D.3    Hemker, H.C.4    Pabinger, I.5    Varadi, K.6
  • 37
    • 0030805611 scopus 로고    scopus 로고
    • Cleavage requirements for activation of factor V by factor Xa
    • 37. Thorelli E, Kaufman RJ, Dahlbäck B. Cleavage requirements for activation of factor V by factor Xa. Eur J Biochem 1997; 247: 12-20.
    • (1997) Eur J Biochem , vol.247 , pp. 12-20
    • Thorelli, E.1    Kaufman, R.J.2    Dahlbäck, B.3
  • 38
    • 0014517882 scopus 로고
    • Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes
    • 38. Chase T Jr, Shaw E. Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes. Biochemistry 1969; 8: 2212-2224.
    • (1969) Biochemistry , vol.8 , pp. 2212-2224
    • Chase T., Jr.1    Shaw, E.2
  • 39
    • 0015919592 scopus 로고
    • Titration of activated bovine Factor X
    • 39. Smith RL. Titration of activated bovine Factor X. J Biol Chem 1973; 248: 2418-2423.
    • (1973) J Biol Chem , vol.248 , pp. 2418-2423
    • Smith, R.L.1
  • 40
    • 0025375266 scopus 로고
    • Vectors used for expression in mammalian cells
    • 40. Kaufman RJ. Vectors used for expression in mammalian cells. Methods Enzymol 1990: 185: 487-511.
    • (1990) Methods Enzymol , vol.185 , pp. 487-511
    • Kaufman, R.J.1
  • 41
    • 0032569021 scopus 로고    scopus 로고
    • The C-terminal region of the factor V B-domain is crucial for the anticoagulant activity of factor V
    • 41. Thorelli E, Kaufman RJ, Dahlbäck B. The C-terminal region of the factor V B-domain is crucial for the anticoagulant activity of factor V. J Biol Chem 1998; 273: 16140-16145.
    • (1998) J Biol Chem , vol.273 , pp. 16140-16145
    • Thorelli, E.1    Kaufman, R.J.2    Dahlbäck, B.3
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 43. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots
    • 44. Blake MS, Johnston KH, Russell Jones GJ, Gotschlich EC. A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal Biochem 1984; 136: 175-179.
    • (1984) Anal Biochem , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell Jones, G.J.3    Gotschlich, E.C.4
  • 45
    • 0008876624 scopus 로고    scopus 로고
    • Identification of a phosphatidylserine binding site within the C2 domain of human factor V using alanine scanning mutagenesis
    • 45. Kim SW, Quinn-Allen MA, Camp T, Macedo-Ribeiro S, Fuentes-Prior P, Bode W, et al. Identification of a phosphatidylserine binding site within the C2 domain of human factor V using alanine scanning mutagenesis [Abstract] Thrombosis Haemostasis 1999; Suppl. 234: 13.
    • (1999) Thrombosis Haemostasis , Issue.SUPPL. 234 , pp. 13
    • Kim, S.W.1    Quinn-Allen, M.A.2    Camp, T.3    Macedo-Ribeiro, S.4    Fuentes-Prior, P.5    Bode, W.6
  • 47
    • 0021229415 scopus 로고
    • Electron microscopy and hydrodynamic properties of blood clotting factor V and activation fragments of factor V with phospholipid vesicles
    • 47. Lampe PD, Pusey ML, Wei GJ, Nelsestuen GL. Electron microscopy and hydrodynamic properties of blood clotting factor V and activation fragments of factor V with phospholipid vesicles. J Biol Chem 1984; 259: 9959-9964.
    • (1984) J Biol Chem , vol.259 , pp. 9959-9964
    • Lampe, P.D.1    Pusey, M.L.2    Wei, G.J.3    Nelsestuen, G.L.4
  • 48
    • 0027998241 scopus 로고
    • Determination of the disulphide bridges in factor Va heavy chain
    • 48. Xue J, Kalafatis M, Silveira JR, Kung C, Mann KG. Determination of the disulphide bridges in factor Va heavy chain. Biochemistry 1994; 33: 13109-13116.
    • (1994) Biochemistry , vol.33 , pp. 13109-13116
    • Xue, J.1    Kalafatis, M.2    Silveira, J.R.3    Kung, C.4    Mann, K.G.5
  • 50
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • 50. Reithmeier RA. Characterization and modeling of membrane proteins using sequence analysis. Curr Opin Struct Biol 1995; 5: 491-500.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 491-500
    • Reithmeier, R.A.1
  • 51
    • 0033557175 scopus 로고    scopus 로고
    • Major structural determinants of transmembrane proteins identified by principal component analysis
    • 51. Koshi JM, Bruno WJ. Major structural determinants of transmembrane proteins identified by principal component analysis. Proteins 1999; 34: 333-340.
    • (1999) Proteins , vol.34 , pp. 333-340
    • Koshi, J.M.1    Bruno, W.J.2
  • 52
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • 52. Pautsch A, Schulz GE. Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 1998; 5: 1013-1017.
    • (1998) Nat Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 53
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • 53. Yau WM, Wimley WC, Gawrisch K, White SH. The preference of tryptophan for membrane interfaces. Biochemistry 1998; 37: 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 54
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • 54. Dougherty DA. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 1996; 271: 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 55
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • 55. Nozaki Y, Tanford C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem 1971; 246: 2211-2217.
