메뉴 건너뛰기




Volumn 70, Issue 1, 1996, Pages 174-181

Theory of allosteric effects in serine proteases

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE; THROMBOMODULIN;

EID: 0030050922     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79558-9     Document Type: Article
Times cited : (38)

References (21)
  • 1
    • 0004058088 scopus 로고
    • MIT Press, Cambridge, MA
    • Beck, W. S. 1991. Hematology MIT Press, Cambridge, MA.
    • (1991) Hematology
    • Beck, W.S.1
  • 2
    • 37049153631 scopus 로고
    • Analytical description of the effects of modifiers and of multivalency upon the steady state catalyzed reaction rate
    • Botts, J., and M. Morales. 1953. Analytical description of the effects of modifiers and of multivalency upon the steady state catalyzed reaction rate. Trans. Faraday Soc. 49:696-707.
    • (1953) Trans. Faraday Soc. , vol.49 , pp. 696-707
    • Botts, J.1    Morales, M.2
  • 3
    • 0029014036 scopus 로고
    • An allosteric switch controls the pro-coagulant and anti-coagulant activities of thrombin
    • Dang, Q. D., A. Vindigni, and E. Di Cera. 1995. An allosteric switch controls the pro-coagulant and anti-coagulant activities of thrombin. Proc. Natl. Acad. Sci USA. 92:5977-5981.
    • (1995) Proc. Natl. Acad. Sci USA , vol.92 , pp. 5977-5981
    • Dang, Q.D.1    Vindigni, A.2    Di Cera, E.3
  • 5
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon, C. T. 1989. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J. Biol. Chem. 264:4743-1746.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743-11746
    • Esmon, C.T.1
  • 7
    • 0003424777 scopus 로고
    • Benjamin/Cummings Publishing Co., Menlo Park, CA
    • Gould, R. 1988. Graph Theory. Benjamin/Cummings Publishing Co., Menlo Park, CA.
    • (1988) Graph Theory
    • Gould, R.1
  • 9
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King, E. L , and C. Altman. 1956 A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. 50:1375-1378.
    • (1956) J. Phys. Chem. , vol.50 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 11
    • 0026733611 scopus 로고
    • Interaction of des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C
    • Le Bonniec, B. F., E. R. Guinto, and C. T. Esmon. 1992. Interaction of des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. J. Biol. Chem. 267:19341-19348.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19341-19348
    • Le Bonniec, B.F.1    Guinto, E.R.2    Esmon, C.T.3
  • 12
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann, K. G., M. E. Nesheim, W. R. Church, P. Haley, and S. Krishnaswamy. 1990. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood. 76:1-16.
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 13
    • 0027983980 scopus 로고
    • Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin
    • Mathews, I. I., K. P. Padmanabhan, A. Tulinsky, and J. E. Sadler. 1994. Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin. Biochemistry. 33:13547-13552
    • (1994) Biochemistry , vol.33 , pp. 13547-13552
    • Mathews, I.I.1    Padmanabhan, K.P.2    Tulinsky, A.3    Sadler, J.E.4
  • 14
    • 0020621644 scopus 로고
    • Kinetics of activation of human prothrombin. Use of a fluorescein-labeled derivative to obtain kinetic constants as a function of factor V concentration and activation state
    • Morrison, S. A. 1983. Kinetics of activation of human prothrombin. Use of a fluorescein-labeled derivative to obtain kinetic constants as a function of factor V concentration and activation state. Biochemistry. 22.4053-4061.
    • (1983) Biochemistry , vol.22 , pp. 4053-4061
    • Morrison, S.A.1
  • 15
    • 0017802964 scopus 로고
    • The effect of metal ions on the amidolytic activity of human factor Xa (activated Stuart-Prower factor)
    • Orthner, C. L , and D. P. Kosow. 1978. The effect of metal ions on the amidolytic activity of human factor Xa (activated Stuart-Prower factor) Arch. Biochem. Biophys. 185:400-406.
    • (1978) Arch. Biochem. Biophys. , vol.185 , pp. 400-406
    • Orthner, C.L.1    Kosow, D.P.2
  • 16
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J., and C. S. Craik. 1995. Structural basis of substrate specificity in the serine proteases. Protein Sci. 4:337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 17
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York
    • Segel, I. H. 1975. Enzyme Kinetics. John Wiley and Sons, New York.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 18
    • 0019324165 scopus 로고
    • Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations
    • Steiner, S. A., G. N. Amphlett, and F. J. Castellino. 1980. Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations. Biochem. Biophys. Res. Commun. 94:340-347.
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 340-347
    • Steiner, S.A.1    Amphlett, G.N.2    Castellino, F.J.3
  • 19
    • 0021984208 scopus 로고
    • Kinetic mechanism for stimulation by monovalent cations of the amidase activity of the plasma protease bovine activated protein C
    • Steiner, S. A., and F. J. Castellino. 1985. Kinetic mechanism for stimulation by monovalent cations of the amidase activity of the plasma protease bovine activated protein C. Biochemistry. 24:609-617.
    • (1985) Biochemistry , vol.24 , pp. 609-617
    • Steiner, S.A.1    Castellino, F.J.2
  • 20
    • 0014947813 scopus 로고
    • Enzymes activated by monovalent cations
    • Suelter, C. H. 1970. Enzymes activated by monovalent cations. Science. 168:789-795.
    • (1970) Science , vol.168 , pp. 789-795
    • Suelter, C.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.