    • (1971) J Biol Chem , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 56
    • 0017157584 scopus 로고
    • A simplified representation of protein conformations for rapid simulation of protein folding
    • 56. Levitt M. A simplified representation of protein conformations for rapid simulation of protein folding. J Mol Biol 1976; 104: 59-107.
    • (1976) J Mol Biol , vol.104 , pp. 59-107
    • Levitt, M.1
  • 57
    • 0028880755 scopus 로고
    • Prothrombin contributes to the assembly of the factor Va-factor Xa complex at phospbatidylserine-containing phospholipid membranes
    • 57. Billy D, Willems GM, Hemker HC, Lindhout T. Prothrombin contributes to the assembly of the factorVa-factor Xa complex at phospbatidylserine-containing phospholipid membranes. J Biol Chem 1995; 270: 26883-26889.
    • (1995) J Biol Chem , vol.270 , pp. 26883-26889
    • Billy, D.1    Willems, G.M.2    Hemker, H.C.3    Lindhout, T.4
  • 58
    • 0016325557 scopus 로고
    • The conversion of prothrombin to thrombin. IV. The function of the fragment 2 region during activation in the presence of factor V
    • 58. Esmon CT, Jackson CM. The conversion of prothrombin to thrombin. IV. The function of the fragment 2 region during activation in the presence of factor V. J Biol Chem 1974; 249: 7791-7797.
    • (1974) J Biol Chem , vol.249 , pp. 7791-7797
    • Esmon, C.T.1    Jackson, C.M.2
  • 59
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor V and human factor Va by activated protein C
    • 59. Kalafatis M, Rand MD, Mann KG. The mechanism of inactivation of human factor V and human factor Va by activated protein C. J Biol Chem 1994; 269: 31869-31880.
    • (1994) J Biol Chem , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 60
    • 2642679231 scopus 로고    scopus 로고
    • Structural investigation of the A domains of human blood coagulation factor V by molecular modeling
    • 60. Villoutreix BO, Dahlbäck B. Structural investigation of the A domains of human blood coagulation factor V by molecular modeling. Protein Sci 1998; 7: 1317-1325.
    • (1998) Protein Sci , vol.7 , pp. 1317-1325
    • Villoutreix, B.O.1    Dahlbäck, B.2
  • 61
    • 0030770425 scopus 로고    scopus 로고
    • Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography
    • 61. Yegneswaran S, Wood GM, Esmon CT, Johnson AE. Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography. J Biol Chem 1997; 272: 25013-25021.
    • (1997) J Biol Chem , vol.272 , pp. 25013-25021
    • Yegneswaran, S.1    Wood, G.M.2    Esmon, C.T.3    Johnson, A.E.4
  • 62
    • 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
    • 62. Husten EJ, Esmon CT, Johnson AE. 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 1987; 262: 12953-12961.
    • (1987) J Biol Chem , vol.262 , pp. 12953-12961
    • Husten, E.J.1    Esmon, C.T.2    Johnson, A.E.3
  • 63
    • 0033579442 scopus 로고    scopus 로고
    • Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers
    • in press
    • 63. Stoylova SS, Lenting PJ, Kemball-Cook G, Holzenburg A. Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers. J Biol Chem 1999; (in press).
    • (1999) J Biol Chem
    • Stoylova, S.S.1    Lenting, P.J.2    Kemball-Cook, G.3    Holzenburg, A.4
  • 64
  • 65
    • 0021718109 scopus 로고
    • Loss of prothrombin and of factor Xa-factor Va interactions upon inactivation of factor Va by activated protein C
    • 65. Guinto ER, Esmon CT. Loss of prothrombin and of factor Xa-factor Va interactions upon inactivation of factor Va by activated protein C. J Biol Chem 1984; 259: 13986-13992.
    • (1984) J Biol Chem , vol.259 , pp. 13986-13992
    • Guinto, E.R.1    Esmon, C.T.2
  • 66
    • 0024582038 scopus 로고
    • Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: Analysis by analytical ultracentrifugation
    • 66. Luckow EA, Lyons DA, Ridgeway TM, Esmon CT, Laue TM. Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: analysis by analytical ultracentrifugation. Biochemistry 1989; 28: 2348-2354.
    • (1989) Biochemistry , vol.28 , pp. 2348-2354
    • Luckow, E.A.1    Lyons, D.A.2    Ridgeway, T.M.3    Esmon, C.T.4    Laue, T.M.5
  • 67
    • 0025816859 scopus 로고
    • The association of coagulation factor Xa and factor Va
    • 67. Pryzdial ELG, Mann KG, The association of coagulation factor Xa and factor Va. J Cell Biochem 1991; 266: 8960-8977.
    • (1991) J Cell Biochem , vol.266 , pp. 8960-8977
    • Pryzdial, E.L.G.1    Mann, K.G.2
  • 68
    • 0028289629 scopus 로고
    • Contribution of the heavy and light chains of factor Va to the interaction with factor Xa
    • 68. Kalafatis M, Xue J, Lawler CM, Mann KG. Contribution of the heavy and light chains of factor Va to the interaction with factor Xa. Biochemistry 1994; 33: 6538-6545.
    • (1994) Biochemistry , vol.33 , pp. 6538-6545
    • Kalafatis, M.1    Xue, J.2    Lawler, C.M.3    Mann, K.G.4


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